|
Name |
Accession |
Description |
Interval |
E-value |
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
24-262 |
5.98e-160 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 443.67 E-value: 5.98e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTrQLTGSALRQLRSRVG 103
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDL-TDSKKDINKLRRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 104 FVFQQFNLYAHLTAQENITLALERVHGWSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQIILF 183
Cdd:COG1126 81 MVFQQFNLFPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504650440 184 DEPTSALDPEMIGEVLQVMKTLAHSGITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAEFFARPQHARTRRFLQKV 262
Cdd:COG1126 161 DEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHERTRAFLSKV 239
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
24-237 |
2.07e-126 |
|
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: 358.00 E-value: 2.07e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQlTGSALRQLRSRVG 103
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTD-DKKNINELRQKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 104 FVFQQFNLYAHLTAQENITLALERVHGWSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQIILF 183
Cdd:cd03262 80 MVFQQFNLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 504650440 184 DEPTSALDPEMIGEVLQVMKTLAHSGITMVVVTHEMQFAREIADRVVFIDGGDI 237
Cdd:cd03262 160 DEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
24-262 |
2.19e-110 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 318.58 E-value: 2.19e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQlTGSALRQLRSRVG 103
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVND-PKVDERLIRQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 104 FVFQQFNLYAHLTAQENITLALERVHGWSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQIILF 183
Cdd:PRK09493 81 MVFQQFYLFPHLTALENVMFGPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504650440 184 DEPTSALDPEMIGEVLQVMKTLAHSGITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAEFFARPQHARTRRFLQKV 262
Cdd:PRK09493 161 DEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEFLQHV 239
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
17-263 |
2.33e-109 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 316.36 E-value: 2.33e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 17 SHLQRASIEFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTGSA-- 94
Cdd:COG4598 2 TDTAPPALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPDRDge 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 95 --------LRQLRSRVGFVFQQFNLYAHLTAQENITLALERVHGWSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQ 166
Cdd:COG4598 82 lvpadrrqLQRIRTRLGMVFQSFNLWSHMTVLENVIEAPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 167 RVAIARALASSPQIILFDEPTSALDPEMIGEVLQVMKTLAHSGITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAEF 246
Cdd:COG4598 162 RAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEV 241
|
250
....*....|....*..
gi 504650440 247 FARPQHARTRRFLQKVL 263
Cdd:COG4598 242 FGNPKSERLRQFLSSSL 258
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
24-265 |
2.07e-106 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 312.01 E-value: 2.07e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSY----GDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTGSALRQLR 99
Cdd:COG1135 2 IELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 100 SRVGFVFQQFNLYAHLTAQENITLALErVHGWSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQ 179
Cdd:COG1135 82 RKIGMIFQHFNLLSSRTVAENVALPLE-IAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 180 IILFDEPTSALDPEMIGEVLQVMKTLAHS-GITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAEFFARPQHARTRRF 258
Cdd:COG1135 161 VLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQSELTRRF 240
|
....*..
gi 504650440 259 LQKVLDP 265
Cdd:COG1135 241 LPTVLND 247
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
22-263 |
5.18e-97 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 284.72 E-value: 5.18e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 22 ASIEFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGG-----EILIDG-KPTRQLTGsAL 95
Cdd:PRK11264 2 SAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGtirvgDITIDTaRSLSQQKG-LI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 96 RQLRSRVGFVFQQFNLYAHLTAQENITLALERVHGWSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALA 175
Cdd:PRK11264 81 RQLRQHVGFVFQNFNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 176 SSPQIILFDEPTSALDPEMIGEVLQVMKTLAHSGITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAEFFARPQHART 255
Cdd:PRK11264 161 MRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPRT 240
|
....*...
gi 504650440 256 RRFLQKVL 263
Cdd:PRK11264 241 RQFLEKFL 248
|
|
| ectoine_ehuA |
TIGR03005 |
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ... |
24-263 |
3.22e-93 |
|
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding protein of a conserved four gene ABC transporter operon found next to ectoine unilization operons and ectoine biosynthesis operons. Ectoine is a compatible solute that protects enzymes from high osmolarity. It is released by some species in response to hypoosmotic shock, and it is taken up by a number of bacteria as a compatible solute or for consumption. This family shows strong sequence similiarity to a number of amino acid ABC transporter ATP-binding proteins.
Pssm-ID: 132050 [Multi-domain] Cd Length: 252 Bit Score: 275.17 E-value: 3.22e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTGSA--------- 94
Cdd:TIGR03005 1 VRFSDVTKRFGILTVLDGLNFSVAAGEKVALIGPSGSGKSTILRILMTLEPIDEGQIQVEGEQLYHMPGRNgplvpadek 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 95 -LRQLRSRVGFVFQQFNLYAHLTAQENITLALERVHGWSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARA 173
Cdd:TIGR03005 81 hLRQMRNKIGMVFQSFNLFPHKTVLDNVTEAPVLVLGMARAEAEKRAMELLDMVGLADKADHMPAQLSGGQQQRVAIARA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 174 LASSPQIILFDEPTSALDPEMIGEVLQVMKTLAH-SGITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAEFFARPQH 252
Cdd:TIGR03005 161 LAMRPKVMLFDEVTSALDPELVGEVLNVIRRLASeHDLTMLLVTHEMGFAREFADRVCFFDKGRIVEQGKPDEIFRQPKE 240
|
250
....*....|.
gi 504650440 253 ARTRRFLQKVL 263
Cdd:TIGR03005 241 ERTREFLSKVI 251
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
24-239 |
7.76e-93 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 273.46 E-value: 7.76e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYGD----HRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTGSALRQLR 99
Cdd:COG1136 5 LELRNLTKSYGTgegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELARLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 100 SR-VGFVFQQFNLYAHLTAQENITLALeRVHGWSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSP 178
Cdd:COG1136 85 RRhIGFVFQFFNLLPELTALENVALPL-LLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504650440 179 QIILFDEPTSALDPEMIGEVLQVMKTLAH-SGITMVVVTHEMQFArEIADRVVFIDGGDILE 239
Cdd:COG1136 164 KLILADEPTGNLDSKTGEEVLELLRELNReLGTTIVMVTHDPELA-ARADRVIRLRDGRIVS 224
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
24-251 |
1.44e-92 |
|
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: 272.92 E-value: 1.44e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYGDHR----VLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTGSALRQLR 99
Cdd:cd03258 2 IELKNVSKVFGDTGgkvtALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 100 SRVGFVFQQFNLYAHLTAQENITLALErVHGWSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQ 179
Cdd:cd03258 82 RRIGMIFQHFNLLSSRTVFENVALPLE-IAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504650440 180 IILFDEPTSALDPEMIGEVLQVMKTLAHS-GITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAEFFARPQ 251
Cdd:cd03258 161 VLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
24-259 |
3.51e-92 |
|
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: 272.24 E-value: 3.51e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTGSALRQLRSRVG 103
Cdd:COG1127 6 IEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELRRRIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 104 FVFQQFNLYAHLTAQENITLALERVHGWSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQIILF 183
Cdd:COG1127 86 MLFQGGALFDSLTVFENVAFPLREHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILLY 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504650440 184 DEPTSALDPEMIGEVLQVMKTLAHS-GITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAEFFArPQHARTRRFL 259
Cdd:COG1127 166 DEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLA-SDDPWVRQFL 241
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
23-259 |
3.06e-88 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 262.26 E-value: 3.06e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 23 SIEFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKP---TRQLTGSALRQLR 99
Cdd:COG4161 2 SIQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQfdfSQKPSEKAIRLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 100 SRVGFVFQQFNLYAHLTAQENITLALERVHGWSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQ 179
Cdd:COG4161 82 QKVGMVFQQYNLWPHLTVMENLIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 180 IILFDEPTSALDPEMIGEVLQVMKTLAHSGITMVVVTHEMQFAREIADRVVFIDGGDILEVApPAEFFARPQHARTRRFL 259
Cdd:COG4161 162 VLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQG-DASHFTQPQTEAFAHYL 240
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
24-264 |
4.83e-87 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 262.81 E-value: 4.83e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSY----GDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTGSALRQLR 99
Cdd:PRK11153 2 IELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 100 SRVGFVFQQFNLYAHLTAQENITLALErVHGWSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQ 179
Cdd:PRK11153 82 RQIGMIFQHFNLLSSRTVFDNVALPLE-LAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 180 IILFDEPTSALDPEMIGEVLQVMK----TLahsGITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAEFFARPQHART 255
Cdd:PRK11153 161 VLLCDEATSALDPATTRSILELLKdinrEL---GLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLT 237
|
....*....
gi 504650440 256 RRFLQKVLD 264
Cdd:PRK11153 238 REFIQSTLH 246
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
24-245 |
2.11e-86 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 256.90 E-value: 2.11e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSY-GDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTGSALRQLRSRV 102
Cdd:COG2884 2 IRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 103 GFVFQQFNLYAHLTAQENITLALeRVHGWSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQIIL 182
Cdd:COG2884 82 GVVFQDFRLLPDRTVYENVALPL-RVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504650440 183 FDEPTSALDPEMIGEVLQVMKTLAHSGITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAE 245
Cdd:COG2884 161 ADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDEARGV 223
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
24-237 |
3.08e-86 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 256.26 E-value: 3.08e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYGD----HRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTGSALRQLR 99
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 100 SR-VGFVFQQFNLYAHLTAQENITLALeRVHGWSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSP 178
Cdd:cd03255 81 RRhIGFVFQSFNLLPDLTALENVELPL-LLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 179 QIILFDEPTSALDPEMIGEVLQVMKTLAH-SGITMVVVTHEMQFArEIADRVVFIDGGDI 237
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVMELLRELNKeAGTTIVVVTHDPELA-EYADRIIELRDGKI 218
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
24-246 |
7.22e-86 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 256.52 E-value: 7.22e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSY-GDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTGSALRQLRSRV 102
Cdd:COG3638 3 LELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLRRRI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 103 GFVFQQFNLYAHLTAQENITL-ALERVHGWS------KSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALA 175
Cdd:COG3638 83 GMIFQQFNLVPRLSVLTNVLAgRLGRTSTWRsllglfPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIARALV 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504650440 176 SSPQIILFDEPTSALDPEMIGEVLQVMKTLAHS-GITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAEF 246
Cdd:COG3638 163 QEPKLILADEPVASLDPKTARQVMDLLRRIAREdGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAEL 234
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
24-258 |
1.11e-83 |
|
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: 250.50 E-value: 1.11e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTGSALRQLRSRVG 103
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 104 FVFQQFNLYAHLTAQENITLALERVHGWSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQIILF 183
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFPLREHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLY 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504650440 184 DEPTSALDPEMIGEVLQVMKTL-AHSGITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAEFFARpQHARTRRF 258
Cdd:cd03261 161 DEPTAGLDPIASGVIDDLIRSLkKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRAS-DDPLVRQF 235
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
23-260 |
1.48e-83 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 250.32 E-value: 1.48e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 23 SIEFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKP---TRQLTGSALRQLR 99
Cdd:PRK11124 2 SIQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHfdfSKTPSDKAIRELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 100 SRVGFVFQQFNLYAHLTAQENITLALERVHGWSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQ 179
Cdd:PRK11124 82 RNVGMVFQQYNLWPHLTVQQNLIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 180 IILFDEPTSALDPEMIGEVLQVMKTLAHSGITMVVVTHEMQFAREIADRVVFIDGGDILEVApPAEFFARPQharTRRFL 259
Cdd:PRK11124 162 VLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQG-DASCFTQPQ---TEAFK 237
|
.
gi 504650440 260 Q 260
Cdd:PRK11124 238 N 238
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
28-263 |
2.70e-83 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 250.27 E-value: 2.70e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 28 DVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTGS----------ALRQ 97
Cdd:PRK10619 10 DLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKdgqlkvadknQLRL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 98 LRSRVGFVFQQFNLYAHLTAQENITLALERVHGWSKSAARERSLALLSQVGLADKARQ-MPAQLSGGQQQRVAIARALAS 176
Cdd:PRK10619 90 LRTRLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGkYPVHLSGGQQQRVSIARALAM 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 177 SPQIILFDEPTSALDPEMIGEVLQVMKTLAHSGITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAEFFARPQHARTR 256
Cdd:PRK10619 170 EPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSPRLQ 249
|
....*..
gi 504650440 257 RFLQKVL 263
Cdd:PRK10619 250 QFLKGSL 256
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
22-259 |
4.76e-83 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 252.71 E-value: 4.76e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 22 ASIEFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPtrqLTGSALRQlRsR 101
Cdd:COG3842 4 PALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRD---VTGLPPEK-R-N 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 102 VGFVFQQFNLYAHLTAQENITLALeRVHGWSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQII 181
Cdd:COG3842 79 VGMVFQDYALFPHLTVAENVAFGL-RMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 182 LFDEPTSALDP----EMIGEVLQVMKTLahsGITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAEFFARPQHARTRR 257
Cdd:COG3842 158 LLDEPLSALDAklreEMREELRRLQREL---GITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVAD 234
|
..
gi 504650440 258 FL 259
Cdd:COG3842 235 FI 236
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
24-249 |
4.92e-83 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 248.83 E-value: 4.92e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRqltgSALRQLRSRVG 103
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVA----RDPAEVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 104 FVFQQFNLYAHLTAQENITLALeRVHGWSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQIILF 183
Cdd:COG1131 77 YVPQEPALYPDLTVRENLRFFA-RLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLIL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504650440 184 DEPTSALDPEMIGEVLQVMKTLAHSGITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAEFFAR 249
Cdd:COG1131 156 DEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
24-251 |
2.64e-81 |
|
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: 244.16 E-value: 2.64e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSY-GDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTgsaLRQLRSRV 102
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKN---LRELRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 103 GFVFQ----QFnlyAHLTAQENITLALERvHGWSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSP 178
Cdd:COG1122 78 GLVFQnpddQL---FAPTVEEDVAFGPEN-LGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEP 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504650440 179 QIILFDEPTSALDPEMIGEVLQVMKTLAHSGITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAEFFARPQ 251
Cdd:COG1122 154 EVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYE 226
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
24-265 |
4.72e-81 |
|
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: 252.90 E-value: 4.72e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSY-----GDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTGSALRQL 98
Cdd:COG1123 261 LEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 99 RSRVGFVFQ----QFNlyAHLTAQENITLALERVHGWSKSAARERSLALLSQVGL-ADKARQMPAQLSGGQQQRVAIARA 173
Cdd:COG1123 341 RRRVQMVFQdpysSLN--PRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIARA 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 174 LASSPQIILFDEPTSALDPEMIGEVLQVMKTLAHS-GITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAEFFARPQH 252
Cdd:COG1123 419 LALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQH 498
|
250
....*....|....*
gi 504650440 253 ARTRRFLQKV--LDP 265
Cdd:COG1123 499 PYTRALLAAVpsLDP 513
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
24-246 |
9.16e-81 |
|
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: 243.24 E-value: 9.16e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYGD-HRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTGSALRQLRSRV 102
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 103 GFVFQQFNLYAHLTAQENITL-ALERVH------GWSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALA 175
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSgRLGRRStwrslfGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504650440 176 SSPQIILFDEPTSALDPEMIGEVLQVMKTLAHS-GITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAEF 246
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
20-272 |
2.86e-78 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 237.68 E-value: 2.86e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 20 QRASIEFRDVAKSY----GDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPtrqltgsaL 95
Cdd:COG1116 4 AAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKP--------V 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 96 RQLRSRVGFVFQQFNLYAHLTAQENITLALErVHGWSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALA 175
Cdd:COG1116 76 TGPGPDRGVVFQEPALLPWLTVLDNVALGLE-LRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 176 SSPQIILFDEPTSALDpEMIGEVLQ--VMKTLAHSGITMVVVTHEMQFAREIADRVVFIDGG-----DILEVAPP----A 244
Cdd:COG1116 155 NDPEVLLMDEPFGALD-ALTRERLQdeLLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSARpgrivEEIDVDLPrprdR 233
|
250 260
....*....|....*....|....*...
gi 504650440 245 EFFARPQHARTRRflqKVLDPLHQESEA 272
Cdd:COG1116 234 ELRTSPEFAALRA---EILDLLREEAER 258
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
22-259 |
3.09e-76 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 235.35 E-value: 3.09e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 22 ASIEFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPtrqLTGSALRQlRsR 101
Cdd:COG3839 2 ASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRD---VTDLPPKD-R-N 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 102 VGFVFQQFNLYAHLTAQENITLALeRVHGWSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQII 181
Cdd:COG3839 77 IAMVFQSYALYPHMTVYENIAFPL-KLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 182 LFDEPTSALDP----EMIGEVLQVMKTLahsGITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAEFFARPQHARTRR 257
Cdd:COG3839 156 LLDEPLSNLDAklrvEMRAEIKRLHRRL---GTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPANLFVAG 232
|
..
gi 504650440 258 FL 259
Cdd:COG3839 233 FI 234
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
24-263 |
5.12e-76 |
|
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: 231.42 E-value: 5.12e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSG-----GEILIDGKptrQLTGSALR-- 96
Cdd:TIGR00972 2 IEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMNDLVPgvrieGKVLFDGQ---DIYDKKIDvv 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 97 QLRSRVGFVFQQFNLYAhLTAQENITLALeRVHGW-SKSAARERSLALLSQVGL----ADKARQMPAQLSGGQQQRVAIA 171
Cdd:TIGR00972 79 ELRRRVGMVFQKPNPFP-MSIYDNIAYGP-RLHGIkDKKELDEIVEESLKKAALwdevKDRLHDSALGLSGGQQQRLCIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 172 RALASSPQIILFDEPTSALDPEMIGEVLQVMKTLAHSgITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAEFFARPQ 251
Cdd:TIGR00972 157 RALAVEPEVLLLDEPTSALDPIATGKIEELIQELKKK-YTIVIVTHNMQQAARISDRTAFFYDGELVEYGPTEQIFTNPK 235
|
250
....*....|..
gi 504650440 252 HARTRRFLQKVL 263
Cdd:TIGR00972 236 EKRTEDYISGRF 247
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
24-246 |
5.17e-76 |
|
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: 230.53 E-value: 5.17e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESL-----SGGEILIDGKPTRQLTGSALRqL 98
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVDVLE-L 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 99 RSRVGFVFQQFNLYaHLTAQENITLALeRVHG-WSKSAARERSLALLSQVGLAD--KARQMPAQLSGGQQQRVAIARALA 175
Cdd:cd03260 80 RRRVGMVFQKPNPF-PGSIYDNVAYGL-RLHGiKLKEELDERVEEALRKAALWDevKDRLHALGLSGGQQQRLCLARALA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504650440 176 SSPQIILFDEPTSALDPEMIGEVLQVMKTLAHSgITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAEF 246
Cdd:cd03260 158 NEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
24-259 |
5.72e-76 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 233.06 E-value: 5.72e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYGD-HRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLtgsALRQLRSRV 102
Cdd:COG1125 2 IEFENVTKRYPDgTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDL---DPVELRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 103 GFVFQQFNLYAHLTAQENITLALeRVHGWSKSAARERSLALLSQVGL--ADKARQMPAQLSGGQQQRVAIARALASSPQI 180
Cdd:COG1125 79 GYVIQQIGLFPHMTVAENIATVP-RLLGWDKERIRARVDELLELVGLdpEEYRDRYPHELSGGQQQRVGVARALAADPPI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 181 ILFDEPTSALDPeMIGEVLQ--VMKTLAHSGITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAEFFARPQHARTRRF 258
Cdd:COG1125 158 LLMDEPFGALDP-ITREQLQdeLLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFVADF 236
|
.
gi 504650440 259 L 259
Cdd:COG1125 237 V 237
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
24-241 |
5.77e-76 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 230.10 E-value: 5.77e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGkptRQLTGSALRqlRSRVG 103
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDG---RDVTGVPPE--RRNIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 104 FVFQQFNLYAHLTAQENITLALeRVHGWSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQIILF 183
Cdd:cd03259 76 MVFQDYALFPHLTVAENIAFGL-KLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504650440 184 DEPTSALDP----EMIGEVLQVMKTLahsGITMVVVTHEMQFAREIADRVVFIDGGDILEVA 241
Cdd:cd03259 155 DEPLSALDAklreELREELKELQREL---GITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
24-235 |
2.95e-75 |
|
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: 227.07 E-value: 2.95e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTGSaLRQLRSRVG 103
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDE-LPPLRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 104 FVFQQFNLYAHLTAQENITLAlervhgwsksaarerslallsqvgladkarqmpaqLSGGQQQRVAIARALASSPQIILF 183
Cdd:cd03229 80 MVFQDFALFPHLTVLENIALG-----------------------------------LSGGQQQRVALARALAMDPDVLLL 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 504650440 184 DEPTSALDPEMIGEVLQVMKTL-AHSGITMVVVTHEMQFAREIADRVVFIDGG 235
Cdd:cd03229 125 DEPTSALDPITRREVRALLKSLqAQLGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
24-230 |
2.17e-74 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 226.20 E-value: 2.17e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYGD----HRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPtrqltgsaLRQLR 99
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEP--------VTGPG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 100 SRVGFVFQQFNLYAHLTAQENITLALErVHGWSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQ 179
Cdd:cd03293 73 PDRGYVFQQDALLPWLTVLDNVALGLE-LQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 504650440 180 IILFDEPTSALDpEMIGEVLQ--VMKTLAHSGITMVVVTHEMQFAREIADRVV 230
Cdd:cd03293 152 VLLLDEPFSALD-ALTREQLQeeLLDIWRETGKTVLLVTHDIDEAVFLADRVV 203
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
24-246 |
1.00e-73 |
|
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: 225.26 E-value: 1.00e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYG-DHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTGSALRQLRSRV 102
Cdd:TIGR02315 2 LEVENLSKVYPnGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 103 GFVFQQFNLYAHLTAQENI-------TLALERVHGWSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALA 175
Cdd:TIGR02315 82 GMIFQHYNLIERLTVLENVlhgrlgyKPTWRSLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARALA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504650440 176 SSPQIILFDEPTSALDPEMIGEVLQVMKTLA-HSGITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAEF 246
Cdd:TIGR02315 162 QQPDLILADEPIASLDPKTSKQVMDYLKRINkEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSEL 233
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
23-259 |
6.63e-73 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 226.95 E-value: 6.63e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 23 SIEFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGkptrQLTGSALRQLRSRV 102
Cdd:COG1118 2 SIEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNG----RDLFTNLPPRERRV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 103 GFVFQQFNLYAHLTAQENITLALeRVHGWSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQIIL 182
Cdd:COG1118 78 GFVFQHYALFPHMTVAENIAFGL-RVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 183 FDEPTSALD----PEMigeVLQVMKTLAHSGITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAEFFARPQHARTRRF 258
Cdd:COG1118 157 LDEPFGALDakvrKEL---RRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARF 233
|
.
gi 504650440 259 L 259
Cdd:COG1118 234 L 234
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
24-261 |
1.63e-71 |
|
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: 219.86 E-value: 1.63e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYGDHR-VLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTGSalrQLRSRV 102
Cdd:cd03295 1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPV---ELRRKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 103 GFVFQQFNLYAHLTAQENITLaLERVHGWSKSAARERSLALLSQVGLADK--ARQMPAQLSGGQQQRVAIARALASSPQI 180
Cdd:cd03295 78 GYVIQQIGLFPHMTVEENIAL-VPKLLKWPKEKIRERADELLALVGLDPAefADRYPHELSGGQQQRVGVARALAADPPL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 181 ILFDEPTSALDPEMIGEVLQVMKTLAH-SGITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAEFFARPQHARTRRFL 259
Cdd:cd03295 157 LLMDEPFGALDPITRDQLQEEFKRLQQeLGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFV 236
|
..
gi 504650440 260 QK 261
Cdd:cd03295 237 GA 238
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
25-235 |
6.05e-71 |
|
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: 216.95 E-value: 6.05e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 25 EFRDVAKSYGDHR--VLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTgsaLRQLRSRV 102
Cdd:cd03225 1 ELKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLS---LKELRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 103 GFVFQ----QFnlyAHLTAQENITLALERvHGWSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSP 178
Cdd:cd03225 78 GLVFQnpddQF---FGPTVEEEVAFGLEN-LGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 504650440 179 QIILFDEPTSALDPEMIGEVLQVMKTLAHSGITMVVVTHEMQFAREIADRVVFIDGG 235
Cdd:cd03225 154 DILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
24-264 |
5.44e-69 |
|
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: 213.51 E-value: 5.44e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYG----DHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPtrqLTGSALRQLR 99
Cdd:COG1124 2 LEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRP---VTRRRRKAFR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 100 SRVGFVFQQ----FNlyAHLTAQENITLALeRVHGwsKSAARERSLALLSQVGLADKARQM-PAQLSGGQQQRVAIARAL 174
Cdd:COG1124 79 RRVQMVFQDpyasLH--PRHTVDRILAEPL-RIHG--LPDREERIAELLEQVGLPPSFLDRyPHQLSGGQRQRVAIARAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 175 ASSPQIILFDEPTSALDPEMIGEVLQVMKTL-AHSGITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAEFFARPQHA 253
Cdd:COG1124 154 ILEPELLLLDEPTSALDVSVQAEILNLLKDLrEERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKHP 233
|
250
....*....|.
gi 504650440 254 RTRRFLQKVLD 264
Cdd:COG1124 234 YTRELLAASLA 244
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
20-259 |
8.71e-69 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 213.36 E-value: 8.71e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 20 QRASIEFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQL-ESLSG----GEILIDGK----PTRQL 90
Cdd:COG1117 8 LEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMnDLIPGarveGEILLDGEdiydPDVDV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 91 TgsalrQLRSRVGFVFQQFNLYAHlTAQENITLALeRVHGW-SKSAARERSLALLSQVGLAD--KAR-QMPAQ-LSGGQQ 165
Cdd:COG1117 88 V-----ELRRRVGMVFQKPNPFPK-SIYDNVAYGL-RLHGIkSKSELDEIVEESLRKAALWDevKDRlKKSALgLSGGQQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 166 QRVAIARALASSPQIILFDEPTSALDP-------EMIGEvlqvmktLAHSgITMVVVTHEMQFAREIADRVVFIDGGDIL 238
Cdd:COG1117 161 QRLCIARALAVEPEVLLMDEPTSALDPistakieELILE-------LKKD-YTIVIVTHNMQQAARVSDYTAFFYLGELV 232
|
250 260
....*....|....*....|.
gi 504650440 239 EVAPPAEFFARPQHARTRRFL 259
Cdd:COG1117 233 EFGPTEQIFTNPKDKRTEDYI 253
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
24-257 |
1.24e-68 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 212.26 E-value: 1.24e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPtrqltgsaLRQLRSRVG 103
Cdd:COG1121 7 IELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKP--------PRRARRRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 104 FVFQQFNLYAH--LTAQENITLALERVHGW---SKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSP 178
Cdd:COG1121 79 YVPQRAEVDWDfpITVRDVVLMGRYGRRGLfrrPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504650440 179 QIILFDEPTSALDPEMIGEVLQVMKTLAHSGITMVVVTHEMQFAREIADRVVFIDGGdILEVAPPAEFFARPQHARTRR 257
Cdd:COG1121 159 DLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRG-LVAHGPPEEVLTPENLSRAYG 236
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
24-241 |
1.60e-67 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 208.90 E-value: 1.60e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSY----GDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTGSALRQLR 99
Cdd:cd03257 2 LEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 100 SRVGFVFQ--QFNLYAHLTAQENITLALeRVHG--WSKSAARERSLALLSQVGLADK-ARQMPAQLSGGQQQRVAIARAL 174
Cdd:cd03257 82 KEIQMVFQdpMSSLNPRMTIGEQIAEPL-RIHGklSKKEARKEAVLLLLVGVGLPEEvLNRYPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504650440 175 ASSPQIILFDEPTSALDPEMIGEVLQVMKTL-AHSGITMVVVTHEMQFAREIADRVVFIDGGDILEVA 241
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLqEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
24-235 |
2.47e-67 |
|
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: 207.87 E-value: 2.47e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSY-GDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTGSALRQLRSRV 102
Cdd:TIGR02673 2 IEFHNVSKAYpGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 103 GFVFQQFNLYAHLTAQENITLALErVHGWSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQIIL 182
Cdd:TIGR02673 82 GVVFQDFRLLPDRTVYENVALPLE-VRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 504650440 183 FDEPTSALDPEMIGEVLQVMKTLAHSGITMVVVTHEMQFAREIADRVVFIDGG 235
Cdd:TIGR02673 161 ADEPTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLSLVDRVAHRVIILDDG 213
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
39-262 |
2.92e-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: 207.11 E-value: 2.92e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 39 LNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTGSALRQLRS-RVGFVFQQFNLYAHLTA 117
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRkKISMVFQSFALLPHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 118 QENITLALErVHGWSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQIILFDEPTSALDP----E 193
Cdd:cd03294 120 LENVAFGLE-VQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPlirrE 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504650440 194 MIGEVLQVMKTLahsGITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAEFFARPQHARTRRFLQKV 262
Cdd:cd03294 199 MQDELLRLQAEL---QKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFFRGV 264
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
24-252 |
1.18e-65 |
|
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: 207.21 E-value: 1.18e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSY----GDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLES---LSGGEILIDGKPTRQLTGSALR 96
Cdd:COG0444 2 LEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 97 QLR-SRVGFVFQqfNLYAHL----TAQENITLALERVHGWSKSAARERSLALLSQVGLADKARQM---PAQLSGGQQQRV 168
Cdd:COG0444 82 KIRgREIQMIFQ--DPMTSLnpvmTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPDPERRLdryPHELSGGMRQRV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 169 AIARALASSPQIILFDEPTSALDPEMIGEVLQVMKTLAHS-GITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAEFF 247
Cdd:COG0444 160 MIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELF 239
|
....*
gi 504650440 248 ARPQH 252
Cdd:COG0444 240 ENPRH 244
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
24-237 |
1.25e-65 |
|
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: 202.24 E-value: 1.25e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPtrqlTGSALRQLRSRVG 103
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKD----IKKEPEEVKRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 104 FVFQQFNLYAHLTAQENItlalervhgwsksaarerslallsqvgladkarqmpaQLSGGQQQRVAIARALASSPQIILF 183
Cdd:cd03230 77 YLPEEPSLYENLTVRENL-------------------------------------KLSGGMKQRLALAQALLHDPELLIL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 504650440 184 DEPTSALDPEMIGEVLQVMKTLAHSGITMVVVTHEMQFAREIADRVVFIDGGDI 237
Cdd:cd03230 120 DEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
24-249 |
2.09e-65 |
|
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: 204.32 E-value: 2.09e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTgsalRQLRSRVG 103
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEP----REARRQIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 104 FVFQQFNLYAHLTAQENITLaLERVHGWSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQIILF 183
Cdd:COG4555 78 VLPDERGLYDRLTVRENIRY-FAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504650440 184 DEPTSALDPEMIGEVLQVMKTLAHSGITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAEFFAR 249
Cdd:COG4555 157 DEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREE 222
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
24-245 |
4.00e-65 |
|
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: 203.05 E-value: 4.00e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYGDHR----VLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTGSALRQLR 99
Cdd:COG4181 9 IELRGLTKTVGTGAgeltILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARARLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 100 SR-VGFVFQQFNLYAHLTAQENITLALERVhgwSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSP 178
Cdd:COG4181 89 ARhVGFVFQSFQLLPTLTALENVMLPLELA---GRRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504650440 179 QIILFDEPTSALDPEMIGEVLQVMKTL-AHSGITMVVVTHEMQFAREiADRVVFIDGGDILEVAPPAE 245
Cdd:COG4181 166 AILFADEPTGNLDAATGEQIIDLLFELnRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLVEDTAATA 232
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
24-245 |
3.18e-64 |
|
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: 201.43 E-value: 3.18e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTgsaLRQLRSRVG 103
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLS---RRELARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 104 FVFQQFNLYAHLTAQENITLA----LERVHGWSKsAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQ 179
Cdd:COG1120 79 YVPQEPPAPFGLTVRELVALGryphLGLFGRPSA-EDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504650440 180 IILFDEPTSALDPEMIGEVLQVMKTLAHS-GITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAE 245
Cdd:COG1120 158 LLLLDEPTSHLDLAHQLEVLELLRRLARErGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEE 224
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
24-259 |
3.22e-64 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 200.93 E-value: 3.22e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTGSalrqlRSRVG 103
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH-----KRPVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 104 FVFQQFNLYAHLTAQENITLALeRVHGWSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQIILF 183
Cdd:cd03300 76 TVFQNYALFPHLTVFENIAFGL-RLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504650440 184 DEPTSALDPEMIGEVLQVMKTLAHS-GITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAEFFARPQHARTRRFL 259
Cdd:cd03300 155 DEPLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFI 231
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
24-237 |
1.37e-63 |
|
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: 198.40 E-value: 1.37e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSY-GDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTGSALRQLRSRV 102
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 103 GFVFQQFNLYAHLTAQENITLALErVHGWSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQIIL 182
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALE-VTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 504650440 183 FDEPTSALDPEMIGEVLQVMKTLAHSGITMVVVTHemqfAREIAD----RVVFIDGGDI 237
Cdd:cd03292 160 ADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATH----AKELVDttrhRVIALERGKL 214
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
28-232 |
3.23e-63 |
|
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: 197.45 E-value: 3.23e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 28 DVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTGSALRQL-RSRVGFVF 106
Cdd:TIGR03608 3 NISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKFrREKLGYLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 107 QQFNLYAHLTAQENITLALERVHGwSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQIILFDEP 186
Cdd:TIGR03608 83 QNFALIENETVEENLDLGLKYKKL-SKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADEP 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 504650440 187 TSALDPEMIGEVLQVMKTLAHSGITMVVVTHEMQFArEIADRVVFI 232
Cdd:TIGR03608 162 TGSLDPKNRDEVLDLLLELNDEGKTIIIVTHDPEVA-KQADRVIEL 206
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
23-259 |
1.54e-62 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 196.79 E-value: 1.54e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 23 SIEFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTgsalrqLRSR- 101
Cdd:cd03296 2 SIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVP------VQERn 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 102 VGFVFQQFNLYAHLTAQENITLALE---RVHGWSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSP 178
Cdd:cd03296 76 VGFVFQHYALFRHMTVFDNVAFGLRvkpRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 179 QIILFDEPTSALDPEMIGEVLQVMKTLAHS-GITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAEFFARPQHARTRR 257
Cdd:cd03296 156 KVLLLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYS 235
|
..
gi 504650440 258 FL 259
Cdd:cd03296 236 FL 237
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
24-251 |
1.78e-62 |
|
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: 204.75 E-value: 1.78e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSY--GDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQL---ESLSGGEILIDGKPTRQLTgsaLRQL 98
Cdd:COG1123 5 LEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLlphGGRISGEVLLDGRDLLELS---EALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 99 RSRVGFVFQ----QFNLyahLTAQENITLALERvHGWSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARAL 174
Cdd:COG1123 82 GRRIGMVFQdpmtQLNP---VTVGDQIAEALEN-LGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504650440 175 ASSPQIILFDEPTSALDPEMIGEVLQVMKTL-AHSGITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAEFFARPQ 251
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDLLRELqRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
24-249 |
2.38e-62 |
|
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: 197.27 E-value: 2.38e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSY--GDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTrqLTGSALRQLRSR 101
Cdd:TIGR04520 1 IEVENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDT--LDEENLWEIRKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 102 VGFVFQ----QFnlyAHLTAQENITLALERvHGWSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASS 177
Cdd:TIGR04520 79 VGMVFQnpdnQF---VGATVEDDVAFGLEN-LGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504650440 178 PQIILFDEPTSALDPEMIGEVLQVMKTLAHS-GITMVVVTHEMQFAREiADRVVFIDGGDILEVAPPAEFFAR 249
Cdd:TIGR04520 155 PDIIILDEATSMLDPKGRKEVLETIRKLNKEeGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGTPREIFSQ 226
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
39-267 |
1.23e-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: 199.17 E-value: 1.23e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 39 LNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTGSALRQLR-SRVGFVFQQFNLYAHLTA 117
Cdd:COG4175 43 VNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGEDITKLSKKELRELRrKKMSMVFQHFALLPHRTV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 118 QENITLALErVHGWSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQIILFDEPTSALDP----E 193
Cdd:COG4175 123 LENVAFGLE-IQGVPKAERRERAREALELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPlirrE 201
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504650440 194 MIGEVLQVMKTLahsGITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAEFFARPQHARTRRFLQKVlDPLH 267
Cdd:COG4175 202 MQDELLELQAKL---KKTIVFITHDLDEALRLGDRIAIMKDGRIVQIGTPEEILTNPANDYVADFVEDV-DRSK 271
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
24-259 |
4.64e-61 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 192.66 E-value: 4.64e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYGDHRVlnGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPtrqLTGSALRQlrsR-V 102
Cdd:COG3840 2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQD---LTALPPAE---RpV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 103 GFVFQQFNLYAHLTAQENITLALeRVHGWSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQIIL 182
Cdd:COG3840 74 SMLFQENNLFPHLTVAQNIGLGL-RPGLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504650440 183 FDEPTSALDPEMIGEVLQVMKTLAHS-GITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAEFFARPQHARTRRFL 259
Cdd:COG3840 153 LDEPFSALDPALRQEMLDLVDELCRErGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYL 230
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
24-251 |
6.63e-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: 192.27 E-value: 6.63e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPtrqLTGSALRQlRSRVG 103
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGED---ITGLPPHE-IARLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 104 FV--FQQFNLYAHLTAQENITLALERVHG---------WSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIAR 172
Cdd:cd03219 77 IGrtFQIPRLFPELTVLENVMVAAQARTGsglllararREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIAR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504650440 173 ALASSPQIILFDEPTSALDPEMIGEVLQVMKTLAHSGITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAEFFARPQ 251
Cdd:cd03219 157 ALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPR 235
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
31-262 |
8.11e-61 |
|
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: 196.23 E-value: 8.11e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 31 KSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTGSALRQLRSR-VGFVFQQF 109
Cdd:TIGR01186 1 KKTGGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPVELREVRRKkIGMVFQQF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 110 NLYAHLTAQENITLALErVHGWSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQIILFDEPTSA 189
Cdd:TIGR01186 81 ALFPHMTILQNTSLGPE-LLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504650440 190 LDP----EMIGEVLQVMKTLahsGITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAEFFARPQHARTRRFLQKV 262
Cdd:TIGR01186 160 LDPlirdSMQDELKKLQATL---QKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIGKV 233
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
24-237 |
1.04e-60 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 190.80 E-value: 1.04e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPtrqLTGSALRQLRSRVG 103
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKP---LSAMPPPEWRRQVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 104 FVFQQFNLYAHlTAQENITLALERVHgwsKSAARERSLALLSQVGLADKARQMPA-QLSGGQQQRVAIARALASSPQIIL 182
Cdd:COG4619 78 YVPQEPALWGG-TVRDNLPFPFQLRE---RKFDRERALELLERLGLPPDILDKPVeRLSGGERQRLALIRALLLQPDVLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 504650440 183 FDEPTSALDPEMIGEVLQVMKTLAHS-GITMVVVTHEMQFAREIADRVVFIDGGDI 237
Cdd:COG4619 154 LDEPTSALDPENTRRVEELLREYLAEeGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
24-250 |
1.96e-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: 192.56 E-value: 1.96e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTrqltgSALRQLRSRVG 103
Cdd:TIGR03265 5 LSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDI-----TRLPPQKRDYG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 104 FVFQQFNLYAHLTAQENITLALERvHGWSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQIILF 183
Cdd:TIGR03265 80 IVFQSYALFPNLTVADNIAYGLKN-RGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504650440 184 DEPTSALDPE----MIGEVLQVMKTLahsGITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAEFFARP 250
Cdd:TIGR03265 159 DEPLSALDARvrehLRTEIRQLQRRL---GVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHP 226
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
25-235 |
1.57e-58 |
|
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: 185.43 E-value: 1.57e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 25 EFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPtrqltgsaLRQLRSRVGF 104
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKP--------LEKERKRIGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 105 VFQQFNL--YAHLTAQENITLALE---RVHGWSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQ 179
Cdd:cd03235 73 VPQRRSIdrDFPISVRDVVLMGLYghkGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 504650440 180 IILFDEPTSALDPEMIGEVLQVMKTLAHSGITMVVVTHEMQFAREIADRVVFIDGG 235
Cdd:cd03235 153 LLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLNRT 208
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
25-245 |
3.75e-58 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 186.01 E-value: 3.75e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 25 EFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPtrqLTGSALRQlRSRVGF 104
Cdd:COG0411 6 EVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRD---ITGLPPHR-IARLGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 105 V--FQQFNLYAHLTAQENITLALERVHGWS--------------KSAARERSLALLSQVGLADKARQMPAQLSGGQQQRV 168
Cdd:COG0411 82 ArtFQNPRLFPELTVLENVLVAAHARLGRGllaallrlprarreEREARERAEELLERVGLADRADEPAGNLSYGQQRRL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504650440 169 AIARALASSPQIILFDEPTSALDPEMIGEVLQVMKTL-AHSGITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAE 245
Cdd:COG0411 162 EIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLrDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAE 239
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
23-250 |
6.04e-58 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 188.75 E-value: 6.04e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 23 SIEFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTrqltgSALRQLRSRV 102
Cdd:PRK10851 2 SIEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDV-----SRLHARDRKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 103 GFVFQQFNLYAHLTAQENITLALE---RVHGWSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQ 179
Cdd:PRK10851 77 GFVFQHYALFRHMTVFDNIAFGLTvlpRRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504650440 180 IILFDEPTSALDPEMIGEVLQVMKTLaHSGI--TMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAEFFARP 250
Cdd:PRK10851 157 ILLLDEPFGALDAQVRKELRRWLRQL-HEELkfTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREP 228
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
24-258 |
1.33e-57 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 188.23 E-value: 1.33e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTGSAlRQlrsrVG 103
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAEN-RH----VN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 104 FVFQQFNLYAHLTAQENITLALeRVHGWSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQIILF 183
Cdd:PRK09452 90 TVFQSYALFPHMTVFENVAFGL-RMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLL 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504650440 184 DEPTSALD----PEMIGEVLQVMKTLahsGITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAEFFARPQHARTRRF 258
Cdd:PRK09452 169 DESLSALDyklrKQMQNELKALQRKL---GITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARF 244
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
21-249 |
1.52e-57 |
|
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: 195.44 E-value: 1.52e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 21 RASIEFRDVAKSYGDHR--VLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTgsaLRQL 98
Cdd:COG2274 471 KGDIELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQID---PASL 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 99 RSRVGFVFQQFNLYaHLTAQENITLalervhgWSKSAARERSLALLSQVGLADKARQMP-----------AQLSGGQQQR 167
Cdd:COG2274 548 RRQIGVVLQDVFLF-SGTIRENITL-------GDPDATDEEIIEAARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQR 619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 168 VAIARALASSPQIILFDEPTSALDPEMIGEVLQVMKTLAHsGITMVVVTHEMQFAReIADRVVFIDGGDILEVAPPAEFF 247
Cdd:COG2274 620 LAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK-GRTVIIIAHRLSTIR-LADRIIVLDKGRIVEDGTHEELL 697
|
..
gi 504650440 248 AR 249
Cdd:COG2274 698 AR 699
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
25-238 |
2.67e-57 |
|
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: 181.09 E-value: 2.67e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 25 EFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTgsaLRQLRSRVGF 104
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLS---PKELARKIAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 105 VFQqfnlyahltaqenitlalervhgwsksaarerslaLLSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQIILFD 184
Cdd:cd03214 78 VPQ-----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLD 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 504650440 185 EPTSALDPEMIGEVLQVMKTLAHS-GITMVVVTHEMQFAREIADRVVFIDGGDIL 238
Cdd:cd03214 123 EPTSHLDIAHQIELLELLRRLARErGKTVVMVLHDLNLAARYADRVILLKDGRIV 177
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
24-234 |
2.71e-56 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 187.92 E-value: 2.71e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTGSALRQLRsrVG 103
Cdd:COG1129 5 LEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAG--IA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 104 FVFQQFNLYAHLTAQENITLALERVHGW--SKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQII 181
Cdd:COG1129 83 IIHQELNLVPNLSVAENIFLGREPRRGGliDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 504650440 182 LFDEPTSALDPEMIGEVLQVMKTLAHSGITMVVVTHEMQFAREIADRV-VFIDG 234
Cdd:COG1129 163 ILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVtVLRDG 216
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
24-235 |
3.29e-56 |
|
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: 177.96 E-value: 3.29e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYGD--HRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTgsaLRQLRSR 101
Cdd:cd03228 1 IEFKNVSFSYPGrpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLD---LESLRKN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 102 VGFVFQQFNLYaHLTAQENItlalervhgwsksaarerslallsqvgladkarqmpaqLSGGQQQRVAIARALASSPQII 181
Cdd:cd03228 78 IAYVPQDPFLF-SGTIRENI--------------------------------------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 504650440 182 LFDEPTSALDPEMIGEVLQVMKTLAHsGITMVVVTHEMQFAReIADRVVFIDGG 235
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALAK-GKTVIVIAHRLSTIR-DADRIIVLDDG 170
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
21-245 |
6.38e-56 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 188.84 E-value: 6.38e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 21 RASIEFRDVAKSY-GDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTgsaLRQLR 99
Cdd:COG1132 337 RGEIEFENVSFSYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLT---LESLR 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 100 SRVGFVFQQFNLYaHLTAQENITLALErvhgwskSAARERSLALLSQVGLADKARQMP-----------AQLSGGQQQRV 168
Cdd:COG1132 414 RQIGVVPQDTFLF-SGTIRENIRYGRP-------DATDEEVEEAAKAAQAHEFIEALPdgydtvvgergVNLSGGQRQRI 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504650440 169 AIARALASSPQIILFDEPTSALDPEMIGEVLQVMKTLAHsGITMVVVTHEMQFAREiADRVVFIDGGDILEVAPPAE 245
Cdd:COG1132 486 AIARALLKDPPILILDEATSALDTETEALIQEALERLMK-GRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQGTHEE 560
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
37-256 |
7.02e-56 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 182.62 E-value: 7.02e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 37 RVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTGSALRQLRSRVGFVFQqfNLYAHL- 115
Cdd:COG4608 32 KAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPLRRRMQMVFQ--DPYASLn 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 116 ---TAQENITLALeRVHG-WSKSAARERSLALLSQVGL-ADKARQMPAQLSGGQQQRVAIARALASSPQIILFDEPTSAL 190
Cdd:COG4608 110 prmTVGDIIAEPL-RIHGlASKAERRERVAELLELVGLrPEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSAL 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504650440 191 DPEMIGEVLQVMKTL-AHSGITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAEFFARPQHARTR 256
Cdd:COG4608 189 DVSIQAQVLNLLEDLqDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPRDELYARPLHPYTQ 255
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
37-237 |
1.87e-55 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 177.99 E-value: 1.87e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 37 RVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTGS---ALRqlRSRVGFVFQQFNLYA 113
Cdd:NF038007 19 KVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNLSYSqkiILR--RELIGYIFQSFNLIP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 114 HLTAQENITLALeRVHGWSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQIILFDEPTSALDPE 193
Cdd:NF038007 97 HLSIFDNVALPL-KYRGVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSNPALLLADEPTGNLDSK 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 504650440 194 MIGEVLQVMKTLAHSGITMVVVTHEMQfAREIADRVVFIDGGDI 237
Cdd:NF038007 176 NARAVLQQLKYINQKGTTIIMVTHSDE-ASTYGNRIINMKDGKL 218
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
24-251 |
5.00e-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: 178.80 E-value: 5.00e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYG-----DHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTGSALRQL 98
Cdd:TIGR04521 1 IKLKNVSYIYQpgtpfEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 99 RSRVGFVFQ----QfnLYAhLTAQENITLALERVhGWSKSAARERSLALLSQVGLADK-ARQMPAQLSGGQQQRVAIARA 173
Cdd:TIGR04521 81 RKKVGLVFQfpehQ--LFE-ETVYKDIAFGPKNL-GLSEEEAEERVKEALELVGLDEEyLERSPFELSGGQMRRVAIAGV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504650440 174 LASSPQIILFDEPTSALDPEMIGEVLQVMKTLAHS-GITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAEFFARPQ 251
Cdd:TIGR04521 157 LAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEkGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDVD 235
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
24-246 |
5.79e-55 |
|
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: 176.86 E-value: 5.79e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPtrqLTGSALRQ-LRSRV 102
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRD---ITGLPPHErARAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 103 GFVFQQFNLYAHLTAQENITLALERVHGWSKSAARERSLALLSQvgLADKARQMPAQLSGGQQQRVAIARALASSPQIIL 182
Cdd:cd03224 78 GYVPEGRRIFPELTVEENLLLGAYARRRAKRKARLERVYELFPR--LKERRKQLAGTLSGGEQQMLAIARALMSRPKLLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504650440 183 FDEPTSALDPEMIGEVLQVMKTLAHSGITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAEF 246
Cdd:cd03224 156 LDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
25-235 |
1.21e-53 |
|
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: 171.27 E-value: 1.21e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 25 EFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTgsaLRQLRSRVGF 104
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLP---LEELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 105 VFQqfnlyahltaqenitlalervhgwsksaarerslallsqvgladkarqmpaqLSGGQQQRVAIARALASSPQIILFD 184
Cdd:cd00267 78 VPQ----------------------------------------------------LSGGQRQRVALARALLLNPDLLLLD 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 504650440 185 EPTSALDPEMIGEVLQVMKTLAHSGITMVVVTHEMQFAREIADRVVFIDGG 235
Cdd:cd00267 106 EPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
23-259 |
3.42e-53 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 180.65 E-value: 3.42e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 23 SIEFRDVAksyGDHRVLNGVNLQVEPGEVVAILGPSGSGKS----TLIRLINQLESLSGGEILIDGKPTRQLTGSALRQL 98
Cdd:COG4172 13 SVAFGQGG---GTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRRI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 99 R-SRVGFVFQQ----FN-LYahlTAQENITLALERVHGWSKSAARERSLALLSQVGLADKARQM---PAQLSGGQQQRVA 169
Cdd:COG4172 90 RgNRIAMIFQEpmtsLNpLH---TIGKQIAEVLRLHRGLSGAAARARALELLERVGIPDPERRLdayPHQLSGGQRQRVM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 170 IARALASSPQIILFDEPTSALDPEMIGEVLQVMKTL-AHSGITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAEFFA 248
Cdd:COG4172 167 IAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLqRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAELFA 246
|
250
....*....|.
gi 504650440 249 RPQHARTRRFL 259
Cdd:COG4172 247 APQHPYTRKLL 257
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
24-259 |
3.71e-52 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 170.73 E-value: 3.71e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSggeilidgkPTRQLTGSALR------- 96
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLN---------PEVTITGSIVYnghniys 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 97 ------QLRSRVGFVFQQFNLYAhLTAQENITLALeRVHGWSKSA----ARERSL---ALLSQVglADKARQMPAQLSGG 163
Cdd:PRK14239 77 prtdtvDLRKEIGMVFQQPNPFP-MSIYENVVYGL-RLKGIKDKQvldeAVEKSLkgaSIWDEV--KDRLHDSALGLSGG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 164 QQQRVAIARALASSPQIILFDEPTSALDPEMIGEVLQVMKTLAHSgITMVVVTHEMQFAREIADRVVFIDGGDILEVAPP 243
Cdd:PRK14239 153 QQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDT 231
|
250
....*....|....*.
gi 504650440 244 AEFFARPQHARTRRFL 259
Cdd:PRK14239 232 KQMFMNPKHKETEDYI 247
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
22-243 |
7.76e-52 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 179.15 E-value: 7.76e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 22 ASIEFRDVAKSY----GDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTGSALRQ 97
Cdd:PRK10535 3 ALLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 98 LR-SRVGFVFQQFNLYAHLTAQENITLALERVhGWSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALAS 176
Cdd:PRK10535 83 LRrEHFGFIFQRYHLLSHLTAAQNVEVPAVYA-GLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504650440 177 SPQIILFDEPTSALDPEMIGEVLQVMKTLAHSGITMVVVTHEMQFAREiADRVVFIDGGDILEVAPP 243
Cdd:PRK10535 162 GGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEIVRNPPA 227
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
31-265 |
1.14e-51 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 176.41 E-value: 1.14e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 31 KSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESlSGGEILIDGKPTRQLTGSALRQLRSRVGFVFQqfN 110
Cdd:COG4172 294 RTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSRRALRPLRRRMQVVFQ--D 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 111 LYAHL----TAQENITLALeRVH--GWSKSAARERSLALLSQVGLADKARQ-MPAQLSGGQQQRVAIARALASSPQIILF 183
Cdd:COG4172 371 PFGSLsprmTVGQIIAEGL-RVHgpGLSAAERRARVAEALEEVGLDPAARHrYPHEFSGGQRQRIAIARALILEPKLLVL 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 184 DEPTSALDPEMIGEVLQVMKTL-AHSGITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAEFFARPQHARTRRFLQKV 262
Cdd:COG4172 450 DEPTSALDVSVQAQILDLLRDLqREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDAPQHPYTRALLAAA 529
|
...
gi 504650440 263 LDP 265
Cdd:COG4172 530 PLL 532
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
23-235 |
1.35e-51 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 170.29 E-value: 1.35e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 23 SIEFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTgsalrqlRSRV 102
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED-------RRRI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 103 GFVFQQFNLYAHLTAQENIT-LAleRVHGWSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQII 181
Cdd:COG4152 74 GYLPEERGLYPKMKVGEQLVyLA--RLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 504650440 182 LFDEPTSALDPEMIGEVLQVMKTLAHSGITMVVVTHEMQFAREIADRVVFIDGG 235
Cdd:COG4152 152 ILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKG 205
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
24-241 |
1.62e-51 |
|
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: 167.43 E-value: 1.62e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLtgsalrQLRSR-V 102
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDL------PPKDRdI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 103 GFVFQQFNLYAHLTAQENITLALeRVHGWSKSA--ARERSLALLSQVG-LADKarqMPAQLSGGQQQRVAIARALASSPQ 179
Cdd:cd03301 75 AMVFQNYALYPHMTVYDNIAFGL-KLRKVPKDEidERVREVAELLQIEhLLDR---KPKQLSGGQRQRVALGRAIVREPK 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504650440 180 IILFDEPTSALDP----EMIGEVLQVMKTLahsGITMVVVTHEMQFAREIADRVVFIDGGDILEVA 241
Cdd:cd03301 151 VFLMDEPLSNLDAklrvQMRAELKRLQQRL---GTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
20-260 |
2.03e-51 |
|
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: 176.50 E-value: 2.03e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 20 QRASIEFRDVAKSY--GDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTGSALRQ 97
Cdd:COG4987 330 GGPSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRR 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 98 lrsRVGFVFQQfnlyAHL---TAQENITLALERvhgwsksAARERSLALLSQVGLADKARQMP-----------AQLSGG 163
Cdd:COG4987 410 ---RIAVVPQR----PHLfdtTLRENLRLARPD-------ATDEELWAALERVGLGDWLAALPdgldtwlgeggRRLSGG 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 164 QQQRVAIARALASSPQIILFDEPTSALDPEMIGEVLQVMKTLAHsGITMVVVTHEMQfAREIADRVVFIDGGDILEVAPP 243
Cdd:COG4987 476 ERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA-GRTVLLITHRLA-GLERMDRILVLEDGRIVEQGTH 553
|
250
....*....|....*..
gi 504650440 244 AEFFArpQHARTRRFLQ 260
Cdd:COG4987 554 EELLA--QNGRYRQLYQ 568
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
22-225 |
2.19e-51 |
|
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: 166.89 E-value: 2.19e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 22 ASIEFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQltgsALRQLRSR 101
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD----AREDYRRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 102 VGFVFQQFNLYAHLTAQENITLALeRVHGwsKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQII 181
Cdd:COG4133 77 LAYLGHADGLKPELTVRENLRFWA-ALYG--LRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLW 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 504650440 182 LFDEPTSALDPEMIGEVLQVMKTLAHSGITMVVVTH---EMQFAREI 225
Cdd:COG4133 154 LLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHqplELAAARVL 200
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
39-188 |
6.44e-51 |
|
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: 163.97 E-value: 6.44e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 39 LNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPtrqLTGSALRQLRSRVGFVFQQFNLYAHLTAQ 118
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQD---LTDDERKSLRKEIGYVFQDPQLFPRLTVR 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504650440 119 ENITLALeRVHGWSKSAARERSLALLSQVGLADKA----RQMPAQLSGGQQQRVAIARALASSPQIILFDEPTS 188
Cdd:pfam00005 78 ENLRLGL-LLKGLSKREKDARAEEALEKLGLGDLAdrpvGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-259 |
1.04e-50 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 167.01 E-value: 1.04e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 21 RASIEFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQL-----ESLSGGEILIDGKPTRQLTgsaL 95
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMD---V 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 96 RQLRSRVGFVFQQFNLYAHLTAQENITLALE--RVHGwSKSAARERSLALLSQVGLADKARQ---MPA-QLSGGQQQRVA 169
Cdd:PRK14247 78 IELRRRVQMVFQIPNPIPNLSIFENVALGLKlnRLVK-SKKELQERVRWALEKAQLWDEVKDrldAPAgKLSGGQQQRLC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 170 IARALASSPQIILFDEPTSALDPEMIGEVLQVMKTLAHSgITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAEFFAR 249
Cdd:PRK14247 157 IARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTN 235
|
250
....*....|
gi 504650440 250 PQHARTRRFL 259
Cdd:PRK14247 236 PRHELTEKYV 245
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
31-266 |
1.11e-50 |
|
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: 168.34 E-value: 1.11e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 31 KSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDG-KPTRQLtgsalRQLRSRVGFVFQQF 109
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGyDVVREP-----RKVRRSIGIVPQYA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 110 NLYAHLTAQENITLaLERVHGWSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQIILFDEPTSA 189
Cdd:TIGR01188 76 SVDEDLTGRENLEM-MGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504650440 190 LDPEMIGEVLQVMKTLAHSGITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAEFFAR--PQHARTRRFLQKVLDPL 266
Cdd:TIGR01188 155 LDPRTRRAIWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKRRlgKDTLESRPRDIQSLKVE 233
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
24-239 |
1.76e-50 |
|
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: 164.70 E-value: 1.76e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTrQLTGSALRqlrsRVG 103
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSY-QKNIEALR----RIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 104 FVFQQFNLYAHLTAQENItLALERVHGWSKSAARErslaLLSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQIILF 183
Cdd:cd03268 76 ALIEAPGFYPNLTARENL-RLLARLLGIRKKRIDE----VLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLIL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 504650440 184 DEPTSALDPEMIGEVLQVMKTLAHSGITMVVVTH---EMQfarEIADRVVFIDGGDILE 239
Cdd:cd03268 151 DEPTNGLDPDGIKELRELILSLRDQGITVLISSHllsEIQ---KVADRIGIINKGKLIE 206
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
25-251 |
1.79e-50 |
|
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: 165.54 E-value: 1.79e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 25 EFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPtrqLTGSALRQL-RSRVG 103
Cdd:COG0410 5 EVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGED---ITGLPPHRIaRLGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 104 FVFQQFNLYAHLTAQENITLALERVHGWSKSAAR-ERSLALLSQvgLADKARQMPAQLSGGQQQRVAIARALASSPQIIL 182
Cdd:COG0410 82 YVPEGRRIFPSLTVEENLLLGAYARRDRAEVRADlERVYELFPR--LKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504650440 183 FDEPTSALDPEMIGEVLQVMKTLAHSGITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAEFFARPQ 251
Cdd:COG0410 160 LDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPE 228
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
28-272 |
2.07e-50 |
|
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: 169.13 E-value: 2.07e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 28 DVAKSYGDHRvLNgVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPtrqLTGSALRQL----RSRVG 103
Cdd:COG4148 6 DFRLRRGGFT-LD-VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEV---LQDSARGIFlpphRRRIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 104 FVFQQFNLYAHLTAQENITLALERVHGWSKSAARERSLALLsqvGLADKARQMPAQLSGGQQQRVAIARALASSPQIILF 183
Cdd:COG4148 81 YVFQEARLFPHLSVRGNLLYGRKRAPRAERRISFDEVVELL---GIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 184 DEPTSALDPEMIGEVLQVMKTLAHS-GITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAEFFARPQhartrrflqkv 262
Cdd:COG4148 158 DEPLAALDLARKAEILPYLERLRDElDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPD----------- 226
|
250
....*....|
gi 504650440 263 LDPLHQESEA 272
Cdd:COG4148 227 LLPLAGGEEA 236
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
20-249 |
4.84e-49 |
|
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: 169.94 E-value: 4.84e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 20 QRASIEFRDVAKSYGDHR-VLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTGSALRQl 98
Cdd:COG4988 333 GPPSIELEDVSFSYPGGRpALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRR- 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 99 rsRVGFVFQQFNLYaHLTAQENITLAlervhgwSKSAARERSLALLSQVGLADKARQMP-----------AQLSGGQQQR 167
Cdd:COG4988 412 --QIAWVPQNPYLF-AGTIRENLRLG-------RPDASDEELEAALEAAGLDEFVAALPdgldtplgeggRGLSGGQAQR 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 168 VAIARALASSPQIILFDEPTSALDPEMIGEVLQVMKTLAHsGITMVVVTHEMQFAREiADRVVFIDGGDILEVAPPAEFF 247
Cdd:COG4988 482 LALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK-GRTVILITHRLALLAQ-ADRILVLDDGRIVEQGTHEELL 559
|
..
gi 504650440 248 AR 249
Cdd:COG4988 560 AK 561
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
22-251 |
5.52e-49 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 165.59 E-value: 5.52e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 22 ASIEFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTGSAlrqlRSr 101
Cdd:PRK11000 2 ASVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAE----RG- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 102 VGFVFQQFNLYAHLTAQENITLALeRVHGWSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQII 181
Cdd:PRK11000 77 VGMVFQSYALYPHLSVAENMSFGL-KLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVF 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504650440 182 LFDEPTSALDP----EMIGEVLQVMKTLahsGITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAEFFARPQ 251
Cdd:PRK11000 156 LLDEPLSNLDAalrvQMRIEISRLHKRL---GRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPA 226
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
28-237 |
1.72e-48 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 159.73 E-value: 1.72e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 28 DVAKSYGDH-RVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTrqltgsALRQLRSRVGFVF 106
Cdd:cd03226 4 NISFSYKKGtEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI------KAKERRKSIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 107 Q--QFNLYAHlTAQENITLALERVHgwsksAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQIILFD 184
Cdd:cd03226 78 QdvDYQLFTD-SVREELLLGLKELD-----AGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 504650440 185 EPTSALDPEMIGEVLQVMKTLAHSGITMVVVTHEMQFAREIADRVVFIDGGDI 237
Cdd:cd03226 152 EPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
24-230 |
1.89e-48 |
|
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: 157.98 E-value: 1.89e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPtrqltgsalrqlrsrvg 103
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKE----------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 104 fvfqqfnlyahltaqenitlalerVHGWSKSAARERSLALLSQvgladkarqmpaqLSGGQQQRVAIARALASSPQIILF 183
Cdd:cd03216 64 ------------------------VSFASPRDARRAGIAMVYQ-------------LSVGERQMVEIARALARNARLLIL 106
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 504650440 184 DEPTSALDPEMIGEVLQVMKTLAHSGITMVVVTHEMQFAREIADRVV 230
Cdd:cd03216 107 DEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVT 153
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
24-259 |
2.66e-48 |
|
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: 160.19 E-value: 2.66e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYGDHRVLNgVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKptrQLTGsaLRQLRSRVG 103
Cdd:cd03299 1 LKVENLSKDWKEFKLKN-VSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGK---DITN--LPPEKRDIS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 104 FVFQQFNLYAHLTAQENITLALeRVHGWSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQIILF 183
Cdd:cd03299 75 YVPQNYALFPHMTVYKNIAYGL-KKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504650440 184 DEPTSALDPEMIGEVLQVMKTLAHS-GITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAEFFARPQHARTRRFL 259
Cdd:cd03299 154 DEPFSALDVRTKEKLREELKKIRKEfGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFL 230
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
24-250 |
3.04e-48 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 163.35 E-value: 3.04e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKptrQLTGSALRQlrSRVG 103
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGE---DVTHRSIQQ--RDIC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 104 FVFQQFNLYAHLTAQENITLALeRVHGWSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQIILF 183
Cdd:PRK11432 82 MVFQSYALFPHMSLGENVGYGL-KMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504650440 184 DEPTSALDP-------EMIGEVLQVMktlahsGITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAEFFARP 250
Cdd:PRK11432 161 DEPLSNLDAnlrrsmrEKIRELQQQF------NITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQP 228
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
39-249 |
1.32e-47 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 159.80 E-value: 1.32e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 39 LNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPtrqLTGSALRQLRSRVGFVFQQ-FNLYAHLTA 117
Cdd:PRK13635 23 LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMV---LSEETVWDVRRQVGMVFQNpDNQFVGATV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 118 QENITLALERvHGWSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQIILFDEPTSALDPEMIGE 197
Cdd:PRK13635 100 QDDVAFGLEN-IGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRRE 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 504650440 198 VLQVMKTL-AHSGITMVVVTHEMQFAREiADRVVFIDGGDILEVAPPAEFFAR 249
Cdd:PRK13635 179 VLETVRQLkEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFKS 230
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
24-238 |
1.53e-47 |
|
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: 157.67 E-value: 1.53e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYGD--HRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRqltgSALRQLRSR 101
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR----TDRKAARQS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 102 VGFVFQQFNLYAHLTAQENITLaLERVHGWSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQII 181
Cdd:cd03263 77 LGYCPQFDALFDELTVREHLRF-YARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 182 LFDEPTSALDPEM---IGEVLQVMKtlahSGITMVVVTHEMQFAREIADRVVFIDGGDIL 238
Cdd:cd03263 156 LLDEPTSGLDPASrraIWDLILEVR----KGRSIILTTHSMDEAEALCDRIAIMSDGKLR 211
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
24-245 |
1.94e-47 |
|
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: 157.53 E-value: 1.94e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTgsalRQLRSRVG 103
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREP----REVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 104 FVFQQFNLYAHLTAQENITLaLERVHGWSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQIILF 183
Cdd:cd03265 77 IVFQDLSVDDELTGWENLYI-HARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504650440 184 DEPTSALDP---EMIGEVLQVMKtlAHSGITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAE 245
Cdd:cd03265 156 DEPTIGLDPqtrAHVWEYIEKLK--EEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEE 218
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
24-235 |
2.37e-47 |
|
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: 156.67 E-value: 2.37e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTgsalrqlRSRVG 103
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA-------RNRIG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 104 FVFQQFNLYAHLTAQENItLALERVHGWSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQIILF 183
Cdd:cd03269 74 YLPEERGLYPKMKVIDQL-VYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLIL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 504650440 184 DEPTSALDPEMIGEVLQVMKTLAHSGITMVVVTHEMQFAREIADRVVFIDGG 235
Cdd:cd03269 153 DEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKG 204
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
24-245 |
4.31e-47 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 163.66 E-value: 4.31e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQltGSALRQLRSRVG 103
Cdd:COG3845 6 LELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRI--RSPRDAIALGIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 104 FVFQQFNLYAHLTAQENITLALERVHGW--SKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQII 181
Cdd:COG3845 84 MVHQHFMLVPNLTVAENIVLGLEPTKGGrlDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARIL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504650440 182 LFDEPTSALDPEMIGEVLQVMKTLAHSGITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAE 245
Cdd:COG3845 164 ILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAE 227
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
24-254 |
7.52e-47 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 157.55 E-value: 7.52e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYGD-HRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRqLTGSALRQLRSRV 102
Cdd:PRK13639 2 LETRDLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIK-YDKKSLLEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 103 GFVFQQFN--LYAHlTAQENITLALERVhGWSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQI 180
Cdd:PRK13639 81 GIVFQNPDdqLFAP-TVEEDVAFGPLNL-GLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504650440 181 ILFDEPTSALDPEMIGEVLQVMKTLAHSGITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAEFFARPQHAR 254
Cdd:PRK13639 159 IVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIETIR 232
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
34-234 |
9.05e-47 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 156.09 E-value: 9.05e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 34 GDHR--VLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTGSALRQLRSR-VGFVFQQFN 110
Cdd:PRK10584 19 GEHElsILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRAKhVGFVFQSFM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 111 LYAHLTAQENITL-ALERvhGWSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQIILFDEPTSA 189
Cdd:PRK10584 99 LIPTLNALENVELpALLR--GESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGN 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 504650440 190 LDPEMIGEVLQVMKTLAHS-GITMVVVTHEMQFAREIADRVVFIDG 234
Cdd:PRK10584 177 LDRQTGDKIADLLFSLNREhGTTLILVTHDLQLAARCDRRLRLVNG 222
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
24-245 |
1.46e-46 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 156.43 E-value: 1.46e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTGSALRQLR---- 99
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRavlp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 100 --SRVGFVFqqfnlyahlTAQENITLALERvHGWSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALA-- 175
Cdd:COG4559 82 qhSSLAFPF---------TVEEVVALGRAP-HGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAql 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504650440 176 -----SSPQIILFDEPTSALDpemIGEVLQVM---KTLAHSGITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAE 245
Cdd:COG4559 152 wepvdGGPRWLFLDEPTSALD---LAHQHAVLrlaRQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEE 226
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
21-272 |
1.94e-46 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 156.18 E-value: 1.94e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 21 RASIEFRDVAKSYG----DHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPtrqLTG-SAL 95
Cdd:COG4525 1 MSMLTVRHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVP---VTGpGAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 96 RqlrsrvGFVFQQFNLYAHLTAQENITLALeRVHGWSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALA 175
Cdd:COG4525 78 R------GVVFQKDALLPWLNVLDNVAFGL-RLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 176 SSPQIILFDEPTSALDpEMIGEVLQ--VMKTLAHSGITMVVVTHEMQFAREIADRVV--------------------FID 233
Cdd:COG4525 151 ADPRFLLMDEPFGALD-ALTREQMQelLLDVWQRTGKGVFLITHSVEEALFLATRLVvmspgpgriverleldfsrrFLA 229
|
250 260 270
....*....|....*....|....*....|....*....
gi 504650440 234 GGDILEVAppaeffARPQHARTRrflQKVLDPLHQESEA 272
Cdd:COG4525 230 GEDARAIK------SDPAFIALR---EELLDIIFAQEEA 259
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
54-259 |
2.62e-46 |
|
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: 157.66 E-value: 2.62e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 54 ILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTGsalrQLRSrVGFVFQQFNLYAHLTAQENITLALeRVHGWSK 133
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPP----HLRH-INMVFQSYALFPHMTVEENVAFGL-KMRKVPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 134 SAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQIILFDEPTSALDPEMIGEVLQVMKTLAHS-GITM 212
Cdd:TIGR01187 75 AEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQlGITF 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 504650440 213 VVVTHEMQFAREIADRVVFIDGGDILEVAPPAEFFARPQHARTRRFL 259
Cdd:TIGR01187 155 VFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFI 201
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
23-263 |
2.93e-46 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 155.39 E-value: 2.93e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 23 SIEFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSG-----GEILIDGKPTRQLTGSALRq 97
Cdd:PRK14267 4 AIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEearveGEVRLFGRNIYSPDVDPIE- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 98 LRSRVGFVFQQFNLYAHLTAQENITLALeRVHGWSKSAAR--ERSLALLSQVGL----ADKARQMPAQLSGGQQQRVAIA 171
Cdd:PRK14267 83 VRREVGMVFQYPNPFPHLTIYDNVAIGV-KLNGLVKSKKEldERVEWALKKAALwdevKDRLNDYPSNLSGGQRQRLVIA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 172 RALASSPQIILFDEPTSALDP---EMIGEVLQVMKTlahsGITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAEFFA 248
Cdd:PRK14267 162 RALAMKPKILLMDEPTANIDPvgtAKIEELLFELKK----EYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFE 237
|
250
....*....|....*
gi 504650440 249 RPQHARTRRFLQKVL 263
Cdd:PRK14267 238 NPEHELTEKYVTGAL 252
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
24-250 |
1.28e-45 |
|
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: 153.08 E-value: 1.28e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGkptRQLTGSALRQlRSRVG 103
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDG---QDITKLPMHK-RARLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 104 FVF--QQFNLYAHLTAQENITLALErVHGWSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQII 181
Cdd:cd03218 77 IGYlpQEASIFRKLTVEENILAVLE-IRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504650440 182 LFDEPTSALDPEMIGEVLQVMKTLAHSGITMVVVTHEmqfARE---IADRVVFIDGGDILEVAPPAEFFARP 250
Cdd:cd03218 156 LLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHN---VREtlsITDRAYIIYEGKVLAEGTPEEIAANE 224
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
24-249 |
1.39e-45 |
|
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: 153.15 E-value: 1.39e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYGDHR-VLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTgsaLRQLRSRV 102
Cdd:cd03253 1 IEFENVTFAYDPGRpVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVT---LDSLRRAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 103 GFVFQQ---FN-------LYAHLTAQEnitlalERVHGWSKSAArerslallsqvgLADKARQMPAQ-----------LS 161
Cdd:cd03253 78 GVVPQDtvlFNdtigyniRYGRPDATD------EEVIEAAKAAQ------------IHDKIMRFPDGydtivgerglkLS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 162 GGQQQRVAIARALASSPQIILFDEPTSALDPEMIGEVLQVMKTLAhSGITMVVVTHEMqfaREI--ADRVVFIDGGDILE 239
Cdd:cd03253 140 GGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVS-KGRTTIVIAHRL---STIvnADKIIVLKDGRIVE 215
|
250
....*....|
gi 504650440 240 VAPPAEFFAR 249
Cdd:cd03253 216 RGTHEELLAK 225
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
36-235 |
1.52e-45 |
|
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: 152.45 E-value: 1.52e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 36 HRVLNGVNLQVE---PGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKP---TRQltGSALRQLRSRVGFVFQQF 109
Cdd:cd03297 7 EKRLPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVlfdSRK--KINLPPQQRKIGLVFQQY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 110 NLYAHLTAQENITLALERVhgwSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQIILFDEPTSA 189
Cdd:cd03297 85 ALFPHLNVRENLAFGLKRK---RNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 504650440 190 LDPEMIGEVLQVM-KTLAHSGITMVVVTHEMQFAREIADRVVFIDGG 235
Cdd:cd03297 162 LDRALRLQLLPELkQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDG 208
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
22-250 |
2.13e-45 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 156.16 E-value: 2.13e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 22 ASIEFRDVAKSY-GDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLtgsalrQLRS 100
Cdd:PRK11650 2 AGLKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNEL------EPAD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 101 R-VGFVFQQFNLYAHLTAQENITLALeRVHGWSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQ 179
Cdd:PRK11650 76 RdIAMVFQNYALYPHMSVRENMAYGL-KIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504650440 180 IILFDEPTSALDP----EMIGEVLQVMKTLahsGITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAEFFARP 250
Cdd:PRK11650 155 VFLFDEPLSNLDAklrvQMRLEIQRLHRRL---KTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKP 226
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
24-249 |
4.11e-45 |
|
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: 151.61 E-value: 4.11e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSY-GDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTgsaLRQLRSRV 102
Cdd:cd03254 3 IEFENVNFSYdEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDIS---RKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 103 GFVFQQFNLYAHlTAQENITLAlervhgwSKSAARERSLALLSQVGLADKARQMP-----------AQLSGGQQQRVAIA 171
Cdd:cd03254 80 GVVLQDTFLFSG-TIMENIRLG-------RPNATDEEVIEAAKEAGAHDFIMKLPngydtvlgengGNLSQGERQLLAIA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504650440 172 RALASSPQIILFDEPTSALDPEMIGEVLQVMKTLAHsGITMVVVTHEMQFAREiADRVVFIDGGDILEVAPPAEFFAR 249
Cdd:cd03254 152 RAMLRDPKILILDEATSNIDTETEKLIQEALEKLMK-GRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDELLAK 227
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
43-245 |
4.81e-45 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 151.66 E-value: 4.81e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 43 NLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTGSalrqlRSRVGFVFQQFNLYAHLTAQENIT 122
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS-----RRPVSMLFQENNLFSHLTVAQNIG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 123 LALERvhGWSKSAARERSL-ALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQIILFDEPTSALDPEMIGEVLQV 201
Cdd:PRK10771 94 LGLNP--GLKLNAAQREKLhAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 504650440 202 MKTLAHS-GITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAE 245
Cdd:PRK10771 172 VSQVCQErQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDE 216
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
19-247 |
5.82e-45 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 152.45 E-value: 5.82e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 19 LQRASIEFRDVAKSYGDHR--VLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKptrQLTGSALR 96
Cdd:PRK13632 3 NKSVMIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGI---TISKENLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 97 QLRSRVGFVFQ----QFnlyAHLTAQENITLALErvhgwSKSAARERSLALLS----QVGLADKARQMPAQLSGGQQQRV 168
Cdd:PRK13632 80 EIRKKIGIIFQnpdnQF---IGATVEDDIAFGLE-----NKKVPPKKMKDIIDdlakKVGMEDYLDKEPQNLSGGQKQRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 169 AIARALASSPQIILFDEPTSALDPEMIGEVLQVMKTLAHSGI-TMVVVTHEMQfarEI--ADRVVFIDGGDILEVAPPAE 245
Cdd:PRK13632 152 AIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLISITHDMD---EAilADKVIVFSEGKLIAQGKPKE 228
|
..
gi 504650440 246 FF 247
Cdd:PRK13632 229 IL 230
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
44-237 |
1.00e-44 |
|
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: 150.34 E-value: 1.00e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 44 LQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTrqltgSALRQLRSRVGFVFQQFNLYAHLTAQENITL 123
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDV-----TAAPPADRPVSMLFQENNLFAHLTVEQNVGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 124 ALE-RVHgwSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQIILFDEPTSALDPEMIGEVLQVM 202
Cdd:cd03298 94 GLSpGLK--LTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLV 171
|
170 180 190
....*....|....*....|....*....|....*.
gi 504650440 203 KTL-AHSGITMVVVTHEMQFAREIADRVVFIDGGDI 237
Cdd:cd03298 172 LDLhAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
24-245 |
1.24e-44 |
|
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: 151.01 E-value: 1.24e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLIN-QLESLSGGEILIDGkptRQLTGSALRQLRSRV 102
Cdd:COG1119 4 LELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITgDLPPTYGNDVRLFG---ERRGGEDVWELRKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 103 GFV--FQQFNLYAHLTAQENI------TLALERVHGWsksAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARAL 174
Cdd:COG1119 81 GLVspALQLRFPRDETVLDVVlsgffdSIGLYREPTD---EQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504650440 175 ASSPQIILFDEPTSALDPEMIGEVLQVMKTLAHSG-ITMVVVTHEMQfarEIAD---RVVFIDGGDILEVAPPAE 245
Cdd:COG1119 158 VKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHHVE---EIPPgitHVLLLKDGRVVAAGPKEE 229
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
24-249 |
1.28e-44 |
|
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: 150.77 E-value: 1.28e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSY---GDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLtgsALRQLRS 100
Cdd:cd03249 1 IEFKNVSFRYpsrPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDL---NLRWLRS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 101 RVGFVFQQFNLYAhLTAQENITLA-----LERVHGWSKSAARERSLALL-----SQVGlaDKArqmpAQLSGGQQQRVAI 170
Cdd:cd03249 78 QIGLVSQEPVLFD-GTIAENIRYGkpdatDEEVEEAAKKANIHDFIMSLpdgydTLVG--ERG----SQLSGGQKQRIAI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 171 ARALASSPQIILFDEPTSALDPEmiGEvLQVMKTL--AHSGITMVVVTHEMQFAREiADRVVFIDGGDILEVAPPAEFFA 248
Cdd:cd03249 151 ARALLRNPKILLLDEATSALDAE--SE-KLVQEALdrAMKGRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGTHDELMA 226
|
.
gi 504650440 249 R 249
Cdd:cd03249 227 Q 227
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
22-251 |
4.11e-44 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 149.41 E-value: 4.11e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 22 ASIEFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPtrqLTGSALRQlRSR 101
Cdd:COG1137 2 MTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGED---ITHLPMHK-RAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 102 --VGFVFQQFNLYAHLTAQENITLALErVHGWSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQ 179
Cdd:COG1137 78 lgIGYLPQEASIFRKLTVEDNILAVLE-LRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504650440 180 IILFDEPTSALDPEMIGEVLQVMKTLAHSGITmVVVT-HEmqfARE---IADRVVFIDGGDILEVAPPAEFFARPQ 251
Cdd:COG1137 157 FILLDEPFAGVDPIAVADIQKIIRHLKERGIG-VLITdHN---VREtlgICDRAYIISEGKVLAEGTPEEILNNPL 228
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
24-238 |
5.60e-44 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 149.78 E-value: 5.60e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQL---ESLSGGEILIDGKpTRQLTGSA---LRQ 97
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGR-TVQREGRLardIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 98 LRSRVGFVFQQFNLYAHLTAQENITLAL-------ERVHGWSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAI 170
Cdd:PRK09984 84 SRANTGYIFQQFNLVNRLSVLENVLIGAlgstpfwRTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504650440 171 ARALASSPQIILFDEPTSALDPEMIGEVLQVMKTLAHS-GITMVVVTHEMQFAREIADRVVFIDGGDIL 238
Cdd:PRK09984 164 ARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYALRYCERIVALRQGHVF 232
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
27-237 |
6.74e-44 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 149.44 E-value: 6.74e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 27 RDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILidgkptrqlTGSA-LRQLRSRVGFV 105
Cdd:PRK11247 16 NAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELL---------AGTApLAEAREDTRLM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 106 FQQFNLYAHLTAQENITLALervhgwsKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQIILFDE 185
Cdd:PRK11247 87 FQDARLLPWKKVIDNVGLGL-------KGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 504650440 186 PTSALDPEMIGEVLQVMKTL-AHSGITMVVVTHEMQFAREIADRVVFIDGGDI 237
Cdd:PRK11247 160 PLGALDALTRIEMQDLIESLwQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
28-250 |
1.86e-43 |
|
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: 151.03 E-value: 1.86e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 28 DVAKSYGDHRVlnGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGK---PTRQltGSALRQLRSRVGF 104
Cdd:TIGR02142 4 RFSKRLGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRtlfDSRK--GIFLPPEKRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 105 VFQQFNLYAHLTAQENITLALERVHGWSKSAARERSLALLsqvGLADKARQMPAQLSGGQQQRVAIARALASSPQIILFD 184
Cdd:TIGR02142 80 VFQEARLFPHLSVRGNLRYGMKRARPSERRISFERVIELL---GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504650440 185 EPTSALDPEMIGEVLQVMKTL-AHSGITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAEFFARP 250
Cdd:TIGR02142 157 EPLAALDDPRKYEILPYLERLhAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
23-237 |
3.15e-43 |
|
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: 146.58 E-value: 3.15e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 23 SIEFRDVAKSYGDHR--VLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTGSALRQlrs 100
Cdd:cd03245 2 RIEFRNVSFSYPNQEipALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRR--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 101 RVGFVFQQFNLYAHlTAQENITLAlervhgwSKSAARERSLALLSQVGLADKARQMP-----------AQLSGGQQQRVA 169
Cdd:cd03245 79 NIGYVPQDVTLFYG-TLRDNITLG-------APLADDERILRAAELAGVTDFVNKHPngldlqigergRGLSGGQRQAVA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504650440 170 IARALASSPQIILFDEPTSALDPEMIGEVLQVMKTLAhSGITMVVVTHEMQFArEIADRVVFIDGGDI 237
Cdd:cd03245 151 LARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLL-GDKTLIIITHRPSLL-DLVDRIIVMDSGRI 216
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
24-238 |
3.36e-43 |
|
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: 146.18 E-value: 3.36e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYGDHRVLNGVNLQVEPGeVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRqltgSALRQLRSRVG 103
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVL----KQPQKLRRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 104 FVFQQFNLYAHLTAQEnitlALE---RVHGWSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQI 180
Cdd:cd03264 76 YLPQEFGVYPNFTVRE----FLDyiaWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSI 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 504650440 181 ILFDEPTSALDPEMIGEVLQVMKTLAhSGITMVVVTHEMQFAREIADRVVFIDGGDIL 238
Cdd:cd03264 152 LIVDEPTAGLDPEERIRFRNLLSELG-EDRIVILSTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
24-262 |
3.93e-43 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 150.76 E-value: 3.93e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTrqltgSALRQLRSRVG 103
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDL-----SHVPPYQRPIN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 104 FVFQQFNLYAHLTAQENITLALERvHGWSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQIILF 183
Cdd:PRK11607 95 MMFQSYALFPHMTVEQNIAFGLKQ-DKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 184 DEPTSALDPEMIGEV-LQVMKTLAHSGITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAEFFARPQHARTRRFLQKV 262
Cdd:PRK11607 174 DEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSV 253
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
36-245 |
4.06e-43 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 147.91 E-value: 4.06e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 36 HRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTGSALRQLRSRVGFVFQQ----FNl 111
Cdd:PRK10419 25 QTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAFRRDIQMVFQDsisaVN- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 112 yAHLTAQENITLALERVHGWSKSAARERSLALLSQVGLADK-ARQMPAQLSGGQQQRVAIARALASSPQIILFDEPTSAL 190
Cdd:PRK10419 104 -PRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLDDSvLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNL 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 504650440 191 DPEMIGEVLQVMKTLAH-SGITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAE 245
Cdd:PRK10419 183 DLVLQAGVIRLLKKLQQqFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGD 238
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
22-245 |
4.18e-43 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 147.23 E-value: 4.18e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 22 ASIEFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTGSALRQLR-- 99
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRav 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 100 ----SRVGFVFqqfnlyahlTAQENITLALervHGWSKSAARERSL--ALLSQVGLADKARQMPAQLSGGQQQRVAIARA 173
Cdd:PRK13548 81 lpqhSSLSFPF---------TVEEVVAMGR---APHGLSRAEDDALvaAALAQVDLAHLAGRDYPQLSGGEQQRVQLARV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504650440 174 LA------SSPQIILFDEPTSALDPEMIGEVLQVMKTLAHS-GITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAE 245
Cdd:PRK13548 149 LAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHErGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAE 227
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
23-234 |
5.89e-43 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 145.32 E-value: 5.89e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 23 SIEFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIR-LINQLE---SLSGgEILIDGkptRQLTgsALRQL 98
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAaIAGTLSpafSASG-EVLLNG---RRLT--ALPAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 99 RSRVGFVFQQFNLYAHLTAQENITLALERvhGWSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSP 178
Cdd:COG4136 75 QRRIGILFQDDLLFPHLSVGENLAFALPP--TIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEP 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 504650440 179 QIILFDEPTSALDPEMIGEVLQ-VMKTLAHSGITMVVVTHEMQFAREiADRVVFIDG 234
Cdd:COG4136 153 RALLLDEPFSKLDAALRAQFREfVFEQIRQRGIPALLVTHDEEDAPA-AGRVLDLGN 208
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
24-264 |
6.18e-43 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 147.22 E-value: 6.18e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTGSALRQLRSRVG 103
Cdd:PRK11831 8 VDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRKRMS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 104 FVFQQFNLYAHLTAQENITLALERVHGWSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQIILF 183
Cdd:PRK11831 88 MLFQSGALFTDMNVFDNVAYPLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMF 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 184 DEPTSALDPEMIGEVLQVMKTLAHS-GITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAEFFARPQHaRTRRFLQKV 262
Cdd:PRK11831 168 DEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPDP-RVRQFLDGI 246
|
..
gi 504650440 263 LD 264
Cdd:PRK11831 247 AD 248
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
27-259 |
8.18e-43 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 148.57 E-value: 8.18e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 27 RDVAKSY--------GDHRV--LNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTGSALR 96
Cdd:PRK11308 9 IDLKKHYpvkrglfkPERLVkaLDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 97 QLRSRVGFVFQqfNLYAHLTAQENITLALE---RVH-GWSKSAARERSLALLSQVGL-ADKARQMPAQLSGGQQQRVAIA 171
Cdd:PRK11308 89 LLRQKIQIVFQ--NPYGSLNPRKKVGQILEeplLINtSLSAAERREKALAMMAKVGLrPEHYDRYPHMFSGGQRQRIAIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 172 RALASSPQIILFDEPTSALDPEMIGEVLQVMKTLAHS-GITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAEFFARP 250
Cdd:PRK11308 167 RALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQElGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNP 246
|
....*....
gi 504650440 251 QHARTRRFL 259
Cdd:PRK11308 247 RHPYTQALL 255
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
38-234 |
8.66e-43 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 145.73 E-value: 8.66e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 38 VLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTGSALRQLRSR-VGFVFQQFNLYAHLT 116
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRNQkLGFIYQFHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 117 AQENITLALeRVHGWSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQIILFDEPTSALDPEMIG 196
Cdd:PRK11629 104 ALENVAMPL-LIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNAD 182
|
170 180 190
....*....|....*....|....*....|....*....
gi 504650440 197 EVLQVMKTL-AHSGITMVVVTHEMQFAREIADRVVFIDG 234
Cdd:PRK11629 183 SIFQLLGELnRLQGTAFLVVTHDLQLAKRMSRQLEMRDG 221
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
33-237 |
2.33e-42 |
|
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: 144.23 E-value: 2.33e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 33 YGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKptrQLTGSAlrQLRSRVGFVFQQFNLY 112
Cdd:TIGR01277 8 YEYEHLPMEFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQ---SHTGLA--PYQRPVSMLFQENNLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 113 AHLTAQENITLALervHGWSKSAA--RERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQIILFDEPTSAL 190
Cdd:TIGR01277 83 AHLTVRQNIGLGL---HPGLKLNAeqQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSAL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 504650440 191 DPEMIGEVLQVMKTLA-HSGITMVVVTHEMQFAREIADRVVFIDGGDI 237
Cdd:TIGR01277 160 DPLLREEMLALVKQLCsERQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
24-247 |
2.49e-42 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 146.00 E-value: 2.49e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYGD------HRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLtgSALRQ 97
Cdd:PRK13633 5 IKCKNVSYKYESneesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDE--ENLWD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 98 LRSRVGFVFQqfNLYAHLTA---QENITLALERVhGWSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARAL 174
Cdd:PRK13633 83 IRNKAGMVFQ--NPDNQIVAtivEEDVAFGPENL-GIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGIL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504650440 175 ASSPQIILFDEPTSALDPEMIGEVLQVMKTL-AHSGITMVVVTHEMQFAREiADRVVFIDGGDILEVAPPAEFF 247
Cdd:PRK13633 160 AMRPECIIFDEPTAMLDPSGRREVVNTIKELnKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIF 232
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
24-219 |
9.56e-42 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 142.71 E-value: 9.56e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSY-GDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTGSALRQLRSRV 102
Cdd:PRK10908 2 IRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 103 GFVFQQFNLYAHLTAQENITLALeRVHGWSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQIIL 182
Cdd:PRK10908 82 GMIFQDHHLLMDRTVYDNVAIPL-IIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLL 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 504650440 183 FDEPTSALDPEMIGEVLQVMKTLAHSGITMVVVTHEM 219
Cdd:PRK10908 161 ADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDI 197
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
24-238 |
1.31e-41 |
|
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: 142.12 E-value: 1.31e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYGDHR----VLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQltgsALRQLR 99
Cdd:cd03266 2 ITADALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK----EPAEAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 100 SRVGFVFQQFNLYAHLTAQENItLALERVHGWSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQ 179
Cdd:cd03266 78 RRLGFVSDSTGLYDRLTARENL-EYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 504650440 180 IILFDEPTSALDPEMIGEVLQVMKTLAHSGITMVVVTHEMQFAREIADRVVFIDGGDIL 238
Cdd:cd03266 157 VLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVV 215
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
22-244 |
1.56e-41 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 144.56 E-value: 1.56e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 22 ASIEFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQltgsALRQLRSR 101
Cdd:PRK13537 6 APIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS----RARHARQR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 102 VGFVFQQFNLYAHLTAQENItLALERVHGWSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQII 181
Cdd:PRK13537 82 VGVVPQFDNLDPDFTVRENL-LVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504650440 182 LFDEPTSALDPEMIGEVLQVMKTLAHSGITMVVVTHEMQFAREIADRVVFIDGG-DILEVAPPA 244
Cdd:PRK13537 161 VLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGrKIAEGAPHA 224
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
21-217 |
1.67e-41 |
|
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: 141.15 E-value: 1.67e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 21 RASIEFRDVAK------SYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIR-LINQLESLS-GGEILIDGKPTRqltg 92
Cdd:cd03213 1 GVTLSFRNLTVtvksspSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNaLAGRRTGLGvSGEVLINGRPLD---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 93 saLRQLRSRVGFVFQQFNLYAHLTAQENITLAlervhgwsksaarerslALLSqvgladkarqmpaQLSGGQQQRVAIAR 172
Cdd:cd03213 77 --KRSFRKIIGYVPQDDILHPTLTVRETLMFA-----------------AKLR-------------GLSGGERKRVSIAL 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 504650440 173 ALASSPQIILFDEPTSALDPEMIGEVLQVMKTLAHSGITMVVVTH 217
Cdd:cd03213 125 ELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIH 169
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
24-249 |
1.77e-41 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 143.72 E-value: 1.77e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYG---DHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKptrQLTGSALRQLRS 100
Cdd:PRK13650 5 IEVKNLTFKYKedqEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGD---LLTEENVWDIRH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 101 RVGFVFQQ-FNLYAHLTAQENITLALERvHGWSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQ 179
Cdd:PRK13650 82 KIGMVFQNpDNQFVGATVEDDVAFGLEN-KGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPK 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504650440 180 IILFDEPTSALDPEMIGEVLQVMKTLAHS-GITMVVVTHEMQfarEIA--DRVVFIDGGDILEVAPPAEFFAR 249
Cdd:PRK13650 161 IIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLD---EVAlsDRVLVMKNGQVESTSTPRELFSR 230
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
43-262 |
1.88e-41 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 146.72 E-value: 1.88e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 43 NLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTGSALRQLR-SRVGFVFQQFNLYAHLTAQENI 121
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRrKKIAMVFQSFALMPHMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 122 TLALErVHGWSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQIILFDEPTSALDPEMIGEVL-Q 200
Cdd:PRK10070 128 AFGME-LAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQdE 206
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504650440 201 VMKTLAHSGITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAEFFARPQHARTRRFLQKV 262
Cdd:PRK10070 207 LVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGV 268
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
24-251 |
3.76e-41 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 143.02 E-value: 3.76e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYGDHR--VLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQL---ESLSGGEILIDGKptrQLTGSALRQL 98
Cdd:PRK13640 6 VEFKHVSFTYPDSKkpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITVDGI---TLTAKTVWDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 99 RSRVGFVFQQ-FNLYAHLTAQENITLALErvhgwSKSAARERSLAL----LSQVGLADKARQMPAQLSGGQQQRVAIARA 173
Cdd:PRK13640 83 REKVGIVFQNpDNQFVGATVGDDVAFGLE-----NRAVPRPEMIKIvrdvLADVGMLDYIDSEPANLSGGQKQRVAIAGI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504650440 174 LASSPQIILFDEPTSALDPEMIGEVLQVMKTLAH-SGITMVVVTHEMQFArEIADRVVFIDGGDILEVAPPAEFFARPQ 251
Cdd:PRK13640 158 LAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKkNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKVE 235
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
23-251 |
4.21e-41 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 143.05 E-value: 4.21e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 23 SIEFRDVAKSYG-----DHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTGS-ALR 96
Cdd:PRK13641 2 SIKFENVDYIYSpgtpmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNkNLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 97 QLRSRVGFVFQ--QFNLYAHlTAQENITLAlERVHGWSKSAARERSLALLSQVGLADK-ARQMPAQLSGGQQQRVAIARA 173
Cdd:PRK13641 82 KLRKKVSLVFQfpEAQLFEN-TVLKDVEFG-PKNFGFSEDEAKEKALKWLKKVGLSEDlISKSPFELSGGQMRRVAIAGV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504650440 174 LASSPQIILFDEPTSALDPEMIGEVLQVMKTLAHSGITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAEFFARPQ 251
Cdd:PRK13641 160 MAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKE 237
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
25-259 |
8.09e-41 |
|
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: 140.74 E-value: 8.09e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 25 EFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLtgSALRQLRSRVGF 104
Cdd:TIGR03410 2 EVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKL--PPHERARAGIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 105 VFQQFNLYAHLTAQENITLALErVHGWSKSAARERSLALLSQvgLADKARQMPAQLSGGQQQRVAIARALASSPQIILFD 184
Cdd:TIGR03410 80 VPQGREIFPRLTVEENLLTGLA-ALPRRSRKIPDEIYELFPV--LKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504650440 185 EPTSALDPEMIGEVLQVMKTLAHS-GITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAEFfarpQHARTRRFL 259
Cdd:TIGR03410 157 EPTEGIQPSIIKDIGRVIRRLRAEgGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL----DEDKVRRYL 228
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
39-252 |
1.54e-40 |
|
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: 139.91 E-value: 1.54e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 39 LNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGkptRQLTGSALRQLrsrvgFVFQQFNLYAHLTAQ 118
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEG---KQITEPGPDRM-----VVFQNYSLLPWLTVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 119 ENITLALERV-HGWSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQIILFDEPTSALDPEMIGE 197
Cdd:TIGR01184 73 ENIALAVDRVlPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGN 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504650440 198 VL-QVMKTLAHSGITMVVVTHEMQFAREIADRVVFIDG------GDILEVAppaefFARPQH 252
Cdd:TIGR01184 153 LQeELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNgpaaniGQILEVP-----FPRPRD 209
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
23-238 |
3.03e-40 |
|
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: 147.71 E-value: 3.03e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 23 SIEFRDVAKSY--GDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTGSALRQlrs 100
Cdd:TIGR03375 463 EIEFRNVSFAYpgQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADLRR--- 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 101 RVGFVFQQFNLYaHLTAQENITLAlervhgwSKSAARERSLALLSQVGLADKARQMP-----------AQLSGGQQQRVA 169
Cdd:TIGR03375 540 NIGYVPQDPRLF-YGTLRDNIALG-------APYADDEEILRAAELAGVTEFVRRHPdgldmqigergRSLSGGQRQAVA 611
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504650440 170 IARALASSPQIILFDEPTSALDPEMIGEVLQVMKTLAhSGITMVVVTHEMQFArEIADRVVFIDGGDIL 238
Cdd:TIGR03375 612 LARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWL-AGKTLVLVTHRTSLL-DLVDRIIVMDNGRIV 678
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
24-249 |
5.64e-40 |
|
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: 138.52 E-value: 5.64e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYGDHR--VLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTgsaLRQLRSR 101
Cdd:cd03251 1 VEFKNVTFRYPGDGppVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYT---LASLRRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 102 VGFVFQQFNLYaHLTAQENITLALERvhgwsksAARERSLALLSQVGLADKARQMP-----------AQLSGGQQQRVAI 170
Cdd:cd03251 78 IGLVSQDVFLF-NDTVAENIAYGRPG-------ATREEVEEAARAANAHEFIMELPegydtvigergVKLSGGQRQRIAI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504650440 171 ARALASSPQIILFDEPTSALDPEMIGEVLQVMKTLAhSGITMVVVTHEMQFAREiADRVVFIDGGDILEVAPPAEFFAR 249
Cdd:cd03251 150 ARALLKDPPILILDEATSALDTESERLVQAALERLM-KNRTTFVIAHRLSTIEN-ADRIVVLEDGKIVERGTHEELLAQ 226
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
24-259 |
2.25e-39 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 137.99 E-value: 2.25e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGeILIDGKPT---RQLTGSALR--QL 98
Cdd:PRK14243 11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPG-FRVEGKVTfhgKNLYAPDVDpvEV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 99 RSRVGFVFQQFNLYAHlTAQENITLAlERVHGWSKSAAR--ERSL---ALLSQVglADKARQMPAQLSGGQQQRVAIARA 173
Cdd:PRK14243 90 RRRIGMVFQKPNPFPK-SIYDNIAYG-ARINGYKGDMDElvERSLrqaALWDEV--KDKLKQSGLSLSGGQQQRLCIARA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 174 LASSPQIILFDEPTSALDPEMIGEVLQVMKTLAHSgITMVVVTHEMQFAREIADRVVFIDG---------GDILEVAPPA 244
Cdd:PRK14243 166 IAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHNMQQAARVSDMTAFFNVeltegggryGYLVEFDRTE 244
|
250
....*....|....*
gi 504650440 245 EFFARPQHARTRRFL 259
Cdd:PRK14243 245 KIFNSPQQQATRDYV 259
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
24-238 |
2.27e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 139.07 E-value: 2.27e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYG-----DHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEI------------------ 80
Cdd:PRK13651 3 IKVKNIVKIFNkklptELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 81 ----LIDGKPTRQLTGSAlRQLRSRVGFVFQ--QFNLYAHlTAQENITLAlERVHGWSKSAARERSLALLSQVGLADKAR 154
Cdd:PRK13651 83 vlekLVIQKTRFKKIKKI-KEIRRRVGVVFQfaEYQLFEQ-TIEKDIIFG-PVSMGVSKEEAKKRAAKYIELVGLDESYL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 155 QM-PAQLSGGQQQRVAIARALASSPQIILFDEPTSALDPEMIGEVLQVMKTLAHSGITMVVVTHEMQFAREIADRVVFID 233
Cdd:PRK13651 160 QRsPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFK 239
|
....*
gi 504650440 234 GGDIL 238
Cdd:PRK13651 240 DGKII 244
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
37-247 |
2.73e-39 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 138.26 E-value: 2.73e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 37 RVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDG-KPTRQltGSALRQLRSRVGFVFQ--QFNLYA 113
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvDITDK--KVKLSDIRKKVGLVFQypEYQLFE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 114 HlTAQENITLALERVhGWSKSAARERSLALLSQVGL-----ADKArqmPAQLSGGQQQRVAIARALASSPQIILFDEPTS 188
Cdd:PRK13637 99 E-TIEKDIAFGPINL-GLSEEEIENRVKRAMNIVGLdyedyKDKS---PFELSGGQKRRVAIAGVVAMEPKILILDEPTA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504650440 189 ALDPEMIGEVLQVMKTLaHS--GITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAEFF 247
Cdd:PRK13637 174 GLDPKGRDEILNKIKEL-HKeyNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVF 233
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
24-260 |
2.99e-39 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 137.66 E-value: 2.99e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYGDHR---------VLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPtrqLTGSA 94
Cdd:COG4167 5 LEVRNLSKTFKYRTglfrrqqfeAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHK---LEYGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 95 LRQLRSRVGFVFQQFN--LYAHLTAQENITLALERVHGWSKSAARERSLALLSQVGL-ADKARQMPAQLSGGQQQRVAIA 171
Cdd:COG4167 82 YKYRCKHIRMIFQDPNtsLNPRLNIGQILEEPLRLNTDLTAEEREERIFATLRLVGLlPEHANFYPHMLSSGQKQRVALA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 172 RALASSPQIILFDEPTSALDPEMIGEVLQVMKTL-AHSGITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAEFFARP 250
Cdd:COG4167 162 RALILQPKIIIADEALAALDMSVRSQIINLMLELqEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAEVFANP 241
|
250
....*....|
gi 504650440 251 QHARTRRFLQ 260
Cdd:COG4167 242 QHEVTKRLIE 251
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
24-237 |
4.23e-39 |
|
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: 135.99 E-value: 4.23e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKP-TRqltgsalRQLRSrV 102
Cdd:TIGR03740 1 LETKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPwTR-------KDLHK-I 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 103 GFVFQQFNLYAHLTAQENItlaleRVHGWSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQIIL 182
Cdd:TIGR03740 73 GSLIESPPLYENLTARENL-----KVHTTLLGLPDSRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLI 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 504650440 183 FDEPTSALDPEMIGEVLQVMKTLAHSGITMVVVTHEMQFAREIADRVVFIDGGDI 237
Cdd:TIGR03740 148 LDEPTNGLDPIGIQELRELIRSFPEQGITVILSSHILSEVQQLADHIGIISEGVL 202
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
34-260 |
4.52e-39 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 142.54 E-value: 4.52e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 34 GDHRVLNGVNLQVEPGEVVAILGPSGSGKST----LIRLINqleslSGGEILIDGKPTRQLTGSALRQLRSRVGFVFQQF 109
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPLHNLNRRQLLPVRHRIQVVFQDP 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 110 N--LYAHLTAQENITLALeRVHGWSKSAAR--ERSLALLSQVGLADKARQ-MPAQLSGGQQQRVAIARALASSPQIILFD 184
Cdd:PRK15134 372 NssLNPRLNVLQIIEEGL-RVHQPTLSAAQreQQVIAVMEEVGLDPETRHrYPAEFSGGQRQRIAIARALILKPSLIILD 450
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504650440 185 EPTSALDPEMIGEVLQVMKTLAHS-GITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAEFFARPQHARTRRFLQ 260
Cdd:PRK15134 451 EPTSSLDKTVQAQILALLKSLQQKhQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEYTRQLLA 527
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
24-237 |
1.26e-38 |
|
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: 134.91 E-value: 1.26e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSY---GDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTGsalRQLRS 100
Cdd:cd03248 12 VKFQNVTFAYptrPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEH---KYLHS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 101 RVGFVFQQFNLYAHlTAQENITLALERVHGWSKSAARERSLA----LLSQVGLADKARQMPAQLSGGQQQRVAIARALAS 176
Cdd:cd03248 89 KVSLVGQEPVLFAR-SLQDNIAYGLQSCSFECVKEAAQKAHAhsfiSELASGYDTEVGEKGSQLSGGQKQRVAIARALIR 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504650440 177 SPQIILFDEPTSALDPEMIGEVLQVMKTlAHSGITMVVVTHEMQFArEIADRVVFIDGGDI 237
Cdd:cd03248 168 NPQVLILDEATSALDAESEQQVQQALYD-WPERRTVLVIAHRLSTV-ERADQILVLDGGRI 226
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
18-262 |
1.27e-38 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 141.89 E-value: 1.27e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 18 HLQRASIEFRDVAKSYGD--HRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTGSAL 95
Cdd:PRK11160 333 AADQVSLTLNNVSFTYPDqpQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAAL 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 96 RQLRSrvgFVFQQFNLYAHlTAQENITLAlervhgwSKSAARERSLALLSQVGLADKARQMPA----------QLSGGQQ 165
Cdd:PRK11160 413 RQAIS---VVSQRVHLFSA-TLRDNLLLA-------APNASDEALIEVLQQVGLEKLLEDDKGlnawlgeggrQLSGGEQ 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 166 QRVAIARALASSPQIILFDEPTSALDPEMIGEVLQVMKTLAhSGITMVVVTHEMQfAREIADRVVFIDGGDILEVAPPAE 245
Cdd:PRK11160 482 RRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHA-QNKTVLMITHRLT-GLEQFDRICVMDNGQIIEQGTHQE 559
|
250
....*....|....*..
gi 504650440 246 FFArpQHARTRRFLQKV 262
Cdd:PRK11160 560 LLA--QQGRYYQLKQRL 574
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
18-249 |
2.21e-38 |
|
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: 141.39 E-value: 2.21e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 18 HLQRAS--IEFRDVAKSYG--DHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTgs 93
Cdd:TIGR02203 323 AIERARgdVEFRNVTFRYPgrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYT-- 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 94 aLRQLRSRVGFVFQQFNLYahltaqeNITLALERVHGWSKSAARERSLALLSQVGLADKARQMP-----------AQLSG 162
Cdd:TIGR02203 401 -LASLRRQVALVSQDVVLF-------NDTIANNIAYGRTEQADRAEIERALAAAYAQDFVDKLPlgldtpigengVLLSG 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 163 GQQQRVAIARALASSPQIILFDEPTSALDPEMIGEVLQVMKTLAHsGITMVVVTHEMQfAREIADRVVFIDGGDILEVAP 242
Cdd:TIGR02203 473 GQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQ-GRTTLVIAHRLS-TIEKADRIVVMDDGRIVERGT 550
|
....*..
gi 504650440 243 PAEFFAR 249
Cdd:TIGR02203 551 HNELLAR 557
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
24-249 |
2.53e-38 |
|
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: 134.54 E-value: 2.53e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSY-GDHR-VLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGkptRQLTGSALRQLRSR 101
Cdd:cd03252 1 ITFEHVRFRYkPDGPvILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDG---HDLALADPAWLRRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 102 VGFVFQQfNLYAHLTAQENITLALErvhgwskSAARERSLALLSQVGLADKARQMP-----------AQLSGGQQQRVAI 170
Cdd:cd03252 78 VGVVLQE-NVLFNRSIRDNIALADP-------GMSMERVIEAAKLAGAHDFISELPegydtivgeqgAGLSGGQRQRIAI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504650440 171 ARALASSPQIILFDEPTSALDPEMIGEVLQVMKTLAhSGITMVVVTHEMQFAREiADRVVFIDGGDILEVAPPAEFFAR 249
Cdd:cd03252 150 ARALIHNPRILIFDEATSALDYESEHAIMRNMHDIC-AGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLAE 226
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
24-237 |
4.66e-38 |
|
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: 131.57 E-value: 4.66e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYGD--HRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLtgsALRQLRSR 101
Cdd:cd03246 1 LEVENVSFRYPGaePPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQW---DPNELGDH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 102 VGFVFQQFNLYAHlTAQENItlalervhgwsksaarerslallsqvgladkarqmpaqLSGGQQQRVAIARALASSPQII 181
Cdd:cd03246 78 VGYLPQDDELFSG-SIAENI--------------------------------------LSGGQRQRLGLARALYGNPRIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 504650440 182 LFDEPTSALDPEMIGEVLQVMKTLAHSGITMVVVTHEMQfAREIADRVVFIDGGDI 237
Cdd:cd03246 119 VLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPE-TLASADRILVLEDGRV 173
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
24-250 |
9.15e-38 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 140.63 E-value: 9.15e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSY---GDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTGsalRQLRS 100
Cdd:TIGR00958 479 IEFQDVSFSYpnrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDH---HYLHR 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 101 RVGFVFQQFNLYAHlTAQENITLALERvhgwsksAARERSLALLSQVGLADKARQMP-----------AQLSGGQQQRVA 169
Cdd:TIGR00958 556 QVALVGQEPVLFSG-SVRENIAYGLTD-------TPDEEIMAAAKAANAHDFIMEFPngydtevgekgSQLSGGQKQRIA 627
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 170 IARALASSPQIILFDEPTSALDPEmIGEVLQVMKTLAhsGITMVVVTHEMQFAREiADRVVFIDGGDILEVAPPAEFFAR 249
Cdd:TIGR00958 628 IARALVRKPRVLILDEATSALDAE-CEQLLQESRSRA--SRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMED 703
|
.
gi 504650440 250 P 250
Cdd:TIGR00958 704 Q 704
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
7-244 |
1.22e-37 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 135.34 E-value: 1.22e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 7 SRSAASSADFSHLQRASIEFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKP 86
Cdd:PRK13536 25 GISEAKASIPGSMSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 87 TRqltgSALRQLRSRVGFVFQQFNLYAHLTAQENItLALERVHGWSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQ 166
Cdd:PRK13536 105 VP----ARARLARARIGVVPQFDNLDLEFTVRENL-LVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKR 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504650440 167 RVAIARALASSPQIILFDEPTSALDPEMIGEVLQVMKTLAHSGITMVVVTHEMQFAREIADRVVFIDGG-DILEVAPPA 244
Cdd:PRK13536 180 RLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGrKIAEGRPHA 258
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
38-250 |
2.01e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 134.21 E-value: 2.01e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 38 VLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILI-------DGKPTRQLTGSALR------QLRSRVGF 104
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdKKNNHELITNPYSKkiknfkELRRRVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 105 VFQ--QFNLYAHlTAQENIT---LALervhGWSKSAARERSLALLSQVGLADK-ARQMPAQLSGGQQQRVAIARALASSP 178
Cdd:PRK13631 121 VFQfpEYQLFKD-TIEKDIMfgpVAL----GVKKSEAKKLAKFYLNKMGLDDSyLERSPFGLSGGQKRRVAIAGILAIQP 195
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504650440 179 QIILFDEPTSALDPEMIGEVLQVMKTLAHSGITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAEFFARP 250
Cdd:PRK13631 196 EILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQ 267
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-259 |
4.00e-37 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 132.53 E-value: 4.00e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 5 LFSRSAASSADFSHLQRASIefrDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQL-ESLSG----GE 79
Cdd:PRK14271 6 LGGQSGAADVDAAAPAMAAV---NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMnDKVSGyrysGD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 80 ILIDGKPTrqLTGSALRQLRSRVGFVFQQFNLYAhLTAQENItLALERVHGW-SKSAARERSLALLSQVGL----ADKAR 154
Cdd:PRK14271 83 VLLGGRSI--FNYRDVLEFRRRVGMLFQRPNPFP-MSIMDNV-LAGVRAHKLvPRKEFRGVAQARLTEVGLwdavKDRLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 155 QMPAQLSGGQQQRVAIARALASSPQIILFDEPTSALDPEMIGEVLQVMKTLAHSgITMVVVTHEMQFAREIADRVVFIDG 234
Cdd:PRK14271 159 DSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFD 237
|
250 260
....*....|....*....|....*
gi 504650440 235 GDILEVAPPAEFFARPQHARTRRFL 259
Cdd:PRK14271 238 GRLVEEGPTEQLFSSPKHAETARYV 262
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
24-265 |
4.11e-37 |
|
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: 137.24 E-value: 4.11e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESL--SGGEILI----------------DGK 85
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYepTSGRIIYhvalcekcgyverpskVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 86 PTRQLTGS--------------ALRQLRSRVGFVFQQ-FNLYAHLTAQENITLALERVhGWSKSAARERSLALLSQVGLA 150
Cdd:TIGR03269 81 PCPVCGGTlepeevdfwnlsdkLRRRIRKRIAIMLQRtFALYGDDTVLDNVLEALEEI-GYEGKEAVGRAVDLIEMVQLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 151 DKARQMPAQLSGGQQQRVAIARALASSPQIILFDEPTSALDPEMIGEVLQVMKTLA-HSGITMVVVTHEMQFAREIADRV 229
Cdd:TIGR03269 160 HRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVkASGISMVLTSHWPEVIEDLSDKA 239
|
250 260 270
....*....|....*....|....*....|....*.
gi 504650440 230 VFIDGGDILEVAPPAEFFArpqhartrRFLQKVLDP 265
Cdd:TIGR03269 240 IWLENGEIKEEGTPDEVVA--------VFMEGVSEV 267
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
34-222 |
7.32e-37 |
|
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: 129.08 E-value: 7.32e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 34 GDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTrQLTGSALRQLRSRVGFVFQQFN--L 111
Cdd:TIGR01166 3 GGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPL-DYSRKGLLERRQRVGLVFQDPDdqL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 112 YAHlTAQENITLALeRVHGWSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQIILFDEPTSALD 191
Cdd:TIGR01166 82 FAA-DVDQDVAFGP-LNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLD 159
|
170 180 190
....*....|....*....|....*....|.
gi 504650440 192 PEMIGEVLQVMKTLAHSGITMVVVTHEMQFA 222
Cdd:TIGR01166 160 PAGREQMLAILRRLRAEGMTVVISTHDVDLA 190
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
35-259 |
7.62e-37 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 131.32 E-value: 7.62e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 35 DHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPT---RQLTGSALRQLRSRVGFVFQQFNL 111
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLyfgKDIFQIDAIKLRKEVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 112 YAHLTAQENITLALeRVHGWS-KSAARERSLALLSQVGL----ADKARQMPAQLSGGQQQRVAIARALASSPQIILFDEP 186
Cdd:PRK14246 102 FPHLSIYDNIAYPL-KSHGIKeKREIKKIVEECLRKVGLwkevYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEP 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504650440 187 TSALDPEMIGEVLQVMKTLAHSgITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAEFFARPQHARTRRFL 259
Cdd:PRK14246 181 TSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKYV 252
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
21-250 |
1.40e-36 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 137.40 E-value: 1.40e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 21 RASIEFRDVAKSYGDH--RVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPtrqLTGSALRQL 98
Cdd:TIGR03797 449 SGAIEVDRVTFRYRPDgpLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQD---LAGLDVQAV 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 99 RSRVGFVFQQFNLYAHlTAQENIT----LALERVhgWSksAARErslallsqVGLADKARQMP-----------AQLSGG 163
Cdd:TIGR03797 526 RRQLGVVLQNGRLMSG-SIFENIAggapLTLDEA--WE--AARM--------AGLAEDIRAMPmgmhtviseggGTLSGG 592
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 164 QQQRVAIARALASSPQIILFDEPTSALDPEMigevlQ--VMKTLAHSGITMVVVTHEMQFAREiADRVVFIDGGDILEVA 241
Cdd:TIGR03797 593 QRQRLLIARALVRKPRILLFDEATSALDNRT-----QaiVSESLERLKVTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQG 666
|
....*....
gi 504650440 242 PPAEFFARP 250
Cdd:TIGR03797 667 TYDELMARE 675
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
23-248 |
1.96e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 130.67 E-value: 1.96e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 23 SIEFRDVAKSYG-----DHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDG-KPTRQLTGSALR 96
Cdd:PRK13646 2 TIRFDNVSYTYQkgtpyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDiTITHKTKDKYIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 97 QLRSRVGFVFQ--QFNLYAHLTAQE------NITLALERVhgwsksaaRERSLALLSQVGLA-DKARQMPAQLSGGQQQR 167
Cdd:PRK13646 82 PVRKRIGMVFQfpESQLFEDTVEREiifgpkNFKMNLDEV--------KNYAHRLLMDLGFSrDVMSQSPFQMSGGQMRK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 168 VAIARALASSPQIILFDEPTSALDPEMIGEVLQVMKTLA-HSGITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAEF 246
Cdd:PRK13646 154 IAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKEL 233
|
..
gi 504650440 247 FA 248
Cdd:PRK13646 234 FK 235
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
23-247 |
2.76e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 130.25 E-value: 2.76e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 23 SIEFRDVAKSYG-----DHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKP-TRQLTGSALR 96
Cdd:PRK13649 2 GINLQNVSYTYQagtpfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLiTSTSKNKDIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 97 QLRSRVGFVFQ--QFNLYAHlTAQENITLALERVhGWSKSAARERSLALLSQVGLADKAR-QMPAQLSGGQQQRVAIARA 173
Cdd:PRK13649 82 QIRKKVGLVFQfpESQLFEE-TVLKDVAFGPQNF-GVSQEEAEALAREKLALVGISESLFeKNPFELSGGQMRRVAIAGI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504650440 174 LASSPQIILFDEPTSALDPEMIGEVLQVMKTLAHSGITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAEFF 247
Cdd:PRK13649 160 LAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIF 233
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
24-250 |
4.96e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 129.54 E-value: 4.96e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSY-GDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPtrqLTGSALRQLRSRV 102
Cdd:PRK13652 4 IETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEP---ITKENIREVRKFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 103 GFVFQQFN-LYAHLTAQENITLALERVhGWSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQII 181
Cdd:PRK13652 81 GLVFQNPDdQIFSPTVEQDIAFGPINL-GLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 182 LFDEPTSALDPEMIGEVLQVMKTLAHS-GITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAEFFARP 250
Cdd:PRK13652 160 VLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
24-245 |
1.25e-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: 133.39 E-value: 1.25e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSY-----GDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLI-NQLESLSG------GEILID-GKPTRQL 90
Cdd:TIGR03269 280 IKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIaGVLEPTSGevnvrvGDEWVDmTKPGPDG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 91 TGSALRQLrsrvGFVFQQFNLYAHLTAQENITLA--LErvhgWSKSAARERSLALLSQVGLAD-KAR----QMPAQLSGG 163
Cdd:TIGR03269 360 RGRAKRYI----GILHQEYDLYPHRTVLDNLTEAigLE----LPDELARMKAVITLKMVGFDEeKAEeildKYPDELSEG 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 164 QQQRVAIARALASSPQIILFDEPTSALDPemIGEVlQVMKTLAHS----GITMVVVTHEMQFAREIADRVVFIDGGDILE 239
Cdd:TIGR03269 432 ERHRVALAQVLIKEPRIVILDEPTGTMDP--ITKV-DVTHSILKAreemEQTFIIVSHDMDFVLDVCDRAALMRDGKIVK 508
|
....*.
gi 504650440 240 VAPPAE 245
Cdd:TIGR03269 509 IGDPEE 514
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
24-251 |
1.87e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 128.21 E-value: 1.87e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYG-----DHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDgkpTRQLTGSA---- 94
Cdd:PRK13634 3 ITFQKVEHRYQyktpfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIG---ERVITAGKknkk 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 95 LRQLRSRVGFVFQ--QFNLYAHlTAQENITLALERVhGWSKSAARERSLALLSQVGLADKAR-QMPAQLSGGQQQRVAIA 171
Cdd:PRK13634 80 LKPLRKKVGIVFQfpEHQLFEE-TVEKDICFGPMNF-GVSEEDAKQKAREMIELVGLPEELLaRSPFELSGGQMRRVAIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 172 RALASSPQIILFDEPTSALDPEMIGEVLQVMKTLAH-SGITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAEFFARP 250
Cdd:PRK13634 158 GVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKeKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADP 237
|
.
gi 504650440 251 Q 251
Cdd:PRK13634 238 D 238
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
24-238 |
4.11e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 127.16 E-value: 4.11e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYGD-HRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGkptRQLTGSALRQLRSRV 102
Cdd:PRK13647 5 IEVEDLHFRYKDgTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMG---REVNAENEKWVRSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 103 GFVFQQFN--LYAhLTAQENITLAlERVHGWSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQI 180
Cdd:PRK13647 82 GLVFQDPDdqVFS-STVWDDVAFG-PVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 504650440 181 ILFDEPTSALDPEMIGEVLQVMKTLAHSGITMVVVTHEMQFAREIADRVVFIDGGDIL 238
Cdd:PRK13647 160 IVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVL 217
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
19-217 |
4.50e-35 |
|
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: 131.71 E-value: 4.50e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 19 LQRASIEFRDVAKSY-GDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTGSALRQ 97
Cdd:TIGR02868 330 LGKPTLELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRR 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 98 lrsRVGFVFQQFNLYAHlTAQENITLAlervhgwSKSAARERSLALLSQVGLADKARQMP-----------AQLSGGQQQ 166
Cdd:TIGR02868 410 ---RVSVCAQDAHLFDT-TVRENLRLA-------RPDATDEELWAALERVGLADWLRALPdgldtvlgeggARLSGGERQ 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 504650440 167 RVAIARALASSPQIILFDEPTSALDPEMIGEVLQVMKTlAHSGITMVVVTH 217
Cdd:TIGR02868 479 RLALARALLADAPILLLDEPTEHLDAETADELLEDLLA-ALSGRTVVLITH 528
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
24-235 |
5.57e-35 |
|
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: 125.24 E-value: 5.57e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYGDHR-------VLNGVNLQVEPGEVVAILGPSGSGKSTLIRLI--NQLESlsGGEILIDGK--------- 85
Cdd:COG4778 5 LEVENLSKTFTLHLqggkrlpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIygNYLPD--SGSILVRHDggwvdlaqa 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 86 PTRQLTgsALRqlRSRVGFVFQQFNLYAHLTAQENITLALeRVHGWSKSAARERSLALLSQVGLADKARQM-PAQLSGGQ 164
Cdd:COG4778 83 SPREIL--ALR--RRTIGYVSQFLRVIPRVSALDVVAEPL-LERGVDREEARARARELLARLNLPERLWDLpPATFSGGE 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504650440 165 QQRVAIARALASSPQIILFDEPTSALDPEMIGEVLQVMKTLAHSGITMVVVTHEMQFAREIADRVVFIDGG 235
Cdd:COG4778 158 QQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
25-238 |
8.20e-35 |
|
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: 125.08 E-value: 8.20e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 25 EFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQL---ESLSGGEILIDGKPTRQltgsalRQLRSR 101
Cdd:cd03234 9 VGLKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRvegGGTTSGQILFNGQPRKP------DQFQKC 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 102 VGFVFQQFNLYAHLTAQENIT-LALERVHGWSKSAARERSLA--LLSQVGLADKARQMPAQLSGGQQQRVAIARALASSP 178
Cdd:cd03234 83 VAYVRQDDILLPGLTVRETLTyTAILRLPRKSSDAIRKKRVEdvLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504650440 179 QIILFDEPTSALDPEMIGEVLQVMKTLAHSGITMVVVTHEMQ---FarEIADRVVFIDGGDIL 238
Cdd:cd03234 163 KVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRsdlF--RLFDRILLLSSGEIV 223
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
33-239 |
8.88e-35 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 125.58 E-value: 8.88e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 33 YGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPtrqLTG-SALRqlrsrvGFVFQQFNL 111
Cdd:PRK11248 11 YGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKP---VEGpGAER------GVVFQNEGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 112 YAHLTAQENITLALErVHGWSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQIILFDEPTSALD 191
Cdd:PRK11248 82 LPWRNVQDNVAFGLQ-LAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 504650440 192 P---EMIGEVLqvMKTLAHSGITMVVVTHEMQFAREIADRVVFI--DGGDILE 239
Cdd:PRK11248 161 AftrEQMQTLL--LKLWQETGKQVLLITHDIEEAVFMATELVLLspGPGRVVE 211
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
24-245 |
9.81e-35 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 125.58 E-value: 9.81e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGK-----PTRQL--TGSALR 96
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLdvattPSRELakRLAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 97 Q---LRSR------VGFvfqqfNLYAH----LTAQENitlalervhgwsksAARERSLALLSQVGLADkaRQMPaQLSGG 163
Cdd:COG4604 82 QenhINSRltvrelVAF-----GRFPYskgrLTAEDR--------------EIIDEAIAYLDLEDLAD--RYLD-ELSGG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 164 QQQRVAIARALASSPQIILFDEPTSALDpemIGEVLQVMKTLAH----SGITMVVVTHEMQFAREIADRVVFIDGGDILE 239
Cdd:COG4604 140 QRQRAFIAMVLAQDTDYVLLDEPLNNLD---MKHSVQMMKLLRRladeLGKTVVIVLHDINFASCYADHIVAMKDGRVVA 216
|
....*.
gi 504650440 240 VAPPAE 245
Cdd:COG4604 217 QGTPEE 222
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
36-268 |
1.10e-34 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 131.52 E-value: 1.10e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 36 HRVLNgVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTGSALRQLRSRVGFVFQqfNLYAHL 115
Cdd:PRK10261 338 HAVEK-VSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRRDIQFIFQ--DPYASL 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 116 TAQENITLALE---RVHGW-SKSAARERSLALLSQVGL-ADKARQMPAQLSGGQQQRVAIARALASSPQIILFDEPTSAL 190
Cdd:PRK10261 415 DPRQTVGDSIMeplRVHGLlPGKAAAARVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSAL 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 191 DPEMIGEVLQVMKTLAHS-GITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAEFFARPQHARTRRFLQK--VLDPLH 267
Cdd:PRK10261 495 DVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLMAAvpVADPSR 574
|
.
gi 504650440 268 Q 268
Cdd:PRK10261 575 Q 575
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
24-245 |
1.45e-34 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 128.42 E-value: 1.45e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTGSALRQlrsRVG 103
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASR---RVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 104 FVFQQ----FNLYAHLTAQENITLALERVHGWSKS--AARERSLAllsQVGLADKARQMPAQLSGGQQQRVAIARALASS 177
Cdd:PRK09536 81 SVPQDtslsFEFDVRQVVEMGRTPHRSRFDTWTETdrAAVERAME---RTGVAQFADRPVTSLSGGERQRVLLARALAQA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504650440 178 PQIILFDEPTSALDPEMIGEVLQVMKTLAHSGITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAE 245
Cdd:PRK09536 158 TPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPAD 225
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
23-259 |
1.50e-34 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 125.15 E-value: 1.50e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 23 SIEFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGgEILIDGKPT--------RQLTgsa 94
Cdd:PRK14258 7 AIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELES-EVRVEGRVEffnqniyeRRVN--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 95 LRQLRSRVGFVFQQFNLYAhLTAQENITLALERVhGWSKSAarERSLALLSQVGLAD-------KARQMPAQLSGGQQQR 167
Cdd:PRK14258 83 LNRLRRQVSMVHPKPNLFP-MSVYDNVAYGVKIV-GWRPKL--EIDDIVESALKDADlwdeikhKIHKSALDLSGGQQQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 168 VAIARALASSPQIILFDEPTSALDPEMIGEVLQVMKTLA-HSGITMVVVTHEMQFAREIADRVVFIDG-----GDILEVA 241
Cdd:PRK14258 159 LCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFG 238
|
250
....*....|....*...
gi 504650440 242 PPAEFFARPQHARTRRFL 259
Cdd:PRK14258 239 LTKKIFNSPHDSRTREYV 256
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
21-248 |
1.91e-34 |
|
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: 130.59 E-value: 1.91e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 21 RASIEFRDVAKSYG---DHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTGsalRQ 97
Cdd:TIGR02204 335 RGEIEFEQVNFAYParpDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDP---AE 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 98 LRSRVGFVFQQFNLYAHlTAQENITLAL-----ERVHGWSKSAARERSLALLSQvGLADKARQMPAQLSGGQQQRVAIAR 172
Cdd:TIGR02204 412 LRARMALVPQDPVLFAA-SVMENIRYGRpdatdEEVEAAARAAHAHEFISALPE-GYDTYLGERGVTLSGGQRQRIAIAR 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504650440 173 ALASSPQIILFDEPTSALDPEMIGEVLQVMKTLAhSGITMVVVTHEMQFAREiADRVVFIDGGDILEVAPPAEFFA 248
Cdd:TIGR02204 490 AILKDAPILLLDEATSALDAESEQLVQQALETLM-KGRTTLIIAHRLATVLK-ADRIVVMDQGRIVAQGTHAELIA 563
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
26-237 |
1.98e-34 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 129.80 E-value: 1.98e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 26 FRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDG--------------------- 84
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKglrigylpqeppldddltvld 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 85 ------KPTRQLtGSALRQLRSRVGFVFQQFNLYAHLTAQenitlaLERVHGWsksAARERSLALLSQVGLADKARQMP- 157
Cdd:COG0488 81 tvldgdAELRAL-EAELEELEAKLAEPDEDLERLAELQEE------FEALGGW---EAEARAEEILSGLGFPEEDLDRPv 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 158 AQLSGGQQQRVAIARALASSPQIILFDEPTSALDPEMIgEVLQvmKTLAHSGITMVVVTHEMQFAREIADRVVFIDGGDI 237
Cdd:COG0488 151 SELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESI-EWLE--EFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKL 227
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
23-243 |
5.84e-34 |
|
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: 122.60 E-value: 5.84e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 23 SIEFRDVAKSYGDHR--VLNGVNLQVEPGEVVAILGPSGSGKSTLI----RLInqleSLSGGEILIDGKPTRQLtgsALR 96
Cdd:cd03244 2 DIEFKNVSLRYRPNLppVLKNISFSIKPGEKVGIVGRTGSGKSSLLlalfRLV----ELSSGSILIDGVDISKI---GLH 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 97 QLRSRVGFVFQ---------QFNLYAHLTAQ-ENITLALERVHGWSKSAARErslallsqVGLADKARQMPAQLSGGQQQ 166
Cdd:cd03244 75 DLRSRISIIPQdpvlfsgtiRSNLDPFGEYSdEELWQALERVGLKEFVESLP--------GGLDTVVEEGGENLSVGQRQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 167 RVAIARALASSPQIILFDEPTSALDPEMIGEVLQVMKTlAHSGITMVVVTHE----MQFareiaDRVVFIDGGDILEVAP 242
Cdd:cd03244 147 LLCLARALLRKSKILVLDEATASVDPETDALIQKTIRE-AFKDCTVLTIAHRldtiIDS-----DRILVLDKGRVVEFDS 220
|
.
gi 504650440 243 P 243
Cdd:cd03244 221 P 221
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
24-247 |
1.05e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 123.32 E-value: 1.05e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSY-GDHR-VLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPtrqLTGSALRQLRSR 101
Cdd:PRK13648 8 IVFKNVSFQYqSDASfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQA---ITDDNFEKLRKH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 102 VGFVFQQ-FNLYAHLTAQENITLALERvHGWSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQI 180
Cdd:PRK13648 85 IGIVFQNpDNQFVGSIVKYDVAFGLEN-HAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSV 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504650440 181 ILFDEPTSALDPEMIGEVLQVMKTL-AHSGITMVVVTHEMQFAREiADRVVFIDGGDILEVAPPAEFF 247
Cdd:PRK13648 164 IILDEATSMLDPDARQNLLDLVRKVkSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIF 230
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
24-254 |
1.21e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 123.42 E-value: 1.21e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYGD-HRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTrQLTGSALRQLRSRV 102
Cdd:PRK13636 6 LKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSRKGLMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 103 GFVFQQ-FNLYAHLTAQENITLALERVhGWSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQII 181
Cdd:PRK13636 85 GMVFQDpDNQLFSASVYQDVSFGAVNL-KLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504650440 182 LFDEPTSALDPEMIGEVLQVMKTLAHS-GITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAEFFARPQHAR 254
Cdd:PRK13636 164 VLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAEKEMLR 237
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
40-262 |
1.24e-33 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 124.43 E-value: 1.24e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 40 NGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTGSALRQLRSRVGFVFQQ--FNLYAHLTA 117
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVRSDIQMIFQDplASLNPRMTI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 118 QENITLALERVH-GWSKSAARERSLALLSQVGL-ADKARQMPAQLSGGQQQRVAIARALASSPQIILFDEPTSALDPEMI 195
Cdd:PRK15079 118 GEIIAEPLRTYHpKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQ 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504650440 196 GEVLQVMKTL-AHSGITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAEFFARPQHARTRRFLQKV 262
Cdd:PRK15079 198 AQVVNLLQQLqREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPYTKALMSAV 265
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
24-239 |
1.88e-33 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 120.11 E-value: 1.88e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYGDHR--VLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTGsalrQLRSR 101
Cdd:cd03247 1 LSINNVSFSYPEQEqqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEK----ALSSL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 102 VGFVFQQFNLYahltaqenitlalervhgwsksaarerSLALLSQVGladkarqmpAQLSGGQQQRVAIARALASSPQII 181
Cdd:cd03247 77 ISVLNQRPYLF---------------------------DTTLRNNLG---------RRFSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 504650440 182 LFDEPTSALDPEMIGEVLQVMKTLAhSGITMVVVTHEMQfAREIADRVVFIDGGDILE 239
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEVL-KDKTLIWITHHLT-GIEHMDKILFLENGKIIM 176
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
39-248 |
1.99e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 122.89 E-value: 1.99e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 39 LNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKptrQLTGSALRQLRSRVGFVFQQ-FNLYAHLTA 117
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGE---LLTAENVWNLRRKIGMVFQNpDNQFVGATV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 118 QENITLALERvHGWSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQIILFDEPTSALDPEMIGE 197
Cdd:PRK13642 100 EDDVAFGMEN-QGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQE 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 504650440 198 VLQVMKTLAHS-GITMVVVTHEMQFAREiADRVVFIDGGDILEVAPPAEFFA 248
Cdd:PRK13642 179 IMRVIHEIKEKyQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFA 229
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
23-259 |
2.61e-33 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 126.74 E-value: 2.61e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 23 SIEFRdvaKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKS-TLIRLINQLES----LSGGEILIDGKPTRQLTGSALRQ 97
Cdd:PRK15134 12 SVAFR---QQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSppvvYPSGDIRFHGESLLHASEQTLRG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 98 LR-SRVGFVFQQ----FNLYAHLTAQENITLALERvhGWSKSAARERSLALLSQVGLADKARQM---PAQLSGGQQQRVA 169
Cdd:PRK15134 89 VRgNKIAMIFQEpmvsLNPLHTLEKQLYEVLSLHR--GMRREAARGEILNCLDRVGIRQAAKRLtdyPHQLSGGERQRVM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 170 IARALASSPQIILFDEPTSALDPEMIGEVLQVMKTLAHS-GITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAEFFA 248
Cdd:PRK15134 167 IAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFS 246
|
250
....*....|.
gi 504650440 249 RPQHARTRRFL 259
Cdd:PRK15134 247 APTHPYTQKLL 257
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
32-230 |
3.66e-33 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 119.65 E-value: 3.66e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 32 SYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLirlinqLESLSGgeILidgkptRQLTGSALRQLRSRVGFVFQQFNL 111
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTL------LKVLAG--VL------RPTSGTVRRAGGARVAYVPQRSEV 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 112 YAHL--TAQENITLALERVHGWSK---SAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQIILFDEP 186
Cdd:NF040873 67 PDSLplTVRDLVAMGRWARRGLWRrltRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEP 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 504650440 187 TSALDPEMIGEVLQVMKTLAHSGITMVVVTHEMQFAREiADRVV 230
Cdd:NF040873 147 TTGLDAESRERIIALLAEEHARGATVVVVTHDLELVRR-ADPCV 189
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
23-230 |
4.01e-33 |
|
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: 126.25 E-value: 4.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 23 SIEFRDVAKSYGDHR-VLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTGSALRQlrsR 101
Cdd:TIGR02857 321 SLEFSGVSVAYPGRRpALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRD---Q 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 102 VGFVFQQFNLYAHlTAQENITLALervhgwsKSAARERSLALLSQVGLADKARQMP-----------AQLSGGQQQRVAI 170
Cdd:TIGR02857 398 IAWVPQHPFLFAG-TIAENIRLAR-------PDASDAEIREALERAGLDEFVAALPqgldtpigeggAGLSGGQAQRLAL 469
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 171 ARALASSPQIILFDEPTSALDPEMIGEVLQVMKTLAhSGITMVVVTHEMQFAREiADRVV 230
Cdd:TIGR02857 470 ARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALA-QGRTVLLVTHRLALAAL-ADRIV 527
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
37-248 |
5.47e-33 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 126.70 E-value: 5.47e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 37 RVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLE---SLSGGEILIDGKPTrqltgsALRQLRSRVGFVFQQFNLYA 113
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSpkgVKGSGSVLLNGMPI------DAKEMRAISAYVQQDDLFIP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 114 HLTAQENITL-ALERVH-GWSKSAARERSLALLSQVGLADKAR---QMPAQ---LSGGQQQRVAIARALASSPQIILFDE 185
Cdd:TIGR00955 113 TLTVREHLMFqAHLRMPrRVTKKEKRERVDEVLQALGLRKCANtriGVPGRvkgLSGGERKRLAFASELLTDPPLLFCDE 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504650440 186 PTSALDPEMIGEVLQVMKTLAHSGITMVVVTHemQFAREIA---DRVVFIDGGDILEVAPP---AEFFA 248
Cdd:TIGR00955 193 PTSGLDSFMAYSVVQVLKGLAQKGKTIICTIH--QPSSELFelfDKIILMAEGRVAYLGSPdqaVPFFS 259
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
18-239 |
1.12e-32 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 125.70 E-value: 1.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 18 HLQRASIEFRDVAKSYGDHR-VLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTGSALR 96
Cdd:COG5265 352 VVGGGEVRFENVSFGYDPERpILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLR 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 97 QlrsRVGFVFQQ---FN-------LYAHLTA-QENITLALERVH----------GWsKSAARERSLallsqvgladkarq 155
Cdd:COG5265 432 A---AIGIVPQDtvlFNdtiayniAYGRPDAsEEEVEAAARAAQihdfieslpdGY-DTRVGERGL-------------- 493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 156 mpaQLSGGQQQRVAIARALASSPQIILFDEPTSALDPEMIGEVLQVMKTLAHsGITMVVVTHEMQFAREiADRVVFIDGG 235
Cdd:COG5265 494 ---KLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVAR-GRTTLVIAHRLSTIVD-ADEILVLEAG 568
|
....
gi 504650440 236 DILE 239
Cdd:COG5265 569 RIVE 572
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
32-264 |
1.24e-32 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 120.12 E-value: 1.24e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 32 SYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPtrqLTGSALRQLRSRVGFVFQQfnl 111
Cdd:PRK11231 11 GYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKP---ISMLSSRQLARRLALLPQH--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 112 yaHLTAqENITLALERVHG-------WSKSAARERSLA--LLSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQIIL 182
Cdd:PRK11231 85 --HLTP-EGITVRELVAYGrspwlslWGRLSAEDNARVnqAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 183 FDEPTSALDPEMIGEVLQVMKTLAHSGITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAEFFarpqharTRRFLQKV 262
Cdd:PRK11231 162 LDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVM-------TPGLLRTV 234
|
..
gi 504650440 263 LD 264
Cdd:PRK11231 235 FD 236
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
24-237 |
3.07e-32 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 123.50 E-value: 3.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLinqlesLSG--------GEILIDGKPtrqLTGSAL 95
Cdd:PRK13549 6 LEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKV------LSGvyphgtyeGEIIFEGEE---LQASNI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 96 RQL-RSRVGFVFQQFNLYAHLTAQENITLALERVHG----WSKSAARerSLALLSQVGLADKARQMPAQLSGGQQQRVAI 170
Cdd:PRK13549 77 RDTeRAGIAIIHQELALVKELSVLENIFLGNEITPGgimdYDAMYLR--AQKLLAQLKLDINPATPVGNLGLGQQQLVEI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504650440 171 ARALASSPQIILFDEPTSALDPEMIGEVLQVMKTLAHSGITMVVVTHEMQFAREIADRVVFI-DGGDI 237
Cdd:PRK13549 155 AKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIrDGRHI 222
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
24-245 |
3.44e-32 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 118.94 E-value: 3.44e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTGsalrQLRSRVG 103
Cdd:PRK11300 6 LSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPG----HQIARMG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 104 FV--FQQFNLYAHLTAQENITLALER------VHGW--------SKSAARERSLALLSQVGLADKARQMPAQLSGGQQQR 167
Cdd:PRK11300 82 VVrtFQHVRLFREMTVIENLLVAQHQqlktglFSGLlktpafrrAESEALDRAATWLERVGLLEHANRQAGNLAYGQQRR 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504650440 168 VAIARALASSPQIILFDEPTSALDPEMIGEVLQVMKTLAHS-GITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAE 245
Cdd:PRK11300 162 LEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEE 240
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
24-239 |
4.79e-32 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 123.25 E-value: 4.79e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIdgkptrqltGSALrqlrsRVG 103
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL---------GETV-----KIG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 104 FVfqqfnlyahltAQENITLALER-----VHGWSKSAARERSLALLSQVGLA-DKARQMPAQLSGGQQQRVAIARALASS 177
Cdd:COG0488 382 YF-----------DQHQEELDPDKtvldeLRDGAPGGTEQEVRGYLGRFLFSgDDAFKPVGVLSGGEKARLALAKLLLSP 450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504650440 178 PQIILFDEPTSALDPEMIgEVLQVMktLAH-SGiTMVVVTHEMQFAREIADRVVFIDGGDILE 239
Cdd:COG0488 451 PNVLLLDEPTNHLDIETL-EALEEA--LDDfPG-TVLLVSHDRYFLDRVATRILEFEDGGVRE 509
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
23-245 |
9.19e-32 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 117.49 E-value: 9.19e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 23 SIEFRDVAKSY----------------------GDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEI 80
Cdd:COG1134 4 MIEVENVSKSYrlyhepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 81 LIDGKPtrqltgSALrqLRSRVGFVfqqfnlyAHLTAQENITLALeRVHGWSKS--AARERSLALLSQVGladKARQMPA 158
Cdd:COG1134 84 EVNGRV------SAL--LELGAGFH-------PELTGRENIYLNG-RLLGLSRKeiDEKFDEIVEFAELG---DFIDQPV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 159 Q-LSGGQQQRVAIARALASSPQIILFDEPTSALDPEMIGEVLQVMKTLAHSGITMVVVTHEMQFAREIADRVVFIDGGDI 237
Cdd:COG1134 145 KtYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRL 224
|
....*...
gi 504650440 238 LEVAPPAE 245
Cdd:COG1134 225 VMDGDPEE 232
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
24-239 |
1.16e-31 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 122.76 E-value: 1.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYGDHR-VLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTgsaLRQLRSRV 102
Cdd:PRK13657 335 VEFDDVSFSYDNSRqGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVT---RASLRRNI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 103 GFVFQQFNLYAHlTAQENITL-----ALERVHGWSKSAA-----RERSLALLSQVGlaDKARqmpaQLSGGQQQRVAIAR 172
Cdd:PRK13657 412 AVVFQDAGLFNR-SIEDNIRVgrpdaTDEEMRAAAERAQahdfiERKPDGYDTVVG--ERGR----QLSGGERQRLAIAR 484
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504650440 173 ALASSPQIILFDEPTSALDPEMIGEVLQVMKTLAHsGITMVVVTHEMQFAREiADRVVFIDGGDILE 239
Cdd:PRK13657 485 ALLKDPPILILDEATSALDVETEAKVKAALDELMK-GRTTFIIAHRLSTVRN-ADRILVFDNGRVVE 549
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
24-250 |
1.20e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 118.17 E-value: 1.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYGDHR-VLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLtgSALRQLRSRV 102
Cdd:PRK13644 2 IRLENVSYSYPDGTpALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDF--SKLQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 103 GFVFQ----QFnlyAHLTAQENITLALERVhGWSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSP 178
Cdd:PRK13644 80 GIVFQnpetQF---VGRTVEEDLAFGPENL-CLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504650440 179 QIILFDEPTSALDPEMIGEVLQVMKTLAHSGITMVVVTHEMQfAREIADRVVFIDGGDILEVAPPAEFFARP 250
Cdd:PRK13644 156 ECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLE-ELHDADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
36-237 |
4.78e-31 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 115.95 E-value: 4.78e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 36 HRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKptrQLTGSALRQlRSR-VGFVFQ--QFNLY 112
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGK---DVTKLPEYK-RAKyIGRVFQdpMMGTA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 113 AHLTAQENITLALERVH----GWSKSAA-RERSLALLSQV--GLADKARQMPAQLSGGQQQRVAIARALASSPQIILFDE 185
Cdd:COG1101 95 PSMTIEENLALAYRRGKrrglRRGLTKKrRELFRELLATLglGLENRLDTKVGLLSGGQRQALSLLMATLTKPKLLLLDE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 504650440 186 PTSALDPEMIGEVLQVMKTL-AHSGITMVVVTHEMQFAREIADRVVFIDGGDI 237
Cdd:COG1101 175 HTAALDPKTAALVLELTEKIvEENNLTTLMVTHNMEQALDYGNRLIMMHEGRI 227
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
27-265 |
5.33e-31 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 115.79 E-value: 5.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 27 RDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGK-----PTRQLTGSALRQL-RS 100
Cdd:PRK11701 10 RGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrDLYALSEAERRRLlRT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 101 RVGFVFQ--QFNLYAHLTAQENITLALERVhGWSKSAA-RERSLALLSQVGL-ADKARQMPAQLSGGQQQRVAIARALAS 176
Cdd:PRK11701 90 EWGFVHQhpRDGLRMQVSAGGNIGERLMAV-GARHYGDiRATAGDWLERVEIdAARIDDLPTTFSGGMQQRLQIARNLVT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 177 SPQIILFDEPTSALDPEMIGEVLQVMKTLAHS-GITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAEFFARPQHART 255
Cdd:PRK11701 169 HPRLVFMDEPTGGLDVSVQARLLDLLRGLVRElGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLTDQVLDDPQHPYT 248
|
250
....*....|
gi 504650440 256 RRFLQKVLDP 265
Cdd:PRK11701 249 QLLVSSVLQV 258
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
37-260 |
8.59e-31 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 116.76 E-value: 8.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 37 RVLNGVNLQVEPGEVVAILGPSGSGKS----TLIRLINQLESLSGGEILIDGKPTRQLTGSALRQL-RSRVGFVFQQ--F 109
Cdd:PRK11022 21 RAVDRISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDLQRISEKERRNLvGAEVAMIFQDpmT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 110 NLYAHLTAQENITLALERVHGWSKSAARERSLALLSQVGLADKARQM---PAQLSGGQQQRVAIARALASSPQIILFDEP 186
Cdd:PRK11022 101 SLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASRLdvyPHQLSGGMSQRVMIAMAIACRPKLLIADEP 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504650440 187 TSALDPEMIGEVLQVMKTLAH-SGITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAEFFARPQHARTRRFLQ 260
Cdd:PRK11022 181 TTALDVTIQAQIIELLLELQQkENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAPRHPYTQALLR 255
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
22-254 |
2.02e-30 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 113.84 E-value: 2.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 22 ASIEFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTGSAlrQLRSR 101
Cdd:PRK10895 2 ATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHA--RARRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 102 VGFVFQQFNLYAHLTAQENITLALERVHGWSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQII 181
Cdd:PRK10895 80 IGYLPQEASIFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504650440 182 LFDEPTSALDPEMIGEVLQVMKTLAHSGITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAEFFARPQHAR 254
Cdd:PRK10895 160 LLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKR 232
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
36-237 |
3.20e-30 |
|
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: 111.75 E-value: 3.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 36 HRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTGSALRQL--------RSRVGfVFQ 107
Cdd:cd03215 13 KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgiayvpedRKREG-LVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 108 QFNLYahltaqENITLalervhgwsksaarerslallsqvgladkarqmPAQLSGGQQQRVAIARALASSPQIILFDEPT 187
Cdd:cd03215 92 DLSVA------ENIAL---------------------------------SSLLSGGNQQKVVLARWLARDPRVLILDEPT 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 504650440 188 SALDPEMIGEVLQVMKTLAHSGITMVVVTHEMQFAREIADRVVFIDGGDI 237
Cdd:cd03215 133 RGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
24-240 |
3.81e-30 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 117.96 E-value: 3.81e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTGSALRQLRsrVG 103
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLG--IG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 104 FVFQQFNLYAHLTAQENI---TLALERVHG-----WSKsaARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALA 175
Cdd:PRK09700 84 IIYQELSVIDELTVLENLyigRHLTKKVCGvniidWRE--MRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLM 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504650440 176 SSPQIILFDEPTSALDPEMIGEVLQVMKTLAHSGITMVVVTHEMQFAREIADRV-VFIDG-----GDILEV 240
Cdd:PRK09700 162 LDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYtVMKDGssvcsGMVSDV 232
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
24-247 |
1.10e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 113.29 E-value: 1.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYGDH-----RVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILI-DGKPTRQLTGSALRQ 97
Cdd:PRK13643 2 IKFEKVNYTYQPNspfasRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVgDIVVSSTSKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 98 LRSRVGFVFQ--QFNLYAHlTAQENITLALERVhGWSKSAARERSLALLSQVGLADKA-RQMPAQLSGGQQQRVAIARAL 174
Cdd:PRK13643 82 VRKKVGVVFQfpESQLFEE-TVLKDVAFGPQNF-GIPKEKAEKIAAEKLEMVGLADEFwEKSPFELSGGQMRRVAIAGIL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504650440 175 ASSPQIILFDEPTSALDPEMIGEVLQVMKTLAHSGITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAEFF 247
Cdd:PRK13643 160 AMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
24-235 |
2.46e-29 |
|
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: 107.92 E-value: 2.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLInqleslSGGEILIDGKPTRqltGSALRqlrsrVG 103
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLI------AGELEPDEGIVTW---GSTVK-----IG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 104 FVfqqfnlyahltaqenitlalervhgwsksaarerslallsqvgladkarqmpAQLSGGQQQRVAIARALASSPQIILF 183
Cdd:cd03221 67 YF----------------------------------------------------EQLSGGEKMRLALAKLLLENPNLLLL 94
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 504650440 184 DEPTSALDPEMIgEVLQVMktLAHSGITMVVVTHEMQFAREIADRVVFIDGG 235
Cdd:cd03221 95 DEPTNHLDLESI-EALEEA--LKEYPGTVILVSHDRYFLDQVATKIIELEDG 143
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
24-238 |
3.53e-29 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 115.15 E-value: 3.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTGSALRQLrsRVG 103
Cdd:PRK15439 12 LCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQL--GIY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 104 FVFQQFNLYAHLTAQENITLALERvhgwsKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQIILF 183
Cdd:PRK15439 90 LVPQEPLLFPNLSVKENILFGLPK-----RQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILIL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 504650440 184 DEPTSALDPEMIGEVLQVMKTLAHSGITMVVVTHEMQFAREIADRV-VFIDGGDIL 238
Cdd:PRK15439 165 DEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRIsVMRDGTIAL 220
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
21-248 |
4.74e-29 |
|
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: 115.61 E-value: 4.74e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 21 RASIEFRDVAKSYGDHR--VLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTGSALRQl 98
Cdd:TIGR01846 453 RGAITFENIRFRYAPDSpeVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRR- 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 99 rsRVGFVFQQfNLYAHLTAQENITLA-----LERVHGWSKSAARERSLALLSQvGLADKARQMPAQLSGGQQQRVAIARA 173
Cdd:TIGR01846 532 --QMGVVLQE-NVLFSRSIRDNIALCnpgapFEHVIHAAKLAGAHDFISELPQ-GYNTEVGEKGANLSGGQRQRIAIARA 607
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504650440 174 LASSPQIILFDEPTSALDPEMIGEVLQVMKTLAhSGITMVVVTHEMQFAREiADRVVFIDGGDILEVAPPAEFFA 248
Cdd:TIGR01846 608 LVGNPRILIFDEATSALDYESEALIMRNMREIC-RGRTVIIIAHRLSTVRA-CDRIIVLEKGQIAESGRHEELLA 680
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
24-235 |
6.19e-29 |
|
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: 108.71 E-value: 6.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDV-----AKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIR-LINQLESLSGgeilidgkptrqltgsaLRQ 97
Cdd:cd03250 1 ISVEDAsftwdSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSaLLGELEKLSG-----------------SVS 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 98 LRSRVGFVFQQ---FNLyahlTAQENITLALERVHGWSKSAAR----ERSLALLS-----QVGladkarQMPAQLSGGQQ 165
Cdd:cd03250 64 VPGSIAYVSQEpwiQNG----TIRENILFGKPFDEERYEKVIKacalEPDLEILPdgdltEIG------EKGINLSGGQK 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504650440 166 QRVAIARALASSPQIILFDEPTSALDPemigevlQVMKTLAHSGI--------TMVVVTHEMQFAREiADRVVFIDGG 235
Cdd:cd03250 134 QRISLARAVYSDADIYLLDDPLSAVDA-------HVGRHIFENCIlglllnnkTRILVTHQLQLLPH-ADQIVVLDNG 203
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
38-249 |
7.71e-29 |
|
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: 114.46 E-value: 7.71e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 38 VLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTGsalRQLRSRVGFVFQQFNLYAHlTA 117
Cdd:COG4618 347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDR---EELGRHIGYLPQDVELFDG-TI 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 118 QENItlAL------ERVHgwskSAARerslallsQVGLADKARQMP-----------AQLSGGQQQRVAIARALASSPQI 180
Cdd:COG4618 423 AENI--ARfgdadpEKVV----AAAK--------LAGVHEMILRLPdgydtrigeggARLSGGQRQRIGLARALYGDPRL 488
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504650440 181 ILFDEPTSALDPEmiGE--VLQVMKTLAHSGITMVVVTHEMQfAREIADRVVFIDGGDILEVAPPAEFFAR 249
Cdd:COG4618 489 VVLDEPNSNLDDE--GEaaLAAAIRALKARGATVVVITHRPS-LLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
36-260 |
8.45e-29 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 109.79 E-value: 8.45e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 36 HRVL-NGVNLQVEPGEVVAILGPSGSGKS-TLIRLINQLES---LSGGEILIDGKPTrqltgsALRQLRSR-VGFVFQQ- 108
Cdd:PRK10418 15 AQPLvHGVSLTLQRGRVLALVGGSGSGKSlTCAAALGILPAgvrQTAGRVLLDGKPV------APCALRGRkIATIMQNp 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 109 ---FNLYAHLTAQenitlALERVHGWSKSAARERSLALLSQVGLADKARQM---PAQLSGGQQQRVAIARALASSPQIIL 182
Cdd:PRK10418 89 rsaFNPLHTMHTH-----ARETCLALGKPADDATLTAALEAVGLENAARVLklyPFEMSGGMLQRMMIALALLCEAPFII 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504650440 183 FDEPTSALDPEMIGEVLQVMKTLAHS-GITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAEFFARPQHARTRRFLQ 260
Cdd:PRK10418 164 ADEPTTDLDVVAQARILDLLESIVQKrALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLVS 242
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
37-230 |
8.92e-29 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 113.96 E-value: 8.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 37 RVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRqlTGSALRQLRSRVGFV---FQQFNLYA 113
Cdd:COG1129 266 GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVR--IRSPRDAIRAGIAYVpedRKGEGLVL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 114 HLTAQENITLA-LERVHGW---SKSAARERSLALLSQVGL-ADKARQMPAQLSGGQQQRVAIARALASSPQIILFDEPTS 188
Cdd:COG1129 344 DLSIRENITLAsLDRLSRGgllDRRRERALAEEYIKRLRIkTPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTR 423
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 504650440 189 ALDpemIG---EVLQVMKTLAHSGITMVVVTHEMQFAREIADRVV 230
Cdd:COG1129 424 GID---VGakaEIYRLIRELAAEGKAVIVISSELPELLGLSDRIL 465
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
42-259 |
1.07e-28 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 109.88 E-value: 1.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 42 VNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPtrqLTGSALRQLRSRVGFVFQqfNLYAHLTAQENI 121
Cdd:PRK15112 32 LSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHP---LHFGDYSYRSQRIRMIFQ--DPSTSLNPRQRI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 122 TLALE---RVHGWSKSAARERSL-ALLSQVGL-ADKARQMPAQLSGGQQQRVAIARALASSPQIILFDEPTSALDPEMIG 196
Cdd:PRK15112 107 SQILDfplRLNTDLEPEQREKQIiETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRS 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504650440 197 EVLQVMKTLAHS-GITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAEFFARPQHARTRRFL 259
Cdd:PRK15112 187 QLINLMLELQEKqGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASPLHELTKRLI 250
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
20-234 |
1.08e-28 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 113.85 E-value: 1.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 20 QRASIEFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRqlTGSALRQLR 99
Cdd:PRK11288 1 SSPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMR--FASTTAALA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 100 SRVGFVFQQFNLYAHLTAQENITL-ALERVHGW-SKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASS 177
Cdd:PRK11288 79 AGVAIIYQELHLVPEMTVAENLYLgQLPHKGGIvNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARN 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 504650440 178 PQIILFDEPTSALDPEMIGEVLQVMKTLAHSGITMVVVTHEMQFAREIADRV-VFIDG 234
Cdd:PRK11288 159 ARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAItVFKDG 216
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
33-269 |
1.66e-28 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 109.71 E-value: 1.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 33 YGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTrQLTGSALRQLRSRVGFVFQ---QF 109
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL-DYSKRGLLALRQQVATVFQdpeQQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 110 NLYAHLTAqeNITLALERVHGWSKSAAR--ERSLALLSqvglADKARQMPAQ-LSGGQQQRVAIARALASSPQIILFDEP 186
Cdd:PRK13638 90 IFYTDIDS--DIAFSLRNLGVPEAEITRrvDEALTLVD----AQHFRHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 187 TSALDPEMIGEVLQVMKTLAHSGITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAEFFARPQHARTRRFLQKVLDPL 266
Cdd:PRK13638 164 TAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFACTEAMEQAGLTQPWLVKL 243
|
...
gi 504650440 267 HQE 269
Cdd:PRK13638 244 HTQ 246
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
24-239 |
2.16e-28 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 112.79 E-value: 2.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRqLTGSALRQlRSRVG 103
Cdd:PRK10762 5 LQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVT-FNGPKSSQ-EAGIG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 104 FVFQQFNLYAHLTAQENITLALERVHGWSK---SAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQI 180
Cdd:PRK10762 83 IIHQELNLIPQLTIAENIFLGREFVNRFGRidwKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 181 ILFDEPTSALDPEMIGEVLQVMKTLAHSGITMVVVTHEMQFAREIADRV-VFIDGGDILE 239
Cdd:PRK10762 163 IIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVtVFRDGQFIAE 222
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
25-237 |
4.32e-28 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 112.19 E-value: 4.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 25 EFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLinqlesLSG--------GEILIDGKPTRqltgsaLR 96
Cdd:NF040905 3 EMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKV------LSGvyphgsyeGEILFDGEVCR------FK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 97 QLRS--RVGFVF--QQFNLYAHLTAQENITLALERVHG----WskSAARERSLALLSQVGLADKARQMPAQLSGGQQQRV 168
Cdd:NF040905 71 DIRDseALGIVIihQELALIPYLSIAENIFLGNERAKRgvidW--NETNRRARELLAKVGLDESPDTLVTDIGVGKQQLV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 169 AIARALASSPQIILFDEPTSALDPEMIGEVLQVMKTLAHSGITMVVVTHEMQFAREIADRVVFI-DGGDI 237
Cdd:NF040905 149 EIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLrDGRTI 218
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
37-238 |
5.05e-28 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 109.41 E-value: 5.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 37 RVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLinqlesLSG------GEILIDGK-PTRQltgsaLRQLRSRVGFVFQQF 109
Cdd:COG4586 36 EAVDDISFTIEPGEIVGFIGPNGAGKSTTIKM------LTGilvptsGEVRVLGYvPFKR-----RKEFARRIGVVFGQR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 110 N-LYAHLTAQENITLaLERVHGWSKSAARERsLALLSQV-GLADKARQMPAQLSGGQQQRVAIARALASSPQIILFDEPT 187
Cdd:COG4586 105 SqLWWDLPAIDSFRL-LKAIYRIPDAEYKKR-LDELVELlDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPT 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 504650440 188 SALDPEMIGEVLQVMKTL-AHSGITMVVVTHEMQFAREIADRVVFIDGGDIL 238
Cdd:COG4586 183 IGLDVVSKEAIREFLKEYnRERGTTILLTSHDMDDIEALCDRVIVIDHGRII 234
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
35-248 |
1.52e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 107.40 E-value: 1.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 35 DHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLE-SLSGGEILIDGK-PTRQLTGSALRQLRSRVGFVFQ--QFN 110
Cdd:PRK13645 23 EFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIiSETGQTIVGDYAiPANLKKIKEVKRLRKEIGLVFQfpEYQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 111 LYahltaQENIT--LALERVH-GWSKSAARERSLALLSQVGLA-DKARQMPAQLSGGQQQRVAIARALASSPQIILFDEP 186
Cdd:PRK13645 103 LF-----QETIEkdIAFGPVNlGENKQEAYKKVPELLKLVQLPeDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEP 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504650440 187 TSALDPEMIGEVLQVMKTL-AHSGITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAEFFA 248
Cdd:PRK13645 178 TGGLDPKGEEDFINLFERLnKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFS 240
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
24-249 |
1.97e-27 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 110.88 E-value: 1.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSY--GDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTgsaLRQLRSR 101
Cdd:PRK11176 342 IEFRNVTFTYpgKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYT---LASLRNQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 102 VGFVFQQFNLYAHlTAQENITLALERVhgWSKS---AARERSLALlsqvglaDKARQMP-----------AQLSGGQQQR 167
Cdd:PRK11176 419 VALVSQNVHLFND-TIANNIAYARTEQ--YSREqieEAARMAYAM-------DFINKMDngldtvigengVLLSGGQRQR 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 168 VAIARALASSPQIILFDEPTSALDPEMIGEVLQVMKTLAHSGiTMVVVTHEMQfAREIADRVVFIDGGDILEVAPPAEFF 247
Cdd:PRK11176 489 IAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNR-TSLVIAHRLS-TIEKADEILVVEDGEIVERGTHAELL 566
|
..
gi 504650440 248 AR 249
Cdd:PRK11176 567 AQ 568
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
29-263 |
2.34e-27 |
|
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: 106.07 E-value: 2.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 29 VAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILID--GKPTRQLTGSA----LRQLRSRV 102
Cdd:TIGR02323 9 LSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYImrSGAELELYQLSeaerRRLMRTEW 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 103 GFVFQQF--NLYAHLTAQENITLALERVHGWSKSAARERSLALLSQVGL-ADKARQMPAQLSGGQQQRVAIARALASSPQ 179
Cdd:TIGR02323 89 GFVHQNPrdGLRMRVSAGANIGERLMAIGARHYGNIRATAQDWLEEVEIdPTRIDDLPRAFSGGMQQRLQIARNLVTRPR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 180 IILFDEPTSALDPEMIGEVLQVMKTLAHS-GITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAEFFARPQHARTRRF 258
Cdd:TIGR02323 169 LVFMDEPTGGLDVSVQARLLDLLRGLVRDlGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVLDDPQHPYTQLL 248
|
....*
gi 504650440 259 LQKVL 263
Cdd:TIGR02323 249 VSSIL 253
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
24-235 |
5.26e-27 |
|
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: 109.14 E-value: 5.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLinqlesLSG--------GEILIDGKPtrqLTGSAL 95
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKI------LSGvyphgtwdGEIYWSGSP---LKASNI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 96 RQL-RSRVGFVFQQFNLYAHLTAQENITLALERVHGWSKSAARE---RSLALLSQVGLADKARQMP-AQLSGGQQQRVAI 170
Cdd:TIGR02633 73 RDTeRAGIVIIHQELTLVPELSVAENIFLGNEITLPGGRMAYNAmylRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504650440 171 ARALASSPQIILFDEPTSALDPEMIGEVLQVMKTLAHSGITMVVVTHEMQFAREIADRVVFIDGG 235
Cdd:TIGR02633 153 AKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDG 217
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
23-239 |
8.56e-27 |
|
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: 109.06 E-value: 8.56e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 23 SIEFRDVAKSYG-DHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTGSALRQLrsr 101
Cdd:TIGR01193 473 DIVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQF--- 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 102 VGFVFQQFNLYAHlTAQENITLalervhGWSKSAARERSLALLSQVGLADKARQMP-----------AQLSGGQQQRVAI 170
Cdd:TIGR01193 550 INYLPQEPYIFSG-SILENLLL------GAKENVSQDEIWAACEIAEIKDDIENMPlgyqtelseegSSISGGQKQRIAL 622
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504650440 171 ARALASSPQIILFDEPTSALDpeMIGEVLQVMKTLAHSGITMVVVTHEMQFAREiADRVVFIDGGDILE 239
Cdd:TIGR01193 623 ARALLTDSKVLILDESTSNLD--TITEKKIVNNLLNLQDKTIIFVAHRLSVAKQ-SDKIIVLDHGKIIE 688
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
28-237 |
1.11e-26 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 106.50 E-value: 1.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 28 DVAKSYGDHRvLNgVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGkptRQL----TGSALRQLRSRVG 103
Cdd:PRK11144 5 NFKQQLGDLC-LT-VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNG---RVLfdaeKGICLPPEKRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 104 FVFQQFNLYAHLTAQENITlalervHGWSKSAaRERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQIILF 183
Cdd:PRK11144 80 YVFQDARLFPHYKVRGNLR------YGMAKSM-VAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLM 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 504650440 184 DEPTSALDPEMIGEVLQVMKTLAHS-GITMVVVTHEMQfarEI---ADRVVFIDGGDI 237
Cdd:PRK11144 153 DEPLASLDLPRKRELLPYLERLAREiNIPILYVSHSLD---EIlrlADRVVVLEQGKV 207
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
24-217 |
1.62e-26 |
|
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: 102.44 E-value: 1.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTGSALRQLrsrvg 103
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENI----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 104 fvfqqfnLYA-HLTAQENITLALERVHGWSK--SAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQI 180
Cdd:TIGR01189 76 -------LYLgHLPGLKPELSALENLHFWAAihGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPL 148
|
170 180 190
....*....|....*....|....*....|....*..
gi 504650440 181 ILFDEPTSALDPEMIGEVLQVMKTLAHSGITMVVVTH 217
Cdd:TIGR01189 149 WILDEPTTALDKAGVALLAGLLRAHLARGGIVLLTTH 185
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
28-218 |
1.89e-26 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 108.04 E-value: 1.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 28 DVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLIN---QLESLSGGEILIDGKPTRQLTgsalrqlrSRVGF 104
Cdd:PLN03211 73 DETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAgriQGNNFTGTILANNRKPTKQIL--------KRTGF 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 105 VFQQFNLYAHLTAQENITL-ALERVhgwSKSAARERSL----ALLSQVGLADKARQMPAQ-----LSGGQQQRVAIARAL 174
Cdd:PLN03211 145 VTQDDILYPHLTVRETLVFcSLLRL---PKSLTKQEKIlvaeSVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEM 221
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 504650440 175 ASSPQIILFDEPTSALDPEMIGEVLQVMKTLAHSGITMVVVTHE 218
Cdd:PLN03211 222 LINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQ 265
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
20-230 |
2.29e-26 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 102.87 E-value: 2.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 20 QRASIEFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTGSALRQlr 99
Cdd:PRK10247 4 NSPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQ-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 100 sRVGFVFQQFNLYAHlTAQENITLALERVHgwsKSAARERSLALLSQVGLADKARQMP-AQLSGGQQQRVAIARALASSP 178
Cdd:PRK10247 82 -QVSYCAQTPTLFGD-TVYDNLIFPWQIRN---QQPDPAIFLDDLERFALPDTILTKNiAELSGGEKQRISLIRNLQFMP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 504650440 179 QIILFDEPTSALDPEMIGEVLQVMKTLA-HSGITMVVVTHEmqfAREI--ADRVV 230
Cdd:PRK10247 157 KVLLLDEITSALDESNKHNVNEIIHRYVrEQNIAVLWVTHD---KDEInhADKVI 208
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
15-245 |
3.41e-26 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 103.33 E-value: 3.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 15 DFSHLQRASIEFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTGSA 94
Cdd:PRK10575 3 EYTNHSDTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 95 LRQlrsRVGFVFQQFNLYAHLTAQENITLALERVHGW---SKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIA 171
Cdd:PRK10575 83 FAR---KVAYLPQQLPAAEGMTVRELVAIGRYPWHGAlgrFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504650440 172 RALASSPQIILFDEPTSALDPEMIGEVLQVMKTLAHS-GITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAE 245
Cdd:PRK10575 160 MLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAE 234
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
24-222 |
1.06e-25 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 100.26 E-value: 1.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTGSALRQLrsrvg 103
Cdd:PRK13538 2 LEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDL----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 104 fvfqqfnLY-AH-------LTAQENITLALeRVHGwskSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALA 175
Cdd:PRK13538 77 -------LYlGHqpgikteLTALENLRFYQ-RLHG---PGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWL 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 504650440 176 SSPQIILFDEPTSALDPEMIGEVLQVM-KTLAHSGitMVVVT--HEMQFA 222
Cdd:PRK13538 146 TRAPLWILDEPFTAIDKQGVARLEALLaQHAEQGG--MVILTthQDLPVA 193
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
35-245 |
1.17e-25 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 101.46 E-value: 1.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 35 DHRVLnGVNLQVEPGEVVAILGPSGSGKSTLirlinqLESLSG-----GEILIDGKPTRQLTGSALRQLRsrvGFVFQQF 109
Cdd:COG4138 9 AGRLG-PISAQVNAGELIHLIGPNGAGKSTL------LARMAGllpgqGEILLNGRPLSDWSAAELARHR---AYLSQQQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 110 NLYAHLTAQENITLALERVHgwSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALA-------SSPQIIL 182
Cdd:COG4138 79 SPPFAMPVFQYLALHQPAGA--SSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLqvwptinPEGQLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504650440 183 FDEPTSALDPEMIGEVLQVMKTLAHSGITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAE 245
Cdd:COG4138 157 LDEPMNSLDVAQQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAE 219
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
24-243 |
1.54e-25 |
|
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: 99.91 E-value: 1.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLES--LSGGEILIDGKPTRQLTgsalRQLRSR 101
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKyeVTEGEILFKGEDITDLP----PEERAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 102 VGfvfqqfnlyahltaqenITLAL---ERVHGwsksaarerslallsqVGLADKARQMPAQLSGGQQQRVAIARALASSP 178
Cdd:cd03217 77 LG-----------------IFLAFqypPEIPG----------------VKNADFLRYVNEGFSGGEKKRNEILQLLLLEP 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504650440 179 QIILFDEPTSALDPEMIGEVLQVMKTLAHSGITMVVVTHEMQFAREI-ADRVVFIDGGDILEVAPP 243
Cdd:cd03217 124 DLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGDK 189
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
34-264 |
4.84e-25 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 101.34 E-value: 4.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 34 GDHRVLNGVNLQVEPGEVVAILGPSGSGKS-TLIRLINQLES--LSGGEILIDGKPTRQLTGSALRQLRS-RVGFVFQ-- 107
Cdd:PRK09473 27 GDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAAngRIGGSATFNGREILNLPEKELNKLRAeQISMIFQdp 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 108 --QFNLYAHLTAQENITLALERvhGWSKSAARERSLALLSQVGLADKARQM---PAQLSGGQQQRVAIARALASSPQIIL 182
Cdd:PRK09473 107 mtSLNPYMRVGEQLMEVLMLHK--GMSKAEAFEESVRMLDAVKMPEARKRMkmyPHEFSGGMRQRVMIAMALLCRPKLLI 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 183 FDEPTSALDPEMIGEVLQVMKTLAHS-GITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAEFFARPQHARTRRFLQK 261
Cdd:PRK09473 185 ADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQPSHPYSIGLLNA 264
|
....*
gi 504650440 262 V--LD 264
Cdd:PRK09473 265 VprLD 269
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
19-238 |
6.24e-25 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 99.18 E-value: 6.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 19 LQRASIEFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTGSalRQL 98
Cdd:PRK11614 1 MEKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTA--KIM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 99 RSRVGFVFQQFNLYAHLTAQENITLALERVHGWSKSAARERSLALLSQvgLADKARQMPAQLSGGQQQRVAIARALASSP 178
Cdd:PRK11614 79 REAVAIVPEGRRVFSRMTVEENLAMGGFFAERDQFQERIKWVYELFPR--LHERRIQRAGTMSGGEQQMLAIGRALMSQP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504650440 179 QIILFDEPTSALDPEMIGEVLQVMKTLAHSGITMVVVTHEMQFAREIADR--------VVFIDGGDIL 238
Cdd:PRK11614 157 RLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRgyvlenghVVLEDTGDAL 224
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
24-238 |
8.60e-25 |
|
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: 98.94 E-value: 8.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYGDHR---------------------VLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILI 82
Cdd:cd03267 1 IEVSNLSKSYRVYSkepgligslkslfkrkyreveALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 83 DGkptrQLTGSALRQLRSRVGFVFQQFN-LYAHLTAQENITLaLERVHGWSKSAARERSLALLSQVGLADKARQMPAQLS 161
Cdd:cd03267 81 AG----LVPWKRRKKFLRRIGVVFGQKTqLWWDLPVIDSFYL-LAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLS 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504650440 162 GGQQQRVAIARALASSPQIILFDEPTSALDPEMIGEVLQVMKTL-AHSGITMVVVTHEMQFAREIADRVVFIDGGDIL 238
Cdd:cd03267 156 LGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYnRERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
34-238 |
1.37e-24 |
|
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: 102.43 E-value: 1.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 34 GDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTgsaLRQLRSRVGFVFQQFNLYA 113
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWD---RETFGKHIGYLPQDVELFP 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 114 HlTAQENITLALERVHGWSKSAArerslALLSQV---------GLADKARQMPAQLSGGQQQRVAIARALASSPQIILFD 184
Cdd:TIGR01842 406 G-TVAENIARFGENADPEKIIEA-----AKLAGVhelilrlpdGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLD 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 504650440 185 EPTSALDPEmiGE--VLQVMKTLAHSGITMVVVTHEMQfAREIADRVVFIDGGDIL 238
Cdd:TIGR01842 480 EPNSNLDEE--GEqaLANAIKALKARGITVVVITHRPS-LLGCVDKILVLQDGRIA 532
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
42-262 |
2.06e-24 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 102.24 E-value: 2.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 42 VNLQVEPGEVVAILGPSGSGKS----TLIRLINQleslSGGEILIDGKPTR----------QLTGSALRQLR-SRVGFVF 106
Cdd:PRK10261 35 LSFSLQRGETLAIVGESGSGKSvtalALMRLLEQ----AGGLVQCDKMLLRrrsrqvielsEQSAAQMRHVRgADMAMIF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 107 QQ--FNLYAHLTAQENITLALERVHGWSKSAARERSLALLSQVGLADKA---RQMPAQLSGGQQQRVAIARALASSPQII 181
Cdd:PRK10261 111 QEpmTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQtilSRYPHQLSGGMRQRVMIAMALSCRPAVL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 182 LFDEPTSALDPEMIGEVLQVMKTLAHS-GITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAEFFARPQHARTRRFLQ 260
Cdd:PRK10261 191 IADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAPQHPYTRALLA 270
|
..
gi 504650440 261 KV 262
Cdd:PRK10261 271 AV 272
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
30-237 |
2.37e-24 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 97.22 E-value: 2.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 30 AKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPtrqltgSALrqLRSRVGFVfqqf 109
Cdd:cd03220 29 KGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRV------SSL--LGLGGGFN---- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 110 nlyAHLTAQENITLALeRVHGWSKS--AARERSLALLSQVGladKARQMP-AQLSGGQQQRVAIARALASSPQIILFDEP 186
Cdd:cd03220 97 ---PELTGRENIYLNG-RLLGLSRKeiDEKIDEIIEFSELG---DFIDLPvKTYSSGMKARLAFAIATALEPDILLIDEV 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 504650440 187 TSALDPEMIGEVLQVMKTLAHSGITMVVVTHEMQFAREIADRVVFIDGGDI 237
Cdd:cd03220 170 LAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKI 220
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
19-239 |
4.43e-24 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 100.95 E-value: 4.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 19 LQRASIEFRDVAKSY-GDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTGSALRQ 97
Cdd:PRK10790 336 LQSGRIDIDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQ 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 98 lrsRVGFVfQQFNLYAHLTAQENITLAlervhgwsKSAARERSLALLSQVGLADKARQMPA-----------QLSGGQQQ 166
Cdd:PRK10790 416 ---GVAMV-QQDPVVLADTFLANVTLG--------RDISEEQVWQALETVQLAELARSLPDglytplgeqgnNLSVGQKQ 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504650440 167 RVAIARALASSPQIILFDEPTSALDP---EMIGEVLQVMKtlAHSgiTMVVVTHEMQFAREiADRVVFIDGGDILE 239
Cdd:PRK10790 484 LLALARVLVQTPQILILDEATANIDSgteQAIQQALAAVR--EHT--TLVVIAHRLSTIVE-ADTILVLHRGQAVE 554
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
23-239 |
5.26e-24 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 100.69 E-value: 5.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 23 SIEFRD-VAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLinqlesLSG-----GEILIDGKPTRQLtgsALR 96
Cdd:PRK11174 349 TIEAEDlEILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNA------LLGflpyqGSLKINGIELREL---DPE 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 97 QLRSRVGFVFQQFNLYaHLTAQENITLAlervhgwSKSAARERSLALLSQVGLADKARQMP-----------AQLSGGQQ 165
Cdd:PRK11174 420 SWRKHLSWVGQNPQLP-HGTLRDNVLLG-------NPDASDEQLQQALENAWVSEFLPLLPqgldtpigdqaAGLSVGQA 491
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504650440 166 QRVAIARALASSPQIILFDEPTSALDpeMIGEVlQVMKTL--AHSGITMVVVTHEMQFAREIaDRVVFIDGGDILE 239
Cdd:PRK11174 492 QRLALARALLQPCQLLLLDEPTASLD--AHSEQ-LVMQALnaASRRQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQ 563
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
23-240 |
7.39e-24 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 96.18 E-value: 7.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 23 SIEFRDVAKSYG------DHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDgKPTRQLTgsalr 96
Cdd:COG2401 24 SERVAIVLEAFGvelrvvERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD-VPDNQFG----- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 97 qlrsrvgfvfQQFNLYAHLTAQENITLALErvhgwsksaarerslaLLSQVGLADKA--RQMPAQLSGGQQQRVAIARAL 174
Cdd:COG2401 98 ----------REASLIDAIGRKGDFKDAVE----------------LLNAVGLSDAVlwLRRFKELSTGQKFRFRLALLL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504650440 175 ASSPQIILFDEPTSALDPEMIGEVLQVMKTLAHS-GITMVVVTHEMQFAREIA-DRVVFIDGGDILEV 240
Cdd:COG2401 152 AERPKLLVIDEFCSHLDRQTAKRVARNLQKLARRaGITLVVATHHYDVIDDLQpDLLIFVGYGGVPEE 219
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
19-234 |
7.46e-24 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 97.26 E-value: 7.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 19 LQRASIEFRDVAKSYGD-HRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQltgsALRQ 97
Cdd:PRK15056 2 MQQAGIVVNDVTVTWRNgHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ----ALQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 98 lrSRVGFVFQQFNL-YAHLTAQENITLALERVH-GW---SKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIAR 172
Cdd:PRK15056 78 --NLVAYVPQSEEVdWSFPVLVEDVVMMGRYGHmGWlrrAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLAR 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504650440 173 ALASSPQIILFDEPTSALDPEMIGEVLQVMKTLAHSGITMVVVTHEMQFAREIADRVVFIDG 234
Cdd:PRK15056 156 AIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMVKG 217
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
10-239 |
1.15e-23 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 99.66 E-value: 1.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 10 AASSADFSHLQRAS----IEFRDVAKSYGDHRV-LNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDG 84
Cdd:PRK10522 305 APYKAEFPRPQAFPdwqtLELRNVTFAYQDNGFsVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDG 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 85 KPtrqLTGSALRQLRSRVGFVFQQFNLYAHLTAQENITLALERVHGWsksaarerslalLSQVGLADK-----ARQMPAQ 159
Cdd:PRK10522 385 KP---VTAEQPEDYRKLFSAVFTDFHLFDQLLGPEGKPANPALVEKW------------LERLKMAHKleledGRISNLK 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 160 LSGGQQQRVAIARALASSPQIILFDEPTSALDPEMIGEVLQV-MKTLAHSGITMVVVTHEMQFArEIADRVVFIDGGDIL 238
Cdd:PRK10522 450 LSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQVlLPLLQEMGKTIFAISHDDHYF-IHADRLLEMRNGQLS 528
|
.
gi 504650440 239 E 239
Cdd:PRK10522 529 E 529
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
33-245 |
2.31e-23 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 95.82 E-value: 2.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 33 YGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKptrQLTGSALRQLRSRVGFVFQQFNLY 112
Cdd:PRK10253 17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGE---HIQHYASKEVARRIGLLAQNATTP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 113 AHLTAQENITLA-------LERvhgWSKSAARERSLALLSqVGLADKARQMPAQLSGGQQQRVAIARALASSPQIILFDE 185
Cdd:PRK10253 94 GDITVQELVARGryphqplFTR---WRKEDEEAVTKAMQA-TGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504650440 186 PTSALDPEMIGEVLQVMKTLAHS-GITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAE 245
Cdd:PRK10253 170 PTTWLDISHQIDLLELLSELNREkGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKE 230
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
20-243 |
2.48e-23 |
|
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: 94.40 E-value: 2.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 20 QRASIEFRDVAKSYGDH--RVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLtgsALRQ 97
Cdd:cd03369 3 EHGEIEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTI---PLED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 98 LRSRVGFVFQQFNLYAHltaqeNITLALERVHGWSKSAARErslAL-LSQVGLadkarqmpaQLSGGQQQRVAIARALAS 176
Cdd:cd03369 80 LRSSLTIIPQDPTLFSG-----TIRSNLDPFDEYSDEEIYG---ALrVSEGGL---------NLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504650440 177 SPQIILFDEPTSALDPEMIGEVLQVMKTLaHSGITMVVVTHEMqfaREIA--DRVVFIDGGDILEVAPP 243
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREE-FTNSTILTIAHRL---RTIIdyDKILVMDAGEVKEYDHP 207
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
24-217 |
4.16e-23 |
|
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: 93.33 E-value: 4.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTGSALRQLrsrvg 103
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGL----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 104 fvfqqfnLY-AHLTAQENITLALERVHGWSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQIIL 182
Cdd:cd03231 76 -------LYlGHAPGIKTTLSVLENLRFWHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWI 148
|
170 180 190
....*....|....*....|....*....|....*
gi 504650440 183 FDEPTSALDPEMIGEVLQVMKTLAHSGITMVVVTH 217
Cdd:cd03231 149 LDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTH 183
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
24-217 |
9.76e-23 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 92.63 E-value: 9.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPtrqltgSALRQLRSRVG 103
Cdd:PRK13539 3 LEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGD------IDDPDVAEACH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 104 FVFQQFNLYAHLTAQENITLalervhgWSKSAARERS--LALLSQVGLADKArQMPAQ-LSGGQQQRVAIARALASSPQI 180
Cdd:PRK13539 77 YLGHRNAMKPALTVAENLEF-------WAAFLGGEELdiAAALEAVGLAPLA-HLPFGyLSAGQKRRVALARLLVSNRPI 148
|
170 180 190
....*....|....*....|....*....|....*..
gi 504650440 181 ILFDEPTSALDPEMIGEVLQVMKTLAHSGITMVVVTH 217
Cdd:PRK13539 149 WILDEPTAALDAAAVALFAELIRAHLAQGGIVIAATH 185
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
29-245 |
2.05e-22 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 95.86 E-value: 2.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 29 VAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTGSALRQL--------RS 100
Cdd:COG3845 264 SVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgvayipedRL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 101 RVGFVfqqfnlyAHLTAQENitLALERVH-------GW-SKSAARERSLALLSQ-----VGLADKARqmpaQLSGGQQQR 167
Cdd:COG3845 344 GRGLV-------PDMSVAEN--LILGRYRrppfsrgGFlDRKAIRAFAEELIEEfdvrtPGPDTPAR----SLSGGNQQK 410
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504650440 168 VAIARALASSPQIILFDEPTSALDPEMIGEVLQVMKTLAHSGITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAE 245
Cdd:COG3845 411 VILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRIVGEVPAAE 488
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
22-217 |
1.21e-21 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 94.10 E-value: 1.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 22 ASIEFRDVA-KSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEI----------------LIDG 84
Cdd:COG4178 361 GALALEDLTlRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIarpagarvlflpqrpyLPLG 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 85 ---------KPTRQLTGSALRQlrsrvgfVFQQFNLyAHLTAQenitlaLERVHGWSKsaarerslallsqvgladkarq 155
Cdd:COG4178 441 tlreallypATAEAFSDAELRE-------ALEAVGL-GHLAER------LDEEADWDQ---------------------- 484
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504650440 156 mpaQLSGGQQQRVAIARALASSPQIILFDEPTSALDPEMIGEVLQVMKTlAHSGITMVVVTH 217
Cdd:COG4178 485 ---VLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLRE-ELPGTTVISVGH 542
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
28-235 |
2.49e-21 |
|
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: 88.45 E-value: 2.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 28 DVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLS--GGEILIDGKPTRQltgsalrQLRSRVGFV 105
Cdd:cd03232 12 TVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGRPLDK-------NFQRSTGYV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 106 FQQFNLYAHLTAQENITLalervhgwskSAA-RErslallsqvgladkarqmpaqLSGGQQQRVAIARALASSPQIILFD 184
Cdd:cd03232 85 EQQDVHSPNLTVREALRF----------SALlRG---------------------LSVEQRKRLTIGVELAAKPSILFLD 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 504650440 185 EPTSALDPEMIGEVLQVMKTLAHSGITMVVVTHemQFAREIA---DRVVFIDGG 235
Cdd:cd03232 134 EPTSGLDSQAAYNIVRFLKKLADSGQAILCTIH--QPSASIFekfDRLLLLKRG 185
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
17-238 |
2.68e-21 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 91.72 E-value: 2.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 17 SHLQRASIEFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIrLINQLESLSGGEilidgKPTRQLTGSALR 96
Cdd:NF000106 7 SNGARNAVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGA-LPAHV*GPDAGR-----RPWRF*TWCANR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 97 Q-LRSRVGFVFQ-QFNLYAHLTAQENITLaLERVHGWSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARAL 174
Cdd:NF000106 81 RaLRRTIG*HRPvR*GRRESFSGRENLYM-IGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASM 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504650440 175 ASSPQIILFDEPTSALDPEMIGEVLQVMKTLAHSGITMVVVTHEMQFAREIADRVVFIDGGDIL 238
Cdd:NF000106 160 IGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVI 223
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
34-234 |
5.13e-21 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 88.97 E-value: 5.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 34 GDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLI--NQLESLSGGEILIDGK------PTRqltgsalrqlRSRVG-F 104
Cdd:COG0396 11 EGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmgHPKYEVTSGSILLDGEdilelsPDE----------RARAGiF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 105 V-FQQ---------FNLyahltaqenITLALERVHGWSKSAARERSLA--LLSQVGLADKA--RQMPAQLSGGQQQRVAI 170
Cdd:COG0396 81 LaFQYpveipgvsvSNF---------LRTALNARRGEELSAREFLKLLkeKMKELGLDEDFldRYVNEGFSGGEKKRNEI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504650440 171 ARALASSPQIILFDEPTSALDPEMIGEVLQVMKTLAHSGITMVVVTHEMQFAREI-ADRV-VFIDG 234
Cdd:COG0396 152 LQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITHYQRILDYIkPDFVhVLVDG 217
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
32-235 |
1.33e-20 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 91.17 E-value: 1.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 32 SYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGK---------PTRQLTGSALRQLRSRV 102
Cdd:PRK11147 12 SFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDlivarlqqdPPRNVEGTVYDFVAEGI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 103 GFVFQQFNLY---AHLTAQE----NIT-LA-----LERVHGWSKSAareRSLALLSQVGL-ADKARqmpAQLSGGQQQRV 168
Cdd:PRK11147 92 EEQAEYLKRYhdiSHLVETDpsekNLNeLAklqeqLDHHNLWQLEN---RINEVLAQLGLdPDAAL---SSLSGGWLRKA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504650440 169 AIARALASSPQIILFDEPTSALDPEMIGEVLQVMKTLAHSgitMVVVTHEMQFAREIADRVVFIDGG 235
Cdd:PRK11147 166 ALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGS---IIFISHDRSFIRNMATRIVDLDRG 229
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
42-235 |
1.58e-20 |
|
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: 91.23 E-value: 1.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 42 VNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRqltgSALRQLRSRVGFVFQQFNLYAHLTAQENI 121
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIE----TNLDAVRQSLGMCPQHNILFHHLTVAEHI 1024
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 122 tLALERVHGWSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQIILFDEPTSALDPEMIGEVLQV 201
Cdd:TIGR01257 1025 -LFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDL 1103
|
170 180 190
....*....|....*....|....*....|....
gi 504650440 202 MKTLaHSGITMVVVTHEMQFAREIADRVVFIDGG 235
Cdd:TIGR01257 1104 LLKY-RSGRTIIMSTHHMDEADLLGDRIAIISQG 1136
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
27-235 |
2.55e-20 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 89.79 E-value: 2.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 27 RDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRqlTGSALRQLRSRVGFVF 106
Cdd:PRK10982 2 SNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEID--FKSSKEALENGISMVH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 107 QQFNLYAHLTAQENITLALERVHGW--SKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQIILFD 184
Cdd:PRK10982 80 QELNLVLQRSVMDNMWLGRYPTKGMfvDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 504650440 185 EPTSALDPEMIGEVLQVMKTLAHSGITMVVVTHEMQFAREIADRVVFIDGG 235
Cdd:PRK10982 160 EPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDG 210
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
24-245 |
4.05e-20 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 89.80 E-value: 4.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPtrqLTGSALrQLRSRVG 103
Cdd:NF033858 267 IEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQP---VDAGDI-ATRRRVG 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 104 FVFQQFNLYAHLTAQENITL-AleRVHGWSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQIIL 182
Cdd:NF033858 343 YMSQAFSLYGELTVRQNLELhA--RLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLI 420
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504650440 183 FDEPTSALDPEMIGEVLQVMKTLA-HSGITMVVVTHEMQFArEIADRVVFIDGGDILEVAPPAE 245
Cdd:NF033858 421 LDEPTSGVDPVARDMFWRLLIELSrEDGVTIFISTHFMNEA-ERCDRISLMHAGRVLASDTPAA 483
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
42-245 |
6.86e-20 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 85.75 E-value: 6.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 42 VNLQVEPGEVVAILGPSGSGKSTLIRLINQLESlSGGEILIDGKPTRQLTGSALRQLR------SRVGF---VFQQFNLy 112
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQPLEAWSAAELARHRaylsqqQTPPFampVFQYLTL- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 113 aHLTAQENITLALERVHgwsksaarerslALLSQVGLADKARQMPAQLSGGQQQRVAIA-------RALASSPQIILFDE 185
Cdd:PRK03695 93 -HQPDKTRTEAVASALN------------EVAEALGLDDKLGRSVNQLSGGEWQRVRLAavvlqvwPDINPAGQLLLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 186 PTSALDPEMIGEVLQVMKTLAHSGITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAE 245
Cdd:PRK03695 160 PMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDE 219
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
28-236 |
6.93e-20 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 85.29 E-value: 6.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 28 DVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRqltgsalRQLRSR-VGFVF 106
Cdd:PRK13543 16 ALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTAT-------RGDRSRfMAYLG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 107 QQFNLYAHLTAQENITLaLERVHGWSKSAARERSLALlsqVGLADKARQMPAQLSGGQQQRVAIARALASSPQIILFDEP 186
Cdd:PRK13543 89 HLPGLKADLSTLENLHF-LCGLHGRRAKQMPGSALAI---VGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 504650440 187 TSALDPEMIGEVLQVMKTLAHSGITMVVVTHEMQFAREIADRVVFIDGGD 236
Cdd:PRK13543 165 YANLDLEGITLVNRMISAHLRGGGAALVTTHGAYAAPPVRTRMLTLEAAA 214
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
24-191 |
7.58e-20 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 85.94 E-value: 7.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEIlidgkptrqltgsaLRQLRSRVG 103
Cdd:PRK09544 5 VSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI--------------KRNGKLRIG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 104 FVFQQFNLYAHLtaqeniTLALERVHGWSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQIILF 183
Cdd:PRK09544 71 YVPQKLYLDTTL------PLTVNRFLRLRPGTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVL 144
|
....*...
gi 504650440 184 DEPTSALD 191
Cdd:PRK09544 145 DEPTQGVD 152
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
24-234 |
8.08e-20 |
|
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: 83.74 E-value: 8.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYGDHRVL-NGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEIlidGKPTRqltgsalrqlrSRV 102
Cdd:cd03223 1 IELENLSLATPDGRVLlKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI---GMPEG-----------EDL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 103 GFVFQQfnlyAHLTAQeniTLALERVHGWSKsaarerslallsqvgladkarqmpaQLSGGQQQRVAIARALASSPQIIL 182
Cdd:cd03223 67 LFLPQR----PYLPLG---TLREQLIYPWDD-------------------------VLSGGEQQRLAFARLLLHKPKFVF 114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 504650440 183 FDEPTSALDPEMIGEVLQVMKTLahsGITMVVVTHEMQFAReIADRVVFIDG 234
Cdd:cd03223 115 LDEATSALDEESEDRLYQLLKEL---GITVISVGHRPSLWK-FHDRVLDLDG 162
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
23-264 |
1.13e-19 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 86.78 E-value: 1.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 23 SIEFRdvaKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLE----SLSGGEILIDGKPTRQLTGSALRQL 98
Cdd:PRK15093 10 TIEFK---TSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTkdnwRVTADRMRFDDIDLLRLSPRERRKL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 99 -RSRVGFVFQQFNlyAHLTAQENITLAL-ERVHGWSKSAA--------RERSLALLSQVGLADKARQM---PAQLSGGQQ 165
Cdd:PRK15093 87 vGHNVSMIFQEPQ--SCLDPSERVGRQLmQNIPGWTYKGRwwqrfgwrKRRAIELLHRVGIKDHKDAMrsfPYELTEGEC 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 166 QRVAIARALASSPQIILFDEPTSALDPEMIGEVLQVMKTL-AHSGITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPA 244
Cdd:PRK15093 165 QKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLnQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSK 244
|
250 260
....*....|....*....|
gi 504650440 245 EFFARPQHARTRRFLQKVLD 264
Cdd:PRK15093 245 ELVTTPHHPYTQALIRAIPD 264
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
23-245 |
1.34e-19 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 88.26 E-value: 1.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 23 SIEFRDVAKSYGDH--RVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLtgsALRQLRS 100
Cdd:PLN03130 1237 SIKFEDVVLRYRPElpPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKF---GLMDLRK 1313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 101 RVGFVFQ---------QFNL---YAHLTAqeNITLALERVHgwSKSAARERSLALLSQVGLADKarqmpaQLSGGQQQRV 168
Cdd:PLN03130 1314 VLGIIPQapvlfsgtvRFNLdpfNEHNDA--DLWESLERAH--LKDVIRRNSLGLDAEVSEAGE------NFSVGQRQLL 1383
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504650440 169 AIARALASSPQIILFDEPTSALDpemIGEVLQVMKTLAHS--GITMVVVTHEMQFAREiADRVVFIDGGDILEVAPPAE 245
Cdd:PLN03130 1384 SLARALLRRSKILVLDEATAAVD---VRTDALIQKTIREEfkSCTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPEN 1458
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
36-264 |
2.25e-19 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 84.88 E-value: 2.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 36 HRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSG--------GEILIDGKPTRQLTGSALRQLR------SR 101
Cdd:PRK13547 14 RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGaprgarvtGDVTLNGEPLAAIDAPRLARLRavlpqaAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 102 VGFVFqqfnlyahlTAQENITLAL---ERVHGWSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALA--- 175
Cdd:PRK13547 94 PAFAF---------SAREIVLLGRyphARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAqlw 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 176 ------SSPQIILFDEPTSALDPEMIGEVLQVMKTLA---HSGITMVVvtHEMQFAREIADRVVFIDGGDILEVAPPAEF 246
Cdd:PRK13547 165 pphdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLArdwNLGVLAIV--HDPNLAARHADRIAMLADGAIVAHGAPADV 242
|
250
....*....|....*....
gi 504650440 247 FaRPQH-ARTRRFLQKVLD 264
Cdd:PRK13547 243 L-TPAHiARCYGFAVRLVD 260
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
39-234 |
2.86e-19 |
|
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: 84.38 E-value: 2.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 39 LNGVNLQVEPG-----EVVAILGPSGSGKSTLIRLINQLESLSGGEILIDG-----KP---TRQLTGSALRQLRSRVGfv 105
Cdd:cd03237 10 LGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELdtvsyKPqyiKADYEGTVRDLLSSITK-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 106 fqqfNLYAHLTAQENIT--LALERVHgwsksaarerslallsqvgladkARQMPaQLSGGQQQRVAIARALASSPQIILF 183
Cdd:cd03237 88 ----DFYTHPYFKTEIAkpLQIEQIL-----------------------DREVP-ELSGGELQRVAIAACLSKDADIYLL 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 504650440 184 DEPTSALDPEMIGEVLQVMKTLA-HSGITMVVVTHEMQFAREIADRVVFIDG 234
Cdd:cd03237 140 DEPSAYLDVEQRLMASKVIRRFAeNNEKTAFVVEHDIIMIDYLADRLIVFEG 191
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
2-244 |
3.59e-19 |
|
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: 86.78 E-value: 3.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 2 LSALFSRSAASSADFSHLQRASIEFRDVAKSY----GDHR-VLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLS 76
Cdd:COG4615 306 LAAAEPAAADAAAPPAPADFQTLELRGVTYRYpgedGDEGfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPE 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 77 GGEILIDGKPtrqLTGSALRQLRSRVGFVFQQFnlyaHLTaqenitlalERVHGWSKSAARERSLALLSQVGLADK---- 152
Cdd:COG4615 386 SGEILLDGQP---VTADNREAYRQLFSAVFSDF----HLF---------DRLLGLDGEADPARARELLERLELDHKvsve 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 153 -ARQMPAQLSGGQQQRVAIARALASSPQIILFDEPTSALDPEM----IGEVLQVMKTLahsGITMVVVTHEMQFArEIAD 227
Cdd:COG4615 450 dGRFSTTDLSQGQRKRLALLVALLEDRPILVFDEWAADQDPEFrrvfYTELLPELKAR---GKTVIAISHDDRYF-DLAD 525
|
250
....*....|....*..
gi 504650440 228 RVVFIDGGDILEVAPPA 244
Cdd:COG4615 526 RVLKMDYGKLVELTGPA 542
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
37-264 |
5.12e-19 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 84.96 E-value: 5.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 37 RVLNGVNLQVEPGEVVAILGPSGSGKS----TLIRLINQLESLSGGEILIDGKPTRQLTGSALRQLRSR-VGFVFQqfNL 111
Cdd:COG4170 21 KAVDRVSLTLNEGEIRGLVGESGSGKSliakAICGITKDNWHVTADRFRWNGIDLLKLSPRERRKIIGReIAMIFQ--EP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 112 YAHLTAQENITLALERV--------HGWSKSAAR-ERSLALLSQVGLADKARQM---PAQLSGGQQQRVAIARALASSPQ 179
Cdd:COG4170 99 SSCLDPSAKIGDQLIEAipswtfkgKWWQRFKWRkKRAIELLHRVGIKDHKDIMnsyPHELTEGECQKVMIAMAIANQPR 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 180 IILFDEPTSALDPEMIGEVLQVMKTLAH-SGITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAEFFARPQHARTRRF 258
Cdd:COG4170 179 LLIADEPTNAMESTTQAQIFRLLARLNQlQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKSPHHPYTKAL 258
|
....*.
gi 504650440 259 LQKVLD 264
Cdd:COG4170 259 LRSMPD 264
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
36-246 |
5.83e-19 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 86.12 E-value: 5.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 36 HRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTR-QLTGSALRQlrsrvGFVF-----QQF 109
Cdd:PRK11288 266 PGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDiRSPRDAIRA-----GIMLcpedrKAE 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 110 NLYAHLTAQENITLALERVH---GWSKSAARERSLALLSQVGLADK---ARQMPAQLSGGQQQRVAIARALASSPQIILF 183
Cdd:PRK11288 341 GIIPVHSVADNINISARRHHlraGCLINNRWEAENADRFIRSLNIKtpsREQLIMNLSGGNQQKAILGRWLSEDMKVILL 420
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504650440 184 DEPTSALDPEMIGEVLQVMKTLAHSGITMVVVTHEMQFAREIADRVVFIDGGDILEVAPPAEF 246
Cdd:PRK11288 421 DEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIAGELAREQA 483
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
24-237 |
1.28e-18 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 85.07 E-value: 1.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLI--NQLESLSGGEILIdGKptRQLTGSALRQLRSR 101
Cdd:PRK10938 261 IVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLItgDHPQGYSNDLTLF-GR--RRGSGETIWDIKKH 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 102 VGFVFQQFNL-YAHLTAQENITLAlervhGWSKS-------AARERSLAL--LSQVGLADKARQMPAQ-LSGGQQQRVAI 170
Cdd:PRK10938 338 IGYVSSSLHLdYRVSTSVRNVILS-----GFFDSigiyqavSDRQQKLAQqwLDILGIDKRTADAPFHsLSWGQQRLALI 412
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504650440 171 ARALASSPQIILFDEPTSALDP---EMIGEVLQVMktLAHSGITMVVVTHEMQFARE-IADRVVFIDGGDI 237
Cdd:PRK10938 413 VRALVKHPTLLILDEPLQGLDPlnrQLVRRFVDVL--ISEGETQLLFVSHHAEDAPAcITHRLEFVPDGDI 481
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
31-235 |
1.32e-18 |
|
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: 81.54 E-value: 1.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 31 KSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLI-NQLESLSG--GEILIDGKPTRQltgsALRQLRSRVGFVFQ 107
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALaNRTEGNVSveGDIHYNGIPYKE----FAEKYPGEIIYVSE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 108 QFNLYAHLTAQENITLALERvhgwsksaarerslallsqvgladKARQMPAQLSGGQQQRVAIARALASSPQIILFDEPT 187
Cdd:cd03233 91 EDVHFPTLTVRETLDFALRC------------------------KGNEFVRGISGGERKRVSIAEALVSRASVLCWDNST 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 504650440 188 SALDPEMIGEVLQVMKTLAHS--GITMVVVTHEMQFAREIADRVVFIDGG 235
Cdd:cd03233 147 RGLDSSTALEILKCIRTMADVlkTTTFVSLYQASDEIYDLFDKVLVLYEG 196
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
21-256 |
2.90e-18 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 84.64 E-value: 2.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 21 RASIEFRDVAKSY--GDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKptrQLTGSALRQL 98
Cdd:PLN03232 1232 RGSIKFEDVHLRYrpGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDC---DVAKFGLTDL 1308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 99 RSRVGFVFQQFNLYAHlTAQENIT-----------LALERVHgwSKSAARERSLALLSQVGLADKarqmpaQLSGGQQQR 167
Cdd:PLN03232 1309 RRVLSIIPQSPVLFSG-TVRFNIDpfsehndadlwEALERAH--IKDVIDRNPFGLDAEVSEGGE------NFSVGQRQL 1379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 168 VAIARALASSPQIILFDEPTSALDPEMIGEVLQVMKTLAHSgITMVVVTHEMQFAREiADRVVFIDGGDILEVAPPAEFF 247
Cdd:PLN03232 1380 LSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKS-CTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELL 1457
|
....*....
gi 504650440 248 ARPQHARTR 256
Cdd:PLN03232 1458 SRDTSAFFR 1466
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
32-239 |
8.14e-18 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 83.25 E-value: 8.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 32 SYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIR-LINQLESLSGGEILIdgkptrqltgsalrqlRSRVGFVFQQ-- 108
Cdd:PLN03130 626 SKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVI----------------RGTVAYVPQVsw 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 109 -FNLyahlTAQENITLAL----ERVHGWSKSAARERSLALLSQVGLADKARQmPAQLSGGQQQRVAIARALASSPQIILF 183
Cdd:PLN03130 690 iFNA----TVRDNILFGSpfdpERYERAIDVTALQHDLDLLPGGDLTEIGER-GVNISGGQKQRVSMARAVYSNSDVYIF 764
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 504650440 184 DEPTSALDPEMIGEVLQVMKTLAHSGITMVVVTHEMQFAREIaDRVVFIDGGDILE 239
Cdd:PLN03130 765 DDPLSALDAHVGRQVFDKCIKDELRGKTRVLVTNQLHFLSQV-DRIILVHEGMIKE 819
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
34-249 |
8.51e-18 |
|
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: 83.07 E-value: 8.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 34 GDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIR-LINQLESLSGGEilidgkptrqltgsalrQLRSRVGFVFQQFNLy 112
Cdd:TIGR00957 649 DLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDKVEGHV-----------------HMKGSVAYVPQQAWI- 710
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 113 AHLTAQENITLALERVHGWSKSAARerSLALLSQVGLADKARQMP-----AQLSGGQQQRVAIARALASSPQIILFDEPT 187
Cdd:TIGR00957 711 QNDSLRENILFGKALNEKYYQQVLE--ACALLPDLEILPSGDRTEigekgVNLSGGQKQRVSLARAVYSNADIYLFDDPL 788
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504650440 188 SALDP----EMIGEVLQVMKTLAhsGITMVVVTHEMQFAREIaDRVVFIDGGDILEVAPPAEFFAR 249
Cdd:TIGR00957 789 SAVDAhvgkHIFEHVIGPEGVLK--NKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLQR 851
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
35-250 |
1.10e-17 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 82.45 E-value: 1.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 35 DHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLtgsALRQLRSRVGFVFQQFNLYAH 114
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKL---QLDSWRSRLAVVSQTPFLFSD 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 115 LTAQeNITLA--------LERVhgwSKSAARERSLALLSQvGLADKARQMPAQLSGGQQQRVAIARALASSPQIILFDEP 186
Cdd:PRK10789 404 TVAN-NIALGrpdatqqeIEHV---ARLASVHDDILRLPQ-GYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDA 478
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504650440 187 TSALDPEMIGEVLQVMKTLAHsGITMVVVTHEMQFAREiADRVVFIDGGDILEVAPPAEFFARP 250
Cdd:PRK10789 479 LSAVDGRTEHQILHNLRQWGE-GRTVIISAHRLSALTE-ASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
35-240 |
1.98e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 81.37 E-value: 1.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 35 DHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKptRQLTGSALRQLRSRVGFVFQ---QFNL 111
Cdd:PRK09700 275 DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGK--DISPRSPLDAVKKGMAYITEsrrDNGF 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 112 YAHLTAQENITLALERVHGWSKSA------ARERSLALLSQVGLADKA---RQMPAQLSGGQQQRVAIARALASSPQIIL 182
Cdd:PRK09700 353 FPNFSIAQNMAISRSLKDGGYKGAmglfheVDEQRTAENQRELLALKChsvNQNITELSGGNQQKVLISKWLCCCPEVII 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 504650440 183 FDEPTSALDPEMIGEVLQVMKTLAHSGITMVVVTHEMQFAREIADRVVFIDGGDILEV 240
Cdd:PRK09700 433 FDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
20-248 |
6.63e-17 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 80.37 E-value: 6.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 20 QRASIEFRDVAKSY--GDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLtgsALRQ 97
Cdd:TIGR00957 1281 PRGRVEFRNYCLRYreDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKI---GLHD 1357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 98 LRSRVGFVFQQFNLYA----------HLTAQENITLALERVHGWSKSAARERslallsqvGLADKARQMPAQLSGGQQQR 167
Cdd:TIGR00957 1358 LRFKITIIPQDPVLFSgslrmnldpfSQYSDEEVWWALELAHLKTFVSALPD--------KLDHECAEGGENLSVGQRQL 1429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 168 VAIARALASSPQIILFDEPTSALDPEMIGEVLQVMKTlAHSGITMVVVTHEMQfarEIAD--RVVFIDGGDILEVAPPAE 245
Cdd:TIGR00957 1430 VCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRT-QFEDCTVLTIAHRLN---TIMDytRVIVLDKGEVAEFGAPSN 1505
|
...
gi 504650440 246 FFA 248
Cdd:TIGR00957 1506 LLQ 1508
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
39-237 |
6.84e-17 |
|
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: 79.87 E-value: 6.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 39 LNGVNLQVEPGEVVAILGPSGSGKSTLIR-LINQLESLSGGEILIDGKPTRqlTGSALRQLRSRVGFV---FQQFNLYAH 114
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQaLFGAYPGKFEGNVFINGKPVD--IRNPAQAIRAGIAMVpedRKRHGIVPI 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 115 LTAQENITLA-LERVHGWSK--SAARERSL-ALLSQVGLADKARQMP-AQLSGGQQQRVAIARALASSPQIILFDEPTSA 189
Cdd:TIGR02633 354 LGVGKNITLSvLKSFCFKMRidAAAELQIIgSAIQRLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRG 433
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 504650440 190 LDPEMIGEVLQVMKTLAHSGITMVVVTHEMQFAREIADRVVFIDGGDI 237
Cdd:TIGR02633 434 VDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
37-237 |
7.78e-17 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 79.59 E-value: 7.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 37 RVLNGVNLQVEPGEVVAILGPSGSGKSTLIrlinqlESLSG-------GEILIDGKPTRQLTGS-ALRQL-------RSR 101
Cdd:PRK13549 276 KRVDDVSFSLRRGEILGIAGLVGAGRTELV------QCLFGaypgrweGEIFIDGKPVKIRNPQqAIAQGiamvpedRKR 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 102 VGFVFQqfnlyahLTAQENITLA-LERVHGWSK-SAARERSLALLSQVGLADKA---RQMPAQLSGGQQQRVAIARALAS 176
Cdd:PRK13549 350 DGIVPV-------MGVGKNITLAaLDRFTGGSRiDDAAELKTILESIQRLKVKTaspELAIARLSGGNQQKAVLAKCLLL 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504650440 177 SPQIILFDEPTSALDpemIG---EVLQVMKTLAHSGITMVVVTHEMQFAREIADRVVFIDGGDI 237
Cdd:PRK13549 423 NPKILILDEPTRGID---VGakyEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
19-251 |
1.89e-16 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 79.05 E-value: 1.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 19 LQRASIEFRDVAKSY--GDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGkptRQLTGSALR 96
Cdd:PTZ00243 1304 VQAGSLVFEGVQMRYreGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNG---REIGAYGLR 1380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 97 QLRSRVGFVFQQFNLYAHlTAQENITLALErvhgwsksAARERSLALLSQVGLadkaRQMPAQLSG-------------- 162
Cdd:PTZ00243 1381 ELRRQFSMIPQDPVLFDG-TVRQNVDPFLE--------ASSAEVWAALELVGL----RERVASESEgidsrvleggsnys 1447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 163 -GQQQRVAIARA-LASSPQIILFDEPTSALDPEMIGEVlQVMKTLAHSGITMVVVTHEMQFAREIaDRVVFIDGGDILEV 240
Cdd:PTZ00243 1448 vGQRQLMCMARAlLKKGSGFILMDEATANIDPALDRQI-QATVMSAFSAYTVITIAHRLHTVAQY-DKIIVMDHGAVAEM 1525
|
250
....*....|.
gi 504650440 241 APPAEFFARPQ 251
Cdd:PTZ00243 1526 GSPRELVMNRQ 1536
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
39-221 |
2.07e-16 |
|
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: 75.83 E-value: 2.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 39 LNGVNLQVEPGEVVAILGPSGSGKSTLI-RLINQLESLSGGEILIDGKPTRQLTGSALRQLRSRVGFVFQQFNLYaHLTA 117
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPWLL-NATV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 118 QENITLAL----ERVHGWSKSAARERSLALL---SQVGLADKArqmpAQLSGGQQQRVAIARALASSPQIILFDEPTSAL 190
Cdd:cd03290 96 EENITFGSpfnkQRYKAVTDACSLQPDIDLLpfgDQTEIGERG----INLSGGQRQRICVARALYQNTNIVFLDDPFSAL 171
|
170 180 190
....*....|....*....|....*....|...
gi 504650440 191 DPEMIGEVLQ--VMKTLAHSGITMVVVTHEMQF 221
Cdd:cd03290 172 DIHLSDHLMQegILKFLQDDKRTLVLVTHKLQY 204
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
24-249 |
2.20e-16 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 78.63 E-value: 2.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQltGSALRQLRSRVG 103
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMAD--ARHRRAVCPRIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 104 FVFQQF--NLYAHLTAQENITLaLERVHGWSKSAARERSLALLSQVGLAD-KARqmPA-QLSGGQQQRVAIARALASSPQ 179
Cdd:NF033858 80 YMPQGLgkNLYPTLSVFENLDF-FGRLFGQDAAERRRRIDELLRATGLAPfADR--PAgKLSGGMKQKLGLCCALIHDPD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504650440 180 IILFDEPTSALDP-------EMIGEVLQvmktlAHSGITMVVVTHEMQFArEIADRVVFIDGGDILEVAPPAEFFAR 249
Cdd:NF033858 157 LLILDEPTTGVDPlsrrqfwELIDRIRA-----ERPGMSVLVATAYMEEA-ERFDWLVAMDAGRVLATGTPAELLAR 227
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
19-237 |
5.39e-16 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 77.24 E-value: 5.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 19 LQRASIEFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIR-LINQLESLSGgeilidgkpTRQLTGSAlrq 97
Cdd:PRK15064 315 LHRNALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRtLVGELEPDSG---------TVKWSENA--- 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 98 lrsRVGFvfqqfnlYAHLTAQE---NITLaLERVHGWSKSAARERSL------ALLSQvglaDKARQMPAQLSGGQQQRV 168
Cdd:PRK15064 383 ---NIGY-------YAQDHAYDfenDLTL-FDWMSQWRQEGDDEQAVrgtlgrLLFSQ----DDIKKSVKVLSGGEKGRM 447
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504650440 169 AIARALASSPQIILFDEPTSALDPEMIgEVLQvMKTLAHSGiTMVVVTHEMQFAREIADRVVFIDGGDI 237
Cdd:PRK15064 448 LFGKLMMQKPNVLVMDEPTNHMDMESI-ESLN-MALEKYEG-TLIFVSHDREFVSSLATRIIEITPDGV 513
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
24-234 |
5.77e-16 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 77.16 E-value: 5.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYGDHRvlngvnLQVEPG-----EVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGK------------- 85
Cdd:PRK13409 341 VEYPDLTKKLGDFS------LEVEGGeiyegEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKisykpqyikpdyd 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 86 -PTRQLTGSALRQLRSrvgfvfqqfNLYahltaQENIT--LALERVHgwsksaarERSLAllsqvgladkarqmpaQLSG 162
Cdd:PRK13409 415 gTVEDLLRSITDDLGS---------SYY-----KSEIIkpLQLERLL--------DKNVK----------------DLSG 456
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504650440 163 GQQQRVAIARALASSPQIILFDEPTSALDPEmigEVLQVMKTLAH----SGITMVVVTHEMQFAREIADRVVFIDG 234
Cdd:PRK13409 457 GELQRVAIAACLSRDADLYLLDEPSAHLDVE---QRLAVAKAIRRiaeeREATALVVDHDIYMIDYISDRLMVFEG 529
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
24-234 |
7.79e-16 |
|
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: 76.90 E-value: 7.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIdgkptrqltGSALrqlrsRVG 103
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI---------GETV-----KLA 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 104 FVFQQF-NLYAHLTAQENITLALERVhgwsKSAARE-RSLALLSQVGLADKARQMPA-QLSGGQQQRVAIARALASSPQI 180
Cdd:TIGR03719 389 YVDQSRdALDPNKTVWEEISGGLDII----KLGKREiPSRAYVGRFNFKGSDQQKKVgQLSGGERNRVHLAKTLKSGGNV 464
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504650440 181 ILFDEPTSALDPEMIGEVLQVMktLAHSGITMV----------VVTHEMQFarEIADRVVFIDG 234
Cdd:TIGR03719 465 LLLDEPTNDLDVETLRALEEAL--LNFAGCAVVishdrwfldrIATHILAF--EGDSHVEWFEG 524
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
24-234 |
8.00e-16 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 76.75 E-value: 8.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYGDHRvlngvnLQVEPG-----EVVAILGPSGSGKSTLIRLInqleslsGGEIlidgKPTrqlTGSALRQL 98
Cdd:COG1245 342 VEYPDLTKSYGGFS------LEVEGGeiregEVLGIVGPNGIGKTTFAKIL-------AGVL----KPD---EGEVDEDL 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 99 RsrVGFVFQ----------QFNLYAHLTA-------QENIT--LALERVHgwsksaarERSLAllsqvgladkarqmpaQ 159
Cdd:COG1245 402 K--ISYKPQyispdydgtvEEFLRSANTDdfgssyyKTEIIkpLGLEKLL--------DKNVK----------------D 455
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504650440 160 LSGGQQQRVAIARALASSPQIILFDEPTSALDPEMIGEVLQVMKTLAHS-GITMVVVTHEMQFAREIADRVVFIDG 234
Cdd:COG1245 456 LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENrGKTAMVVDHDIYLIDYISDRLMVFEG 531
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
29-235 |
1.51e-15 |
|
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: 76.13 E-value: 1.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 29 VAKSYGDHR-VLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEilidgkptrqltgsALRQLRSRVGFVFQ 107
Cdd:TIGR03719 10 VSKVVPPKKeILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGE--------------ARPQPGIKVGYLPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 108 QFNLYAHLTAQENITLALERVHG------------------WSKSAARERSLA----------LLSQVGLADKARQMP-- 157
Cdd:TIGR03719 76 EPQLDPTKTVRENVEEGVAEIKDaldrfneisakyaepdadFDKLAAEQAELQeiidaadawdLDSQLEIAMDALRCPpw 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 158 ----AQLSGGQQQRVAIARALASSPQIILFDEPTSALDPEMIGEVLQVMKTlaHSGiTMVVVTHEMQFAREIADRVVFID 233
Cdd:TIGR03719 156 dadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQE--YPG-TVVAVTHDRYFLDNVAGWILELD 232
|
..
gi 504650440 234 GG 235
Cdd:TIGR03719 233 RG 234
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
24-220 |
1.63e-15 |
|
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: 74.51 E-value: 1.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSY--GDHRVLNGVNLQVEPGEVVAILGPSGSGKSTL----IRLINqleslSGGEILIDGKPTRQLTgsaLRQ 97
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLlsafLRLLN-----TEGDIQIDGVSWNSVP---LQK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 98 LRSRVGFVFQQFNLYAHlTAQENitlaLERVHGWSKsaarERSLALLSQVGLADKARQMPAQL-----------SGGQQQ 166
Cdd:cd03289 75 WRKAFGVIPQKVFIFSG-TFRKN----LDPYGKWSD----EEIWKVAEEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQ 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 504650440 167 RVAIARALASSPQIILFDEPTSALDPEMIGEVLQVMKTlAHSGITMVVVTHEMQ 220
Cdd:cd03289 146 LMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQ-AFADCTVILSEHRIE 198
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
36-240 |
2.30e-15 |
|
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: 71.97 E-value: 2.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 36 HRVLNGVNLQVEPGEVVAILGPSGSGKSTLIrliNQLESLSGGEILIDGKPTrqltgsalrqlrsrvgfvfqqfnlyahl 115
Cdd:cd03238 8 VHNLQNLDVSIPLNVLVVVTGVSGSGKSTLV---NEGLYASGKARLISFLPK---------------------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 116 tAQENITLALErvhgwsksaarerSLALLSQVGLADKARQMPAQ-LSGGQQQRVAIARALASSPQ--IILFDEPTSALDP 192
Cdd:cd03238 57 -FSRNKLIFID-------------QLQFLIDVGLGYLTLGQKLStLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQ 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 504650440 193 EMIGEVLQVMKTLAHSGITMVVVTHEMQFAREiADRVVFI------DGGDILEV 240
Cdd:cd03238 123 QDINQLLEVIKGLIDLGNTVILIEHNLDVLSS-ADWIIDFgpgsgkSGGKVVFS 175
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
39-247 |
8.19e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 74.24 E-value: 8.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 39 LNGVNLQVEPGEVVAILGPSGSGKSTLIRLInqLESLSGGEilidgkptrqltgSALRQLRSRVGFVfQQFNLYAHLTAQ 118
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAM--LGELSHAE-------------TSSVVIRGSVAYV-PQVSWIFNATVR 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 119 ENITLA--LERVHGWS--KSAARERSLALLSQVGLADKARQmPAQLSGGQQQRVAIARALASSPQIILFDEPTSALDPEM 194
Cdd:PLN03232 697 ENILFGsdFESERYWRaiDVTALQHDLDLLPGRDLTEIGER-GVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHV 775
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 504650440 195 IGEVLQVMKTLAHSGITMVVVTHEMQFAREIaDRVVFIDGGDILEVAPPAEFF 247
Cdd:PLN03232 776 AHQVFDSCMKDELKGKTRVLVTNQLHFLPLM-DRIILVSEGMIKEEGTFAELS 827
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
24-193 |
1.48e-14 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 73.23 E-value: 1.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYGDhRVL-NGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIdGkPTRQLtgSALRQLRSrv 102
Cdd:PRK11819 325 IEAENLSKSFGD-RLLiDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-G-ETVKL--AYVDQSRD-- 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 103 gfvfqqfNLYAHLTAQENITLALERVhgwsKSAARE-RSLALLSQVGLADKARQMPA-QLSGGQQQRVAIARALASSPQI 180
Cdd:PRK11819 398 -------ALDPNKTVWEEISGGLDII----KVGNREiPSRAYVGRFNFKGGDQQKKVgVLSGGERNRLHLAKTLKQGGNV 466
|
170
....*....|...
gi 504650440 181 ILFDEPTSALDPE 193
Cdd:PRK11819 467 LLLDEPTNDLDVE 479
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
38-220 |
1.64e-14 |
|
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: 73.41 E-value: 1.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 38 VLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESlSGGEILIDGKPTRQLTgsaLRQLRSRVGFVFQQFNLYAHlTA 117
Cdd:TIGR01271 1234 VLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVT---LQTWRKAFGVIPQKVFIFSG-TF 1308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 118 QENitlaLERVHGWSKsaarERSLALLSQVGLADKARQMPAQL-----------SGGQQQRVAIARALASSPQIILFDEP 186
Cdd:TIGR01271 1309 RKN----LDPYEQWSD----EEIWKVAEEVGLKSVIEQFPDKLdfvlvdggyvlSNGHKQLMCLARSILSKAKILLLDEP 1380
|
170 180 190
....*....|....*....|....*....|....*..
gi 504650440 187 TSALDPemigEVLQVM-KTLAH--SGITMVVVTHEMQ 220
Cdd:TIGR01271 1381 SAHLDP----VTLQIIrKTLKQsfSNCTVILSEHRVE 1413
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
42-237 |
2.84e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 72.01 E-value: 2.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 42 VNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQL-TGSALRQlrsrvGFVF-----QQFNLYAHL 115
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALsTAQRLAR-----GLVYlpedrQSSGLYLDA 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 116 TAQENITLALERVHGWSKSAARERslALLSQVGLA-----DKARQMPAQLSGGQQQRVAIARALASSPQIILFDEPTSAL 190
Cdd:PRK15439 357 PLAWNVCALTHNRRGFWIKPAREN--AVLERYRRAlnikfNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGV 434
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 504650440 191 DPEMIGEVLQVMKTLAHSGITMVVVTHEMQFAREIADRVVFIDGGDI 237
Cdd:PRK15439 435 DVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
24-217 |
3.15e-14 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 70.44 E-value: 3.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLI--NQLESLSGGEILIDGKPTRQLTGsalrQLRSR 101
Cdd:CHL00131 8 LEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIagHPAYKILEGDILFKGESILDLEP----EERAH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 102 VGfVFQQFNLYAHLTAQENIT---LALErvhgwsksaARERSLAL---------------LSQVGLADK--ARQMPAQLS 161
Cdd:CHL00131 84 LG-IFLAFQYPIEIPGVSNADflrLAYN---------SKRKFQGLpeldplefleiinekLKLVGMDPSflSRNVNEGFS 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 504650440 162 GGQQQRVAIARALASSPQIILFDEPTSALDPEMIGEVLQVMKTLAHSGITMVVVTH 217
Cdd:CHL00131 154 GGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITH 209
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
46-235 |
3.57e-14 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 72.35 E-value: 3.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 46 VEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRqltgSALRQLRSRVGFVFQQFNLYAHLTAQENITL-- 123
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIL----TNISDVHQNMGYCPQFDAIDDLLTGREHLYLya 2037
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 124 --------ALERVHGWSksaarerslalLSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQIILFDEPTSALDPEMI 195
Cdd:TIGR01257 2038 rlrgvpaeEIEKVANWS-----------IQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQAR 2106
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 504650440 196 GEVLQVMKTLAHSGITMVVVTHEMQFAREIADRVVFIDGG 235
Cdd:TIGR01257 2107 RMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
28-218 |
4.40e-14 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 72.06 E-value: 4.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 28 DVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLES---LSGGEILIDGKPtrqLTGSALRqlrsRVGF 104
Cdd:TIGR00956 768 EVKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTtgvITGGDRLVNGRP---LDSSFQR----SIGY 840
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 105 VFQQFNLYAHLTAQENITLA--LERVHGWSKSAAR---ERSLALLSQVGLADKARQMPAQ-LSGGQQQRVAIARALASSP 178
Cdd:TIGR00956 841 VQQQDLHLPTSTVRESLRFSayLRQPKSVSKSEKMeyvEEVIKLLEMESYADAVVGVPGEgLNVEQRKRLTIGVELVAKP 920
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 504650440 179 QIILF-DEPTSALDPEMIGEVLQVMKTLAHSGITMVVVTHE 218
Cdd:TIGR00956 921 KLLLFlDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQ 961
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
37-265 |
7.55e-14 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 71.29 E-value: 7.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 37 RVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLI----NQLESLSGGEILIDGKPTRQLtgsaLRQLRSRVGFVFQQFNLY 112
Cdd:TIGR00956 75 DILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIasntDGFHIGVEGVITYDGITPEEI----KKHYRGDVVYNAETDVHF 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 113 AHLTAQENITLALE------RVHGWSKS--AARERSLAL----LSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQI 180
Cdd:TIGR00956 151 PHLTVGETLDFAARcktpqnRPDGVSREeyAKHIADVYMatygLSHTRNTKVGNDFVRGVSGGERKRVSIAEASLGGAKI 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 181 ILFDEPTSALDPEMIGEVLQVMKTLAHSGITMVVVT--HEMQFAREIADRVVFIDGGDILEVAP---PAEFFAR-----P 250
Cdd:TIGR00956 231 QCWDNATRGLDSATALEFIRALKTSANILDTTPLVAiyQCSQDAYELFDKVIVLYEGYQIYFGPadkAKQYFEKmgfkcP 310
|
250
....*....|....*
gi 504650440 251 QHARTRRFLQKVLDP 265
Cdd:TIGR00956 311 DRQTTADFLTSLTSP 325
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
38-217 |
2.47e-13 |
|
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: 69.39 E-value: 2.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 38 VLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGK------PTRQLTGsaLRQLRSRVGF---VFQQ 108
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKgklfyvPQRPYMT--LGTLRDQIIYpdsSEDM 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 109 F-------NLYAHLtaqENITLA--LERVHGWSksaarerSLALLSQVgladkarqmpaqLSGGQQQRVAIARALASSPQ 179
Cdd:TIGR00954 545 KrrglsdkDLEQIL---DNVQLThiLEREGGWS-------AVQDWMDV------------LSGGEKQRIAMARLFYHKPQ 602
|
170 180 190
....*....|....*....|....*....|....*...
gi 504650440 180 IILFDEPTSALDPEMIGEVLQVMKTLahsGITMVVVTH 217
Cdd:TIGR00954 603 FAILDECTSAVSVDVEGYMYRLCREF---GITLFSVSH 637
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
24-217 |
5.69e-13 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 66.74 E-value: 5.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLE--SLSGGEILIDGKPTRQLTGSAlrqlRSR 101
Cdd:PRK09580 2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPED----RAG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 102 VGfVFQQFNLYAHLTAQEN---ITLALERVHGWSKSAARERslaLLSQVGLADKAR--QMPAQL---------SGGQQQR 167
Cdd:PRK09580 78 EG-IFMAFQYPVEIPGVSNqffLQTALNAVRSYRGQEPLDR---FDFQDLMEEKIAllKMPEDLltrsvnvgfSGGEKKR 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 504650440 168 VAIARALASSPQIILFDEPTSALDPEMIGEVLQVMKTLAHSGITMVVVTH 217
Cdd:PRK09580 154 NDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTH 203
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
48-236 |
8.04e-13 |
|
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: 64.32 E-value: 8.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 48 PGEVVAILGPSGSGKSTLIRLI-NQLESLSGGEILIDGKPTRQLTGSALRQLRSRVGfvfqqfnlyahltaqenitlale 126
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALaRELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGK----------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 127 rvhgwsksaarerslallsqvgladkarqmPAQLSGGQQQRVAIARALASSPQIILFDEPTSALDPEMIGEVLQ------ 200
Cdd:smart00382 58 ------------------------------KASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLleelrl 107
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 504650440 201 VMKTLAHSGITMVVVTHEMQF-----AREIADRVVFIDGGD 236
Cdd:smart00382 108 LLLLKSEKNLTVILTTNDEKDlgpalLRRRFDRRIVLLLIL 148
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
47-219 |
9.99e-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: 67.50 E-value: 9.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 47 EPGEVVAILGPSGSGKSTLIRLinqlesLSGGEI----LIDGKPT-----RQLTGSALrqlrsrvgfvfqqfnlYAHLT- 116
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKI------LSGELKpnlgDYDEEPSwdevlKRFRGTEL----------------QDYFKk 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 117 -AQENITLAL---------ERVHGWSK---SAARERSLA--LLSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQII 181
Cdd:COG1245 155 lANGEIKVAHkpqyvdlipKVFKGTVRellEKVDERGKLdeLAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFY 234
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 504650440 182 LFDEPTSALDpemIGE---VLQVMKTLAHSGITMVVVTHEM 219
Cdd:COG1245 235 FFDEPSSYLD---IYQrlnVARLIRELAEEGKYVLVVEHDL 272
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
24-191 |
2.37e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 66.98 E-value: 2.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYG---DHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGkpTRQLTGSALRQLRS 100
Cdd:PTZ00265 383 IQFKNVRFHYDtrkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIND--SHNLKDINLKWWRS 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 101 RVGFVFQQFNLYAHlTAQENITLALERVHGW-------------------SKSAARERSLALLSQV-------------- 147
Cdd:PTZ00265 461 KIGVVSQDPLLFSN-SIKNNIKYSLYSLKDLealsnyynedgndsqenknKRNSCRAKCAGDLNDMsnttdsneliemrk 539
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504650440 148 ------------------------GLADKARQM----PAQLSGGQQQRVAIARALASSPQIILFDEPTSALD 191
Cdd:PTZ00265 540 nyqtikdsevvdvskkvlihdfvsALPDKYETLvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
27-240 |
2.71e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 66.30 E-value: 2.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 27 RDVAKSYGDHR-VLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEI----------------LIDGKPTRQ 89
Cdd:PRK11819 10 NRVSKVVPPKKqILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEArpapgikvgylpqepqLDPEKTVRE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 90 LTGSALRQLRSrvgfVFQQFN----LYAHLTAQENITLA--------LERVHGWSksaarerslaLLSQVGLADKARQMP 157
Cdd:PRK11819 90 NVEEGVAEVKA----ALDRFNeiyaAYAEPDADFDALAAeqgelqeiIDAADAWD----------LDSQLEIAMDALRCP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 158 ------AQLSGGQQQRVAIARALASSPQIILFDEPTSALDPEmigEVLQVMKTLAHSGITMVVVTHemqfareiaDRvVF 231
Cdd:PRK11819 156 pwdakvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAE---SVAWLEQFLHDYPGTVVAVTH---------DR-YF 222
|
250
....*....|.
gi 504650440 232 ID--GGDILEV 240
Cdd:PRK11819 223 LDnvAGWILEL 233
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
38-249 |
5.88e-12 |
|
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: 64.16 E-value: 5.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 38 VLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLtgsALRQLRSRVGFVFQQFNLYAHlta 117
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKL---PLHTLRSRLSIILQDPILFSG--- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 118 qeNITLALERvhgwSKSAARERSLALLSQVGLADKARQMPAQL-----------SGGQQQRVAIARALASSPQIILFDEP 186
Cdd:cd03288 110 --SIRFNLDP----ECKCTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILIMDEA 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504650440 187 TSALDpeMIGE-VLQVMKTLAHSGITMVVVTHEMQFAREiADRVVFIDGGDILEVAPPAEFFAR 249
Cdd:cd03288 184 TASID--MATEnILQKVVMTAFADRTVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLAQ 244
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
38-256 |
7.23e-12 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 65.57 E-value: 7.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 38 VLNGVNLQVEPGEVVAILGPSGSGKSTLIR-LINQLEsLSGGEILIDgkptrqltgsalrqlRSrVGFVFQQfNLYAHLT 116
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQsLLSQFE-ISEGRVWAE---------------RS-IAYVPQQ-AWIMNAT 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 117 AQENITLALE----RVHGWSKSAARERSLALLSQvGLADKARQMPAQLSGGQQQRVAIARALASSPQIILFDEPTSALDP 192
Cdd:PTZ00243 737 VRGNILFFDEedaaRLADAVRVSQLEADLAQLGG-GLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDA 815
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504650440 193 EMIGEVLQVMKTLAHSGITMVVVTHEMQFArEIADRVVFIDGGDILEVAPPAEFFARPQHARTR 256
Cdd:PTZ00243 816 HVGERVVEECFLGALAGKTRVLATHQVHVV-PRADYVVALGDGRVEFSGSSADFMRTSLYATLA 878
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
39-230 |
1.85e-11 |
|
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: 62.28 E-value: 1.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 39 LNGVNLQVEPGEVVAILGPSGSGKSTL----IRLINQ---LESLSG------GEI------LIDG-KPT---RQLTGSal 95
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLafdtIYAEGQrryVESLSAyarqflGQMdkpdvdSIEGlSPAiaiDQKTTS-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 96 RQLRSRVGFVFQQFNLYAHLTAQENItlalervhgwsksaaRERsLALLSQVGLA--DKARQMPAqLSGGQQQRVAIARA 173
Cdd:cd03270 89 RNPRSTVGTVTEIYDYLRLLFARVGI---------------RER-LGFLVDVGLGylTLSRSAPT-LSGGEAQRIRLATQ 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 504650440 174 LAS--SPQIILFDEPTSALDPEMIGEVLQVMKTLAHSGITMVVVTHEMQFAREiADRVV 230
Cdd:cd03270 152 IGSglTGVLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIRA-ADHVI 209
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
37-218 |
2.17e-11 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 64.10 E-value: 2.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 37 RVLNGVNLQVEPGEVVAILGPSGSGKSTLirlinqLESLSG--------GEILIDGKPTRQLTgsalrqlRSRVGFVFQQ 108
Cdd:PLN03140 894 QLLREVTGAFRPGVLTALMGVSGAGKTTL------MDVLAGrktggyieGDIRISGFPKKQET-------FARISGYCEQ 960
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 109 FNLYA-HLTAQEN-ITLALERVhgwSKSAARERSLALLSQV-------GLADKARQMPA--QLSGGQQQRVAIARALASS 177
Cdd:PLN03140 961 NDIHSpQVTVRESlIYSAFLRL---PKEVSKEEKMMFVDEVmelveldNLKDAIVGLPGvtGLSTEQRKRLTIAVELVAN 1037
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 504650440 178 PQIILFDEPTSALDPEMIGEVLQVMKTLAHSGITMVVVTHE 218
Cdd:PLN03140 1038 PSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQ 1078
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
38-235 |
2.39e-11 |
|
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: 62.57 E-value: 2.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 38 VLNGVNLQVEPGEVVAILGPSGSGKSTLIRLI-NQLESlSGGEILIDGkptrqltgsalrqlrsRVGFVfQQFNLYAHLT 116
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLIlGELEP-SEGKIKHSG----------------RISFS-SQFSWIMPGT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 117 AQENItlalerVHGWSKSAARERSLALLSQV-----GLADKARQMPAQ----LSGGQQQRVAIARALASSPQIILFDEPT 187
Cdd:cd03291 114 IKENI------IFGVSYDEYRYKSVVKACQLeeditKFPEKDNTVLGEggitLSGGQRARISLARAVYKDADLYLLDSPF 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 504650440 188 SALDPEMIGEVLQ--VMKTLAHSgiTMVVVTHEMQFAReIADRVVFIDGG 235
Cdd:cd03291 188 GYLDVFTEKEIFEscVCKLMANK--TRILVTSKMEHLK-KADKILILHEG 234
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
39-249 |
2.74e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 63.10 E-value: 2.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 39 LNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTrqLTGSALRQL----------RSRVGFVFQq 108
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEV--VTRSPQDGLangivyisedRKRDGLVLG- 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 109 fnlyahLTAQENITL-ALERV-HGWSKSAARERSLALLSQVGLAD-KARQMPAQ---LSGGQQQRVAIARALASSPQIIL 182
Cdd:PRK10762 345 ------MSVKENMSLtALRYFsRAGGSLKHADEQQAVSDFIRLFNiKTPSMEQAiglLSGGNQQKVAIARGLMTRPKVLI 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504650440 183 FDEPTSALDPEMIGEVLQVMKTLAHSGITMVVVTHEMQFAREIADRVVFIDGGDIlevapPAEFFAR 249
Cdd:PRK10762 419 LDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRI-----SGEFTRE 480
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
24-234 |
4.02e-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: 60.28 E-value: 4.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSYGDHRVLngVNL-QVEPGEVVAILGPSGSGKSTLIRLinqlesLSGGEilidgKPTrqltgsalrqlrsrv 102
Cdd:cd03222 1 QLYPDCVKRYGVFFLL--VELgVVKEGEVIGIVGPNGTGKTTAVKI------LAGQL-----IPN--------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 103 gfvfqqfnlyahltaQENITLALERVhgwsksaarerslallsqvglADKARQMpaQLSGGQQQRVAIARALASSPQIIL 182
Cdd:cd03222 53 ---------------GDNDEWDGITP---------------------VYKPQYI--DLSGGELQRVAIAAALLRNATFYL 94
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 504650440 183 FDEPTSALDPEMIGEVLQVMKTLA-HSGITMVVVTHEMQFAREIADRVVFIDG 234
Cdd:cd03222 95 FDEPSAYLDIEQRLNAARAIRRLSeEGKKTALVVEHDLAVLDYLSDRIHVFEG 147
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
78-236 |
4.29e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 63.12 E-value: 4.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 78 GEILIDGKptrQLTGSALRQLRSRVGFVFQQFNLYaHLTAQENITLA-----LERVHGWSKSAARERSLALL-----SQV 147
Cdd:PTZ00265 1277 GKILLDGV---DICDYNLKDLRNLFSIVSQEPMLF-NMSIYENIKFGkedatREDVKRACKFAAIDEFIESLpnkydTNV 1352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 148 GLADKArqmpaqLSGGQQQRVAIARALASSPQIILFDEPTSALDP---EMIGEVLQVMKTLAHSgiTMVVVTHEMQFARE 224
Cdd:PTZ00265 1353 GPYGKS------LSGGQKQRIAIARALLREPKILLLDEATSSLDSnseKLIEKTIVDIKDKADK--TIITIAHRIASIKR 1424
|
170
....*....|..
gi 504650440 225 iADRVVFIDGGD 236
Cdd:PTZ00265 1425 -SDKIVVFNNPD 1435
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
35-237 |
4.47e-11 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 62.50 E-value: 4.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 35 DHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRlinqleSLSG--------GEILIDGKPTRqlTGSALRQLRSRVGFVF 106
Cdd:NF040905 272 ERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAM------SVFGrsygrnisGTVFKDGKEVD--VSTVSDAIDAGLAYVT 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 107 Q---QFNLYAHLTAQENITLA-LERV--HGW------SKSAARERSlallsqvGLADKA---RQMPAQLSGGQQQRVAIA 171
Cdd:NF040905 344 EdrkGYGLNLIDDIKRNITLAnLGKVsrRGVideneeIKVAEEYRK-------KMNIKTpsvFQKVGNLSGGNQQKVVLS 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504650440 172 RALASSPQIILFDEPTSALDpemIG---EVLQVMKTLAHSGITMVVVTHEMQFAREIADRVVFIDGGDI 237
Cdd:NF040905 417 KWLFTDPDVLILDEPTRGID---VGakyEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMNEGRI 482
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
29-237 |
4.52e-11 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 62.88 E-value: 4.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 29 VAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLI-NQLESLSGGEILIDGkptrqltgsalrqlrSRVGFvFQ 107
Cdd:PRK10636 318 VSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLaGELAPVSGEIGLAKG---------------IKLGY-FA 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 108 QFNLyAHLTAQENITLALERVhgwsksAARERSLALLSQVG----LADKARQMPAQLSGGQQQRVAIARALASSPQIILF 183
Cdd:PRK10636 382 QHQL-EFLRADESPLQHLARL------APQELEQKLRDYLGgfgfQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLL 454
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 504650440 184 DEPTSALDPEMIGEVLQVMKTLAHSgitMVVVTHEMQFAREIADRVVFIDGGDI 237
Cdd:PRK10636 455 DEPTNHLDLDMRQALTEALIDFEGA---LVVVSHDRHLLRSTTDDLYLVHDGKV 505
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
46-219 |
5.28e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 62.52 E-value: 5.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 46 VEPGEVVAILGPSGSGKSTLIRLinqlesLSGgeILI------DGKPT-----RQLTGSAL----RQLRS---RVGFVFQ 107
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKI------LSG--ELIpnlgdyEEEPSwdevlKRFRGTELqnyfKKLYNgeiKVVHKPQ 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 108 qfnlYAHL-------TAQENITLALERvhgwskSAARErslaLLSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQI 180
Cdd:PRK13409 168 ----YVDLipkvfkgKVRELLKKVDER------GKLDE----VVERLGLENILDRDISELSGGELQRVAIAAALLRDADF 233
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 504650440 181 ILFDEPTSALDpemIGE---VLQVMKTLAhSGITMVVVTHEM 219
Cdd:PRK13409 234 YFFDEPTSYLD---IRQrlnVARLIRELA-EGKYVLVVEHDL 271
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
39-243 |
8.85e-11 |
|
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: 60.71 E-value: 8.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 39 LNGVNLQVEPGEVVAILGPSGSGKSTLI---------RLIN-------QLESLSGGE-----ILID----GKPTRQ---- 89
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLIndtlypalaRRLHlkkeqpgNHDRIEGLEhidkvIVIDqspiGRTPRSnpat 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 90 LTG--SALRQLRSRV--GfvfQQFN------LYAHLTAQENITLALERVHGWSKSAAR-ERSLALLSQVGLAD-KARQMP 157
Cdd:cd03271 91 YTGvfDEIRELFCEVckG---KRYNretlevRYKGKSIADVLDMTVEEALEFFENIPKiARKLQTLCDVGLGYiKLGQPA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 158 AQLSGGQQQRVAIARAL---ASSPQIILFDEPTSALDPEMIGEVLQVMKTLAHSGITMVVVTHEMQFAReIADRVvfID- 233
Cdd:cd03271 168 TTLSGGEAQRIKLAKELskrSTGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIK-CADWI--IDl 244
|
250
....*....|....*..
gi 504650440 234 -------GGDILEVAPP 243
Cdd:cd03271 245 gpeggdgGGQVVASGTP 261
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
46-219 |
1.05e-10 |
|
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: 60.46 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 46 VEPGEVVAILGPSGSGKSTLIRLinqlesLSGGEI----LIDGKPT-----RQLTGSALRQLRSRV------GFVFQQFN 110
Cdd:cd03236 23 PREGQVLGLVGPNGIGKSTALKI------LAGKLKpnlgKFDDPPDwdeilDEFRGSELQNYFTKLlegdvkVIVKPQYV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 111 LYAHLTAQENITLALERVHgwsKSAARERSLALLSQVGLADKARQmpaQLSGGQQQRVAIARALASSPQIILFDEPTSAL 190
Cdd:cd03236 97 DLIPKAVKGKVGELLKKKD---ERGKLDELVDQLELRHVLDRNID---QLSGGELQRVAIAAALARDADFYFFDEPSSYL 170
|
170 180
....*....|....*....|....*....
gi 504650440 191 DPEMIGEVLQVMKTLAHSGITMVVVTHEM 219
Cdd:cd03236 171 DIKQRLNAARLIRELAEDDNYVLVVEHDL 199
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
33-218 |
1.12e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 59.58 E-value: 1.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 33 YGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTGSALRQLrsrvGFVFQQFNLY 112
Cdd:PRK13540 11 YHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQL----CFVGHRSGIN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 113 AHLTAQENitlALERVHGWSKSAARERSLALLSQVGLADkarqMP-AQLSGGQQQRVAIARALASSPQIILFDEPTSALD 191
Cdd:PRK13540 87 PYLTLREN---CLYDIHFSPGAVGITELCRLFSLEHLID----YPcGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD 159
|
170 180
....*....|....*....|....*..
gi 504650440 192 PEMIGEVLQVMKTLAHSGITMVVVTHE 218
Cdd:PRK13540 160 ELSLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
35-215 |
1.34e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 61.18 E-value: 1.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 35 DHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRlinqleSLSGGEILIDGKPTRQLTGSAL---RQLRSRVGFVFQQFNl 111
Cdd:PRK10938 15 DTKTLQLPSLTLNAGDSWAFVGANGSGKSALAR------ALAGELPLLSGERQSQFSHITRlsfEQLQKLVSDEWQRNN- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 112 YAHLTAQENIT--LALERVHGWSKSAARERSLAllSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQIILFDEPTSA 189
Cdd:PRK10938 88 TDMLSPGEDDTgrTTAEIIQDEVKDPARCEQLA--QQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDG 165
|
170 180
....*....|....*....|....*.
gi 504650440 190 LDPEMIGEVLQVMKTLAHSGITMVVV 215
Cdd:PRK10938 166 LDVASRQQLAELLASLHQSGITLVLV 191
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
38-235 |
2.22e-10 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 61.08 E-value: 2.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 38 VLNGVNLQVEPGEVVAILGPSGSGKSTLIRLI-NQLESlSGGEILIDGkptrqltgsalrqlrsRVGFVfQQFNLYAHLT 116
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMImGELEP-SEGKIKHSG----------------RISFS-PQTSWIMPGT 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 117 AQENITLALE----RVHGWSKSAARERSLALLSQvglADKARQMPA--QLSGGQQQRVAIARALASSPQIILFDEPTSAL 190
Cdd:TIGR01271 503 IKDNIIFGLSydeyRYTSVIKACQLEEDIALFPE---KDKTVLGEGgiTLSGGQRARISLARAVYKDADLYLLDSPFTHL 579
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 504650440 191 DPEMIGEVLQ--VMKTLAHSgiTMVVVTHEMQFAREiADRVVFIDGG 235
Cdd:TIGR01271 580 DVVTEKEIFEscLCKLMSNK--TRILVTSKLEHLKK-ADKILLLHEG 623
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
38-239 |
2.41e-10 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 60.57 E-value: 2.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 38 VLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDG--------KPTRQLTGSAL----------RQLR 99
Cdd:PRK10636 16 LLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGnwqlawvnQETPALPQPALeyvidgdreyRQLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 100 SRVGFVFQQF--NLYAHLTAQenitlaLERVHGWSksaARERSLALLSQVGLADKARQMPAQ-LSGGQQQRVAIARALAS 176
Cdd:PRK10636 96 AQLHDANERNdgHAIATIHGK------LDAIDAWT---IRSRAASLLHGLGFSNEQLERPVSdFSGGWRMRLNLAQALIC 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504650440 177 SPQIILFDEPTSALDpemIGEVLQVMKTLAHSGITMVVVTHEMQFAREIADRVVFIDGGDILE 239
Cdd:PRK10636 167 RSDLLLLDEPTNHLD---LDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFE 226
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
24-213 |
3.03e-10 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 60.26 E-value: 3.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 24 IEFRDVAKSY-GDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINqleslsgGEIlidgKPTrqlTGSALRQLRSRV 102
Cdd:PLN03073 509 ISFSDASFGYpGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIS-------GEL----QPS---SGTVFRSAKVRM 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 103 GfVFQQFNLYAhLTAQENITLALERVHgwsKSAARERSLALLSQVGLA-DKARQMPAQLSGGQQQRVAIARALASSPQII 181
Cdd:PLN03073 575 A-VFSQHHVDG-LDLSSNPLLYMMRCF---PGVPEQKLRAHLGSFGVTgNLALQPMYTLSGGQKSRVAFAKITFKKPHIL 649
|
170 180 190
....*....|....*....|....*....|..
gi 504650440 182 LFDEPTSALDPEMIGEVLQVMkTLAHSGITMV 213
Cdd:PLN03073 650 LLDEPSNHLDLDAVEALIQGL-VLFQGGVLMV 680
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
36-241 |
3.60e-10 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 59.90 E-value: 3.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 36 HRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTGSALRqlrsrvgfvfqqfnlyAHL 115
Cdd:PRK13545 37 HYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLN----------------GQL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 116 TAQENITLAlERVHGWSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQIILFDEPTSALDPEMI 195
Cdd:PRK13545 101 TGIENIELK-GLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFT 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 504650440 196 GEVLQVMKTLAHSGITMVVVTHEMQFAREIADRVVFI------DGGDILEVA 241
Cdd:PRK13545 180 KKCLDKMNEFKEQGKTIFFISHSLSQVKSFCTKALWLhygqvkEYGDIKEVV 231
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
141-263 |
1.80e-09 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 58.30 E-value: 1.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 141 LALLSQVGLA--DKARQMpAQLSGGQQQRVAIARALASSPQIILF--DEPTSALDPEMIGEVLQVMKTLAHSGITMVVVT 216
Cdd:PRK00635 457 LSILIDLGLPylTPERAL-ATLSGGEQERTALAKHLGAELIGITYilDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVE 535
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 504650440 217 HEMQFArEIADRVVFID------GGDILEVAPPAEFFARpQHARTRRFLQKVL 263
Cdd:PRK00635 536 HDEQMI-SLADRIIDIGpgagifGGEVLFNGSPREFLAK-SDSLTAKYLRQEL 586
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
160-235 |
4.71e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 56.66 E-value: 4.71e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504650440 160 LSGGQQQRVAIARALASSPQIILFDEPTSALDPEMIGEVLQVMKTLAHSGITMVVVTHEMQFAREIADRVVFIDGG 235
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNG 467
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
39-247 |
9.97e-09 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 54.82 E-value: 9.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 39 LNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKptrqltgsalrqlrsrVGFVFQQFNLYAHLTAQ 118
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE----------------VSVIAISAGLSGQLTGI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 119 ENITLALeRVHGWSKSAARERSLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQIILFDEPTSALDPEMIGEV 198
Cdd:PRK13546 104 ENIEFKM-LCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKC 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 504650440 199 LQVMKTLAHSGITMVVVTHEMQFAREIADRVVFIDG------GDILEVAPPAEFF 247
Cdd:PRK13546 183 LDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGgklkdyGELDDVLPKYEAF 237
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
51-232 |
1.02e-08 |
|
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: 54.15 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 51 VVAILGPSGSGKSTLIrlinqlESLSGGeilidgkptrqLTGSALRQLRSRVGFvfqqfnlyAHLTA-QEN---ITLALE 126
Cdd:cd03240 24 LTLIVGQNGAGKTTII------EALKYA-----------LTGELPPNSKGGAHD--------PKLIReGEVraqVKLAFE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 127 RVHGWSKSAARE----RSLALLSQVGLADKARQMPAQLSGGQQQ------RVAIARALASSPQIILFDEPTSALDPEMIG 196
Cdd:cd03240 79 NANGKKYTITRSlailENVIFCHQGESNWPLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIE 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 504650440 197 EVL-QVMKTLAHSGI-TMVVVTHEMQFaREIADRVVFI 232
Cdd:cd03240 159 ESLaEIIEERKSQKNfQLIVITHDEEL-VDAADHIYRV 195
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
138-236 |
2.22e-08 |
|
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: 54.63 E-value: 2.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 138 ERSLALLSQVGLADKARQMPA-QLSGGQQQRVAIARAL---ASSPQIILFDEPTSALDPEMIGEVLQVMKTLAHSGITMV 213
Cdd:TIGR00630 807 SRKLQTLCDVGLGYIRLGQPAtTLSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVV 886
|
90 100
....*....|....*....|....*
gi 504650440 214 VVTHEMQFAReIADRVVFI--DGGD 236
Cdd:TIGR00630 887 VIEHNLDVIK-TADYIIDLgpEGGD 910
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
35-217 |
2.37e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 52.95 E-value: 2.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 35 DHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRLINQLESLSGGEILIDGKPTRQLTgsalrqlRSRVGFVFQQFNLYAH 114
Cdd:PRK13541 12 EQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIA-------KPYCTYIGHNLGLKLE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 115 LTAQENITLalervhgWSKSAARERSL-ALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQIILFDEPTSALDPE 193
Cdd:PRK13541 85 MTVFENLKF-------WSEIYNSAETLyAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKE 157
|
170 180
....*....|....*....|....*.
gi 504650440 194 MIGEV--LQVMKtlAHSGITMVVVTH 217
Cdd:PRK13541 158 NRDLLnnLIVMK--ANSGGIVLLSSH 181
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
48-230 |
5.25e-08 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 51.21 E-value: 5.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 48 PGEVVAILGPSGSGKSTLIRLInqleslsggeILIDGkptrqltgsaLRQLRSRVGFVFQQfnlyAHLTAQENITLALER 127
Cdd:cd03227 20 EGSLTIITGPNGSGKSTILDAI----------GLALG----------GAQSATRRRSGVKA----GCIVAAVSAELIFTR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 128 VhgwsksaarerslallsqvgladkarqmpaQLSGGQQQRVAIARALAS----SPQIILFDEPTSALDPEMIGEVLQVMK 203
Cdd:cd03227 76 L------------------------------QLSGGEKELSALALILALaslkPRPLYILDEIDRGLDPRDGQALAEAIL 125
|
170 180
....*....|....*....|....*..
gi 504650440 204 TLAHSGITMVVVTHEMQFArEIADRVV 230
Cdd:cd03227 126 EHLVKGAQVIVITHLPELA-ELADKLI 151
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
160-237 |
4.62e-07 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 50.98 E-value: 4.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 160 LSGGQQQRVAIARALASS---PQIILFDEPTSALDPEMIGEVLQVMKTLAHSGITMVVVTHEMQFAReIADRVVFI--DG 234
Cdd:PRK00635 810 LSGGEIQRLKLAYELLAPskkPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMHVVK-VADYVLELgpEG 888
|
...
gi 504650440 235 GDI 237
Cdd:PRK00635 889 GNL 891
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
119-230 |
9.41e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 49.86 E-value: 9.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 119 ENITLALERVHGWSKSAARERSLALLSQVglADKARQMPAQLSGGQQQRVAIARALASSPQIILFDEPTSALDpemIGEV 198
Cdd:PLN03073 306 EEIYKRLELIDAYTAEARAASILAGLSFT--PEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD---LHAV 380
|
90 100 110
....*....|....*....|....*....|..
gi 504650440 199 LQVMKTLAHSGITMVVVTHemqfAREIADRVV 230
Cdd:PLN03073 381 LWLETYLLKWPKTFIVVSH----AREFLNTVV 408
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
137-251 |
1.65e-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: 48.86 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 137 RERsLALLSQVGLADKARQMPAQ-LSGGQQQRVAIARALASSPQIILF--DEPTSALDPEMIGEVLQVMKTLAHSGITMV 213
Cdd:TIGR00630 466 RER-LGFLIDVGLDYLSLSRAAGtLSGGEAQRIRLATQIGSGLTGVLYvlDEPSIGLHQRDNRRLINTLKRLRDLGNTLI 544
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 504650440 214 VVTHEMQFAREiADRVVFI------DGGDILEVAPPAEFFARPQ 251
Cdd:TIGR00630 545 VVEHDEDTIRA-ADYVIDIgpgageHGGEVVASGTPEEILANPD 587
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
25-221 |
1.75e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 48.79 E-value: 1.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 25 EFRDVAKSYGDHRVLNGVNLQVEPGEVVAILGPSGSGKSTLIRL-INQLESLSGgeilidgkptRQLTGSALrqlrsRVG 103
Cdd:PRK11147 321 EMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLmLGQLQADSG----------RIHCGTKL-----EVA 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 104 FvFQQF--NLYAHLTAQENitLALER----VHGwsksaaRERSLALLSQVGLADKARQM-PAQ-LSGGQQQRVAIARALA 175
Cdd:PRK11147 386 Y-FDQHraELDPEKTVMDN--LAEGKqevmVNG------RPRHVLGYLQDFLFHPKRAMtPVKaLSGGERNRLLLARLFL 456
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 504650440 176 SSPQIILFDEPTSALDPEMIgEVLQVMktLAHSGITMVVVTHEMQF 221
Cdd:PRK11147 457 KPSNLLILDEPTNDLDVETL-ELLEEL--LDSYQGTVLLVSHDRQF 499
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
139-265 |
2.24e-06 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 48.48 E-value: 2.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 139 RSLALLSQVGLaDKAR--QmPA-QLSGGQQQRVAIARALASSPQ---IILFDEPTSALDPEMIGEVLQVMKTLAHSGITM 212
Cdd:COG0178 805 RKLQTLQDVGL-GYIKlgQ-PAtTLSGGEAQRVKLASELSKRSTgktLYILDEPTTGLHFHDIRKLLEVLHRLVDKGNTV 882
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504650440 213 VVVTHEMQFareI--ADRVvfID--------GGDILEVAPPAEFFARPQ-HarTRRFLQKVLDP 265
Cdd:COG0178 883 VVIEHNLDV---IktADWI--IDlgpeggdgGGEIVAEGTPEEVAKVKAsY--TGRYLKEYLEA 939
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
18-233 |
9.42e-06 |
|
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: 46.15 E-value: 9.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 18 HLQRASIE-FRdvakSYGDhrvlngVNLQVEPGeVVAILGPSGSGKSTLIRLInqleslsggEILIDGKPTRQLT----- 91
Cdd:COG3593 2 KLEKIKIKnFR----SIKD------LSIELSDD-LTVLVGENNSGKSSILEAL---------RLLLGPSSSRKFDeedfy 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 92 -GSALRQLRSRVGFVFQQ-----FNLYAHLTAQENITLAL---------------ERVHGWSKSAARERSLALLSQ---- 146
Cdd:COG3593 62 lGDDPDLPEIEIELTFGSllsrlLRLLLKEEDKEELEEALeelneelkealkalnELLSEYLKELLDGLDLELELSldel 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 147 --------VGLADKARQMPAQLSGGQQQRVAIA--RALA-----SSPQIILFDEPTSALDPEMIGEVLQVMKTLAHSGIT 211
Cdd:COG3593 142 edllkslsLRIEDGKELPLDRLGSGFQRLILLAllSALAelkraPANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQ 221
|
250 260
....*....|....*....|...
gi 504650440 212 MVVVTHEMQFAREI-ADRVVFID 233
Cdd:COG3593 222 VIITTHSPHLLSEVpLENIRRLR 244
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
157-217 |
5.41e-05 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 43.92 E-value: 5.41e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504650440 157 PAQLSGGQQQ---RVAIARALASSPQIILFDEPTSALDPEMIGEVLQVMKTLAHSGITMVVVTH 217
Cdd:pfam13304 234 AFELSDGTKRllaLLAALLSALPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTH 297
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
45-230 |
2.12e-04 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 41.49 E-value: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 45 QVEPGEVVAILGPSGSGKSTLIRLInqleSLSggeilIDGKPTRQLTGSALRQLRS------RVGFVFQqfnlyahltaQ 118
Cdd:cd03279 24 GLDNNGLFLICGPTGAGKSTILDAI----TYA-----LYGKTPRYGRQENLRSVFApgedtaEVSFTFQ----------L 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 119 ENITLALERVHGWSKSAARErsLALLSQVGLADKARQMPAQLSGGQQQRVAIARALASSPQI----------ILFDEPTS 188
Cdd:cd03279 85 GGKKYRVERSRGLDYDQFTR--IVLLPQGEFDRFLARPVSTLSGGETFLASLSLALALSEVLqnrggarleaLFIDEGFG 162
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 504650440 189 ALDPEMIGEVLQVMKTLAHSGITMVVVTHEMQFAREIADRVV 230
Cdd:cd03279 163 TLDPEALEAVATALELIRTENRMVGVISHVEELKERIPQRLE 204
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
136-221 |
2.19e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 42.19 E-value: 2.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 136 ARERSLALLSQVGLADKARQMP-AQLSGGQQQRVAIARALASSPQIILFDEPTSALDPEMIGEVLQVmktLAHSGITMVV 214
Cdd:PRK15064 131 AEARAGELLLGVGIPEEQHYGLmSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDV---LNERNSTMII 207
|
....*..
gi 504650440 215 VTHEMQF 221
Cdd:PRK15064 208 ISHDRHF 214
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
139-264 |
3.61e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 41.60 E-value: 3.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 139 RSLALLSQVGLAD-KARQMPAQLSGGQQQRVAIARALASSPQ---IILFDEPTSALDPEMIGEVLQVMKTLAHSGITMVV 214
Cdd:PRK00349 809 RKLQTLVDVGLGYiKLGQPATTLSGGEAQRVKLAKELSKRSTgktLYILDEPTTGLHFEDIRKLLEVLHRLVDKGNTVVV 888
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 504650440 215 VTHEMQFAReIADRVvfID--------GGDILEVAPPaEFFARPQHARTRRFLQKVLD 264
Cdd:PRK00349 889 IEHNLDVIK-TADWI--IDlgpeggdgGGEIVATGTP-EEVAKVEASYTGRYLKPVLE 942
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
154-204 |
3.84e-04 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 38.76 E-value: 3.84e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504650440 154 RQMPAQLSGGQQQR---VAIARALAS----------SPQIILFDEPTSALDPEMIGEVLQVMKT 204
Cdd:pfam13558 27 YRRSGGLSGGEKQLlayLPLAAALAAqygsaegrppAPRLVFLDEAFAKLDEENIRTALELLRA 90
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
103-230 |
4.34e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. 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: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 41.49 E-value: 4.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 103 GFVFQQFnlYAHLTAQENITLALE-------RVHGWSKSAARERSLALLSqVGLADKARQMPAQLSGGQQQRVAIARALA 175
Cdd:TIGR00618 890 GDALIKF--LHEITLYANVRLANQsegrfhgRYADSHVNARKYQGLALLV-ADAYTGSVRPSATLSGGETFLASLSLALA 966
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504650440 176 SSP----------QIILFDEPTSALDPEMIGEVLQVMKTLAHSGITMVVVTHEMQFAREIADRVV 230
Cdd:TIGR00618 967 LADllstsggtvlDSLFIDEGFGSLDEDSLDRAIGILDAIREGSKMIGIISHVPEFRERIPHRIL 1031
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
51-217 |
1.48e-03 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 38.84 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 51 VVAILGPSGSGKSTLIRLI-----NQLESLSGG----------------EILIDGKPTR----QLTGSALRQLRS--RVG 103
Cdd:COG0419 25 LNLIVGPNGAGKSTILEAIryalyGKARSRSKLrsdlinvgseeasvelEFEHGGKRYRierrQGEFAEFLEAKPseRKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 104 FVFQQFNL------YAHLTA-QENITLALERVHgwSKSAARERSLALLSqvGLADkarqmPAQLSGGQQQRVAIARALAs 176
Cdd:COG0419 105 ALKRLLGLeiyeelKERLKElEEALESALEELA--ELQKLKQEILAQLS--GLDP-----IETLSGGERLRLALADLLS- 174
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 504650440 177 spqiILFDepTSALDPEMIGEVLQVMKTLAhsgitmvVVTH 217
Cdd:COG0419 175 ----LILD--FGSLDEERLERLLDALEELA-------IITH 202
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
40-66 |
1.50e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 36.04 E-value: 1.50e-03
10 20
....*....|....*....|....*..
gi 504650440 40 NGVNLQVEPGEVVAILGPSGSGKSTLI 66
Cdd:pfam13555 13 DGHTIPIDPRGNTLLTGPSGSGKSTLL 39
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
49-80 |
2.12e-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: 38.53 E-value: 2.12e-03
10 20 30
....*....|....*....|....*....|..
gi 504650440 49 GEVVAILGPSGSGKSTLIRLINQLESLSGGEI 80
Cdd:cd01854 85 GKTSVLVGQSGVGKSTLLNALLPELVLATGEI 116
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
132-225 |
2.28e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 39.26 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 132 SKSAARERSLALLSQVGlaDKARQMPAQLSGGQQQ------RVAIARALASSPQIILFDEPTSALDPEMIGEVLQVMKTL 205
Cdd:TIGR00606 1174 ASDKRRNYNYRVVMLKG--DTALDMRGRCSAGQKVlasliiRLALAETFCLNCGIIALDEPTTNLDRENIESLAHALVEI 1251
|
90 100
....*....|....*....|....*
gi 504650440 206 AHS-----GITMVVVTHEMQFAREI 225
Cdd:TIGR00606 1252 IKSrsqqrNFQLLVITHDEDFVELL 1276
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
141-235 |
3.88e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 38.66 E-value: 3.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 141 LALLSQVGLAD-KARQMPAQLSGGQQQRVAIARALAS--SPQIILFDEPTSALDPEMIGEVLQVMKTLAHSGITmVVVTH 217
Cdd:PRK00635 1368 LTFIDKVGLSYiTLGQEQDTLSDGEHYRLHLAKKISSnlTDIIYLLEDPLSGLHPQDAPTLLQLIKELVTNNNT-VIATD 1446
|
90
....*....|....*...
gi 504650440 218 EMQFAREIADRVVFIDGG 235
Cdd:PRK00635 1447 RSGSLAEHADHLIHLGPG 1464
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
159-208 |
3.98e-03 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213239 [Multi-domain] Cd Length: 243 Bit Score: 37.62 E-value: 3.98e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 504650440 159 QLSGGQQQRVAIARALA-----SSPqIILFDEPTSALDPEMIGEVLQVMKTLAHS 208
Cdd:cd03272 158 QLSGGQKSLVALALIFAiqkcdPAP-FYLFDEIDAALDAQYRTAVANMIKELSDG 211
|
|
| CMPK |
cd02020 |
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine ... |
51-80 |
4.98e-03 |
|
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine monophosphate (CMP) to produce cytidine diphosphate (CDP), using ATP as the preferred phosphoryl donor.
Pssm-ID: 238978 [Multi-domain] Cd Length: 147 Bit Score: 36.70 E-value: 4.98e-03
10 20 30
....*....|....*....|....*....|...
gi 504650440 51 VVAILGPSGSGKSTLIRLINQ---LESLSGGEI 80
Cdd:cd02020 1 IIAIDGPAGSGKSTVAKLLAKklgLPYLDTGGI 33
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
155-243 |
7.39e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 37.89 E-value: 7.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504650440 155 QMPAQLSGGQQQRVAIARALASSPQ---IILFDEPTSALDPEMIGEVLQVMKTLAHSGITMVVVTHEMQFAREiADRVVF 231
Cdd:PRK00635 1695 QNLSSLSLSEKIAIKIAKFLYLPPKhptLFLLDEIATSLDNQQKSALLVQLRTLVSLGHSVIYIDHDPALLKQ-ADYLIE 1773
|
90
....*....|....*...
gi 504650440 232 ID------GGDILEVAPP 243
Cdd:PRK00635 1774 MGpgsgktGGKILFSGPP 1791
|
|
| |
