|
Name |
Accession |
Description |
Interval |
E-value |
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
2-257 |
0e+00 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 512.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 2 AEATPALEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKLKAAKNGEL 81
Cdd:COG4598 3 DTAPPALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPDRDGEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 82 VAADGKQINRLRSEIGFVFQNFNLWPHMSVLDNIIEAPRRVLGQSKAEATEIAEALLAKVGISDKRHAYPAQLSGGQQQR 161
Cdd:COG4598 83 VPADRRQLQRIRTRLGMVFQSFNLWSHMTVLENVIEAPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 162 AAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHEMGFARQVSSEVVFLHQGLVEEQGSPQQVF 241
Cdd:COG4598 163 AAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVF 242
|
250
....*....|....*.
gi 489310645 242 ENPLSARCKQFMSSNR 257
Cdd:COG4598 243 GNPKSERLRQFLSSSL 258
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
8-254 |
6.64e-161 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 445.59 E-value: 6.64e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVageelklkaakNGELVAADGK 87
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITV-----------DGEDLTDSKK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 88 QINRLRSEIGFVFQNFNLWPHMSVLDNIIEAPRRVLGQSKAEATEIAEALLAKVGISDKRHAYPAQLSGGQQQRAAIART 167
Cdd:COG1126 71 DINKLRRKVGMVFQQFNLFPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 168 LAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHEMGFARQVSSEVVFLHQGLVEEQGSPQQVFENPLSA 247
Cdd:COG1126 151 LAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHE 230
|
....*..
gi 489310645 248 RCKQFMS 254
Cdd:COG1126 231 RTRAFLS 237
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
8-229 |
3.94e-131 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 369.17 E-value: 3.94e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVageelklkaakNGELVAADGK 87
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIII-----------DGLKLTDDKK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 88 QINRLRSEIGFVFQNFNLWPHMSVLDNIIEAPRRVLGQSKAEATEIAEALLAKVGISDKRHAYPAQLSGGQQQRAAIART 167
Cdd:cd03262 70 NINELRQKVGMVFQQFNLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489310645 168 LAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHEMGFARQVSSEVVFLHQG 229
Cdd:cd03262 150 LAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDG 211
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
8-254 |
3.19e-117 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 335.79 E-value: 3.19e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKLKAAKNGELVAADGK 87
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQLKVADKN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 88 QINRLRSEIGFVFQNFNLWPHMSVLDNIIEAPRRVLGQSKAEATEIAEALLAKVGISDK-RHAYPAQLSGGQQQRAAIAR 166
Cdd:PRK10619 86 QLRLLRTRLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERaQGKYPVHLSGGQQQRVSIAR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 167 TLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHEMGFARQVSSEVVFLHQGLVEEQGSPQQVFENPLS 246
Cdd:PRK10619 166 ALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQS 245
|
....*...
gi 489310645 247 ARCKQFMS 254
Cdd:PRK10619 246 PRLQQFLK 253
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
8-253 |
9.81e-106 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 305.86 E-value: 9.81e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKlkaakngelvaaDGK 87
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVN------------DPK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 88 QINRL-RSEIGFVFQNFNLWPHMSVLDNIIEAPRRVLGQSKAEATEIAEALLAKVGISDKRHAYPAQLSGGQQQRAAIAR 166
Cdd:PRK09493 70 VDERLiRQEAGMVFQQFYLFPHLTALENVMFGPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 167 TLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHEMGFARQVSSEVVFLHQGLVEEQGSPQQVFENPLS 246
Cdd:PRK09493 150 ALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPS 229
|
....*..
gi 489310645 247 ARCKQFM 253
Cdd:PRK09493 230 QRLQEFL 236
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
7-254 |
1.91e-104 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 303.21 E-value: 1.91e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 7 ALEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAgeELKLKAAKNgelVAADG 86
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVG--DITIDTARS---LSQQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 87 KQINRLRSEIGFVFQNFNLWPHMSVLDNIIEAPRRVLGQSKAEATEIAEALLAKVGISDKRHAYPAQLSGGQQQRAAIAR 166
Cdd:PRK11264 78 GLIRQLRQHVGFVFQNFNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 167 TLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHEMGFARQVSSEVVFLHQGLVEEQGSPQQVFENPLS 246
Cdd:PRK11264 158 ALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQ 237
|
....*...
gi 489310645 247 ARCKQFMS 254
Cdd:PRK11264 238 PRTRQFLE 245
|
|
| ectoine_ehuA |
TIGR03005 |
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ... |
8-255 |
2.09e-97 |
|
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: 285.19 E-value: 2.09e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKLKAAKNGELVAADGK 87
Cdd:TIGR03005 1 VRFSDVTKRFGILTVLDGLNFSVAAGEKVALIGPSGSGKSTILRILMTLEPIDEGQIQVEGEQLYHMPGRNGPLVPADEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 88 QINRLRSEIGFVFQNFNLWPHMSVLDNIIEAPRRVLGQSKAEATEIAEALLAKVGISDKRHAYPAQLSGGQQQRAAIART 167
Cdd:TIGR03005 81 HLRQMRNKIGMVFQSFNLFPHKTVLDNVTEAPVLVLGMARAEAEKRAMELLDMVGLADKADHMPAQLSGGQQQRVAIARA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 168 LAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGR-TMLLVTHEMGFARQVSSEVVFLHQGLVEEQGSPQQVFENPLS 246
Cdd:TIGR03005 161 LAMRPKVMLFDEVTSALDPELVGEVLNVIRRLASEHDlTMLLVTHEMGFAREFADRVCFFDKGRIVEQGKPDEIFRQPKE 240
|
....*....
gi 489310645 247 ARCKQFMSS 255
Cdd:TIGR03005 241 ERTREFLSK 249
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
7-254 |
5.27e-95 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 278.82 E-value: 5.27e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 7 ALEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKLKAAkngelvaADG 86
Cdd:COG4161 2 SIQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDFSQK-------PSE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 87 KQINRLRSEIGFVFQNFNLWPHMSVLDNIIEAPRRVLGQSKAEATEIAEALLAKVGISDKRHAYPAQLSGGQQQRAAIAR 166
Cdd:COG4161 75 KAIRLLRQKVGMVFQQYNLWPHLTVMENLIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIAR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 167 TLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHEMGFARQVSSEVVFLHQGLVEEQGSpQQVFENPLS 246
Cdd:COG4161 155 ALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGD-ASHFTQPQT 233
|
....*...
gi 489310645 247 ARCKQFMS 254
Cdd:COG4161 234 EAFAHYLS 241
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
7-254 |
2.18e-93 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 274.58 E-value: 2.18e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 7 ALEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKLKAAkngelvaADG 86
Cdd:PRK11124 2 SIQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSKT-------PSD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 87 KQINRLRSEIGFVFQNFNLWPHMSVLDNIIEAPRRVLGQSKAEATEIAEALLAKVGISDKRHAYPAQLSGGQQQRAAIAR 166
Cdd:PRK11124 75 KAIRELRRNVGMVFQQYNLWPHLTVQQNLIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIAR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 167 TLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHEMGFARQVSSEVVFLHQGLVEEQGSpQQVFENPLS 246
Cdd:PRK11124 155 ALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGD-ASCFTQPQT 233
|
....*...
gi 489310645 247 ARCKQFMS 254
Cdd:PRK11124 234 EAFKNYLS 241
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
8-255 |
5.05e-87 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 261.94 E-value: 5.05e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRY----GELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELklkaakngelVA 83
Cdd:COG1135 2 IELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDL----------TA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 84 ADGKQINRLRSEIGFVFQNFNLWPHMSVLDNIiEAPRRVLGQSKAEATEIAEALLAKVGISDKRHAYPAQLSGGQQQRAA 163
Cdd:COG1135 72 LSERELRAARRKIGMIFQHFNLLSSRTVAENV-ALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 164 IARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEE-GRTMLLVTHEMGFARQVSSEVVFLHQGLVEEQGSPQQVFE 242
Cdd:COG1135 151 IARALANNPKVLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFA 230
|
250
....*....|...
gi 489310645 243 NPLSARCKQFMSS 255
Cdd:COG1135 231 NPQSELTRRFLPT 243
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
5-234 |
1.06e-84 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 251.89 E-value: 1.06e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 5 TPALEIRNLHKRYG----ELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKlkaaknge 80
Cdd:COG1136 2 SPLLELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDIS-------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 81 lvAADGKQINRLRSE-IGFVFQNFNLWPHMSVLDNIiEAPRRVLGQSKAEATEIAEALLAKVGISDKRHAYPAQLSGGQQ 159
Cdd:COG1136 74 --SLSERELARLRRRhIGFVFQFFNLLPELTALENV-ALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489310645 160 QRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEE-GRTMLLVTHEMGFARQVSSeVVFLHQGLVEEQ 234
Cdd:COG1136 151 QRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHDPELAARADR-VIRLRDGRIVSD 225
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
4-253 |
7.58e-82 |
|
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: 245.27 E-value: 7.58e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 4 ATPALEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELklkaakngelVA 83
Cdd:COG1127 2 SEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDI----------TG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 84 ADGKQINRLRSEIGFVFQNFNLWPHMSVLDNIiEAP-RRVLGQSKAEATEIAEALLAKVGISDKRHAYPAQLSGGQQQRA 162
Cdd:COG1127 72 LSEKELYELRRRIGMLFQGGALFDSLTVFENV-AFPlREHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 163 AIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEE-GRTMLLVTHEMGFARQVSSEVVFLHQGLVEEQGSPQQVF 241
Cdd:COG1127 151 ALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELL 230
|
250
....*....|..
gi 489310645 242 ENPlSARCKQFM 253
Cdd:COG1127 231 ASD-DPWVRQFL 241
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
8-244 |
2.17e-81 |
|
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: 244.03 E-value: 2.17e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRYG----ELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKLKaakngelva 83
Cdd:cd03258 2 IELKNVSKVFGdtggKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLL--------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 84 aDGKQINRLRSEIGFVFQNFNLWPHMSVLDNIiEAPRRVLGQSKAEATEIAEALLAKVGISDKRHAYPAQLSGGQQQRAA 163
Cdd:cd03258 73 -SGKELRKARRRIGMIFQHFNLLSSRTVFENV-ALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 164 IARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEE-GRTMLLVTHEMGFARQVSSEVVFLHQGLVEEQGSPQQVFE 242
Cdd:cd03258 151 IARALANNPKVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFA 230
|
..
gi 489310645 243 NP 244
Cdd:cd03258 231 NP 232
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
4-247 |
1.36e-80 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 246.16 E-value: 1.36e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 4 ATPALEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVageelklkaakngelva 83
Cdd:COG3842 2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILL----------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 84 aDGKQINRLRSE---IGFVFQNFNLWPHMSVLDNIiEAPRRVLGQSKAEATEIAEALLAKVGISDKRHAYPAQLSGGQQQ 160
Cdd:COG3842 65 -DGRDVTGLPPEkrnVGMVFQDYALFPHLTVAENV-AFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 161 RAAIARTLAMQPKVILFDEPTSALDP----EMVQEVLNVIRALaeeGRTMLLVTHEMGFARQVSSEVVFLHQGLVEEQGS 236
Cdd:COG3842 143 RVALARALAPEPRVLLLDEPLSALDAklreEMREELRRLQREL---GITFIYVTHDQEEALALADRIAVMNDGRIEQVGT 219
|
250
....*....|.
gi 489310645 237 PQQVFENPLSA 247
Cdd:COG3842 220 PEEIYERPATR 230
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
7-254 |
3.67e-80 |
|
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: 241.43 E-value: 3.67e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 7 ALEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENphqgqiLVAGEELKLKAAKNGELVAADG 86
Cdd:TIGR00972 1 AIEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMND------LVPGVRIEGKVLFDGQDIYDKK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 87 KQINRLRSEIGFVFQNFNLWPhMSVLDNIIEAPRRVLGQSKAEATEIAEALLAKVGI----SDKRHAYPAQLSGGQQQRA 162
Cdd:TIGR00972 75 IDVVELRRRVGMVFQKPNPFP-MSIYDNIAYGPRLHGIKDKKELDEIVEESLKKAALwdevKDRLHDSALGLSGGQQQRL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 163 AIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEgRTMLLVTHEMGFARQVSSEVVFLHQGLVEEQGSPQQVFE 242
Cdd:TIGR00972 154 CIARALAVEPEVLLLDEPTSALDPIATGKIEELIQELKKK-YTIVIVTHNMQQAARISDRTAFFYDGELVEYGPTEQIFT 232
|
250
....*....|..
gi 489310645 243 NPLSARCKQFMS 254
Cdd:TIGR00972 233 NPKEKRTEDYIS 244
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-247 |
1.81e-79 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 248.28 E-value: 1.81e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 2 AEATPALEIRNLHKRY-----GELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKlkaa 76
Cdd:COG1123 255 AAAEPLLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLT---- 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 77 kngelvAADGKQINRLRSEIGFVFQN----FNlwPHMSVLDNIIEAPRRVLGQSKAEATEIAEALLAKVGIS-DKRHAYP 151
Cdd:COG1123 331 ------KLSRRSLRELRRRVQMVFQDpyssLN--PRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLPpDLADRYP 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 152 AQLSGGQQQRAAIARTLAMQPKVILFDEPTSALDPeMVQ-EVLNVIRALAEE-GRTMLLVTHEMGFARQVSSEVVFLHQG 229
Cdd:COG1123 403 HELSGGQRQRVAIARALALEPKLLILDEPTSALDV-SVQaQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDG 481
|
250
....*....|....*...
gi 489310645 230 LVEEQGSPQQVFENPLSA 247
Cdd:COG1123 482 RIVEDGPTEEVFANPQHP 499
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-211 |
4.09e-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: 236.52 E-value: 4.09e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 1 MAEATPALEIRNLHKRY----GELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVageelklkaa 76
Cdd:COG1116 1 MSAAAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLV---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 77 kngelvaaDGKQINRLRSEIGFVFQNFNLWPHMSVLDNIiEAPRRVLGQSKAEATEIAEALLAKVGISDKRHAYPAQLSG 156
Cdd:COG1116 71 --------DGKPVTGPGPDRGVVFQEPALLPWLTVLDNV-ALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSG 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489310645 157 GQQQRAAIARTLAMQPKVILFDEPTSALDP---EMVQEVLnvIRALAEEGRTMLLVTH 211
Cdd:COG1116 142 GMRQRVAIARALANDPEVLLMDEPFGALDAltrERLQDEL--LRLWQETGKTVLFVTH 197
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
8-231 |
2.03e-77 |
|
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: 233.15 E-value: 2.03e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRYG----ELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKlkaakngelvA 83
Cdd:cd03255 1 IELKNLSKTYGgggeKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDIS----------K 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 84 ADGKQINRLRSE-IGFVFQNFNLWPHMSVLDNIiEAPRRVLGQSKAEATEIAEALLAKVGISDKRHAYPAQLSGGQQQRA 162
Cdd:cd03255 71 LSEKELAAFRRRhIGFVFQSFNLLPDLTALENV-ELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 163 AIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEE-GRTMLLVTHEMGFARQvSSEVVFLHQGLV 231
Cdd:cd03255 150 AIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHDPELAEY-ADRIIELRDGKI 218
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
8-244 |
4.97e-77 |
|
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: 232.61 E-value: 4.97e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRY-GELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKlkaakngelvaadG 86
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDIT-------------K 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 87 KQINRLRSEIGFVFQN-----FNlwphMSVLDNIIEAPRRvLGQSKAEATEIAEALLAKVGISDKRHAYPAQLSGGQQQR 161
Cdd:COG1122 68 KNLRELRRKVGLVFQNpddqlFA----PTVEEDVAFGPEN-LGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 162 AAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHEMGFARQVSSEVVFLHQGLVEEQGSPQQVF 241
Cdd:COG1122 143 VAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVF 222
|
...
gi 489310645 242 ENP 244
Cdd:COG1122 223 SDY 225
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
6-240 |
1.10e-73 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 224.94 E-value: 1.10e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 6 PALEIRNLHKRY-GELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELklkaakngelVAA 84
Cdd:COG3638 1 PMLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDV----------TAL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 85 DGKQINRLRSEIGFVFQNFNLWPHMSVLDNI-------IEAPRRVLGQSKAEATEIAEALLAKVGISDKRHAYPAQLSGG 157
Cdd:COG3638 71 RGRALRRLRRRIGMIFQQFNLVPRLSVLTNVlagrlgrTSTWRSLLGLFPPEDRERALEALERVGLADKAYQRADQLSGG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 158 QQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEE-GRTMLLVTHEMGFARQVSSEVVFLHQGLVEEQGS 236
Cdd:COG3638 151 QQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREdGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGP 230
|
....
gi 489310645 237 PQQV 240
Cdd:COG3638 231 PAEL 234
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
9-255 |
2.18e-73 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 227.38 E-value: 2.18e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 9 EIRNLHKRY----GELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELklkaakngelVAA 84
Cdd:PRK11153 3 ELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDL----------TAL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 85 DGKQINRLRSEIGFVFQNFNLWPHMSVLDNIieA-PRRVLGQSKAEATEIAEALLAKVGISDKRHAYPAQLSGGQQQRAA 163
Cdd:PRK11153 73 SEKELRKARRQIGMIFQHFNLLSSRTVFDNV--AlPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 164 IARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEE-GRTMLLVTHEMGFARQVSSEVVFLHQGLVEEQGSPQQVFE 242
Cdd:PRK11153 151 IARALASNPKVLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFS 230
|
250
....*....|...
gi 489310645 243 NPLSARCKQFMSS 255
Cdd:PRK11153 231 HPKHPLTREFIQS 243
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
8-244 |
3.22e-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: 3.22e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKlkaakngelvaadgk 87
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLF--------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 88 qINR--LRSEIGFVFQNFNLWPHMSVLDNIIEAPRrVLGQSKAEATEIAEALLAKVGISDKRHAYPAQLSGGQQQRAAIA 165
Cdd:COG1118 68 -TNLppRERRVGFVFQHYALFPHMTVAENIAFGLR-VRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 166 RTLAMQPKVILFDEPTSALD----PEMVQEVLNViraLAEEGRTMLLVTHEMGFARQVSSEVVFLHQGLVEEQGSPQQVF 241
Cdd:COG1118 146 RALAVEPEVLLLDEPFGALDakvrKELRRWLRRL---HDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVY 222
|
...
gi 489310645 242 ENP 244
Cdd:COG1118 223 DRP 225
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
8-235 |
3.81e-71 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 217.00 E-value: 3.81e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVageelklkaakngelvaaDGK 87
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILI------------------DGR 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 88 QINRL---RSEIGFVFQNFNLWPHMSVLDNIIEAPRRvLGQSKAEATEIAEALLAKVGISDKRHAYPAQLSGGQQQRAAI 164
Cdd:cd03259 63 DVTGVppeRRNIGMVFQDYALFPHLTVAENIAFGLKL-RGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVAL 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489310645 165 ARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRAL-AEEGRTMLLVTHEMGFARQVSSEVVFLHQGLVEEQG 235
Cdd:cd03259 142 ARALAREPSLLLLDEPLSALDAKLREELREELKELqRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
8-240 |
8.37e-71 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 216.85 E-value: 8.37e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEElklkaakngelVAADGK 87
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGED-----------VARDPA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 88 QInrlRSEIGFVFQNFNLWPHMSVLDNIIEApRRVLGQSKAEATEIAEALLAKVGISDKRHAYPAQLSGGQQQRAAIART 167
Cdd:COG1131 70 EV---RRRIGYVPQEPALYPDLTVRENLRFF-ARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489310645 168 LAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHEMGFARQVSSEVVFLHQGLVEEQGSPQQV 240
Cdd:COG1131 146 LLHDPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-255 |
2.00e-70 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 219.94 E-value: 2.00e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 1 MAEatpaLEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVageelklkaaknge 80
Cdd:COG3839 1 MAS----LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILI-------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 81 lvaaDGKQINRLRSE---IGFVFQNFNLWPHMSVLDNIiEAPRRVLGQSKAEATEIAEALLAKVGISDKRHAYPAQLSGG 157
Cdd:COG3839 63 ----GGRDVTDLPPKdrnIAMVFQSYALYPHMTVYENI-AFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 158 QQQRAAIARTLAMQPKVILFDEPTSALDP----EMVQEvlnvIRAL-AEEGRTMLLVTHE----MGFArqvsSEVVFLHQ 228
Cdd:COG3839 138 QRQRVALGRALVREPKVFLLDEPLSNLDAklrvEMRAE----IKRLhRRLGTTTIYVTHDqveaMTLA----DRIAVMND 209
|
250 260
....*....|....*....|....*..
gi 489310645 229 GLVEEQGSPQQVFENPLSARCKQFMSS 255
Cdd:COG3839 210 GRIQQVGTPEELYDRPANLFVAGFIGS 236
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
8-238 |
4.31e-70 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 214.92 E-value: 4.31e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRY-GELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEEL-KLKAakngelvaad 85
Cdd:COG2884 2 IRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLsRLKR---------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 86 gKQINRLRSEIGFVFQNFNLWPHMSVLDNIiEAPRRVLGQSKAEATEIAEALLAKVGISDKRHAYPAQLSGGQQQRAAIA 165
Cdd:COG2884 72 -REIPYLRRRIGVVFQDFRLLPDRTVYENV-ALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489310645 166 RTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHEMGFARQVSSEVVFLHQG-LVEEQGSPQ 238
Cdd:COG2884 150 RALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGrLVRDEARGV 223
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
8-229 |
4.48e-70 |
|
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: 213.20 E-value: 4.48e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVageelklkaakNGELVAADGK 87
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILI-----------DGEDLTDLED 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 88 QINRLRSEIGFVFQNFNLWPHMSVLDNIIEAprrvlgqskaeateiaeallakvgisdkrhaypaqLSGGQQQRAAIART 167
Cdd:cd03229 70 ELPPLRRRIGMVFQDFALFPHLTVLENIALG-----------------------------------LSGGQQQRVALARA 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489310645 168 LAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEE-GRTMLLVTHEMGFARQVSSEVVFLHQG 229
Cdd:cd03229 115 LAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
8-252 |
2.44e-69 |
|
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: 213.13 E-value: 2.44e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELklkaakngelVAADGK 87
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDI----------SGLSEA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 88 QINRLRSEIGFVFQNFNLWPHMSVLDNIiEAPRRVLGQ-SKAEATEIAEALLAKVGISDKRHAYPAQLSGGQQQRAAIAR 166
Cdd:cd03261 71 ELYRLRRRMGMLFQSGALFDSLTVFENV-AFPLREHTRlSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 167 TLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEE-GRTMLLVTHEMGFARQVSSEVVFLHQGLVEEQGSPQQVF--EN 243
Cdd:cd03261 150 ALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRasDD 229
|
....*....
gi 489310645 244 PlsaRCKQF 252
Cdd:cd03261 230 P---LVRQF 235
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
8-245 |
4.84e-69 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 211.95 E-value: 4.84e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRYG----ELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVageelklkaakngelva 83
Cdd:cd03293 1 LEVRNVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLV----------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 84 aDGKQINRLRSEIGFVFQNFNLWPHMSVLDNIiEAPRRVLGQSKAEATEIAEALLAKVGISDKRHAYPAQLSGGQQQRAA 163
Cdd:cd03293 64 -DGEPVTGPGPDRGYVFQQDALLPWLTVLDNV-ALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 164 IARTLAMQPKVILFDEPTSALDP----EMVQEVLNVIRalaEEGRTMLLVTHEMGFARQVSSEVVFLHQglveEQGSPQQ 239
Cdd:cd03293 142 LARALAVDPDVLLLDEPFSALDAltreQLQEELLDIWR---ETGKTVLLVTHDIDEAVFLADRVVVLSA----RPGRIVA 214
|
....*.
gi 489310645 240 VFENPL 245
Cdd:cd03293 215 EVEVDL 220
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
9-229 |
3.99e-68 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 209.25 E-value: 3.99e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 9 EIRNLHKRYGELE--VLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKlkaakngelvaadG 86
Cdd:cd03225 1 ELKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLT-------------K 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 87 KQINRLRSEIGFVFQN-----FNLwphmSVLDNIIEAPRRvLGQSKAEATEIAEALLAKVGISDKRHAYPAQLSGGQQQR 161
Cdd:cd03225 68 LSLKELRRKVGLVFQNpddqfFGP----TVEEEVAFGLEN-LGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQR 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489310645 162 AAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHEMGFARQVSSEVVFLHQG 229
Cdd:cd03225 143 VAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
8-235 |
2.66e-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: 207.74 E-value: 2.66e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRY----GELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELklkaakngelVA 83
Cdd:cd03257 2 LEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDL----------LK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 84 ADGKQINRLRSEIGFVFQN----FNlwPHMSVLDNIIEAPRRVLGQSKAEATEIAEALLA-KVGISDKR-HAYPAQLSGG 157
Cdd:cd03257 72 LSRRLRKIRRKEIQMVFQDpmssLN--PRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLvGVGLPEEVlNRYPHELSGG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489310645 158 QQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEE-GRTMLLVTHEMGFARQVSSEVVFLHQGLVEEQG 235
Cdd:cd03257 150 QRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-248 |
3.95e-67 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 208.35 E-value: 3.95e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 1 MAEATPALEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCIN----LLENPH-QGQILVAGEElklka 75
Cdd:COG1117 5 ASTLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNrmndLIPGARvEGEILLDGED----- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 76 akngelVAADGKQINRLRSEIGFVFQNFNLWPhMSVLDNIIEAPRRVLGQSKAEATEIAEALLAKVGI----SDKRHAYP 151
Cdd:COG1117 80 ------IYDPDVDVVELRRRVGMVFQKPNPFP-KSIYDNVAYGLRLHGIKSKSELDEIVEESLRKAALwdevKDRLKKSA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 152 AQLSGGQQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEgRTMLLVTHEMGFARQVSSEVVFLHQGLV 231
Cdd:COG1117 153 LGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD-YTIVIVTHNMQQAARVSDYTAFFYLGEL 231
|
250
....*....|....*..
gi 489310645 232 EEQGSPQQVFENPLSAR 248
Cdd:COG1117 232 VEFGPTEQIFTNPKDKR 248
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
8-240 |
7.10e-67 |
|
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: 206.65 E-value: 7.10e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLEN-----PHQGQILVAGEElklkaakngelV 82
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKD-----------I 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 83 AADGKQINRLRSEIGFVFQNFNLWPhMSVLDNIIEAPRRVLGQSKAEATEIAEALLAKVGISD--KRHAYPAQLSGGQQQ 160
Cdd:cd03260 70 YDLDVDVLELRRRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWDevKDRLHALGLSGGQQQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 161 RAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEgRTMLLVTHEMGFARQVSSEVVFLHQGLVEEQGSPQQV 240
Cdd:cd03260 149 RLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
8-245 |
1.47e-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: 206.44 E-value: 1.47e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRY----GELEVLKGISLTARDGDVISILGSSGSGKSTFLRCI-NLLENPHQ--GQILVAGEELklkaaknge 80
Cdd:COG0444 2 LEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAIlGLLPPPGItsGEILFDGEDL--------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 81 lVAADGKQINRLR-SEIGFVFQN----FNlwPHMSVLDNIIEAPRRVLGQSKAEATEIAEALLAKVGISDKR---HAYPA 152
Cdd:COG0444 73 -LKLSEKELRKIRgREIQMIFQDpmtsLN--PVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPDPErrlDRYPH 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 153 QLSGGQQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEE-GRTMLLVTHEMGFARQVSSEVVFLHQGLV 231
Cdd:COG0444 150 ELSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFITHDLGVVAEIADRVAVMYAGRI 229
|
250
....*....|....
gi 489310645 232 EEQGSPQQVFENPL 245
Cdd:COG0444 230 VEEGPVEELFENPR 243
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
7-257 |
1.97e-65 |
|
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: 203.88 E-value: 1.97e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 7 ALEIRNLHKRYGE----LEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKLKAAKngelv 82
Cdd:COG1124 1 MLEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRK----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 83 aadgkqinRLRSEIGFVFQN----FNlwPHMSVLDnIIEAPRRVLGQSKAEAtEIAEaLLAKVGISDK-RHAYPAQLSGG 157
Cdd:COG1124 76 --------AFRRRVQMVFQDpyasLH--PRHTVDR-ILAEPLRIHGLPDREE-RIAE-LLEQVGLPPSfLDRYPHQLSGG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 158 QQQRAAIARTLAMQPKVILFDEPTSALDPeMVQ-EVLNVIRAL-AEEGRTMLLVTHEMGFARQVSSEVVFLHQGLVEEQG 235
Cdd:COG1124 143 QRQRVAIARALILEPELLLLDEPTSALDV-SVQaEILNLLKDLrEERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEEL 221
|
250 260
....*....|....*....|..
gi 489310645 236 SPQQVFENPLSARCKQFMSSNR 257
Cdd:COG1124 222 TVADLLAGPKHPYTRELLAASL 243
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
8-240 |
1.59e-64 |
|
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: 201.26 E-value: 1.59e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRYGEL-EVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEEL-KLKaakngelvaad 85
Cdd:cd03256 1 IEVENLSKTYPNGkKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDInKLK----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 86 GKQINRLRSEIGFVFQNFNLWPHMSVLDNIIEA--PRRVLGQS-----KAEATEIAEALLAKVGISDKRHAYPAQLSGGQ 158
Cdd:cd03256 70 GKALRQLRRQIGMIFQQFNLIERLSVLENVLSGrlGRRSTWRSlfglfPKEEKQRALAALERVGLLDKAYQRADQLSGGQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 159 QQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALA-EEGRTMLLVTHEMGFARQVSSEVVFLHQGLVEEQGSP 237
Cdd:cd03256 150 QQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINrEEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPP 229
|
...
gi 489310645 238 QQV 240
Cdd:cd03256 230 AEL 232
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
8-244 |
3.84e-62 |
|
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: 194.96 E-value: 3.84e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEEL-KLKAAkngelvaadg 86
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDItGLPPH---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 87 kQINRLRseIGFVFQNFNLWPHMSVLDNIIEAPRRVLG---------QSKAEATEIAEALLAKVGISDKRHAYPAQLSGG 157
Cdd:cd03219 71 -EIARLG--IGRTFQIPRLFPELTVLENVMVAAQARTGsglllararREEREARERAEELLERVGLADLADRPAGELSYG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 158 QQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHEMGFARQVSSEVVFLHQGLVEEQGSP 237
Cdd:cd03219 148 QQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTP 227
|
....*..
gi 489310645 238 QQVFENP 244
Cdd:cd03219 228 DEVRNNP 234
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
7-253 |
4.34e-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: 194.87 E-value: 4.34e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 7 ALEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEelklkaakngelvaaDG 86
Cdd:cd03296 2 SIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGE---------------DA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 87 KQINRLRSEIGFVFQNFNLWPHMSVLDNI---IEAPRRVLGQSKAEATEIAEALLAKVGISDKRHAYPAQLSGGQQQRAA 163
Cdd:cd03296 67 TDVPVQERNVGFVFQHYALFRHMTVFDNVafgLRVKPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 164 IARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEE-GRTMLLVTHEMGFARQVSSEVVFLHQGLVEEQGSPQQVFE 242
Cdd:cd03296 147 LARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYD 226
|
250
....*....|.
gi 489310645 243 NPLSARCKQFM 253
Cdd:cd03296 227 HPASPFVYSFL 237
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
8-240 |
2.00e-61 |
|
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: 193.28 E-value: 2.00e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRYGE-LEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKlkaakngelvAADG 86
Cdd:TIGR02315 2 LEVENLSKVYPNgKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDIT----------KLRG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 87 KQINRLRSEIGFVFQNFNLWPHMSVLDNIIEAP-------RRVLGQSKAEATEIAEALLAKVGISDKRHAYPAQLSGGQQ 159
Cdd:TIGR02315 72 KKLRKLRRRIGMIFQHYNLIERLTVLENVLHGRlgykptwRSLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 160 QRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEE-GRTMLLVTHEMGFARQVSSEVVFLHQGLVEEQGSPQ 238
Cdd:TIGR02315 152 QRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEdGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPS 231
|
..
gi 489310645 239 QV 240
Cdd:TIGR02315 232 EL 233
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
5-244 |
2.80e-61 |
|
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: 200.90 E-value: 2.80e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 5 TPALEIRNLHKRY--GELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPH---QGQILVAGEELKlkaakng 79
Cdd:COG1123 2 TPLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLL------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 80 elvaadGKQINRLRSEIGFVFQNF--NLWPhMSVLDNIIEAPRRvLGQSKAEATEIAEALLAKVGISDKRHAYPAQLSGG 157
Cdd:COG1123 75 ------ELSEALRGRRIGMVFQDPmtQLNP-VTVGDQIAEALEN-LGLSRAEARARVLELLEAVGLERRLDRYPHQLSGG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 158 QQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRAL-AEEGRTMLLVTHEMGFARQVSSEVVFLHQGLVEEQGS 236
Cdd:COG1123 147 QRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELqRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGP 226
|
....*...
gi 489310645 237 PQQVFENP 244
Cdd:COG1123 227 PEEILAAP 234
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
7-241 |
4.10e-61 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 192.95 E-value: 4.10e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 7 ALEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEEL-KLKAakngelvaad 85
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLaSLSR---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 86 gKQINRLrseIGFVFQNFNLWPHMSVLDnIIE---AP-RRVLGQSKAEATEIAEALLAKVGISDKRHAYPAQLSGGQQQR 161
Cdd:COG1120 71 -RELARR---IAYVPQEPPAPFGLTVRE-LVAlgrYPhLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 162 AAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALA-EEGRTMLLVTHEMGFARQVSSEVVFLHQGLVEEQGSPQQV 240
Cdd:COG1120 146 VLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLArERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEV 225
|
.
gi 489310645 241 F 241
Cdd:COG1120 226 L 226
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
8-243 |
8.07e-61 |
|
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: 191.99 E-value: 8.07e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKlkaakngelvaadgK 87
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVR--------------K 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 88 QINRLRSEIGFVFQNFNLWPHMSVLDNIiEAPRRVLGQSKAEATEIAEALLAKVGISDKRHAYPAQLSGGQQQRAAIART 167
Cdd:COG4555 68 EPREARRQIGVLPDERGLYDRLTVRENI-RYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489310645 168 LAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHEMGFARQVSSEVVFLHQGLVEEQGSPQQVFEN 243
Cdd:COG4555 147 LVHDPKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREE 222
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
4-244 |
7.45e-60 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 189.86 E-value: 7.45e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 4 ATPALEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEEL-KLKAAkngelv 82
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDItGLPPH------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 83 aadgkQINRL---RSeigfvFQNFNLWPHMSVLDNIIEAPRRVLGQS--------------KAEATEIAEALLAKVGISD 145
Cdd:COG0411 75 -----RIARLgiaRT-----FQNPRLFPELTVLENVLVAAHARLGRGllaallrlprarreEREARERAEELLERVGLAD 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 146 KRHAYPAQLSGGQQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRAL-AEEGRTMLLVTHEMGFARQVSSEVV 224
Cdd:COG0411 145 RADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLrDERGITILLIEHDMDLVMGLADRIV 224
|
250 260
....*....|....*....|
gi 489310645 225 FLHQGLVEEQGSPQQVFENP 244
Cdd:COG0411 225 VLDFGRVIAEGTPAEVRADP 244
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
8-244 |
3.21e-59 |
|
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: 187.44 E-value: 3.21e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVageelklkaakngelvaaDGK 87
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILL------------------DGK 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 88 QINRL---RSEIGFVFQNFNLWPHMSVLDNIiEAPRRVLGQSKAEATEIAEALLAKVGISDKRHAYPAQLSGGQQQRAAI 164
Cdd:cd03300 63 DITNLpphKRPVNTVFQNYALFPHLTVFENI-AFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAI 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 165 ARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEE-GRTMLLVTHEMGFARQVSSEVVFLHQGLVEEQGSPQQVFEN 243
Cdd:cd03300 142 ARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEE 221
|
.
gi 489310645 244 P 244
Cdd:cd03300 222 P 222
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-241 |
6.48e-59 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 186.83 E-value: 6.48e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 1 MAeATPALEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKLKaaknge 80
Cdd:COG1121 1 MM-MMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 81 lvaadgkqinrlRSEIGFVFQNFNL---WPhMSVLDnIIE----APRRVLGQSKAEATEIAEALLAKVGISDKRHAYPAQ 153
Cdd:COG1121 74 ------------RRRIGYVPQRAEVdwdFP-ITVRD-VVLmgryGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 154 LSGGQQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHEMGFARQVSSEVVFLHQGLVEE 233
Cdd:COG1121 140 LSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLVAH 219
|
....*...
gi 489310645 234 qGSPQQVF 241
Cdd:COG1121 220 -GPPEEVL 226
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
8-257 |
1.58e-58 |
|
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: 185.97 E-value: 1.58e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRYGELE-VLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEelklkaakngelvaaDG 86
Cdd:cd03295 1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGE---------------DI 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 87 KQIN--RLRSEIGFVFQNFNLWPHMSVLDNIIEAPRrVLGQSKAEATEIAEALLAKVGISDK--RHAYPAQLSGGQQQRA 162
Cdd:cd03295 66 REQDpvELRRKIGYVIQQIGLFPHMTVEENIALVPK-LLKWPKEKIRERADELLALVGLDPAefADRYPHELSGGQQQRV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 163 AIARTLAMQPKVILFDEPTSALDP----EMVQEVLNVIRALaeeGRTMLLVTHEMGFARQVSSEVVFLHQGLVEEQGSPQ 238
Cdd:cd03295 145 GVARALAADPPLLLMDEPFGALDPitrdQLQEEFKRLQQEL---GKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPD 221
|
250
....*....|....*....
gi 489310645 239 QVFENPLSARCKQFMSSNR 257
Cdd:cd03295 222 EILRSPANDFVAEFVGADR 240
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
8-244 |
3.35e-58 |
|
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: 186.12 E-value: 3.35e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRYG-----ELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKLKaakngelv 82
Cdd:TIGR04521 1 IKLKNVSYIYQpgtpfEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAK-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 83 aaDGKQINRLRSEIGFVFQN-----FNLwphmSVLDNIIEAPRRvLGQSKAEATEIAEALLAKVGISDK-RHAYPAQLSG 156
Cdd:TIGR04521 73 --KKKKLKDLRKKVGLVFQFpehqlFEE----TVYKDIAFGPKN-LGLSEEEAEERVKEALELVGLDEEyLERSPFELSG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 157 GQQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALA-EEGRTMLLVTHEMGFARQVSSEVVFLHQGLVEEQG 235
Cdd:TIGR04521 146 GQMRRVAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHkEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDG 225
|
....*....
gi 489310645 236 SPQQVFENP 244
Cdd:TIGR04521 226 TPREVFSDV 234
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
9-257 |
1.01e-57 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 186.06 E-value: 1.01e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 9 EIRNLHKRYGEL-EVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKlkaakngelvaadGK 87
Cdd:COG1125 3 EFENVTKRYPDGtVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIR-------------DL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 88 QINRLRSEIGFVFQNFNLWPHMSVLDNIIEAPRrVLGQSKAEATEIAEALLAKVGISDK--RHAYPAQLSGGQQQRAAIA 165
Cdd:COG1125 70 DPVELRRRIGYVIQQIGLFPHMTVAENIATVPR-LLGWDKERIRARVDELLELVGLDPEeyRDRYPHELSGGQQQRVGVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 166 RTLAMQPKVILFDEPTSALDPeMVQEVL-NVIRALAEE-GRTMLLVTHEMGFARQVSSEVVFLHQGLVEEQGSPQQVFEN 243
Cdd:COG1125 149 RALAADPPILLMDEPFGALDP-ITREQLqDELLRLQRElGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILAN 227
|
250
....*....|....
gi 489310645 244 PLSARCKQFMSSNR 257
Cdd:COG1125 228 PANDFVADFVGADR 241
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
4-233 |
3.99e-57 |
|
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: 181.86 E-value: 3.99e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 4 ATPALEIRNLHKRY----GELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELklkaakng 79
Cdd:COG4181 5 SAPIIELRGLTKTVgtgaGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDL-------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 80 elVAADGKQINRLRSE-IGFVFQNFNLWPHMSVLDNI-IEAPRRvlgqSKAEATEIAEALLAKVGISDKRHAYPAQLSGG 157
Cdd:COG4181 77 --FALDEDARARLRARhVGFVFQSFQLLPTLTALENVmLPLELA----GRRDARARARALLERVGLGHRLDHYPAQLSGG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489310645 158 QQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEE-GRTMLLVTHEMGFARQvSSEVVFLHQGLVEE 233
Cdd:COG4181 151 EQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRErGTTLVLVTHDPALAAR-CDRVLRLRAGRLVE 226
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
6-247 |
1.28e-56 |
|
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: 184.47 E-value: 1.28e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 6 PALEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVageelklkaakngelvaaD 85
Cdd:TIGR03265 3 PYLSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQ------------------G 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 86 GKQINRL---RSEIGFVFQNFNLWPHMSVLDNIIEA--PRrvlGQSKAEATEIAEALLAKVGISDKRHAYPAQLSGGQQQ 160
Cdd:TIGR03265 65 GRDITRLppqKRDYGIVFQSYALFPNLTVADNIAYGlkNR---GMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 161 RAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEE-GRTMLLVTHEMGFARQVSSEVVFLHQGLVEEQGSPQQ 239
Cdd:TIGR03265 142 RVALARALATSPGLLLLDEPLSALDARVREHLRTEIRQLQRRlGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQE 221
|
....*...
gi 489310645 240 VFENPLSA 247
Cdd:TIGR03265 222 IYRHPATP 229
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
8-241 |
4.55e-56 |
|
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: 180.32 E-value: 4.55e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRY--GELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGeelklkaakngeLVAAD 85
Cdd:TIGR04520 1 IEVENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDG------------LDTLD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 86 GKQINRLRSEIGFVFQNfnlwPhmsvlDNIIEAPRrV----------LGQSKAEATEIAEALLAKVGISDKRHAYPAQLS 155
Cdd:TIGR04520 69 EENLWEIRKKVGMVFQN----P-----DNQFVGAT-VeddvafglenLGVPREEMRKRVDEALKLVGMEDFRDREPHLLS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 156 GGQQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRAL-AEEGRTMLLVTHEMGFARQvSSEVVFLHQGLVEEQ 234
Cdd:TIGR04520 139 GGQKQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLnKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVAE 217
|
....*..
gi 489310645 235 GSPQQVF 241
Cdd:TIGR04520 218 GTPREIF 224
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
8-229 |
4.82e-56 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 178.47 E-value: 4.82e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELklkaakngelvaaDGK 87
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPL-------------SAM 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 88 QINRLRSEIGFVFQNFNLWPhMSVLDNIIEAPRRvlgQSKAEATEIAEALLAKVGIS----DKRhayPAQLSGGQQQRAA 163
Cdd:COG4619 68 PPPEWRRQVAYVPQEPALWG-GTVRDNLPFPFQL---RERKFDRERALELLERLGLPpdilDKP---VERLSGGERQRLA 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489310645 164 IARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRAL-AEEGRTMLLVTHEMGFARQVSSEVVFLHQG 229
Cdd:COG4619 141 LIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYlAEEGRAVLWVSHDPEQIERVADRVLTLEAG 207
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
8-229 |
9.02e-56 |
|
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: 176.43 E-value: 9.02e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKlkaakngelvaadgK 87
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIK--------------K 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 88 QINRLRSEIGFVFQNFNLWPHMSVLDNIieaprrvlgqskaeateiaeallakvgisdkrhaypaQLSGGQQQRAAIART 167
Cdd:cd03230 67 EPEEVKRRIGYLPEEPSLYENLTVRENL-------------------------------------KLSGGMKQRLALAQA 109
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489310645 168 LAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHEMGFARQVSSEVVFLHQG 229
Cdd:cd03230 110 LLHDPELLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNG 171
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
8-229 |
1.37e-55 |
|
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: 177.44 E-value: 1.37e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRY-GELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKlkaakngelvAADG 86
Cdd:TIGR02673 2 IEFHNVSKAYpGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVN----------RLRG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 87 KQINRLRSEIGFVFQNFNLWPHMSVLDNIiEAPRRVLGQSKAEATEIAEALLAKVGISDKRHAYPAQLSGGQQQRAAIAR 166
Cdd:TIGR02673 72 RQLPLLRRRIGVVFQDFRLLPDRTVYENV-ALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIAR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489310645 167 TLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHEMGFARQVSSEVVFLHQG 229
Cdd:TIGR02673 151 AIVNSPPLLLADEPTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLSLVDRVAHRVIILDDG 213
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
13-252 |
2.79e-54 |
|
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: 175.91 E-value: 2.79e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 13 LHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKlkaakngelvAADGKQINRL 92
Cdd:cd03294 30 ILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIA----------AMSRKELREL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 93 RSE-IGFVFQNFNLWPHMSVLDNIiEAPRRVLGQSKAEATEIAEALLAKVGISDKRHAYPAQLSGGQQQRAAIARTLAMQ 171
Cdd:cd03294 100 RRKkISMVFQSFALLPHRTVLENV-AFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVD 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 172 PKVILFDEPTSALDP----EMVQEVLnviRALAEEGRTMLLVTHEMGFARQVSSEVVFLHQGLVEEQGSPQQVFENPLSA 247
Cdd:cd03294 179 PDILLMDEAFSALDPlirrEMQDELL---RLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPAND 255
|
....*
gi 489310645 248 RCKQF 252
Cdd:cd03294 256 YVREF 260
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
8-240 |
1.34e-53 |
|
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: 172.62 E-value: 1.34e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELklkAAKNGELVAADGk 87
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDI---TGLPPHERARAG- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 88 qinrlrseIGFVFQNFNLWPHMSVLDNIiEAPRRVLGQSKAEATeIAEAL-----LAkvgisDKRHAYPAQLSGGQQQRA 162
Cdd:cd03224 77 --------IGYVPEGRRIFPELTVEENL-LLGAYARRRAKRKAR-LERVYelfprLK-----ERRKQLAGTLSGGEQQML 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489310645 163 AIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHEMGFARQVSSEVVFLHQGLVEEQGSPQQV 240
Cdd:cd03224 142 AIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-244 |
6.99e-53 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 175.52 E-value: 6.99e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 1 MAEATPALEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELklkaakNGe 80
Cdd:PRK09452 8 PSSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDI------TH- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 81 lVAADGKQINRlrseigfVFQNFNLWPHMSVLDNIIEAprrvLGQSKAEATEIA----EAlLAKVGISDKRHAYPAQLSG 156
Cdd:PRK09452 81 -VPAENRHVNT-------VFQSYALFPHMTVFENVAFG----LRMQKTPAAEITprvmEA-LRMVQLEEFAQRKPHQLSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 157 GQQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEE-GRTMLLVTHEMGFARQVSSEVVFLHQGLVEEQG 235
Cdd:PRK09452 148 GQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDG 227
|
....*....
gi 489310645 236 SPQQVFENP 244
Cdd:PRK09452 228 TPREIYEEP 236
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
2-244 |
2.19e-52 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 177.95 E-value: 2.19e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 2 AEATPALEIRNLHKRY-----------GELEVLKGISLTARDGDVISILGSSGSGKSTFLRCI-NLLenPHQGQILVAGE 69
Cdd:COG4172 270 PDAPPLLEARDLKVWFpikrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALlRLI--PSEGEIRFDGQ 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 70 ELklkaakngelVAADGKQINRLRSEIGFVFQN----FNlwPHMSVLDnIIEAPRRVL--GQSKAEATEIAEALLAKVGI 143
Cdd:COG4172 348 DL----------DGLSRRALRPLRRRMQVVFQDpfgsLS--PRMTVGQ-IIAEGLRVHgpGLSAAERRARVAEALEEVGL 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 144 S-DKRHAYPAQLSGGQQQRAAIARTLAMQPKVILFDEPTSALDpeM-VQ-EVLNVIRAL-AEEGRTMLLVTHEMGFARQV 219
Cdd:COG4172 415 DpAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALD--VsVQaQILDLLRDLqREHGLAYLFISHDLAVVRAL 492
|
250 260
....*....|....*....|....*
gi 489310645 220 SSEVVFLHQGLVEEQGSPQQVFENP 244
Cdd:COG4172 493 AHRVMVMKDGKVVEQGPTEQVFDAP 517
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
8-256 |
3.98e-52 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 169.44 E-value: 3.98e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRYGELEvLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVageelklkaakngelvaaDGK 87
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILL------------------NGK 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 88 QINRLRSE---IGFVFQNFNLWPHMSVLDNI-----------IEAPRRVLgqskaeatEIAEALlakvGISDKRHAYPAQ 153
Cdd:cd03299 62 DITNLPPEkrdISYVPQNYALFPHMTVYKNIayglkkrkvdkKEIERKVL--------EIAEML----GIDHLLNRKPET 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 154 LSGGQQQRAAIARTLAMQPKVILFDEPTSALDP---EMVQEVLNVIRalAEEGRTMLLVTHEMGFARQVSSEVVFLHQGL 230
Cdd:cd03299 130 LSGGEQQRVAIARALVVNPKILLLDEPFSALDVrtkEKLREELKKIR--KEFGVTVLHVTHDFEEAWALADKVAIMLNGK 207
|
250 260
....*....|....*....|....*.
gi 489310645 231 VEEQGSPQQVFENPLSARCKQFMSSN 256
Cdd:cd03299 208 LIQVGKPEEVFKKPKNEFVAEFLGFN 233
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
8-253 |
1.44e-51 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 171.44 E-value: 1.44e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKLKAAKNgelvaadgk 87
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQ--------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 88 qinrlrSEIGFVFQNFNLWPHMSVLDNIiEAPRRVLGQSKAE-ATEIAEAL----LAkvGISDKrhaYPAQLSGGQQQRA 162
Cdd:PRK11432 78 ------RDICMVFQSYALFPHMSLGENV-GYGLKMLGVPKEErKQRVKEALelvdLA--GFEDR---YVDQISGGQQQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 163 AIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEE-GRTMLLVTHEMGFARQVSSEVVFLHQGLVEEQGSPQQVF 241
Cdd:PRK11432 146 ALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELY 225
|
250
....*....|..
gi 489310645 242 ENPLSARCKQFM 253
Cdd:PRK11432 226 RQPASRFMASFM 237
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
7-254 |
2.49e-51 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 171.03 E-value: 2.49e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 7 ALEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKLKAAKNgelvaadg 86
Cdd:PRK10851 2 SIEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD-------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 87 kqinrlrSEIGFVFQNFNLWPHMSVLDNIIEA----PRRVLgQSKAEATEIAEALLAKVGISDKRHAYPAQLSGGQQQRA 162
Cdd:PRK10851 74 -------RKVGFVFQHYALFRHMTVFDNIAFGltvlPRRER-PNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 163 AIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGR-TMLLVTHEMGFARQVSSEVVFLHQGLVEEQGSPQQVF 241
Cdd:PRK10851 146 ALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKfTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVW 225
|
250
....*....|...
gi 489310645 242 ENPLSARCKQFMS 254
Cdd:PRK10851 226 REPATRFVLEFMG 238
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
4-244 |
2.78e-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: 174.87 E-value: 2.78e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 4 ATPALEIRNLHKRYG----ELEVLKGISLTARDGDVISILGSSGSGKS-TFLRCINLLENPH---QGQILVAGEELklka 75
Cdd:COG4172 3 SMPLLSVEDLSVAFGqgggTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILRLLPDPAahpSGSILFDGQDL---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 76 akngelVAADGKQINRLR-SEIGFVFQ------NfnlwPHMSVLDNIIEAPRRVLGQSKAEATEIAEALLAKVGISDKR- 147
Cdd:COG4172 79 ------LGLSERELRRIRgNRIAMIFQepmtslN----PLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGIPDPEr 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 148 --HAYPAQLSGGQQQRAAIARTLAMQPKVILFDEPTSALDPeMVQ-EVLNVIRAL-AEEGRTMLLVTHEMGFARQVSSEV 223
Cdd:COG4172 149 rlDAYPHQLSGGQRQRVMIAMALANEPDLLIADEPTTALDV-TVQaQILDLLKDLqRELGMALLLITHDLGVVRRFADRV 227
|
250 260
....*....|....*....|.
gi 489310645 224 VFLHQGLVEEQGSPQQVFENP 244
Cdd:COG4172 228 AVMRQGEIVEQGPTAELFAAP 248
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
10-226 |
2.79e-51 |
|
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: 166.25 E-value: 2.79e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 10 IRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEE-LKLKAAKNGELvaadgkq 88
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQEtPPLNSKKASKF------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 89 inrLRSEIGFVFQNFNLWPHMSVLDNIiEAPRRVLGQSKAEATEIAEALLAKVGISDKRHAYPAQLSGGQQQRAAIARTL 168
Cdd:TIGR03608 74 ---RREKLGYLFQNFALIENETVEENL-DLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489310645 169 AMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHEMGFARQvSSEVVFL 226
Cdd:TIGR03608 150 LKPPPLILADEPTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHDPEVAKQ-ADRVIEL 206
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
5-244 |
9.37e-51 |
|
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: 165.93 E-value: 9.37e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 5 TPALEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEEL-KLKAAKngelVA 83
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDItGLPPHR----IA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 84 ADGkqinrlrseIGFVFQNFNLWPHMSVLDNIiEAPRRVLGQSKAEATEIAEAL-----LAkvgisDKRHAYPAQLSGGQ 158
Cdd:COG0410 77 RLG---------IGYVPEGRRIFPSLTVEENL-LLGAYARRDRAEVRADLERVYelfprLK-----ERRRQRAGTLSGGE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 159 QQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHEMGFARQVSSEVVFLHQGLVEEQGSPQ 238
Cdd:COG0410 142 QQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAA 221
|
....*.
gi 489310645 239 QVFENP 244
Cdd:COG0410 222 ELLADP 227
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
8-235 |
9.56e-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: 165.12 E-value: 9.56e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVageelklkaakngelvaaDGK 87
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYI------------------GGR 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 88 QINRLRSE---IGFVFQNFNLWPHMSVLDNiIEAPRRVLGQSKAEATEIAEALLAKVGISDKRHAYPAQLSGGQQQRAAI 164
Cdd:cd03301 63 DVTDLPPKdrdIAMVFQNYALYPHMTVYDN-IAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVAL 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489310645 165 ARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEE-GRTMLLVTHEMGFARQVSSEVVFLHQGLVEEQG 235
Cdd:cd03301 142 GRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
8-253 |
1.35e-50 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 165.31 E-value: 1.35e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRYGELevLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEEL-KLKAAKngelvaadg 86
Cdd:COG3840 2 LRLDDLTYRYGDF--PLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLtALPPAE--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 87 kqinRLRSeigFVFQNFNLWPHMSVLDNIIEAPRRVLGQSKAEATEIAEALlAKVGISDKRHAYPAQLSGGQQQRAAIAR 166
Cdd:COG3840 71 ----RPVS---MLFQENNLFPHLTVAQNIGLGLRPGLKLTAEQRAQVEQAL-ERVGLAGLLDRLPGQLSGGQRQRVALAR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 167 TLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEE-GRTMLLVTHEMGFARQVSSEVVFLHQGLVEEQGSPQQVFENPL 245
Cdd:COG3840 143 CLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRErGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEP 222
|
....*...
gi 489310645 246 SARCKQFM 253
Cdd:COG3840 223 PPALAAYL 230
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
5-211 |
2.40e-50 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 169.13 E-value: 2.40e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 5 TPALEIRNLHKRYG-------EL--------EVLK---------GISLTARDGDVISILGSSGSGKSTFLRCINLLENPH 60
Cdd:COG4175 1 MPKIEVRNLYKIFGkrperalKLldqgkskdEILEktgqtvgvnDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 61 QGQILVAGEELklkaakngelVAADGKQINRLRSE-IGFVFQNFNLWPHMSVLDNIiEAPRRVLGQSKAEATEIAEALLA 139
Cdd:COG4175 81 AGEVLIDGEDI----------TKLSKKELRELRRKkMSMVFQHFALLPHRTVLENV-AFGLEIQGVPKAERRERAREALE 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489310645 140 KVGISDKRHAYPAQLSGGQQQRAAIARTLAMQPKVILFDEPTSALDP----EMVQEVLnvirAL-AEEGRTMLLVTH 211
Cdd:COG4175 150 LVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPlirrEMQDELL----ELqAKLKKTIVFITH 222
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
9-231 |
5.38e-50 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 163.09 E-value: 5.38e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 9 EIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVageelklkaakngelvaaDGKQ 88
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRV------------------FGKP 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 89 INRLRSEIGFVFQNFNL---WPhMSVLDNI---IEAPRRVLGQSKAEATEIAEALLAKVGISDKRHAYPAQLSGGQQQRA 162
Cdd:cd03235 63 LEKERKRIGYVPQRRSIdrdFP-ISVRDVVlmgLYGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRV 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489310645 163 AIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHEMGFARQVSSEVVFLHQGLV 231
Cdd:cd03235 142 LLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLNRTVV 210
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-245 |
6.74e-50 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 166.45 E-value: 6.74e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 1 MAEATPALEIRNLHKRY--------GELEVLK---GISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGE 69
Cdd:COG4608 1 AAMAEPLLEVRDLKKHFpvrgglfgRTVGVVKavdGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 70 ELklkaakngelVAADGKQINRLRSEIGFVFQN----FNlwPHMSVLDnIIEAPRRVLGQ-SKAEATEIAEALLAKVGIs 144
Cdd:COG4608 81 DI----------TGLSGRELRPLRRRMQMVFQDpyasLN--PRMTVGD-IIAEPLRIHGLaSKAERRERVAELLELVGL- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 145 DKRHA--YPAQLSGGQQQRAAIARTLAMQPKVILFDEPTSALDPEmVQ-EVLNVIRALAEE-GRTMLLVTHEMGFARQVS 220
Cdd:COG4608 147 RPEHAdrYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVS-IQaQVLNLLEDLQDElGLTYLFISHDLSVVRHIS 225
|
250 260
....*....|....*....|....*
gi 489310645 221 SEVVFLHQGLVEEQGSPQQVFENPL 245
Cdd:COG4608 226 DRVAVMYLGKIVEIAPRDELYARPL 250
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
9-229 |
4.61e-49 |
|
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: 158.95 E-value: 4.61e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 9 EIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKLKAAKngelvaadgkq 88
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLE----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 89 inRLRSEIGFVFQnfnlwphmsvldniieaprrvlgqskaeateiaeallakvgisdkrhaypaqLSGGQQQRAAIARTL 168
Cdd:cd00267 70 --ELRRRIGYVPQ----------------------------------------------------LSGGQRQRVALARAL 95
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489310645 169 AMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHEMGFARQVSSEVVFLHQG 229
Cdd:cd00267 96 LLNPDLLLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
9-229 |
4.92e-49 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 159.52 E-value: 4.92e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 9 EIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKlkaakngelvAADGKQ 88
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLA----------SLSPKE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 89 INRLrseIGFVFQnfnlwphmsvldniieaprrvlgqskaeateiaeaLLAKVGISDKRHAYPAQLSGGQQQRAAIARTL 168
Cdd:cd03214 71 LARK---IAYVPQ-----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARAL 112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489310645 169 AMQPKVILFDEPTSALDPEMVQEVLNVIRALA-EEGRTMLLVTHEMGFARQVSSEVVFLHQG 229
Cdd:cd03214 113 AQEPPILLLDEPTSHLDIAHQIELLELLRRLArERGKTVVMVLHDLNLAARYADRVILLKDG 174
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
8-239 |
7.32e-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: 155.36 E-value: 7.32e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRYGELE--VLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKlkaakngelvaad 85
Cdd:cd03263 1 LQIRNLTKTYKKGTkpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 86 gKQINRLRSEIGFVFQNFNLWPHMSVLDNI-IEAprRVLGQSKAEATEIAEALLAKVGISDKRHAYPAQLSGGQQQRAAI 164
Cdd:cd03263 68 -TDRKAARQSLGYCPQFDALFDELTVREHLrFYA--RLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489310645 165 ARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAeEGRTMLLVTHEMGFARQVSSEVVFLHQGLVEEQGSPQQ 239
Cdd:cd03263 145 AIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVR-KGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQE 218
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
8-231 |
9.63e-47 |
|
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: 154.87 E-value: 9.63e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRY-GELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEEL-KLKaakngelvaad 85
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVsDLR----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 86 GKQINRLRSEIGFVFQNFNLWPHMSVLDNIIeAPRRVLGQSKAEATEIAEALLAKVGISDKRHAYPAQLSGGQQQRAAIA 165
Cdd:cd03292 70 GRAIPYLRRKIGVVFQDFRLLPDRNVYENVA-FALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489310645 166 RTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHEMGFARQVSSEVVFLHQGLV 231
Cdd:cd03292 149 RAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
23-182 |
3.90e-46 |
|
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: 151.26 E-value: 3.90e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 23 LKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELklkaakngelvaaDGKQINRLRSEIGFVFQN 102
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDL-------------TDDERKSLRKEIGYVFQD 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 103 FNLWPHMSVLDNIIEaPRRVLGQSKAEATEIAEALLAKVGISDKRH----AYPAQLSGGQQQRAAIARTLAMQPKVILFD 178
Cdd:pfam00005 68 PQLFPRLTVRENLRL-GLLLKGLSKREKDARAEEALEKLGLGDLADrpvgERPGTLSGGQRQRVAIARALLTKPKLLLLD 146
|
....
gi 489310645 179 EPTS 182
Cdd:pfam00005 147 EPTA 150
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
8-211 |
5.16e-46 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 153.34 E-value: 5.16e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRYG----ELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELklkaakngeLVA 83
Cdd:NF038007 2 LNMQNAEKCYItktiKTKVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEV---------TNL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 84 ADGKQINRLRSEIGFVFQNFNLWPHMSVLDNIiEAPRRVLGQSKAEATEIAEALLAKVGISDKRHAYPAQLSGGQQQRAA 163
Cdd:NF038007 73 SYSQKIILRRELIGYIFQSFNLIPHLSIFDNV-ALPLKYRGVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489310645 164 IARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTH 211
Cdd:NF038007 152 IARAMVSNPALLLADEPTGNLDSKNARAVLQQLKYINQKGTTIIMVTH 199
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
7-244 |
7.39e-46 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 153.84 E-value: 7.39e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 7 ALEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLEnphqgqilvageELKLKAAKNGElVAADG 86
Cdd:PRK14267 4 AIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLL------------ELNEEARVEGE-VRLFG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 87 KQIN-------RLRSEIGFVFQNFNLWPHMSVLDNI-IEAPRRVLGQSKAEATEIAEALLAKVG----ISDKRHAYPAQL 154
Cdd:PRK14267 71 RNIYspdvdpiEVRREVGMVFQYPNPFPHLTIYDNVaIGVKLNGLVKSKKELDERVEWALKKAAlwdeVKDRLNDYPSNL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 155 SGGQQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEgRTMLLVTHEMGFARQVSSEVVFLHQGLVEEQ 234
Cdd:PRK14267 151 SGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLGKLIEV 229
|
250
....*....|
gi 489310645 235 GSPQQVFENP 244
Cdd:PRK14267 230 GPTRKVFENP 239
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
6-244 |
8.76e-46 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 153.78 E-value: 8.76e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 6 PALEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLE--NPhqgQILVAGEelklkAAKNGELVA 83
Cdd:PRK14239 4 PILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNdlNP---EVTITGS-----IVYNGHNIY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 84 ADGKQINRLRSEIGFVFQNFNLWPhMSVLDNIIEAPRRVLGQSKAEATEIAEALLAKVGI----SDKRHAYPAQLSGGQQ 159
Cdd:PRK14239 76 SPRTDTVDLRKEIGMVFQQPNPFP-MSIYENVVYGLRLKGIKDKQVLDEAVEKSLKGASIwdevKDRLHDSALGLSGGQQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 160 QRAAIARTLAMQPKVILFDEPTSALDP---EMVQEVLNVIRalaeEGRTMLLVTHEMGFARQVSSEVVFLHQGLVEEQGS 236
Cdd:PRK14239 155 QRVCIARVLATSPKIILLDEPTSALDPisaGKIEETLLGLK----DDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYND 230
|
....*...
gi 489310645 237 PQQVFENP 244
Cdd:PRK14239 231 TKQMFMNP 238
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
5-218 |
1.56e-45 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 161.43 E-value: 1.56e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 5 TPALEIRNLHKRY----GELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELklkaaknge 80
Cdd:PRK10535 2 TALLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDV--------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 81 lVAADGKQINRLRSE-IGFVFQNFNLWPHMSVLDNIiEAPRRVLGQSKAEATEIAEALLAKVGISDKRHAYPAQLSGGQQ 159
Cdd:PRK10535 73 -ATLDADALAQLRREhFGFIFQRYHLLSHLTAAQNV-EVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQ 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489310645 160 QRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHEMGFARQ 218
Cdd:PRK10535 151 QRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQ 209
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
6-242 |
3.31e-45 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 160.77 E-value: 3.31e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 6 PALEIRNLHKRYGELE--VLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKlkaakngelva 83
Cdd:COG2274 472 GDIELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLR----------- 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 84 adgkQINR--LRSEIGFVFQNFNLWpHMSVLDNIieaprrVLGQSKAEATEIAEALlAKVGISD--KRHayP-------- 151
Cdd:COG2274 541 ----QIDPasLRRQIGVVLQDVFLF-SGTIRENI------TLGDPDATDEEIIEAA-RLAGLHDfiEAL--Pmgydtvvg 606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 152 ---AQLSGGQQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAeEGRTMLLVTHEMGFARQVsSEVVFLHQ 228
Cdd:COG2274 607 eggSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLL-KGRTVIIIAHRLSTIRLA-DRIIVLDK 684
|
250
....*....|....
gi 489310645 229 GLVEEQGSPQQVFE 242
Cdd:COG2274 685 GRIVEDGTHEELLA 698
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-255 |
1.23e-44 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 150.96 E-value: 1.23e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 1 MAEATPALEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLeNPHQGQILVAGeelklKAAKNGE 80
Cdd:PRK14258 1 MSKLIPAIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRM-NELESEVRVEG-----RVEFFNQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 81 LVAADGKQINRLRSEIGFVFQNFNLWPhMSVLDNIIEAPRRVLGQSKAEATEIAEALLAKVGISD----KRHAYPAQLSG 156
Cdd:PRK14258 75 NIYERRVNLNRLRRQVSMVHPKPNLFP-MSVYDNVAYGVKIVGWRPKLEIDDIVESALKDADLWDeikhKIHKSALDLSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 157 GQQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGR-TMLLVTHEMGFARQVSSEVVFLHQ-----GL 230
Cdd:PRK14258 154 GQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSElTMVIVSHNLHQVSRLSDFTAFFKGnenriGQ 233
|
250 260
....*....|....*....|....*
gi 489310645 231 VEEQGSPQQVFENPLSARCKQFMSS 255
Cdd:PRK14258 234 LVEFGLTKKIFNSPHDSRTREYVLS 258
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
15-257 |
1.48e-44 |
|
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: 153.47 E-value: 1.48e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 15 KRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELklkaakngeLVAADGKQINRLRS 94
Cdd:TIGR01186 1 KKTGGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENI---------MKQSPVELREVRRK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 95 EIGFVFQNFNLWPHMSVLDNIIEAPRrVLGQSKAEATEIAEALLAKVGISDKRHAYPAQLSGGQQQRAAIARTLAMQPKV 174
Cdd:TIGR01186 72 KIGMVFQQFALFPHMTILQNTSLGPE-LLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 175 ILFDEPTSALDP----EMVQEVLNVIRALaeeGRTMLLVTHEMGFARQVSSEVVFLHQGLVEEQGSPQQVFENPLSARCK 250
Cdd:TIGR01186 151 LLMDEAFSALDPlirdSMQDELKKLQATL---QKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVE 227
|
....*..
gi 489310645 251 QFMSSNR 257
Cdd:TIGR01186 228 EFIGKVD 234
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
6-244 |
2.16e-44 |
|
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: 152.95 E-value: 2.16e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 6 PALEIRnLHKRYG--ELEVlkgiSLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVageelklkaakNGELVA 83
Cdd:COG4148 1 MMLEVD-FRLRRGgfTLDV----DFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRL-----------GGEVLQ 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 84 ADGKQINRL--RSEIGFVFQNFNLWPHMSVLDNIIEAPRRV-LGQSKAEATEIAEALlakvGISDKRHAYPAQLSGGQQQ 160
Cdd:COG4148 65 DSARGIFLPphRRRIGYVFQEARLFPHLSVRGNLLYGRKRApRAERRISFDEVVELL----GIGHLLDRRPATLSGGERQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 161 RAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRT-MLLVTHEMGFARQVSSEVVFLHQGLVEEQGSPQQ 239
Cdd:COG4148 141 RVAIGRALLSSPRLLLMDEPLAALDLARKAEILPYLERLRDELDIpILYVSHSLDEVARLADHVVLLEQGRVVASGPLAE 220
|
....*
gi 489310645 240 VFENP 244
Cdd:COG4148 221 VLSRP 225
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
6-212 |
4.45e-44 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 147.63 E-value: 4.45e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 6 PALEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKlkaakngelvaad 85
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIR------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 86 gKQINRLRSEIGFVFQNFNLWPHMSVLDNIiEAPRRVLGQSKAEATeiAEALLAKVGISDKRHAYPAQLSGGQQQRAAIA 165
Cdd:COG4133 68 -DAREDYRRRLAYLGHADGLKPELTVRENL-RFWAALYGLRADREA--IDEALEAVGLAGLADLPVRQLSAGQKRRVALA 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489310645 166 RTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHE 212
Cdd:COG4133 144 RLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQ 190
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
7-240 |
7.97e-44 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 149.87 E-value: 7.97e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 7 ALEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKlkaakngelvAADG 86
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD----------PEDR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 87 KQINRLRSEIGfvfqnfnLWPHMSVLDNIIeaprrVLGQ----SKAEATEIAEALLAKVGISDKRHAYPAQLSGGQQQRA 162
Cdd:COG4152 71 RRIGYLPEERG-------LYPKMKVGEQLV-----YLARlkglSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKV 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489310645 163 AIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHEMGFARQVSSEVVFLHQGLVEEQGSPQQV 240
Cdd:COG4152 139 QLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI 216
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
8-243 |
9.22e-44 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 149.85 E-value: 9.22e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRYG-----ELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQI-LVAGEELKLKAAKNGEL 81
Cdd:PRK13651 3 IKVKNIVKIFNkklptELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIeWIFKDEKNKKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 82 VAADG----------KQINRLRSEIGFVFQ--NFNLWpHMSVLDNIIEAPRRvLGQSKAEATEIAEALLAKVGISD---K 146
Cdd:PRK13651 83 VLEKLviqktrfkkiKKIKEIRRRVGVVFQfaEYQLF-EQTIEKDIIFGPVS-MGVSKEEAKKRAAKYIELVGLDEsylQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 147 RHayPAQLSGGQQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHEMGFARQVSSEVVFL 226
Cdd:PRK13651 161 RS--PFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFF 238
|
250
....*....|....*..
gi 489310645 227 HQGLVEEQGSPQQVFEN 243
Cdd:PRK13651 239 KDGKIIKDGDTYDILSD 255
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
8-229 |
9.31e-44 |
|
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: 145.60 E-value: 9.31e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRYG--ELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKlkaakngelvaad 85
Cdd:cd03228 1 IEFKNVSFSYPgrPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLR------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 86 gkQINR--LRSEIGFVFQNFNLWpHMSVLDNIieaprrvlgqskaeateiaeallakvgisdkrhaypaqLSGGQQQRAA 163
Cdd:cd03228 68 --DLDLesLRKNIAYVPQDPFLF-SGTIRENI--------------------------------------LSGGQRQRIA 106
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489310645 164 IARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAeEGRTMLLVTHEMGFARQVsSEVVFLHQG 229
Cdd:cd03228 107 IARALLRDPPILILDEATSALDPETEALILEALRALA-KGKTVIVIAHRLSTIRDA-DRIIVLDDG 170
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-213 |
1.04e-43 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 154.02 E-value: 1.04e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 4 ATPALEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKLK----AAKNG 79
Cdd:COG1129 1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRsprdAQAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 80 elvaadgkqinrlrseIGFVFQNFNLWPHMSVLDNII--EAPRRVLGQSKAEATEIAEALLAKVGISDKRHAYPAQLSGG 157
Cdd:COG1129 81 ----------------IAIIHQELNLVPNLSVAENIFlgREPRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVA 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489310645 158 QQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHEM 213
Cdd:COG1129 145 QQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRL 200
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
6-211 |
1.19e-43 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 148.47 E-value: 1.19e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 6 PALEIRNLHKRYG----ELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVageelklkaakngel 81
Cdd:COG4525 2 SMLTVRHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITL--------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 82 vaaDGKQINRLRSEIGFVFQNFNLWPHMSVLDNIiEAPRRVLGQSKAEATEIAEALLAKVGISDKRHAYPAQLSGGQQQR 161
Cdd:COG4525 67 ---DGVPVTGPGADRGVVFQKDALLPWLNVLDNV-AFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQR 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489310645 162 AAIARTLAMQPKVILFDEPTSALDP---EMVQEVLnvIRALAEEGRTMLLVTH 211
Cdd:COG4525 143 VGIARALAADPRFLLMDEPFGALDAltrEQMQELL--LDVWQRTGKGVFLITH 193
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
5-226 |
1.45e-43 |
|
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: 147.20 E-value: 1.45e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 5 TPALEIRNLHKRY-------GELEVLKGISLTARDGDVISILGSSGSGKSTFLRCI--NLLenPHQGQILV--AGEELkl 73
Cdd:COG4778 2 TTLLEVENLSKTFtlhlqggKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIygNYL--PDSGSILVrhDGGWV-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 74 kaakngELVAADGKQINRLR-SEIGFVFQNFNLWPHMSVLDnIIEAPRRVLGQSKAEATEIAEALLAKVGISDKR-HAYP 151
Cdd:COG4778 78 ------DLAQASPREILALRrRTIGYVSQFLRVIPRVSALD-VVAEPLLERGVDREEARARARELLARLNLPERLwDLPP 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489310645 152 AQLSGGQQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHEMGFARQVSSEVVFL 226
Cdd:COG4778 151 ATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDV 225
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
4-255 |
1.45e-43 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 151.14 E-value: 1.45e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 4 ATPALEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELklkaakngelva 83
Cdd:PRK11607 16 LTPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDL------------ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 84 adgKQINRLRSEIGFVFQNFNLWPHMSVLDNIIEAprrvLGQSKAEATEIA---EALLAKVGISDKRHAYPAQLSGGQQQ 160
Cdd:PRK11607 84 ---SHVPPYQRPINMMFQSYALFPHMTVEQNIAFG----LKQDKLPKAEIAsrvNEMLGLVHMQEFAKRKPHQLSGGQRQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 161 RAAIARTLAMQPKVILFDEPTSALDPEMVQEV-LNVIRALAEEGRTMLLVTHEMGFARQVSSEVVFLHQGLVEEQGSPQQ 239
Cdd:PRK11607 157 RVALARSLAKRPKLLLLDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEE 236
|
250
....*....|....*.
gi 489310645 240 VFENPLSARCKQFMSS 255
Cdd:PRK11607 237 IYEHPTTRYSAEFIGS 252
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
8-244 |
4.54e-43 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 147.15 E-value: 4.54e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRYGE-LEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKLkaakngelvaaDG 86
Cdd:PRK13639 2 LETRDLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKY-----------DK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 87 KQINRLRSEIGFVFQNfnlwPhmsvlDNIIEAPRRV---------LGQSKAEATEIAEALLAKVGISDKRHAYPAQLSGG 157
Cdd:PRK13639 71 KSLLEVRKTVGIVFQN----P-----DDQLFAPTVEedvafgplnLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 158 QQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHEMGFARQVSSEVVFLHQGLVEEQGSP 237
Cdd:PRK13639 142 QKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTP 221
|
....*..
gi 489310645 238 QQVFENP 244
Cdd:PRK13639 222 KEVFSDI 228
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
8-244 |
9.95e-43 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 147.69 E-value: 9.95e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLH-----KRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKLKAAKNGELV 82
Cdd:PRK13631 22 LRVKNLYcvfdeKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHELIT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 83 AADGKQIN---RLRSEIGFVFQnfnlWPHMSVLDNIIE-----APRrVLGQSKAEATEIAEALLAKVGI-SDKRHAYPAQ 153
Cdd:PRK13631 102 NPYSKKIKnfkELRRRVSMVFQ----FPEYQLFKDTIEkdimfGPV-ALGVKKSEAKKLAKFYLNKMGLdDSYLERSPFG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 154 LSGGQQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHEMGFARQVSSEVVFLHQGLVEE 233
Cdd:PRK13631 177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILK 256
|
250
....*....|.
gi 489310645 234 QGSPQQVFENP 244
Cdd:PRK13631 257 TGTPYEIFTDQ 267
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
4-245 |
1.02e-42 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 147.80 E-value: 1.02e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 4 ATPALEIRNLHKRY----------GELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELkl 73
Cdd:PRK11308 2 QQPLLQAIDLKKHYpvkrglfkpeRLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDL-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 74 kaakngelVAADGKQINRLRSEIGFVFQNfnlwPHMSVldNiieaPRRVLGQ------------SKAEATEIAEALLAKV 141
Cdd:PRK11308 80 --------LKADPEAQKLLRQKIQIVFQN----PYGSL--N----PRKKVGQileepllintslSAAERREKALAMMAKV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 142 GISDKrHA--YPAQLSGGQQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEE-GRTMLLVTHEMGFARQ 218
Cdd:PRK11308 142 GLRPE-HYdrYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQElGLSYVFISHDLSVVEH 220
|
250 260
....*....|....*....|....*..
gi 489310645 219 VSSEVVFLHQGLVEEQGSPQQVFENPL 245
Cdd:PRK11308 221 IADEVMVMYLGRCVEKGTKEQIFNNPR 247
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-239 |
1.34e-42 |
|
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: 152.22 E-value: 1.34e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 2 AEATPALEIRNLHKRY-GELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKlkaakngE 80
Cdd:COG4988 331 AAGPPSIELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLS-------D 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 81 LVAADgkqinrLRSEIGFVFQNfNLWPHMSVLDNIieaprrVLGQSKAEATEIAEALlAKVGISDKRHAYP--------- 151
Cdd:COG4988 404 LDPAS------WRRQIAWVPQN-PYLFAGTIRENL------RLGRPDASDEELEAAL-EAAGLDEFVAALPdgldtplge 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 152 --AQLSGGQQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAeEGRTMLLVTHEMGFARQvSSEVVFLHQG 229
Cdd:COG4988 470 ggRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLA-KGRTVILITHRLALLAQ-ADRILVLDDG 547
|
250
....*....|
gi 489310645 230 LVEEQGSPQQ 239
Cdd:COG4988 548 RIVEQGTHEE 557
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
23-244 |
1.35e-42 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 146.32 E-value: 1.35e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 23 LKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVaGEELKLKAAKNgelvaadgKQINRLRSEIGFVFQn 102
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVITAGKKN--------KKLKPLRKKVGIVFQ- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 103 fnlWP-HM----SVLDNIIEAPRRvLGQSKAEATEIAEALLAKVGISDK-RHAYPAQLSGGQQQRAAIARTLAMQPKVIL 176
Cdd:PRK13634 93 ---FPeHQlfeeTVEKDICFGPMN-FGVSEEDAKQKAREMIELVGLPEElLARSPFELSGGQMRRVAIAGVLAMEPEVLV 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489310645 177 FDEPTSALDPEMVQEVLNVIRAL-AEEGRTMLLVTHEMGFARQVSSEVVFLHQGLVEEQGSPQQVFENP 244
Cdd:PRK13634 169 LDEPTAGLDPKGRKEMMEMFYKLhKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADP 237
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
32-235 |
2.91e-42 |
|
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: 143.20 E-value: 2.91e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 32 DGDVISILGSSGSGKSTFLRCINLLENPHQGQILVageelklkaakNGELVAADGKQIN--RLRSEIGFVFQNFNLWPHM 109
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVL-----------NGTVLFDSRKKINlpPQQRKIGLVFQQYALFPHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 110 SVLDNIIEAPRRvlgQSKAEATEIAEALLAKVGISDKRHAYPAQLSGGQQQRAAIARTLAMQPKVILFDEPTSALDPEMV 189
Cdd:cd03297 91 NVRENLAFGLKR---KRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489310645 190 QEVLNVIRALAEE-GRTMLLVTHEMGFARQVSSEVVFLHQGLVEEQG 235
Cdd:cd03297 168 LQLLPELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
18-216 |
5.73e-42 |
|
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: 141.79 E-value: 5.73e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 18 GELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKLkaakngelvaaDGKQINRLRSEIG 97
Cdd:TIGR01166 3 GGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDY-----------SRKGLLERRQRVG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 98 FVFQNFN---LWPhmSVLDNIIEAPRRvLGQSKAEATEIAEALLAKVGISDKRHAYPAQLSGGQQQRAAIARTLAMQPKV 174
Cdd:TIGR01166 72 LVFQDPDdqlFAA--DVDQDVAFGPLN-LGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDV 148
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489310645 175 ILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHEMGFA 216
Cdd:TIGR01166 149 LLLDEPTAGLDPAGREQMLAILRRLRAEGMTVVISTHDVDLA 190
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
8-244 |
1.35e-41 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 142.74 E-value: 1.35e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLEnphqgqilvageELKLKAAKNGElVAADGK 87
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLI------------ELYPEARVSGE-VYLDGQ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 88 QINR-----LRSEIGFVFQNFNLWPHMSVLDNIIEAPR-RVLGQSKAEATEIAEALLAKVG----ISDKRHAYPAQLSGG 157
Cdd:PRK14247 71 DIFKmdvieLRRRVQMVFQIPNPIPNLSIFENVALGLKlNRLVKSKKELQERVRWALEKAQlwdeVKDRLDAPAGKLSGG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 158 QQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEgRTMLLVTHEMGFARQVSSEVVFLHQGLVEEQGSP 237
Cdd:PRK14247 151 QQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPT 229
|
....*..
gi 489310645 238 QQVFENP 244
Cdd:PRK14247 230 REVFTNP 236
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
38-255 |
2.42e-41 |
|
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: 144.17 E-value: 2.42e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 38 ILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKLKAAKngelvaadgkqinrLRSeIGFVFQNFNLWPHMSVLDNIiE 117
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPH--------------LRH-INMVFQSYALFPHMTVEENV-A 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 118 APRRVLGQSKAEATEIAEALLAKVGISDKRHAYPAQLSGGQQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIR 197
Cdd:TIGR01187 65 FGLKMRKVPRAEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELK 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489310645 198 ALAEE-GRTMLLVTHEMGFARQVSSEVVFLHQGLVEEQGSPQQVFENPLSARCKQFMSS 255
Cdd:TIGR01187 145 TIQEQlGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGE 203
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
7-238 |
2.42e-41 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 142.95 E-value: 2.42e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 7 ALEIRNLHKRYGE-LEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKLKAAKngelvaad 85
Cdd:PRK13647 4 IIEVEDLHFRYKDgTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEK-------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 86 gkqinRLRSEIGFVFQN-----FNlwphMSVLDNIIEAPRRvLGQSKAEATEIAEALLAKVGISDKRHAYPAQLSGGQQQ 160
Cdd:PRK13647 76 -----WVRSKVGLVFQDpddqvFS----STVWDDVAFGPVN-MGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKK 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489310645 161 RAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHEMGFARQVSSEVVFLHQGLVEEQGSPQ 238
Cdd:PRK13647 146 RVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKS 223
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
6-241 |
2.45e-41 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 142.22 E-value: 2.45e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 6 PALEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKlkaakngelvAAD 85
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLA----------DWS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 86 GKQINRLR------SEIGFVFqnfnlwphmSVLDnIIEAPRRVLGQSKAEATEIAEALLAKVGISDKRH-AYPaQLSGGQ 158
Cdd:PRK13548 71 PAELARRRavlpqhSSLSFPF---------TVEE-VVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGrDYP-QLSGGE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 159 QQRAAIARTLA------MQPKVILFDEPTSALDPEMVQEVLNVIRALA-EEGRTMLLVTHEMGFARQVSSEVVFLHQGLV 231
Cdd:PRK13548 140 QQRVQLARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAhERGLAVIVVLHDLNLAARYADRIVLLHQGRL 219
|
250
....*....|
gi 489310645 232 EEQGSPQQVF 241
Cdd:PRK13548 220 VADGTPAEVL 229
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
8-236 |
2.71e-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: 141.51 E-value: 2.71e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEEL-KLKAAKngelvaadg 86
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDItKLPPHE--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 87 kqinRLRSEIGFVFQNFNLWPHMSVLDNIieapRRVLGQSKAEATEIAEALLAKVGI-SDKRHAYPAQLSGGQQQRAAIA 165
Cdd:TIGR03410 72 ----RARAGIAYVPQGREIFPRLTVEENL----LTGLAALPRRSRKIPDEIYELFPVlKEMLGRRGGDLSGGQQQQLAIA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489310645 166 RTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGR-TMLLVTHEMGFARQVSSEVVFLHQGLVEEQGS 236
Cdd:TIGR03410 144 RALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGmAILLVEQYLDFARELADRYYVMERGRVVASGA 215
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
9-229 |
4.52e-41 |
|
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: 140.08 E-value: 4.52e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 9 EIRNLHKRYGEL-EVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKLKaakngelvaadgk 87
Cdd:cd03226 1 RIENISFSYKKGtEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAK------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 88 qinRLRSEIGFVFQN--FNLWPHmSVLDNIIEAPRRVlgqskAEATEIAEALLAKVGISDKRHAYPAQLSGGQQQRAAIA 165
Cdd:cd03226 68 ---ERRKSIGYVMQDvdYQLFTD-SVREELLLGLKEL-----DAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIA 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489310645 166 RTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHEMGFARQVSSEVVFLHQG 229
Cdd:cd03226 139 AALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANG 202
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
19-243 |
5.23e-41 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 142.11 E-value: 5.23e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 19 ELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKLKAAKngelvaadgkqINRLRSEIGF 98
Cdd:PRK13637 19 EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVK-----------LSDIRKKVGL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 99 VFQnfnlWPHMSVLDNIIE-----APRRvLGQSKAEATEIAEALLAKVGIS--DKRHAYPAQLSGGQQQRAAIARTLAMQ 171
Cdd:PRK13637 88 VFQ----YPEYQLFEETIEkdiafGPIN-LGLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAME 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489310645 172 PKVILFDEPTSALDPEMVQEVLNVIRALAEE-GRTMLLVTHEMGFARQVSSEVVFLHQGLVEEQGSPQQVFEN 243
Cdd:PRK13637 163 PKILILDEPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKE 235
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
8-235 |
5.52e-41 |
|
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: 140.11 E-value: 5.52e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKlkaakngelvAADGK 87
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD----------IAARN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 88 QINRLRSEIGfvfqnfnLWPHMSVLDNIIEAPRrVLGQSKAEATEIAEALLAKVGISDKRHAYPAQLSGGQQQRAAIART 167
Cdd:cd03269 71 RIGYLPEERG-------LYPKMKVIDQLVYLAQ-LKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAA 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489310645 168 LAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHEMGFARQVSSEVVFLHQGLVEEQG 235
Cdd:cd03269 143 VIHDPELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
8-249 |
6.07e-41 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 141.41 E-value: 6.07e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELklkAAKNGELVAadgk 87
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPL---AAWSPWELA---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 88 qinRLR------SEIGFVFqnfnlwphmSVLDnIIEAPRRVLGQSKAEATEIAEALLAKVGISDKRH-AYPaQLSGGQQQ 160
Cdd:COG4559 75 ---RRRavlpqhSSLAFPF---------TVEE-VVALGRAPHGSSAAQDRQIVREALALVGLAHLAGrSYQ-TLSGGEQQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 161 RAAIARTLA-------MQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHEMGFARQVSSEVVFLHQGLVEE 233
Cdd:COG4559 141 RVQLARVLAqlwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVA 220
|
250
....*....|....*.
gi 489310645 234 QGSPQQVFENPLSARC 249
Cdd:COG4559 221 QGTPEEVLTDELLERV 236
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
5-243 |
1.05e-40 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 140.90 E-value: 1.05e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 5 TPALEIRNLHKRYGELE--VLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKlkaAKNgelv 82
Cdd:PRK13632 5 SVMIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITIS---KEN---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 83 aadgkqINRLRSEIGFVFQN-FNLWPHMSVLDNI---IEApRRVlgqSKAEATEIAEALLAKVGISDKRHAYPAQLSGGQ 158
Cdd:PRK13632 78 ------LKEIRKKIGIIFQNpDNQFIGATVEDDIafgLEN-KKV---PPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 159 QQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEG-RTMLLVTHEMGFARQVSSEVVFLHQGLVeEQGSP 237
Cdd:PRK13632 148 KQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkKTLISITHDMDEAILADKVIVFSEGKLI-AQGKP 226
|
....*.
gi 489310645 238 QQVFEN 243
Cdd:PRK13632 227 KEILNN 232
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-229 |
3.13e-40 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 144.78 E-value: 3.13e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 3 EATPALEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKLK----AAKN 78
Cdd:COG3845 1 MMPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRsprdAIAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 79 GelvaadgkqinrlrseIGFVFQNFNLWPHMSVLDNII--EAPRRVLGQSKAEATEIAEALLAKVGISDKRHAYPAQLSG 156
Cdd:COG3845 81 G----------------IGMVHQHFMLVPNLTVAENIVlgLEPTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSV 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489310645 157 GQQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHEMGFARQVSSEVVFLHQG 229
Cdd:COG3845 145 GEQQRVEILKALYRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRG 217
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
15-238 |
4.03e-40 |
|
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: 140.22 E-value: 4.03e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 15 KRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKLKAAKngelvaadgkqinrLRS 94
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRK--------------VRR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 95 EIGFVFQNFNLWPHMSVLDNIiEAPRRVLGQSKAEATEIAEALLAKVGISDKRHAYPAQLSGGQQQRAAIARTLAMQPKV 174
Cdd:TIGR01188 67 SIGIVPQYASVDEDLTGRENL-EMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDV 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489310645 175 ILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHEMGFARQVSSEVVFLHQGLVEEQGSPQ 238
Cdd:TIGR01188 146 LFLDEPTTGLDPRTRRAIWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPE 209
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-239 |
1.10e-39 |
|
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: 144.14 E-value: 1.10e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 2 AEATPALEIRNLHKRY--GELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKlkaakng 79
Cdd:COG4987 328 APGGPSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLR------- 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 80 ELVAADgkqinrLRSEIGFVFQNFNLWpHMSVLDNIIeaprrvLGQSKAEATEIAEALlAKVGISDKRHAYP-------- 151
Cdd:COG4987 401 DLDEDD------LRRRIAVVPQRPHLF-DTTLRENLR------LARPDATDEELWAAL-ERVGLGDWLAALPdgldtwlg 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 152 ---AQLSGGQQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAeEGRTMLLVTHEMGFARQVsSEVVFLHQ 228
Cdd:COG4987 467 eggRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEAL-AGRTVLLITHRLAGLERM-DRILVLED 544
|
250
....*....|.
gi 489310645 229 GLVEEQGSPQQ 239
Cdd:COG4987 545 GRIVEQGTHEE 555
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
23-229 |
1.85e-39 |
|
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: 136.83 E-value: 1.85e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 23 LKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVageelklkaakngelvaaDGKQINRLRSEIGFVFQN 102
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVIL------------------EGKQITEPGPDRMVVFQN 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 103 FNLWPHMSVLDNIIEAPRRVLGQ-SKAEATEIAEALLAKVGISDKRHAYPAQLSGGQQQRAAIARTLAMQPKVILFDEPT 181
Cdd:TIGR01184 63 YSLLPWLTVRENIALAVDRVLPDlSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPF 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489310645 182 SALDP---EMVQEVLnvIRALAEEGRTMLLVTHEMGFARQVSSEVVFLHQG 229
Cdd:TIGR01184 143 GALDAltrGNLQEEL--MQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-242 |
3.06e-39 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 137.45 E-value: 3.06e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 1 MAEatPALEIRNLHKRYGELE--VLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELklkaakn 78
Cdd:PRK13635 1 MKE--EIIRVEHISFRYPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVL------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 79 gelvaaDGKQINRLRSEIGFVFQN-FNLWPHMSVLDNIIEAPRRVlGQSKAEATEIAEALLAKVGISDKRHAYPAQLSGG 157
Cdd:PRK13635 72 ------SEETVWDVRRQVGMVFQNpDNQFVGATVQDDVAFGLENI-GVPREEMVERVDQALRQVGMEDFLNREPHRLSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 158 QQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGR-TMLLVTHEMGFARQvSSEVVFLHQGLVEEQGS 236
Cdd:PRK13635 145 QKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGiTVLSITHDLDEAAQ-ADRVIVMNKGEILEEGT 223
|
....*.
gi 489310645 237 PQQVFE 242
Cdd:PRK13635 224 PEEIFK 229
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
7-239 |
3.51e-39 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 143.00 E-value: 3.51e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 7 ALEIRNLHKRY-GELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKlkaakngelvaad 85
Cdd:COG1132 339 EIEFENVSFSYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIR------------- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 86 gkQINR--LRSEIGFVFQNFNLWpHMSVLDNIIeaprrvLGQSKAEATEIAEALlAKVGISDKRHAYP-----------A 152
Cdd:COG1132 406 --DLTLesLRRQIGVVPQDTFLF-SGTIRENIR------YGRPDATDEEVEEAA-KAAQAHEFIEALPdgydtvvgergV 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 153 QLSGGQQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAeEGRTMLLVTHEMGFARQVsSEVVFLHQGLVE 232
Cdd:COG1132 476 NLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLM-KGRTTIVIAHRLSTIRNA-DRILVLDDGRIV 553
|
....*..
gi 489310645 233 EQGSPQQ 239
Cdd:COG1132 554 EQGTHEE 560
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
8-239 |
3.72e-39 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 135.58 E-value: 3.72e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKLKAAKngelvaadgk 87
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPRE---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 88 qinrLRSEIGFVFQNFNLWPHMSVLDNI-IEAprRVLGQSKAEATEIAEALLAKVGISDKRHAYPAQLSGGQQQRAAIAR 166
Cdd:cd03265 71 ----VRRRIGIVFQDLSVDDELTGWENLyIHA--RLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIAR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489310645 167 TLAMQPKVILFDEPTSALDPEMVQEVLNVIRAL-AEEGRTMLLVTHEMGFARQVSSEVVFLHQGLVEEQGSPQQ 239
Cdd:cd03265 145 SLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLkEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEE 218
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
8-231 |
4.07e-39 |
|
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: 133.71 E-value: 4.07e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKLK----AAKNGelva 83
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFAsprdARRAG---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 84 adgkqinrlrseIGFVFQnfnlwphmsvldniieaprrvlgqskaeateiaeallakvgisdkrhaypaqLSGGQQQRAA 163
Cdd:cd03216 77 ------------IAMVYQ----------------------------------------------------LSVGERQMVE 92
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489310645 164 IARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHEMGFARQVSSEVVFLHQGLV 231
Cdd:cd03216 93 IARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
8-235 |
6.50e-39 |
|
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: 134.80 E-value: 6.50e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRYGELE----VLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGeelkLKAAKNGELVa 83
Cdd:cd03266 2 ITADALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG----FDVVKEPAEA- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 84 adgkqinrlRSEIGFVFQNFNLWPHMSVLDNIiEAPRRVLGQSKAEATEIAEALLAKVGISDKRHAYPAQLSGGQQQRAA 163
Cdd:cd03266 77 ---------RRRLGFVSDSTGLYDRLTARENL-EYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489310645 164 IARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHEMGFARQVSSEVVFLHQGLVEEQG 235
Cdd:cd03266 147 IARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-246 |
7.16e-39 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 138.44 E-value: 7.16e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 1 MAeatpALEIRNLHKRY-GELEVLKGISLTARDGDVISILGSSGSGKSTFLRcinllenphqgqiLVAGeelkLKAAKNG 79
Cdd:PRK11650 1 MA----GLKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLR-------------MVAG----LERITSG 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 80 ElVAADGKQINRL----RsEIGFVFQNFNLWPHMSVLDNIiEAPRRVLGQSKAE-ATEIAEAllAKV----GISDKRhay 150
Cdd:PRK11650 60 E-IWIGGRVVNELepadR-DIAMVFQNYALYPHMSVRENM-AYGLKIRGMPKAEiEERVAEA--ARIlelePLLDRK--- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 151 PAQLSGGQQQRAAIARTLAMQPKVILFDEPTSALDPEM-VQEVLNvIRALAEE-GRTMLLVTHE----MGFARQvsseVV 224
Cdd:PRK11650 132 PRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLrVQMRLE-IQRLHRRlKTTSLYVTHDqveaMTLADR----VV 206
|
250 260
....*....|....*....|..
gi 489310645 225 FLHQGLVEEQGSPQQVFENPLS 246
Cdd:PRK11650 207 VMNGGVAEQIGTPVEVYEKPAS 228
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-254 |
1.03e-38 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 135.99 E-value: 1.03e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 4 ATPALEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENP-----HQGQILVAGEELklkaakn 78
Cdd:PRK14271 18 AAPAMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSI------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 79 gelvaADGKQINRLRSEIGFVFQNFNLWPhMSVLDNIIEAPRRVLGQSKAEATEIAEALLAKVG----ISDKRHAYPAQL 154
Cdd:PRK14271 91 -----FNYRDVLEFRRRVGMLFQRPNPFP-MSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGlwdaVKDRLSDSPFRL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 155 SGGQQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEgRTMLLVTHEMGFARQVSSEVVFLHQGLVEEQ 234
Cdd:PRK14271 165 SGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFDGRLVEE 243
|
250 260
....*....|....*....|
gi 489310645 235 GSPQQVFENPLSARCKQFMS 254
Cdd:PRK14271 244 GPTEQLFSSPKHAETARYVA 263
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
23-242 |
1.58e-38 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 135.64 E-value: 1.58e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 23 LKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKlKAAKNgelvaadgKQINRLRSEIGFVFQn 102
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLIT-STSKN--------KDIKQIRKKVGLVFQ- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 103 fnlWPHM-----SVLDNIIEAPRRvLGQSKAEATEIAEALLAKVGISDK-RHAYPAQLSGGQQQRAAIARTLAMQPKVIL 176
Cdd:PRK13649 93 ---FPESqlfeeTVLKDVAFGPQN-FGVSQEEAEALAREKLALVGISESlFEKNPFELSGGQMRRVAIAGILAMEPKILV 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489310645 177 FDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHEMGFARQVSSEVVFLHQGLVEEQGSPQQVFE 242
Cdd:PRK13649 169 LDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQ 234
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-244 |
4.25e-38 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 134.02 E-value: 4.25e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 4 ATPALEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKLkaakngelvA 83
Cdd:PRK14246 7 AEDVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYF---------G 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 84 ADGKQIN--RLRSEIGFVFQNFNLWPHMSVLDNIIEAPRRVLGQSKAEATEIAEALLAKVG----ISDKRHAYPAQLSGG 157
Cdd:PRK14246 78 KDIFQIDaiKLRKEVGMVFQQPNPFPHLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGlwkeVYDRLNSPASQLSGG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 158 QQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEgRTMLLVTHEMGFARQVSSEVVFLHQGLVEEQGSP 237
Cdd:PRK14246 158 QQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSS 236
|
....*..
gi 489310645 238 QQVFENP 244
Cdd:PRK14246 237 NEIFTSP 243
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
22-243 |
6.54e-38 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 134.06 E-value: 6.54e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 22 VLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGeelklkaakngeLVAADGKQINRLRSEIGFVFQ 101
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDG------------LDTSDEENLWDIRNKAGMVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 102 NfnlwPHMSVLDNIIE-----APRRvLGQSKAEATEIAEALLAKVGISD-KRHAyPAQLSGGQQQRAAIARTLAMQPKVI 175
Cdd:PRK13633 93 N----PDNQIVATIVEedvafGPEN-LGIPPEEIRERVDESLKKVGMYEyRRHA-PHLLSGGQKQRVAIAGILAMRPECI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489310645 176 LFDEPTSALDPEMVQEVLNVIRAL-AEEGRTMLLVTHEMGFARQvSSEVVFLHQGLVEEQGSPQQVFEN 243
Cdd:PRK13633 167 IFDEPTAMLDPSGRREVVNTIKELnKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-244 |
7.33e-38 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 135.93 E-value: 7.33e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 1 MAEATpaleIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELK-LKAAKNG 79
Cdd:PRK11000 1 MASVT----LRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNdVPPAERG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 80 elvaadgkqinrlrseIGFVFQNFNLWPHMSVLDNI-----------IEAPRRVlgQSKAEATEIAEALlakvgisDKRh 148
Cdd:PRK11000 77 ----------------VGMVFQSYALYPHLSVAENMsfglklagakkEEINQRV--NQVAEVLQLAHLL-------DRK- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 149 ayPAQLSGGQQQRAAIARTLAMQPKVILFDEPTSALDPEM-VQEVLNVIRALAEEGRTMLLVTHEMGFARQVSSEVVFLH 227
Cdd:PRK11000 131 --PKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALrVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLD 208
|
250
....*....|....*..
gi 489310645 228 QGLVEEQGSPQQVFENP 244
Cdd:PRK11000 209 AGRVAQVGKPLELYHYP 225
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
2-254 |
7.48e-38 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 139.07 E-value: 7.48e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 2 AEATPALEIRNLH-----------KRYGELEVLKGISLTARDGDVISILGSSGSGKST----FLRCINllenpHQGQILV 66
Cdd:PRK15134 270 EPASPLLDVEQLQvafpirkgilkRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWF 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 67 AGEELKLkaakngelvaADGKQINRLRSEIGFVFQNFN--LWPHMSVLdNIIEAPRRVLGQ--SKAEATEIAEALLAKVG 142
Cdd:PRK15134 345 DGQPLHN----------LNRRQLLPVRHRIQVVFQDPNssLNPRLNVL-QIIEEGLRVHQPtlSAAQREQQVIAVMEEVG 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 143 IS-DKRHAYPAQLSGGQQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGR-TMLLVTHEMGFARQVS 220
Cdd:PRK15134 414 LDpETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQlAYLFISHDLHVVRALC 493
|
250 260 270
....*....|....*....|....*....|....
gi 489310645 221 SEVVFLHQGLVEEQGSPQQVFENPLSARCKQFMS 254
Cdd:PRK15134 494 HQVIVLRQGEVVEQGDCERVFAAPQQEYTRQLLA 527
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
5-223 |
9.10e-38 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 132.25 E-value: 9.10e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 5 TPALEIRNLHKRYGE----LEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEEL-KLKAAKNG 79
Cdd:PRK11629 3 KILLQCDNLCKRYQEgsvqTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMsKLSSAAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 80 ELVaadgkqiNRlrsEIGFVFQNFNLWPHMSVLDNIiEAPRRVLGQSKAEATEIAEALLAKVGISDKRHAYPAQLSGGQQ 159
Cdd:PRK11629 83 ELR-------NQ---KLGFIYQFHHLLPDFTALENV-AMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGER 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489310645 160 QRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRAL-AEEGRTMLLVTHEMGFARQVSSEV 223
Cdd:PRK11629 152 QRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDLQLAKRMSRQL 216
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
9-240 |
2.50e-37 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 131.74 E-value: 2.50e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 9 EIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKlkAAKNGELvaadGKQ 88
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVA--TTPSREL----AKR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 89 INRLRSEIGFVFQ-------NFNLWPHmsvldniieaprrvlgqSKAEATE-----IAEALlAKVGISDKRHAYPAQLSG 156
Cdd:COG4604 77 LAILRQENHINSRltvrelvAFGRFPY-----------------SKGRLTAedreiIDEAI-AYLDLEDLADRYLDELSG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 157 GQQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEE-GRTMLLVTHEMGFARQVSSEVVFLHQGLVEEQG 235
Cdd:COG4604 139 GQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADElGKTVVIVLHDINFASCYADHIVAMKDGRVVAQG 218
|
....*
gi 489310645 236 SPQQV 240
Cdd:COG4604 219 TPEEI 223
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
8-235 |
3.31e-37 |
|
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: 130.01 E-value: 3.31e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRYGELEVLKGISLTARDGdVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKlkaakngelvaadgK 87
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVL--------------K 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 88 QINRLRSEIGFVFQNFNLWPHMSVLD--NIIEAPRRVlgqSKAEATEIAEALLAKVGISDKRHAYPAQLSGGQQQRAAIA 165
Cdd:cd03264 66 QPQKLRRRIGYLPQEFGVYPNFTVREflDYIAWLKGI---PSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIA 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 166 RTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEgRTMLLVTHEMGFARQVSSEVVFLHQGLVEEQG 235
Cdd:cd03264 143 QALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGED-RIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
8-233 |
3.56e-37 |
|
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: 130.03 E-value: 3.56e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKlkaaKNGELVaadgK 87
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQ----KNIEAL----R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 88 QINRLRSEIGFVfqnfnlwPHMSVLDNIiEAPRRVLGQSKAEATEIaealLAKVGISDKRHAYPAQLSGGQQQRAAIART 167
Cdd:cd03268 73 RIGALIEAPGFY-------PNLTARENL-RLLARLLGIRKKRIDEV----LDVVGLKDSAKKKVKGFSLGMKQRLGIALA 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489310645 168 LAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHEMGFARQVSSEVVFLHQG-LVEE 233
Cdd:cd03268 141 LLGNPDLLILDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGkLIEE 207
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
9-243 |
1.13e-36 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 129.58 E-value: 1.13e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 9 EIRNLHKRY---GELEVLKGISLTARDGDVISILGSSGSGKSTflrCINLLE---NPHQGQILVAGEELKlkaakngELv 82
Cdd:cd03249 2 EFKNVSFRYpsrPDVPILKGLSLTIPPGKTVALVGSSGCGKST---VVSLLErfyDPTSGEILLDGVDIR-------DL- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 83 aadgkQINRLRSEIGFVFQNFNLWPhMSVLDNIieaprrVLGQSKAEATEIAEAllAKVG-----ISDKRHAYP------ 151
Cdd:cd03249 71 -----NLRWLRSQIGLVSQEPVLFD-GTIAENI------RYGKPDATDEEVEEA--AKKAnihdfIMSLPDGYDtlvger 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 152 -AQLSGGQQQRAAIARTLAMQPKVILFDEPTSALDPE---MVQEVLNVIRalaeEGRTMLLVTHEMGfARQVSSEVVFLH 227
Cdd:cd03249 137 gSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAEsekLVQEALDRAM----KGRTTIVIAHRLS-TIRNADLIAVLQ 211
|
250
....*....|....*.
gi 489310645 228 QGLVEEQGSPQQVFEN 243
Cdd:cd03249 212 NGQVVEQGTHDELMAQ 227
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
5-231 |
1.16e-36 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 130.18 E-value: 1.16e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 5 TPaLEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILvageelklkaAKNGELVAA 84
Cdd:PRK11247 11 TP-LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELL----------AGTAPLAEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 85 dgkqinrlRSEIGFVFQNFNLWPHMSVLDNIIEAPRrvlGQSKAEATEIAEAllakVGISDKRHAYPAQLSGGQQQRAAI 164
Cdd:PRK11247 80 --------REDTRLMFQDARLLPWKKVIDNVGLGLK---GQWRDAALQALAA----VGLADRANEWPAALSGGQKQRVAL 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489310645 165 ARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRAL-AEEGRTMLLVTHEMGFARQVSSEVVFLHQGLV 231
Cdd:PRK11247 145 ARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLwQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
5-246 |
1.57e-36 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 130.19 E-value: 1.57e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 5 TPALEIRNLHKRY---------GELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKlka 75
Cdd:PRK10419 1 MTLLNVSGLSHHYahgglsgkhQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLA--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 76 akngelvAADGKQINRLRSEIGFVFQN----FNlwPHMSVLDNIIEAPRRVLGQSKAEATEIAEALLAKVG----ISDKR 147
Cdd:PRK10419 78 -------KLNRAQRKAFRRDIQMVFQDsisaVN--PRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDlddsVLDKR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 148 hayPAQLSGGQQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRT-MLLVTHEMGFARQVSSEVVFL 226
Cdd:PRK10419 149 ---PPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTaCLFITHDLRLVERFCQRVMVM 225
|
250 260
....*....|....*....|..
gi 489310645 227 HQG-LVEEQG-SPQQVFENPLS 246
Cdd:PRK10419 226 DNGqIVETQPvGDKLTFSSPAG 247
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
8-252 |
1.58e-36 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 133.23 E-value: 1.58e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRYGE------------------LEV------LKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQ 63
Cdd:PRK10070 5 LEIKNLYKIFGEhpqrafkyieqglskeqiLEKtglslgVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 64 ILVAGEELklkaaknGELVAADGKQINrlRSEIGFVFQNFNLWPHMSVLDNIIEApRRVLGQSKAEATEIAEALLAKVGI 143
Cdd:PRK10070 85 VLIDGVDI-------AKISDAELREVR--RKKIAMVFQSFALMPHMTVLDNTAFG-MELAGINAEERREKALDALRQVGL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 144 SDKRHAYPAQLSGGQQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLN-VIRALAEEGRTMLLVTHEMGFARQVSSE 222
Cdd:PRK10070 155 ENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDeLVKLQAKHQRTIVFISHDLDEAMRIGDR 234
|
250 260 270
....*....|....*....|....*....|
gi 489310645 223 VVFLHQGLVEEQGSPQQVFENPLSARCKQF 252
Cdd:PRK10070 235 IAIMQNGEVVQVGTPDEILNNPANDYVRTF 264
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1-254 |
2.35e-36 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 129.52 E-value: 2.35e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 1 MAEATPALEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENphqgqiLVAGEELKLKAAKNGE 80
Cdd:PRK14243 4 LNGTETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLND------LIPGFRVEGKVTFHGK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 81 LVAADGKQINRLRSEIGFVFQNFNLWPHmSVLDNIIEAPRrVLGQsKAEATEIAEALLAKVG----ISDKRHAYPAQLSG 156
Cdd:PRK14243 78 NLYAPDVDPVEVRRRIGMVFQKPNPFPK-SIYDNIAYGAR-INGY-KGDMDELVERSLRQAAlwdeVKDKLKQSGLSLSG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 157 GQQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEgRTMLLVTHEMGFARQVSSEVVFLHQGLVEEQG- 235
Cdd:PRK14243 155 GQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHNMQQAARVSDMTAFFNVELTEGGGr 233
|
250 260
....*....|....*....|....*..
gi 489310645 236 --------SPQQVFENPLSARCKQFMS 254
Cdd:PRK14243 234 ygylvefdRTEKIFNSPQQQATRDYVS 260
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
8-211 |
4.24e-36 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 127.21 E-value: 4.24e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPH---QGQILVAGEELklkaakngelvaa 84
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRL------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 85 DGKQINRLRseIGFVFQNFNLWPHMSVLDNIIEA-PRRVlgqSKAEATEIAEALLAKVGISDKRHAYPAQLSGGQQQRAA 163
Cdd:COG4136 69 TALPAEQRR--IGILFQDDLLFPHLSVGENLAFAlPPTI---GRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVA 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489310645 164 IARTLAMQPKVILFDEPTSALDPEMVQEVLN-VIRALAEEGRTMLLVTH 211
Cdd:COG4136 144 LLRALLAEPRALLLDEPFSKLDAALRAQFREfVFEQIRQRGIPALLVTH 192
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
8-245 |
6.42e-36 |
|
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: 127.66 E-value: 6.42e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEEL-KLKAAKngelvaadg 86
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDItKLPMHK--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 87 kqinRLRSEIGFVFQNFNLWPHMSVLDNIIeAPRRVLGQSKAEATEIAEALLAKVGISDKRHAYPAQLSGGQQQRAAIAR 166
Cdd:cd03218 72 ----RARLGIGYLPQEASIFRKLTVEENIL-AVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIAR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489310645 167 TLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHEMGFARQVSSEVVFLHQGLVEEQGSPQQVFENPL 245
Cdd:cd03218 147 ALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANEL 225
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
23-244 |
7.62e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 128.79 E-value: 7.62e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 23 LKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKLKAAKngelvaadgKQINRLRSEIGFVFQn 102
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGN---------KNLKKLRKKVSLVFQ- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 103 fnlWPHM-----SVLDNIIEAPRRvLGQSKAEATEIAEALLAKVGISDK-RHAYPAQLSGGQQQRAAIARTLAMQPKVIL 176
Cdd:PRK13641 93 ---FPEAqlfenTVLKDVEFGPKN-FGFSEDEAKEKALKWLKKVGLSEDlISKSPFELSGGQMRRVAIAGVMAYEPEILC 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489310645 177 FDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHEMGFARQVSSEVVFLHQGLVEEQGSPQQVFENP 244
Cdd:PRK13641 169 LDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDK 236
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
8-241 |
9.64e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 128.43 E-value: 9.64e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRYGE-LEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKLKAakngelvaadg 86
Cdd:PRK13636 6 LKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSR----------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 87 KQINRLRSEIGFVFQN-FNLWPHMSVLDNIIEAPRRvLGQSKAEATEIAEALLAKVGISDKRHAYPAQLSGGQQQRAAIA 165
Cdd:PRK13636 75 KGLMKLRESVGMVFQDpDNQLFSASVYQDVSFGAVN-LKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489310645 166 RTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEE-GRTMLLVTHEMGFARQVSSEVVFLHQGLVEEQGSPQQVF 241
Cdd:PRK13636 154 GVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
20-255 |
1.45e-35 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 129.06 E-value: 1.45e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 20 LEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELklkaakngelVAADGKQINRLRSEIGFV 99
Cdd:PRK15079 34 LKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDL----------LGMKDDEWRAVRSDIQMI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 100 FQN--FNLWPHMSVLDnIIEAPRRVL--GQSKAEATEIAEALLAKVGI-SDKRHAYPAQLSGGQQQRAAIARTLAMQPKV 174
Cdd:PRK15079 104 FQDplASLNPRMTIGE-IIAEPLRTYhpKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 175 ILFDEPTSALDPEMVQEVLNVIRALAEE-GRTMLLVTHEMGFARQVSSEVVFLHQGLVEEQGSPQQVFENPLSARCKQFM 253
Cdd:PRK15079 183 IICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPYTKALM 262
|
..
gi 489310645 254 SS 255
Cdd:PRK15079 263 SA 264
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
18-229 |
1.64e-35 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 126.14 E-value: 1.64e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 18 GELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEEL-KLKAakngelvaadgKQINRLRSEI 96
Cdd:PRK10908 13 GGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItRLKN-----------REVPFLRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 97 GFVFQNFNLWPHMSVLDNIiEAPRRVLGQSKAEATEIAEALLAKVGISDKRHAYPAQLSGGQQQRAAIARTLAMQPKVIL 176
Cdd:PRK10908 82 GMIFQDHHLLMDRTVYDNV-AIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489310645 177 FDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHEMGFARQVSSEVVFLHQG 229
Cdd:PRK10908 161 ADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDG 213
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
16-235 |
2.43e-35 |
|
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: 125.30 E-value: 2.43e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 16 RYGELEVlkGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELklkaakngelVAADGKqinrlRSE 95
Cdd:cd03298 9 SYGEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDV----------TAAPPA-----DRP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 96 IGFVFQNFNLWPHMSVLDNIieaprrVLGQS-----KAEATEIAEALLAKVGISDKRHAYPAQLSGGQQQRAAIARTLAM 170
Cdd:cd03298 72 VSMLFQENNLFAHLTVEQNV------GLGLSpglklTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489310645 171 QPKVILFDEPTSALDPEMVQEVLNVIRAL-AEEGRTMLLVTHEMGFARQVSSEVVFLHQGLVEEQG 235
Cdd:cd03298 146 DKPVLLLDEPFAALDPALRAEMLDLVLDLhAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
19-243 |
2.68e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 127.43 E-value: 2.68e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 19 ELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKLKAAKNgelvaadgKQINRLRSEIGF 98
Cdd:PRK13645 23 EFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKI--------KEVKRLRKEIGL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 99 VFQnfnlWPHMSVLDNIIE-----APRRvLGQSKAEATEIAEALLAKVGI-SDKRHAYPAQLSGGQQQRAAIARTLAMQP 172
Cdd:PRK13645 95 VFQ----FPEYQLFQETIEkdiafGPVN-LGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDG 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489310645 173 KVILFDEPTSALDPEMVQEVLNVIRAL-AEEGRTMLLVTHEMGFARQVSSEVVFLHQGLVEEQGSPQQVFEN 243
Cdd:PRK13645 170 NTLVLDEPTGGLDPKGEEDFINLFERLnKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN 241
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
2-244 |
4.51e-35 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 126.19 E-value: 4.51e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 2 AEATPALEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKLKaakngEL 81
Cdd:PRK11701 1 MMDQPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLR-----DL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 82 VAADGKQINRL-RSEIGFVFQN--FNLWPHMSVLDNIIE----APRRVLGQSKAEATEiaeaLLAKVGISDKR-HAYPAQ 153
Cdd:PRK11701 76 YALSEAERRRLlRTEWGFVHQHprDGLRMQVSAGGNIGErlmaVGARHYGDIRATAGD----WLERVEIDAARiDDLPTT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 154 LSGGQQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRAL-AEEGRTMLLVTHEMGFARQVSSEVVFLHQGLVE 232
Cdd:PRK11701 152 FSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLvRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVV 231
|
250
....*....|..
gi 489310645 233 EQGSPQQVFENP 244
Cdd:PRK11701 232 ESGLTDQVLDDP 243
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
12-244 |
5.59e-35 |
|
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: 128.31 E-value: 5.59e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 12 NLHKRYGELEVlkGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKlkaakngelVAADGKQINR 91
Cdd:TIGR02142 4 RFSKRLGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLF---------DSRKGIFLPP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 92 LRSEIGFVFQNFNLWPHMSVLDNIIEAPRRVLGQSKAEATEiaeALLAKVGISDKRHAYPAQLSGGQQQRAAIARTLAMQ 171
Cdd:TIGR02142 73 EKRRIGYVFQEARLFPHLSVRGNLRYGMKRARPSERRISFE---RVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSS 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489310645 172 PKVILFDEPTSALDPEMVQEVLNVIRALAEEGRT-MLLVTHEMGFARQVSSEVVFLHQGLVEEQGSPQQVFENP 244
Cdd:TIGR02142 150 PRLLLMDEPLAALDDPRKYEILPYLERLHAEFGIpILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
7-242 |
7.91e-35 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 125.20 E-value: 7.91e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 7 ALEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVageelklkaakngelvaaDG 86
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITL------------------DG 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 87 KQINRLRSEIGFVFQNFNLWPHMSVLDNIiEAPRRVLGQSKAEATEIAEALLAKVGISDKRHAYPAQLSGGQQQRAAIAR 166
Cdd:PRK11248 63 KPVEGPGAERGVVFQNEGLLPWRNVQDNV-AFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIAR 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489310645 167 TLAMQPKVILFDEPTSALDP---EMVQEVLnvIRALAEEGRTMLLVTHEMgfarqvsSEVVFLHQGLVEEQGSPQQVFE 242
Cdd:PRK11248 142 ALAANPQLLLLDEPFGALDAftrEQMQTLL--LKLWQETGKQVLLITHDI-------EEAVFMATELVLLSPGPGRVVE 211
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
8-216 |
1.33e-34 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 124.12 E-value: 1.33e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRYGE----LEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKlkaakngelvA 83
Cdd:PRK10584 7 VEVHHLKKSVGQgeheLSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLH----------Q 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 84 ADGKQINRLRSE-IGFVFQNFNLWPHMSVLDNIiEAPRRVLGQSKAEATEIAEALLAKVGISDKRHAYPAQLSGGQQQRA 162
Cdd:PRK10584 77 MDEEARAKLRAKhVGFVFQSFMLIPTLNALENV-ELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRV 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489310645 163 AIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEE-GRTMLLVTHEMGFA 216
Cdd:PRK10584 156 ALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHDLQLA 210
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
8-241 |
1.36e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 125.23 E-value: 1.36e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRYGELE---VLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKLKAAKNgelvaa 84
Cdd:PRK13650 5 IEVKNLTFKYKEDQekyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWD------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 85 dgkqinrLRSEIGFVFQN-FNLWPHMSVLDNI---IEAPrrvlGQSKAEATEIAEALLAKVGISDKRHAYPAQLSGGQQQ 160
Cdd:PRK13650 79 -------IRHKIGMVFQNpDNQFVGATVEDDVafgLENK----GIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 161 RAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEE-GRTMLLVTHEMGfARQVSSEVVFLHQGLVEEQGSPQQ 239
Cdd:PRK13650 148 RVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLD-EVALSDRVLVMKNGQVESTSTPRE 226
|
..
gi 489310645 240 VF 241
Cdd:PRK13650 227 LF 228
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
8-245 |
1.38e-34 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 124.37 E-value: 1.38e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEEL-KL---KAAKNGelva 83
Cdd:COG1137 4 LEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDItHLpmhKRARLG---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 84 adgkqinrlrseIGF------VFQNfnlwphMSVLDNIIeAPRRVLGQSKAEATEIAEALLAKVGISDKRHAYPAQLSGG 157
Cdd:COG1137 80 ------------IGYlpqeasIFRK------LTVEDNIL-AVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 158 QQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEG----------RTMLLVTHemgfaRqvsseVVFLH 227
Cdd:COG1137 141 ERRRVEIARALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKERGigvlitdhnvRETLGICD-----R-----AYIIS 210
|
250
....*....|....*...
gi 489310645 228 QGLVEEQGSPQQVFENPL 245
Cdd:COG1137 211 EGKVLAEGTPEEILNNPL 228
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
8-229 |
1.69e-34 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 124.81 E-value: 1.69e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRYG-----ELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEEL-KLKAAKngel 81
Cdd:COG1101 2 LELKNLSKTFNpgtvnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVtKLPEYK---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 82 vaadgkqinrlRSE-IGFVFQNFNL--WPHMSVLDNIIEAPRR------VLGQSKAEATEIAEaLLAKV--GISDKRHAY 150
Cdd:COG1101 78 -----------RAKyIGRVFQDPMMgtAPSMTIEENLALAYRRgkrrglRRGLTKKRRELFRE-LLATLglGLENRLDTK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 151 PAQLSGGQQQraaiARTLAM----QPKVILFDEPTSALDPEMVQEVLNVIRALAEEGR-TMLLVTHEMGFARQVSSEVVF 225
Cdd:COG1101 146 VGLLSGGQRQ----ALSLLMatltKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNlTTLMVTHNMEQALDYGNRLIM 221
|
....
gi 489310645 226 LHQG 229
Cdd:COG1101 222 MHEG 225
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
5-247 |
2.28e-34 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 124.04 E-value: 2.28e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 5 TPALEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQ-ILVAGEELklkaakngelva 83
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERR------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 84 aDGKQINRLRSEIGFV----FQNFNlwPHMSVLDNIIEAPRRVLG---QSKAEATEIAEALLAKVGISDKRHAYPAQLSG 156
Cdd:COG1119 69 -GGEDVWELRKRIGLVspalQLRFP--RDETVLDVVLSGFFDSIGlyrEPTDEQRERARELLELLGLAHLADRPFGTLSQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 157 GQQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEG-RTMLLVTH---EM--GFarqvsSEVVFLHQGL 230
Cdd:COG1119 146 GEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHhveEIppGI-----THVLLLKDGR 220
|
250
....*....|....*...
gi 489310645 231 VEEQGSPQQVF-ENPLSA 247
Cdd:COG1119 221 VVAAGPKEEVLtSENLSE 238
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
8-243 |
2.42e-34 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 124.35 E-value: 2.42e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRcinllenpHQGQILVAGEELKLKAAKNGELVAADGK 87
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLR--------HLSGLITGDKSAGSHIELLGRTVQREGR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 88 ---QINRLRSEIGFVFQNFNLWPHMSVLDNII-----EAP--RRVLGQSKAEATEIAEALLAKVGISDKRHAYPAQLSGG 157
Cdd:PRK09984 77 larDIRKSRANTGYIFQQFNLVNRLSVLENVLigalgSTPfwRTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 158 QQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAE-EGRTMLLVTHEMGFARQVSSEVVFLHQGLVEEQGS 236
Cdd:PRK09984 157 QQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQnDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGS 236
|
....*..
gi 489310645 237 PQQvFEN 243
Cdd:PRK09984 237 SQQ-FDN 242
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
8-239 |
2.70e-34 |
|
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: 123.49 E-value: 2.70e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRYG-ELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKlkaakngelvaadG 86
Cdd:cd03253 1 IEFENVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIR-------------E 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 87 KQINRLRSEIGFVFQNFNLWpHMSVLDNIieaprrVLGQSKAEATEIAEAllAKVG-ISDKRHAYPAQ-----------L 154
Cdd:cd03253 68 VTLDSLRRAIGVVPQDTVLF-NDTIGYNI------RYGRPDATDEEVIEA--AKAAqIHDKIMRFPDGydtivgerglkL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 155 SGGQQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAeEGRTMLLVTHEMgfaRQVSS--EVVFLHQGLVE 232
Cdd:cd03253 139 SGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVS-KGRTTIVIAHRL---STIVNadKIIVLKDGRIV 214
|
....*..
gi 489310645 233 EQGSPQQ 239
Cdd:cd03253 215 ERGTHEE 221
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
8-244 |
2.92e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 124.53 E-value: 2.92e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRY-GELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKlkaakngelvaadG 86
Cdd:PRK13652 4 IETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPIT-------------K 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 87 KQINRLRSEIGFVFQNFNLWPHMSVLDNIIEAPRRVLGQSKAEATEIAEALLAKVGISDKRHAYPAQLSGGQQQRAAIAR 166
Cdd:PRK13652 71 ENIREVRKFVGLVFQNPDDQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489310645 167 TLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEE-GRTMLLVTHEMGFARQVSSEVVFLHQGLVEEQGSPQQVFENP 244
Cdd:PRK13652 151 VIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
19-241 |
3.56e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 124.51 E-value: 3.56e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 19 ELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKLKAAKngelvaadgKQINRLRSEIGF 98
Cdd:PRK13646 19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKD---------KYIRPVRKRIGM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 99 VFQnfnlWPHMSVLDNIIEapRRVL------GQSKAEATEIAEALLAKVGIS-DKRHAYPAQLSGGQQQRAAIARTLAMQ 171
Cdd:PRK13646 90 VFQ----FPESQLFEDTVE--REIIfgpknfKMNLDEVKNYAHRLLMDLGFSrDVMSQSPFQMSGGQMRKIAIVSILAMN 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489310645 172 PKVILFDEPTSALDPEMVQEVLNVIRAL-AEEGRTMLLVTHEMGFARQVSSEVVFLHQGLVEEQGSPQQVF 241
Cdd:PRK13646 164 PDIIVLDEPTAGLDPQSKRQVMRLLKSLqTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELF 234
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
6-244 |
1.59e-33 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 125.34 E-value: 1.59e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 6 PALEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELK-LKAAKNGELVAA 84
Cdd:PRK09536 2 PMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEaLSARAASRRVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 85 -----------DGKQINRL-RSeigfvfqnfnlwPHMSVLDNIIEAPRRVLGQSkAEATEIAEalLAKVGISdkrhaypa 152
Cdd:PRK09536 82 vpqdtslsfefDVRQVVEMgRT------------PHRSRFDTWTETDRAAVERA-MERTGVAQ--FADRPVT-------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 153 QLSGGQQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHEMGFARQVSSEVVFLHQGLVE 232
Cdd:PRK09536 139 SLSGGERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVR 218
|
250
....*....|..
gi 489310645 233 EQGSPQQVFENP 244
Cdd:PRK09536 219 AAGPPADVLTAD 230
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
23-244 |
1.63e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 122.40 E-value: 1.63e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 23 LKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEElklkaakngelvAADGKQINRLRSEIGFVFQN 102
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGID------------TGDFSKLQGIRKLVGIVFQN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 103 fnlwPHMSVLDNIIE-----APRRvLGQSKAEATEIAEALLAKVGISDKRHAYPAQLSGGQQQRAAIARTLAMQPKVILF 177
Cdd:PRK13644 86 ----PETQFVGRTVEedlafGPEN-LCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIF 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489310645 178 DEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHEMGfARQVSSEVVFLHQGLVEEQGSPQQVFENP 244
Cdd:PRK13644 161 DEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLE-ELHDADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
27-235 |
1.88e-33 |
|
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: 120.74 E-value: 1.88e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 27 SLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVageelklkaakngelvaaDGKQINRL---RSEIGFVFQNF 103
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKV------------------NDQSHTGLapyQRPVSMLFQEN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 104 NLWPHMSVLDNIIEAPRRVLgQSKAEATEIAEALLAKVGISDKRHAYPAQLSGGQQQRAAIARTLAMQPKVILFDEPTSA 183
Cdd:TIGR01277 80 NLFAHLTVRQNIGLGLHPGL-KLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489310645 184 LDPEMVQEVLNVIRALAEE-GRTMLLVTHEMGFARQVSSEVVFLHQGLVEEQG 235
Cdd:TIGR01277 159 LDPLLREEMLALVKQLCSErQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
6-244 |
3.21e-33 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 121.09 E-value: 3.21e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 6 PALEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVA---GEELKLKAakngeLV 82
Cdd:TIGR02323 2 PLLQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYImrsGAELELYQ-----LS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 83 AADGKQInrLRSEIGFVFQNF--NLWPHMSVLDNIIEAPRRVLGQSKAEATEIAEALLAKVGISDKR-HAYPAQLSGGQQ 159
Cdd:TIGR02323 77 EAERRRL--MRTEWGFVHQNPrdGLRMRVSAGANIGERLMAIGARHYGNIRATAQDWLEEVEIDPTRiDDLPRAFSGGMQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 160 QRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEE-GRTMLLVTHEMGFARQVSSEVVFLHQGLVEEQGSPQ 238
Cdd:TIGR02323 155 QRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDlGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTD 234
|
....*.
gi 489310645 239 QVFENP 244
Cdd:TIGR02323 235 QVLDDP 240
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
6-211 |
3.36e-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: 3.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 6 PALEIRNLHKRY-GELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKlkaakngELVAA 84
Cdd:TIGR02857 320 SSLEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLA-------DADAD 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 85 DgkqinrLRSEIGFVFQNfnlwPHM---SVLDNIieaprrVLGQSKAEATEIAEALlAKVGISDKRHAYP---------- 151
Cdd:TIGR02857 393 S------WRDQIAWVPQH----PFLfagTIAENI------RLARPDASDAEIREAL-ERAGLDEFVAALPqgldtpigeg 455
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489310645 152 -AQLSGGQQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAeEGRTMLLVTH 211
Cdd:TIGR02857 456 gAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALA-QGRTVLLVTH 515
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
7-244 |
5.98e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 121.06 E-value: 5.98e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 7 ALEIRNLHKRYGELE--VLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPH---QGQILVAGEELklkaakngel 81
Cdd:PRK13640 5 IVEFKHVSFTYPDSKkpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDdnpNSKITVDGITL---------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 82 vaaDGKQINRLRSEIGFVFQN-FNLWPHMSVLDNI---IEApRRVlgqSKAEATEIAEALLAKVGISDKRHAYPAQLSGG 157
Cdd:PRK13640 75 ---TAKTVWDIREKVGIVFQNpDNQFVGATVGDDVafgLEN-RAV---PRPEMIKIVRDVLADVGMLDYIDSEPANLSGG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 158 QQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEE-GRTMLLVTHEMGFARQvSSEVVFLHQGLVEEQGS 236
Cdd:PRK13640 148 QKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKnNLTVISITHDIDEANM-ADQVLVLDDGKLLAQGS 226
|
....*...
gi 489310645 237 PQQVFENP 244
Cdd:PRK13640 227 PVEIFSKV 234
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
8-242 |
6.44e-33 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 125.30 E-value: 6.44e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLEN--PHQGQIL-------------------- 65
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIIyhvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 66 ---VAGEELKLKAAkngELVAADGKQINRLRSEIGFVFQ-NFNLWPHMSVLDNIIEAPRRvLGQSKAEATEIAEALLAKV 141
Cdd:TIGR03269 81 pcpVCGGTLEPEEV---DFWNLSDKLRRRIRKRIAIMLQrTFALYGDDTVLDNVLEALEE-IGYEGKEAVGRAVDLIEMV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 142 GISDKRHAYPAQLSGGQQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALA-EEGRTMLLVTHEMGFARQVS 220
Cdd:TIGR03269 157 QLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVkASGISMVLTSHWPEVIEDLS 236
|
250 260
....*....|....*....|..
gi 489310645 221 SEVVFLHQGLVEEQGSPQQVFE 242
Cdd:TIGR03269 237 DKAIWLENGEIKEEGTPDEVVA 258
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
9-242 |
1.67e-32 |
|
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: 118.48 E-value: 1.67e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 9 EIRNLHKRYGELE-VLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEelklkaakngelvaaDGK 87
Cdd:cd03254 4 EFENVNFSYDEKKpVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGI---------------DIR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 88 QINR--LRSEIGFVFQNFNLWPHmSVLDNIIeaprrvLGQSKAEATEIAEALLAKVG---ISDKRHAYPAQ-------LS 155
Cdd:cd03254 69 DISRksLRSMIGVVLQDTFLFSG-TIMENIR------LGRPNATDEEVIEAAKEAGAhdfIMKLPNGYDTVlgenggnLS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 156 GGQQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALaEEGRTMLLVTHEMGFARQvSSEVVFLHQGLVEEQG 235
Cdd:cd03254 142 QGERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKL-MKGRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEG 219
|
....*..
gi 489310645 236 SPQQVFE 242
Cdd:cd03254 220 THDELLA 226
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
4-244 |
1.70e-32 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 119.32 E-value: 1.70e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 4 ATPALEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKlkaakngelvA 83
Cdd:PRK11300 2 SQPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIE----------G 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 84 ADGKQINRLrseiGFV--FQNFNLWPHMSVLDNIIEAPRRVLG--------------QSKAEATEIAEALLAKVGISDKR 147
Cdd:PRK11300 72 LPGHQIARM----GVVrtFQHVRLFREMTVIENLLVAQHQQLKtglfsgllktpafrRAESEALDRAATWLERVGLLEHA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 148 HAYPAQLSGGQQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEE-GRTMLLVTHEMGFARQVSSEVVFL 226
Cdd:PRK11300 148 NRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVV 227
|
250
....*....|....*...
gi 489310645 227 HQGLVEEQGSPQQVFENP 244
Cdd:PRK11300 228 NQGTPLANGTPEEIRNNP 245
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
26-242 |
3.84e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 119.07 E-value: 3.84e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 26 ISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVaGEELKLKAAKNgelvaadgKQINRLRSEIGFVFQnfnl 105
Cdd:PRK13643 25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTV-GDIVVSSTSKQ--------KEIKPVRKKVGVVFQ---- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 106 WPHM-----SVLDNIIEAPRRvLGQSKAEATEIAEALLAKVGISDK-RHAYPAQLSGGQQQRAAIARTLAMQPKVILFDE 179
Cdd:PRK13643 92 FPESqlfeeTVLKDVAFGPQN-FGIPKEKAEKIAAEKLEMVGLADEfWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489310645 180 PTSALDPEMVQEVLNVIRALAEEGRTMLLVTHEMGFARQVSSEVVFLHQGLVEEQGSPQQVFE 242
Cdd:PRK13643 171 PTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQ 233
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
18-231 |
4.15e-32 |
|
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: 116.50 E-value: 4.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 18 GELEVLKGISLTARDGDVISILGSSGSGKSTFLRCI-NLLENPH-QGQILVAGEELKLkaakngelvaadgkqiNRLRSE 95
Cdd:cd03213 20 SGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALaGRRTGLGvSGEVLINGRPLDK----------------RSFRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 96 IGFVFQNFNLWPHMSVldniieaprrvlgqskaeateiAEALLakvgisdkrhaYPAQL---SGGQQQRAAIARTLAMQP 172
Cdd:cd03213 84 IGYVPQDDILHPTLTV----------------------RETLM-----------FAAKLrglSGGERKRVSIALELVSNP 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489310645 173 KVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHemgfarQVSSE-------VVFLHQGLV 231
Cdd:cd03213 131 SLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIH------QPSSEifelfdkLLLLSQGRV 190
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
6-242 |
6.99e-32 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 122.22 E-value: 6.99e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 6 PALEIRNLHKRY-----GELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILV-AGEELkLKAAKNG 79
Cdd:TIGR03269 278 PIIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrVGDEW-VDMTKPG 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 80 elvaADGKqiNRLRSEIGFVFQNFNLWPHMSVLDNIIEA-----PRRvLGQSKAEATeiaealLAKVGISDKR-----HA 149
Cdd:TIGR03269 357 ----PDGR--GRAKRYIGILHQEYDLYPHRTVLDNLTEAiglelPDE-LARMKAVIT------LKMVGFDEEKaeeilDK 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 150 YPAQLSGGQQQRAAIARTLAMQPKVILFDEPTSALDP-EMVQEVLNVIRALAEEGRTMLLVTHEMGFARQVSSEVVFLHQ 228
Cdd:TIGR03269 424 YPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPiTKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRD 503
|
250
....*....|....
gi 489310645 229 GLVEEQGSPQQVFE 242
Cdd:TIGR03269 504 GKIVKIGDPEEIVE 517
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
8-241 |
8.01e-32 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 117.42 E-value: 8.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKLKAAKN--------- 78
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQlarrlallp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 79 GELVAADGKQINRL----RSEigfvfqNFNLWPHMSVLDNiieapRRVlgQSKAEATEIAEalLAKVGISDkrhaypaqL 154
Cdd:PRK11231 83 QHHLTPEGITVRELvaygRSP------WLSLWGRLSAEDN-----ARV--NQAMEQTRINH--LADRRLTD--------L 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 155 SGGQQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHEMGFARQVSSEVVFLHQGLVEEQ 234
Cdd:PRK11231 140 SGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQ 219
|
....*..
gi 489310645 235 GSPQQVF 241
Cdd:PRK11231 220 GTPEEVM 226
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
5-242 |
9.19e-32 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 118.75 E-value: 9.19e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 5 TPALEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKLKAakngelvaa 84
Cdd:PRK13537 5 VAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRA--------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 85 dgkqiNRLRSEIGFVFQNFNLWPHMSVLDNIIeAPRRVLGQSKAEATEIAEALLAKVGISDKRHAYPAQLSGGQQQRAAI 164
Cdd:PRK13537 76 -----RHARQRVGVVPQFDNLDPDFTVRENLL-VFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489310645 165 ARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHEMGFARQVSSEVVFLHQGLVEEQGSPQQVFE 242
Cdd:PRK13537 150 ARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIE 227
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
8-241 |
1.21e-31 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 117.42 E-value: 1.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKLkaAKNGELVaadgk 87
Cdd:PRK13638 2 LATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDY--SKRGLLA----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 88 qinrLRSEIGFVFQNFNLWPHMSVLDNIIEAPRRVLGQSKAEATEIAEALLAKVGISDKRHAyPAQ-LSGGQQQRAAIAR 166
Cdd:PRK13638 75 ----LRQQVATVFQDPEQQIFYTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQ-PIQcLSHGQKKRVAIAG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489310645 167 TLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHEMGFARQVSSEVVFLHQGLVEEQGSPQQVF 241
Cdd:PRK13638 150 ALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
27-239 |
2.56e-31 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 115.45 E-value: 2.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 27 SLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEelklkaakngelvaaDGKQINRLRSEIGFVFQNFNLW 106
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQ---------------DHTTTPPSRRPVSMLFQENNLF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 107 PHMSVLDNI---IEAPRRVLGQSKAEATEIAEallaKVGISDKRHAYPAQLSGGQQQRAAIARTLAMQPKVILFDEPTSA 183
Cdd:PRK10771 84 SHLTVAQNIglgLNPGLKLNAAQREKLHAIAR----QMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489310645 184 LDPEMVQEVLNVIRALAEEGR-TMLLVTHEMGFARQVSSEVVFLHQGLVEEQGSPQQ 239
Cdd:PRK10771 160 LDPALRQEMLTLVSQVCQERQlTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDE 216
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-242 |
3.33e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 116.39 E-value: 3.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 1 MAEATPALEIRNLHKRYGELE--VLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVageelklkaakN 78
Cdd:PRK13648 1 MEDKNSIIVFKNVSFQYQSDAsfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFY-----------N 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 79 GELVAADGKQinRLRSEIGFVFQN---------------FNLWPHMSVLDNIIEaprrvlgqskaeatEIAEALlAKVGI 143
Cdd:PRK13648 70 NQAITDDNFE--KLRKHIGIVFQNpdnqfvgsivkydvaFGLENHAVPYDEMHR--------------RVSEAL-KQVDM 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 144 SDKRHAYPAQLSGGQQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGR-TMLLVTHEMGFARQvSSE 222
Cdd:PRK13648 133 LERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNiTIISITHDLSEAME-ADH 211
|
250 260
....*....|....*....|
gi 489310645 223 VVFLHQGLVEEQGSPQQVFE 242
Cdd:PRK13648 212 VIVMNKGTVYKEGTPTEIFD 231
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
19-244 |
4.26e-31 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 120.98 E-value: 4.26e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 19 ELEVLKGISLTARDGDVISILGSSGSGKSTflrCINLLEN---PHQGQILVAGEELKlkaakngelvaadgkQINR--LR 93
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKST---VAALLQNlyqPTGGQVLLDGVPLV---------------QYDHhyLH 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 94 SEIGFVFQNFNLWPHmSVLDNIIEAPRRVlgqSKAEATEIAEALLAKVGISDKRHAYP-------AQLSGGQQQRAAIAR 166
Cdd:TIGR00958 555 RQVALVGQEPVLFSG-SVRENIAYGLTDT---PDEEIMAAAKAANAHDFIMEFPNGYDtevgekgSQLSGGQKQRIAIAR 630
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489310645 167 TLAMQPKVILFDEPTSALDPEmVQEVLNVIRALAeeGRTMLLVTHEMGFARQvSSEVVFLHQGLVEEQGSPQQVFENP 244
Cdd:TIGR00958 631 ALVRKPRVLILDEATSALDAE-CEQLLQESRSRA--SRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-255 |
7.28e-31 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 120.35 E-value: 7.28e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 1 MAEATPALEIRNLHKRYG-----------ELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGE 69
Cdd:PRK10261 307 VVDGEPILQVRNLVTRFPlrsgllnrvtrEVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQ 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 70 ELKLKAAKngelvaadgkQINRLRSEIGFVFQN--FNLWPHMSVLDNIIEaPRRV--LGQSKAEATEIAEaLLAKVGISD 145
Cdd:PRK10261 387 RIDTLSPG----------KLQALRRDIQFIFQDpyASLDPRQTVGDSIME-PLRVhgLLPGKAAAARVAW-LLERVGLLP 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 146 KrHA--YPAQLSGGQQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEE-GRTMLLVTHEMGFARQVSSE 222
Cdd:PRK10261 455 E-HAwrYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHR 533
|
250 260 270
....*....|....*....|....*....|...
gi 489310645 223 VVFLHQGLVEEQGSPQQVFENPLSARCKQFMSS 255
Cdd:PRK10261 534 VAVMYLGQIVEIGPRRAVFENPQHPYTRKLMAA 566
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
8-240 |
4.07e-30 |
|
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: 112.58 E-value: 4.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRYG--ELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKLKAAkngelvaad 85
Cdd:cd03252 1 ITFEHVRFRYKpdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADP--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 86 gkqiNRLRSEIGFVFQNfNLWPHMSVLDNIIEAPRrvlGQSKAEATEIAEALLAKVGISDKRHAYP-------AQLSGGQ 158
Cdd:cd03252 72 ----AWLRRQVGVVLQE-NVLFNRSIRDNIALADP---GMSMERVIEAAKLAGAHDFISELPEGYDtivgeqgAGLSGGQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 159 QQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAeEGRTMLLVTHEMGFARQvSSEVVFLHQGLVEEQGSPQ 238
Cdd:cd03252 144 RQRIAIARALIHNPRILIFDEATSALDYESEHAIMRNMHDIC-AGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHD 221
|
..
gi 489310645 239 QV 240
Cdd:cd03252 222 EL 223
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
6-229 |
7.37e-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: 110.21 E-value: 7.37e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 6 PALEIRNLHKRYgeleVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKLK----AAKNG-E 80
Cdd:cd03215 3 PVLEVRGLSVKG----AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRsprdAIRAGiA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 81 LVAADgkqinrlRSEIGFVfqnfnlwPHMSVLDNIIeaprrvlgqskaeateiaeallakvgisdkrhaYPAQLSGGQQQ 160
Cdd:cd03215 79 YVPED-------RKREGLV-------LDLSVAENIA---------------------------------LSSLLSGGNQQ 111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489310645 161 RAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHEMGFARQVSSEVVFLHQG 229
Cdd:cd03215 112 KVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEG 180
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
7-239 |
8.86e-30 |
|
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: 117.36 E-value: 8.86e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 7 ALEIRNLHKRYGE--LEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELklkaakngelvaa 84
Cdd:TIGR03797 451 AIEVDRVTFRYRPdgPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDL------------- 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 85 DGKQINRLRSEIGFVFQNFNLWPHmSVLDNIIEAPRRVLgqskAEATEIAEallaKVGISDKRHAYP-----------AQ 153
Cdd:TIGR03797 518 AGLDVQAVRRQLGVVLQNGRLMSG-SIFENIAGGAPLTL----DEAWEAAR----MAGLAEDIRAMPmgmhtviseggGT 588
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 154 LSGGQQQRAAIARTLAMQPKVILFDEPTSALDPEMvQEVlnVIRALAEEGRTMLLVTHEMGFARQVSSEVVfLHQGLVEE 233
Cdd:TIGR03797 589 LSGGQRQRLLIARALVRKPRILLFDEATSALDNRT-QAI--VSESLERLKVTRIVIAHRLSTIRNADRIYV-LDAGRVVQ 664
|
....*.
gi 489310645 234 QGSPQQ 239
Cdd:TIGR03797 665 QGTYDE 670
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
22-229 |
9.95e-30 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 111.21 E-value: 9.95e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 22 VLKGISLTARDGDVISILGSSGSGKSTFLRCI-NLLENPH--QGQILVAGEELKlkaakngelvaadgkqINRLRSEIGF 98
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAIsGRVEGGGttSGQILFNGQPRK----------------PDQFQKCVAY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 99 VFQNFNLWPHMSVLDNIIEAPRRVLG--QSKAEATEIAE-ALLAKVGISDKRHAYPAQLSGGQQQRAAIARTLAMQPKVI 175
Cdd:cd03234 86 VRQDDILLPGLTVRETLTYTAILRLPrkSSDAIRKKRVEdVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489310645 176 LFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHEMG---FarQVSSEVVFLHQG 229
Cdd:cd03234 166 ILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRsdlF--RLFDRILLLSSG 220
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
8-231 |
1.91e-29 |
|
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: 108.84 E-value: 1.91e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRYGELE--VLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKLKAAkngelvaad 85
Cdd:cd03246 1 LEVENVSFRYPGAEppVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDP--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 86 gkqiNRLRSEIGFVFQNFNLWPHmSVLDNIieaprrvlgqskaeateiaeallakvgisdkrhaypaqLSGGQQQRAAIA 165
Cdd:cd03246 72 ----NELGDHVGYLPQDDELFSG-SIAENI--------------------------------------LSGGQRQRLGLA 108
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489310645 166 RTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHEMGFARQVsSEVVFLHQGLV 231
Cdd:cd03246 109 RALYGNPRILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLASA-DRILVLEDGRV 173
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
6-211 |
4.02e-29 |
|
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: 114.77 E-value: 4.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 6 PALEIRNLHKRY-GELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGeelklkaakngelVAA 84
Cdd:TIGR02868 333 PTLELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDG-------------VPV 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 85 DGKQINRLRSEIGFVFQNFNLWpHMSVLDNIIEAprrvlgqsKAEAT-EIAEALLAKVGISDKRHAYP-----------A 152
Cdd:TIGR02868 400 SSLDQDEVRRRVSVCAQDAHLF-DTTVRENLRLA--------RPDATdEELWAALERVGLADWLRALPdgldtvlgeggA 470
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489310645 153 QLSGGQQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRAlAEEGRTMLLVTH 211
Cdd:TIGR02868 471 RLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLA-ALSGRTVVLITH 528
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
7-236 |
4.85e-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: 115.22 E-value: 4.85e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 7 ALEIRNLHKRYGE--LEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKLkaakngelvaA 84
Cdd:TIGR01846 455 AITFENIRFRYAPdsPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAI----------A 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 85 DGkqiNRLRSEIGFVFQNfNLWPHMSVLDNI-IEAPrrvlGQSKAEATEIAEALLAKVGISDKRHAYPAQ-------LSG 156
Cdd:TIGR01846 525 DP---AWLRRQMGVVLQE-NVLFSRSIRDNIaLCNP----GAPFEHVIHAAKLAGAHDFISELPQGYNTEvgekganLSG 596
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 157 GQQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAeEGRTMLLVTHEMGFARQvSSEVVFLHQGLVEEQGS 236
Cdd:TIGR01846 597 GQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREIC-RGRTVIIIAHRLSTVRA-CDRIIVLEKGQIAESGR 674
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
8-255 |
4.95e-29 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 110.65 E-value: 4.95e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHK---------RYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKLkaakn 78
Cdd:PRK15112 5 LEVRNLSKtfryrtgwfRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHF----- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 79 GELvaadgkqinRLRSE-IGFVFQN--FNLWPHMSVlDNIIEAPRRVLGQSKAEATEIA-EALLAKVGI-SDKRHAYPAQ 153
Cdd:PRK15112 80 GDY---------SYRSQrIRMIFQDpsTSLNPRQRI-SQILDFPLRLNTDLEPEQREKQiIETLRQVGLlPDHASYYPHM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 154 LSGGQQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEE-GRTMLLVTHEMGFARQVSSEVVFLHQGLVE 232
Cdd:PRK15112 150 LAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKqGISYIYVTQHLGMMKHISDQVLVMHQGEVV 229
|
250 260
....*....|....*....|...
gi 489310645 233 EQGSPQQVFENPLSARCKQFMSS 255
Cdd:PRK15112 230 ERGSTADVLASPLHELTKRLIAG 252
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
5-242 |
7.92e-29 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 109.40 E-value: 7.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 5 TPALEIRNLHKRY----------------------GELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQG 62
Cdd:COG1134 2 SSMIEVENVSKSYrlyhepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 63 QILVAGeelklkaakngelvaadgkqinRLRS--EIGFVFQnfnlwPHMSVLDNIieapR---RVLGQSKAEATEIAEAL 137
Cdd:COG1134 82 RVEVNG----------------------RVSAllELGAGFH-----PELTGRENI----YlngRLLGLSRKEIDEKFDEI 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 138 LAKVGISDKRHA----YpaqlSGGQQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHEM 213
Cdd:COG1134 131 VEFAELGDFIDQpvktY----SSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSM 206
|
250 260
....*....|....*....|....*....
gi 489310645 214 GFARQVSSEVVFLHQGLVEEQGSPQQVFE 242
Cdd:COG1134 207 GAVRRLCDRAIWLEKGRLVMDGDPEEVIA 235
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
8-239 |
1.54e-28 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 108.09 E-value: 1.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRYG--ELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKlkaakngelvaad 85
Cdd:cd03251 1 VEFKNVTFRYPgdGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVR------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 86 GKQINRLRSEIGFVFQNFNLWpHMSVLDNIIEAPRrvlGQSKAEATEIAEALLAKVGISDKRHAYPA-------QLSGGQ 158
Cdd:cd03251 68 DYTLASLRRQIGLVSQDVFLF-NDTVAENIAYGRP---GATREEVEEAARAANAHEFIMELPEGYDTvigergvKLSGGQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 159 QQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAeEGRTMLLVTHEMGFARQvSSEVVFLHQGLVEEQGSPQ 238
Cdd:cd03251 144 RQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLM-KNRTTFVIAHRLSTIEN-ADRIVVLEDGKIVERGTHE 221
|
.
gi 489310645 239 Q 239
Cdd:cd03251 222 E 222
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
7-225 |
1.64e-28 |
|
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: 107.68 E-value: 1.64e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 7 ALEIRNLHKRYGELE--VLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGeelklkaakngelvaA 84
Cdd:cd03245 2 RIEFRNVSFSYPNQEipALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDG---------------T 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 85 DGKQINR--LRSEIGFVFQNFNLWpHMSVLDNIieaprrVLGQSKAEATEIAEAL-LAKVGISDKRHAYP---------A 152
Cdd:cd03245 67 DIRQLDPadLRRNIGYVPQDVTLF-YGTLRDNI------TLGAPLADDERILRAAeLAGVTDFVNKHPNGldlqigergR 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489310645 153 QLSGGQQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAeEGRTMLLVTHEMGFARQVSSEVVF 225
Cdd:cd03245 140 GLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLL-GDKTLIIITHRPSLLDLVDRIIVM 211
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-242 |
1.77e-28 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 110.69 E-value: 1.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 1 MAEATPALEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKLKAaknge 80
Cdd:PRK13536 35 GSMSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARA----- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 81 lvaadgkqinRL-RSEIGFVFQNFNLWPHMSVLDNIIeAPRRVLGQSKAEATEIAEALLAKVGISDKRHAYPAQLSGGQQ 159
Cdd:PRK13536 110 ----------RLaRARIGVVPQFDNLDLEFTVRENLL-VFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMK 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 160 QRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHEMGFARQVSSEVVFLHQGLVEEQGSPQQ 239
Cdd:PRK13536 179 RRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHA 258
|
...
gi 489310645 240 VFE 242
Cdd:PRK13536 259 LID 261
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-213 |
4.44e-28 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 111.65 E-value: 4.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 2 AEATPALEIRNLHKRygelEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKLK----AAK 77
Cdd:COG1129 251 APGEVVLEVEGLSVG----GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRsprdAIR 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 78 NG-ELVAADgkqinrlRSEIGFVfqnfnlwPHMSVLDNIIEAPRRVLGQ----SKAEATEIAEALLAKVGIsdkRHAYPA 152
Cdd:COG1129 327 AGiAYVPED-------RKGEGLV-------LDLSIRENITLASLDRLSRggllDRRRERALAEEYIKRLRI---KTPSPE 389
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489310645 153 Q----LSGGQQQRAAIARTLAMQPKVILFDEPTSALDpemV---QEVLNVIRALAEEGRTMLLVTHEM 213
Cdd:COG1129 390 QpvgnLSGGNQQKVVLAKWLATDPKVLILDEPTRGID---VgakAEIYRLIRELAAEGKAVIVISSEL 454
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-244 |
6.60e-28 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 108.66 E-value: 6.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 1 MAEATPALEIRNLHKRY----GELEVLKGISLTARDGDVISILGSSGSGKS-TFLRCINLLENphQGQIlvAGEelklkA 75
Cdd:PRK09473 6 QQQADALLDVKDLRVTFstpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAA--NGRI--GGS-----A 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 76 AKNG-ELVAADGKQINRLRSE-IGFVFQN--FNLWPHMSVLDNIIEaprrVL----GQSKAEATEIAEALLAKVGISDKR 147
Cdd:PRK09473 77 TFNGrEILNLPEKELNKLRAEqISMIFQDpmTSLNPYMRVGEQLME----VLmlhkGMSKAEAFEESVRMLDAVKMPEAR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 148 ---HAYPAQLSGGQQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRT-MLLVTHEMGFARQVSSEV 223
Cdd:PRK09473 153 krmKMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaIIMITHDLGVVAGICDKV 232
|
250 260
....*....|....*....|.
gi 489310645 224 VFLHQGLVEEQGSPQQVFENP 244
Cdd:PRK09473 233 LVMYAGRTMEYGNARDVFYQP 253
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-253 |
8.43e-28 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 107.16 E-value: 8.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 1 MAEATPALEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKlkAAKNGE 80
Cdd:PRK11831 1 EQSVANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIP--AMSRSR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 81 LVAAdgkqinrlRSEIGFVFQNFNLWPHMSVLDNIiEAPRRvlgqskaEATEIAEAL--------LAKVGISDKRHAYPA 152
Cdd:PRK11831 79 LYTV--------RKRMSMLFQSGALFTDMNVFDNV-AYPLR-------EHTQLPAPLlhstvmmkLEAVGLRGAAKLMPS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 153 QLSGGQQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEE-GRTMLLVTHEMGFARQVSSEVVFLHQGLV 231
Cdd:PRK11831 143 ELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSHDVPEVLSIADHAYIVADKKI 222
|
250 260
....*....|....*....|..
gi 489310645 232 EEQGSPQQVFENPlSARCKQFM 253
Cdd:PRK11831 223 VAHGSAQALQANP-DPRVRQFL 243
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
7-242 |
9.66e-28 |
|
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: 111.50 E-value: 9.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 7 ALEIRNLHKRYGELE--VLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGeelklkaakngelvaA 84
Cdd:TIGR03375 463 EIEFRNVSFAYPGQEtpALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDG---------------V 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 85 DGKQINR--LRSEIGFVFQNFNLWpHMSVLDNIIeaprrvLGQSKAEATEIAEALlAKVGISD--KRHayP--------- 151
Cdd:TIGR03375 528 DIRQIDPadLRRNIGYVPQDPRLF-YGTLRDNIA------LGAPYADDEEILRAA-ELAGVTEfvRRH--Pdgldmqige 597
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 152 --AQLSGGQQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAeEGRTMLLVTHEMGFARQVSSEVVfLHQG 229
Cdd:TIGR03375 598 rgRSLSGGQRQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWL-AGKTLVLVTHRTSLLDLVDRIIV-MDNG 675
|
250
....*....|...
gi 489310645 230 LVEEQGSPQQVFE 242
Cdd:TIGR03375 676 RIVADGPKDQVLE 688
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
3-244 |
1.16e-27 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 111.10 E-value: 1.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 3 EATPALEIRNL----HKRYGELEVLKGISLTARDGDVISILGSSGSGKS-TFLRCINLLENPhQGQILVAGEELKLKAAK 77
Cdd:PRK10261 8 DARDVLAVENLniafMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQA-GGLVQCDKMLLRRRSRQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 78 NGELVAADGKQINRLR-SEIGFVFQN--FNLWPHMSVLDNIIEAPRRVLGQSKAEATEIAEALLAKVGISDKRHA---YP 151
Cdd:PRK10261 87 VIELSEQSAAQMRHVRgADMAMIFQEpmTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTIlsrYP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 152 AQLSGGQQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEE-GRTMLLVTHEMGFARQVSSEVVFLHQGL 230
Cdd:PRK10261 167 HQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLVMYQGE 246
|
250
....*....|....
gi 489310645 231 VEEQGSPQQVFENP 244
Cdd:PRK10261 247 AVETGSVEQIFHAP 260
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
8-236 |
2.02e-27 |
|
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: 105.17 E-value: 2.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKLKAAKNgelvaadgk 87
Cdd:TIGR03740 1 LETKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWTRKDLHK--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 88 qinrlrseIGFVFQNFNLWPHMSVLDNIiEAPRRVLGQSKAEATEIaealLAKVGISDKRHAYPAQLSGGQQQRAAIART 167
Cdd:TIGR03740 72 --------IGSLIESPPLYENLTARENL-KVHTTLLGLPDSRIDEV----LNIVDLTNTGKKKAKQFSLGMKQRLGIAIA 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489310645 168 LAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHEMGFARQVSSEVVFLHQGLVEEQGS 236
Cdd:TIGR03740 139 LLNHPKLLILDEPTNGLDPIGIQELRELIRSFPEQGITVILSSHILSEVQQLADHIGIISEGVLGYQGK 207
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
8-235 |
2.34e-27 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 103.55 E-value: 2.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRYGELE--VLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVageelklkaakNGELVAAD 85
Cdd:cd03247 1 LSINNVSFSYPEQEqqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITL-----------DGVPVSDL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 86 GKQinrLRSEIGFVFQNfnlwPHMsvldniieaprrvlgqskaeateIAEALLAKVGIsdkrhaypaQLSGGQQQRAAIA 165
Cdd:cd03247 70 EKA---LSSLISVLNQR----PYL-----------------------FDTTLRNNLGR---------RFSGGERQRLALA 110
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 166 RTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEgRTMLLVTHEMGFARQVsSEVVFLHQGLVEEQG 235
Cdd:cd03247 111 RILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVLKD-KTLIWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
15-239 |
2.95e-27 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 109.75 E-value: 2.95e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 15 KRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLrciNLLENPHQGQILVAGEELKlkaakNGElvAADGKQInRLRS 94
Cdd:TIGR00955 33 RERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLM---NALAFRSPKGVKGSGSVLL-----NGM--PIDAKEM-RAIS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 95 eiGFVFQNFNLWPHMSVLDNII-----EAPRRVlgqSKAEATEIAEALLAKVGISDKRH---AYPAQ---LSGGQQQRAA 163
Cdd:TIGR00955 102 --AYVQQDDLFIPTLTVREHLMfqahlRMPRRV---TKKEKRERVDEVLQALGLRKCANtriGVPGRvkgLSGGERKRLA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 164 IARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHemgfarQVSSE-------VVFLHQGLVEEQGS 236
Cdd:TIGR00955 177 FASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIH------QPSSElfelfdkIILMAEGRVAYLGS 250
|
...
gi 489310645 237 PQQ 239
Cdd:TIGR00955 251 PDQ 253
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
8-241 |
9.76e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 104.79 E-value: 9.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNL---HKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKLKAAKNgelvaa 84
Cdd:PRK13642 5 LEVENLvfkYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWN------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 85 dgkqinrLRSEIGFVFQN-FNLWPHMSVLDNIIEAPRRVLGQSKAEATEIAEALLAkVGISDKRHAYPAQLSGGQQQRAA 163
Cdd:PRK13642 79 -------LRRKIGMVFQNpDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLA-VNMLDFKTREPARLSGGQKQRVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489310645 164 IARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGR-TMLLVTHEMGFARQvSSEVVFLHQGLVEEQGSPQQVF 241
Cdd:PRK13642 151 VAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQlTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELF 228
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
10-229 |
1.64e-26 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 107.46 E-value: 1.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 10 IRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAgeelklkaakngelvaadgkqi 89
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP---------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 90 NRLRseIGFVFQNFNLWPHMSVLDNIIEA--PRRVLGQSKAEATEI-----------------------------AEALL 138
Cdd:COG0488 59 KGLR--IGYLPQEPPLDDDLTVLDTVLDGdaELRALEAELEELEAKlaepdedlerlaelqeefealggweaearAEEIL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 139 AKVGISDKRHAYP-AQLSGGQQQRAAIARTLAMQPKVILFDEPTSALDPEMVQ--EvlnviRALAEEGRTMLLVTHEMGF 215
Cdd:COG0488 137 SGLGFPEEDLDRPvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEwlE-----EFLKNYPGTVLVVSHDRYF 211
|
250
....*....|....
gi 489310645 216 ARQVSSEVVFLHQG 229
Cdd:COG0488 212 LDRVATRILELDRG 225
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
16-217 |
1.72e-26 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 101.54 E-value: 1.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 16 RYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCInllenphqgqilvAGeelkLKAAKNGELVAADGKQINRL--R 93
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVL-------------AG----VLRPTSGTVRRAGGARVAYVpqR 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 94 SEIGFVFQ-------NFNLWPHmsvldniieapRRVLGQSKAEATEIAEALLAKVGISDKRHAYPAQLSGGQQQRAAIAR 166
Cdd:NF040873 64 SEVPDSLPltvrdlvAMGRWAR-----------RGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQ 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489310645 167 TLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHEMGFAR 217
Cdd:NF040873 133 GLAQEADLLLLDEPTTGLDAESRERIIALLAEEHARGATVVVVTHDLELVR 183
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
4-213 |
2.36e-26 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 106.92 E-value: 2.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 4 ATPALEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKLKAAKngelvA 83
Cdd:PRK11288 1 SSPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTT-----A 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 84 AdgkqinrLRSEIGFVFQNFNLWPHMSVLDNIIeaprrvLGQ--------SKAEATEIAEALLAKVGISDKRHAYPAQLS 155
Cdd:PRK11288 76 A-------LAAGVAIIYQELHLVPEMTVAENLY------LGQlphkggivNRRLLNYEAREQLEHLGVDIDPDTPLKYLS 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489310645 156 GGQQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHEM 213
Cdd:PRK11288 143 IGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRM 200
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
4-255 |
2.47e-26 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 106.71 E-value: 2.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 4 ATPALEIRNLH---KRYGEL-EVLKGISLTARDGDVISILGSSGSGKS-TFLRCINLLENPH----QGQILVAGEELklk 74
Cdd:PRK15134 2 TQPLLAIENLSvafRQQQTVrTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESL--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 75 aakngelVAADGKQINRLR-SEIGFVFQNfnlwPHMSV--LDNIIEAPRRVLGQSKAEATEIAEA----LLAKVGI--SD 145
Cdd:PRK15134 79 -------LHASEQTLRGVRgNKIAMIFQE----PMVSLnpLHTLEKQLYEVLSLHRGMRREAARGeilnCLDRVGIrqAA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 146 KR-HAYPAQLSGGQQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEE-GRTMLLVTHEMGFARQVSSEV 223
Cdd:PRK15134 148 KRlTDYPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRV 227
|
250 260 270
....*....|....*....|....*....|..
gi 489310645 224 VFLHQGLVEEQGSPQQVFENPLSARCKQFMSS 255
Cdd:PRK15134 228 AVMQNGRCVEQNRAATLFSAPTHPYTQKLLNS 259
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-233 |
6.37e-26 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 105.53 E-value: 6.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 6 PALEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQIlVAGEELKlkaakngelvaad 85
Cdd:COG0488 314 KVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV-KLGETVK------------- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 86 gkqinrlrseIGFVFQNF-NLWPHMSVLDNIIEAprrvlgqsKAEATEI-AEALLAKVGIS-DKRHAYPAQLSGGQQQRA 162
Cdd:COG0488 380 ----------IGYFDQHQeELDPDKTVLDELRDG--------APGGTEQeVRGYLGRFLFSgDDAFKPVGVLSGGEKARL 441
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489310645 163 AIARTLAMQPKVILFDEPTSALDPEMVqEVLNviRALAE-EGrTMLLVTHEMGFARQVSSEVVFLHQGLVEE 233
Cdd:COG0488 442 ALAKLLLSPPNVLLLDEPTNHLDIETL-EALE--EALDDfPG-TVLLVSHDRYFLDRVATRILEFEDGGVRE 509
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
2-231 |
1.67e-25 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 104.36 E-value: 1.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 2 AEATPALEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEEL-KLKAAKNGE 80
Cdd:PRK15439 6 TTAPPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCaRLTPAKAHQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 81 LvaadgkqinrlrsEIGFVFQNFNLWPHMSVLDNII-EAPRRvlgqskAEATEIAEALLAKVGISDKRHAYPAQLSGGQQ 159
Cdd:PRK15439 86 L-------------GIYLVPQEPLLFPNLSVKENILfGLPKR------QASMQKMKQLLAALGCQLDLDSSAGSLEVADR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489310645 160 QRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHEMGFARQVSSEVVFLHQGLV 231
Cdd:PRK15439 147 QIVEILRGLMRDSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTI 218
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
8-229 |
1.75e-25 |
|
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: 104.14 E-value: 1.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLeNPH---QGQILVAGEELKLKAAKNGElvaa 84
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGV-YPHgtwDGEIYWSGSPLKASNIRDTE---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 85 dgkqinrlRSEIGFVFQNFNLWPHMSVLDNII---EAPRRVLGQSKAEATEIAEALLAKVGISDKRHAYP-AQLSGGQQQ 160
Cdd:TIGR02633 77 --------RAGIVIIHQELTLVPELSVAENIFlgnEITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQ 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489310645 161 RAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHEMGFARQVSSEVVFLHQG 229
Cdd:TIGR02633 149 LVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDG 217
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
22-231 |
4.02e-25 |
|
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: 99.08 E-value: 4.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 22 VLKGISLTARDGDVISILGSSGSGKSTflrCINLLEN---PHQGQILVageelklkaakngelvaaDGKQINR-----LR 93
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKST---VVALLENfyqPQGGQVLL------------------DGKPISQyehkyLH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 94 SEIGFVFQNFNLWPHmSVLDNIIEAprrVLGQSKAEATEIAEALLAKVGISDKRHAYP-------AQLSGGQQQRAAIAR 166
Cdd:cd03248 88 SKVSLVGQEPVLFAR-SLQDNIAYG---LQSCSFECVKEAAQKAHAHSFISELASGYDtevgekgSQLSGGQKQRVAIAR 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489310645 167 TLAMQPKVILFDEPTSALDPEMVQEVLNVIRAlAEEGRTMLLVTHEMGFARQvSSEVVFLHQGLV 231
Cdd:cd03248 164 ALIRNPQVLILDEATSALDAESEQQVQQALYD-WPERRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
8-245 |
4.46e-25 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 101.49 E-value: 4.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIrNLHKRYGELEVLKGISLTARDgdVISILGSSGSGKSTFLRCINLLENPHQGQILVageelklkaakNGELVAADGK 87
Cdd:PRK11144 2 LEL-NFKQQLGDLCLTVNLTLPAQG--ITAIFGRSGAGKTSLINAISGLTRPQKGRIVL-----------NGRVLFDAEK 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 88 QINrLRSE---IGFVFQNFNLWPHMSVLDNIIEAPRRVlgqSKAEATEIAEALlakvGISDKRHAYPAQLSGGQQQRAAI 164
Cdd:PRK11144 68 GIC-LPPEkrrIGYVFQDARLFPHYKVRGNLRYGMAKS---MVAQFDKIVALL----GIEPLLDRYPGSLSGGEKQRVAI 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 165 ARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRT-MLLVTHEMGFARQVSSEVVFLHQGLVEEQGSPQQVFEN 243
Cdd:PRK11144 140 GRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREINIpILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWAS 219
|
..
gi 489310645 244 PL 245
Cdd:PRK11144 220 SA 221
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
8-211 |
4.64e-25 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 99.37 E-value: 4.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCI--NLLENPHQGQILVAGEELKlkaakngELvAAD 85
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmgHPKYEVTSGSILLDGEDIL-------EL-SPD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 86 gkqiNRLRSEIGFVFQN---FnlwPHMSVLD--NIIEAPRRVLGQSKAEATEIAEALLAKVGISD---KRHAYpAQLSGG 157
Cdd:COG0396 73 ----ERARAGIFLAFQYpveI---PGVSVSNflRTALNARRGEELSAREFLKLLKEKMKELGLDEdflDRYVN-EGFSGG 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489310645 158 QQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTH 211
Cdd:COG0396 145 EKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITH 198
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
3-242 |
4.90e-25 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 103.26 E-value: 4.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 3 EATPALEIRNLHKRYG--ELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKlkaakngE 80
Cdd:TIGR02203 326 RARGDVEFRNVTFRYPgrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLA-------D 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 81 LVAADgkqinrLRSEIGFVFQNFNLWPHmSVLDNIIEAPRRVLGQSKAEATEIAEALLAKVGISDKRHAYP-----AQLS 155
Cdd:TIGR02203 399 YTLAS------LRRQVALVSQDVVLFND-TIANNIAYGRTEQADRAEIERALAAAYAQDFVDKLPLGLDTPigengVLLS 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 156 GGQQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALaEEGRTMLLVTHEMGfARQVSSEVVFLHQGLVEEQG 235
Cdd:TIGR02203 472 GGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERL-MQGRTTLVIAHRLS-TIEKADRIVVMDDGRIVERG 549
|
....*..
gi 489310645 236 SPQQVFE 242
Cdd:TIGR02203 550 THNELLA 556
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
8-247 |
1.18e-24 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 98.62 E-value: 1.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLhKRYGELEVLKGISLTARDGDVISILGSSGSGKStfLRCINLLE------NPHQGQILVAGEELkLKAAKNGEL 81
Cdd:PRK10418 5 IELRNI-ALQAAQPLVHGVSLTLQRGRVLALVGGSGSGKS--LTCAAALGilpagvRQTAGRVLLDGKPV-APCALRGRK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 82 VAAdgkqinrlrseigfVFQN----FNlwPHMSVLDNIIEApRRVLGQSKAEATeIAEALLAkVGISDKR---HAYPAQL 154
Cdd:PRK10418 81 IAT--------------IMQNprsaFN--PLHTMHTHARET-CLALGKPADDAT-LTAALEA-VGLENAArvlKLYPFEM 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 155 SGGQQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEE-GRTMLLVTHEMGFARQVSSEVVFLHQGLVEE 233
Cdd:PRK10418 142 SGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKrALGMLLVTHDMGVVARLADDVAVMSHGRIVE 221
|
250
....*....|....
gi 489310645 234 QGSPQQVFENPLSA 247
Cdd:PRK10418 222 QGDVETLFNAPKHA 235
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
14-229 |
1.23e-24 |
|
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: 98.17 E-value: 1.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 14 HKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEelklkaakngelvaADGKQINRLR 93
Cdd:cd03267 28 KRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGL--------------VPWKRRKKFL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 94 SEIGFVF-QNFNLWPHMSVLDNiIEAPRRVLGQSKAEATEIAEALLAKVGISDKRHAYPAQLSGGQQQRAAIARTLAMQP 172
Cdd:cd03267 94 RRIGVVFgQKTQLWWDLPVIDS-FYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489310645 173 KVILFDEPTSALDPEMVQEVLNVIRAL-AEEGRTMLLVTHEMGFARQVSSEVVFLHQG 229
Cdd:cd03267 173 EILFLDEPTIGLDVVAQENIRNFLKEYnRERGTTVLLTSHYMKDIEALARRVLVIDKG 230
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
26-245 |
1.34e-24 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 99.82 E-value: 1.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 26 ISLTARDGDVISILGSSGSGKS-TFLRCINLLENPHQgqilVAGEELKLKaakNGELVAADGKQINRL-RSEIGFVFQN- 102
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYPGR----VMAEKLEFN---GQDLQRISEKERRNLvGAEVAMIFQDp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 103 -FNLWPHMSVLDNIIEAPRRVLGQSKAEATEIAEALLAKVGISD---KRHAYPAQLSGGQQQRAAIARTLAMQPKVILFD 178
Cdd:PRK11022 99 mTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDpasRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIAD 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489310645 179 EPTSALDPEMVQEVLNVIRALAE-EGRTMLLVTHEMGFARQVSSEVVFLHQGLVEEQGSPQQVFENPL 245
Cdd:PRK11022 179 EPTTALDVTIQAQIIELLLELQQkENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAPR 246
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
8-243 |
1.41e-24 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 98.04 E-value: 1.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKLKAAKNgelvaadgk 87
Cdd:PRK10895 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHA--------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 88 qinRLRSEIGFVFQNFNLWPHMSVLDNIIEAPRRVLGQSKAEATEIAEALLAKVGISDKRHAYPAQLSGGQQQRAAIART 167
Cdd:PRK10895 75 ---RARRGIGYLPQEASIFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489310645 168 LAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHEMGFARQVSSEVVFLHQGLVEEQGSPQQVFEN 243
Cdd:PRK10895 152 LAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQD 227
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
6-245 |
1.70e-24 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 99.59 E-value: 1.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 6 PALEIRNL----HKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCI-NLL-ENPH--------QGQILvageeL 71
Cdd:COG4170 2 PLLDIRNLtieiDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAIcGITkDNWHvtadrfrwNGIDL-----L 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 72 KLKAAKNGELVaadgkqinrlRSEIGFVFQNFN--LWPHMSVLDNIIEA-PRRVLG----QSKAEATEIAEALLAKVGIS 144
Cdd:COG4170 77 KLSPRERRKII----------GREIAMIFQEPSscLDPSAKIGDQLIEAiPSWTFKgkwwQRFKWRKKRAIELLHRVGIK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 145 DKRH---AYPAQLSGGQQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAE-EGRTMLLVTHEMGFARQVS 220
Cdd:COG4170 147 DHKDimnSYPHELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQlQGTSILLISHDLESISQWA 226
|
250 260
....*....|....*....|....*
gi 489310645 221 SEVVFLHQGLVEEQGSPQQVFENPL 245
Cdd:COG4170 227 DTITVLYCGQTVESGPTEQILKSPH 251
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-239 |
1.93e-24 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 101.44 E-value: 1.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 2 AEATPALEIRNLHKRY--GELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKlkaakng 79
Cdd:PRK11160 333 AADQVSLTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIA------- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 80 elvAADGKQinrLRSEIGFVFQNFNLWPHmSVLDNIIEAprrvlgqsKAEAT-EIAEALLAKVGIS---DKRHAYPA--- 152
Cdd:PRK11160 406 ---DYSEAA---LRQAISVVSQRVHLFSA-TLRDNLLLA--------APNASdEALIEVLQQVGLEkllEDDKGLNAwlg 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 153 ----QLSGGQQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAeEGRTMLLVTHEMGFARQVSSeVVFLHQ 228
Cdd:PRK11160 471 eggrQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHA-QNKTVLMITHRLTGLEQFDR-ICVMDN 548
|
250
....*....|.
gi 489310645 229 GLVEEQGSPQQ 239
Cdd:PRK11160 549 GQIIEQGTHQE 559
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
26-239 |
3.80e-24 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 100.69 E-value: 3.80e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 26 ISLTARDGDVISILGSSGSGKSTFLrciNLLEN--PHQGQILVAGEELKlkaakngELVAADgkqinrLRSEIGFVFQNF 103
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLL---NALLGflPYQGSLKINGIELR-------ELDPES------WRKHLSWVGQNP 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 104 NLwPHMSVLDNIieaprrVLGQSKAEATEIaEALLAKVGISDKRHAYP-----------AQLSGGQQQRAAIARTLAMQP 172
Cdd:PRK11174 433 QL-PHGTLRDNV------LLGNPDASDEQL-QQALENAWVSEFLPLLPqgldtpigdqaAGLSVGQAQRLALARALLQPC 504
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489310645 173 KVILFDEPTSALDPEMVQEVLNVIRAlAEEGRTMLLVTHEMGFARQVsSEVVFLHQGLVEEQGSPQQ 239
Cdd:PRK11174 505 QLLLLDEPTASLDAHSEQLVMQALNA-ASRRQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGDYAE 569
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
8-229 |
4.14e-24 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 94.05 E-value: 4.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVageelklkaakngelvaadgk 87
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW--------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 88 qinrlrseigfvfqnfnlwphmsvldniieaprrvlgqskaeateiaeallakvgISDKRHAYPAQLSGGQQQRAAIART 167
Cdd:cd03221 60 -------------------------------------------------------GSTVKIGYFEQLSGGEKMRLALAKL 84
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489310645 168 LAMQPKVILFDEPTSALDPEMVQEvlnVIRALAEEGRTMLLVTHEMGFARQVSSEVVFLHQG 229
Cdd:cd03221 85 LLENPNLLLLDEPTNHLDLESIEA---LEEALKEYPGTVILVSHDRYFLDQVATKIIELEDG 143
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
4-211 |
7.94e-24 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 99.62 E-value: 7.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 4 ATPALEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLEnPH---QGQILVAGEELKLKAAKNGE 80
Cdd:PRK13549 2 MEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEELQASNIRDTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 81 lvaadgkqinrlRSEIGFVFQNFNLWPHMSVLDNIIeaprrvLGQ--------SKAEATEIAEALLAKVGISDKRHAYPA 152
Cdd:PRK13549 81 ------------RAGIAIIHQELALVKELSVLENIF------LGNeitpggimDYDAMYLRAQKLLAQLKLDINPATPVG 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489310645 153 QLSGGQQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTH 211
Cdd:PRK13549 143 NLGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISH 201
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-229 |
8.53e-24 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 99.47 E-value: 8.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 4 ATPALEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEEL-KLK---AAKNG 79
Cdd:PRK09700 2 ATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYnKLDhklAAQLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 80 elvaadgkqinrlrseIGFVFQNFNLWPHMSVLDNII---EAPRRVLGQSK---AEATEIAEALLAKVGISDKRHAYPAQ 153
Cdd:PRK09700 82 ----------------IGIIYQELSVIDELTVLENLYigrHLTKKVCGVNIidwREMRVRAAMMLLRVGLKVDLDEKVAN 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489310645 154 LSGGQQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHEMGFARQVSSEVVFLHQG 229
Cdd:PRK09700 146 LSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1-240 |
1.09e-23 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 96.21 E-value: 1.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 1 MAEATPALEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKLKAAknge 80
Cdd:PRK10253 1 MTESVARLRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYAS---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 81 lvaadgKQINRlrsEIGFVFQNFNLWPHMSVLDNIIEA--PRRVLGQ--SKAEATEIAEALLAkVGISDKRHAYPAQLSG 156
Cdd:PRK10253 77 ------KEVAR---RIGLLAQNATTPGDITVQELVARGryPHQPLFTrwRKEDEEAVTKAMQA-TGITHLADQSVDTLSG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 157 GQQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRAL-AEEGRTMLLVTHEMGFARQVSSEVVFLHQGLVEEQG 235
Cdd:PRK10253 147 GQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELnREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQG 226
|
....*
gi 489310645 236 SPQQV 240
Cdd:PRK10253 227 APKEI 231
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
22-242 |
2.54e-23 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 98.28 E-value: 2.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 22 VLKGISLTARDGDVISILGSSGSGKSTFLRCI-NLLEnPHQGQILVAGeelklkaakngelvaADGKQINR--LRSEIGF 98
Cdd:COG4618 347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLvGVWP-PTAGSVRLDG---------------ADLSQWDReeLGRHIGY 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 99 VFQNFNLWPHmSVLDNI-----------IEAPRR------VLGQSKAEATEIAEAllakvgisdkrhayPAQLSGGQQQR 161
Cdd:COG4618 411 LPQDVELFDG-TIAENIarfgdadpekvVAAAKLagvhemILRLPDGYDTRIGEG--------------GARLSGGQRQR 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 162 AAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHEMGFARQVSSeVVFLHQGLVEEQGSPQQVF 241
Cdd:COG4618 476 IGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPSLLAAVDK-LLVLRDGRVQAFGPRDEVL 554
|
.
gi 489310645 242 E 242
Cdd:COG4618 555 A 555
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-212 |
4.13e-23 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 93.63 E-value: 4.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 1 MAEATPALEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELklkAAKNGE 80
Cdd:PRK10247 1 MQENSPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDI---STLKPE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 81 lvaadgkqinRLRSEIGFVFQNFNLWPHmSVLDNIIeAPRRVLGQSKAEATEIAEalLAKVGISDKRHAYP-AQLSGGQQ 159
Cdd:PRK10247 78 ----------IYRQQVSYCAQTPTLFGD-TVYDNLI-FPWQIRNQQPDPAIFLDD--LERFALPDTILTKNiAELSGGEK 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489310645 160 QRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEE-GRTMLLVTHE 212
Cdd:PRK10247 144 QRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREqNIAVLWVTHD 197
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
8-211 |
5.49e-23 |
|
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: 92.81 E-value: 5.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELklkaakngelvaadGK 87
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPL--------------AE 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 88 QINRLRSEIGFVFQNFNLWPHMSVLDNIieaprRVLGQSKAEATEIAEALLAKVGISDKRHAYPAQLSGGQQQRAAIART 167
Cdd:TIGR01189 67 QRDEPHENILYLGHLPGLKPELSALENL-----HFWAAIHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARL 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489310645 168 LAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTH 211
Cdd:TIGR01189 142 WLSRRPLWILDEPTTALDKAGVALLAGLLRAHLARGGIVLLTTH 185
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
8-237 |
5.59e-23 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 92.59 E-value: 5.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCInlLENPH----QGQILVAGEELKlkaakngELVA 83
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTI--MGHPKyevtEGEILFKGEDIT-------DLPP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 84 ADgkqinRLRSEIGFVFQNfnlwphmsvldniieaPRRVLGQSKAEateiaeaLLAKVGISdkrhaypaqLSGGQQQRAA 163
Cdd:cd03217 72 EE-----RARLGIFLAFQY----------------PPEIPGVKNAD-------FLRYVNEG---------FSGGEKKRNE 114
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489310645 164 IARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHEMGFARQVSSEVVF-LHQGLVEEQGSP 237
Cdd:cd03217 115 ILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHYQRLLDYIKPDRVHvLYDGRIVKSGDK 189
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
8-211 |
4.63e-22 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 90.32 E-value: 4.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEElklkaakngelvaadgK 87
Cdd:PRK13539 3 LEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGD----------------I 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 88 QINRLRSEIGFV-FQNFnLWPHMSVLDNIiEAPRRVLGQskaEATEIAEALlAKVGISDKRHAYPAQLSGGQQQRAAIAR 166
Cdd:PRK13539 67 DDPDVAEACHYLgHRNA-MKPALTVAENL-EFWAAFLGG---EELDIAAAL-EAVGLAPLAHLPFGYLSAGQKRRVALAR 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489310645 167 TLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTH 211
Cdd:PRK13539 141 LLVSNRPIWILDEPTAALDAAAVALFAELIRAHLAQGGIVIAATH 185
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
16-211 |
5.47e-22 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 90.79 E-value: 5.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 16 RYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCInllenphqgqilvAGEELKLKAAKNGELvaadgkqinrlrse 95
Cdd:COG2401 39 RVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLL-------------AGALKGTPVAGCVDV-------------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 96 igfvfQNFNLWPHMSVLDNIieaPRRvlgQSKAEATEIaealLAKVGISDkrhAY-----PAQLSGGQQQRAAIARTLAM 170
Cdd:COG2401 92 -----PDNQFGREASLIDAI---GRK---GDFKDAVEL----LNAVGLSD---AVlwlrrFKELSTGQKFRFRLALLLAE 153
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489310645 171 QPKVILFDEPTSALDPEMVQEV-LNVIRALAEEGRTMLLVTH 211
Cdd:COG2401 154 RPKLLVIDEFCSHLDRQTAKRVaRNLQKLARRAGITLVVATH 195
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
23-236 |
5.62e-22 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 94.64 E-value: 5.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 23 LKGISLTARDGDVISILGSSGSGKSTFlrcINLLE---NPHQGQILVAGEelklkaakngelvaaDGKQINR--LRSEIG 97
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTL---INLLQrvfDPQSGRILIDGT---------------DIRTVTRasLRRNIA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 98 FVFQN---FNlwphMSVLDNIieaprRVlGQSKA------EATEIAEALLAkvgISDKRHAYPA-------QLSGGQQQR 161
Cdd:PRK13657 413 VVFQDaglFN----RSIEDNI-----RV-GRPDAtdeemrAAAERAQAHDF---IERKPDGYDTvvgergrQLSGGERQR 479
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489310645 162 AAIARTLAMQPKVILFDEPTSALDPEM---VQEVLNVIRalaeEGRTMLLVTHEMGFARQvSSEVVFLHQGLVEEQGS 236
Cdd:PRK13657 480 LAIARALLKDPPILILDEATSALDVETeakVKAALDELM----KGRTTFIIAHRLSTVRN-ADRILVFDNGRVVESGS 552
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
10-235 |
8.11e-22 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 90.28 E-value: 8.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 10 IRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGeelklkaakngelvaadgkqi 89
Cdd:cd03220 25 ILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG--------------------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 90 nRLRS--EIGFVFQnfnlwPHMSVLDNIieapR---RVLGQSKAEATEIAEALLAKVGISDKRHAYPAQLSGGQQQRAAI 164
Cdd:cd03220 84 -RVSSllGLGGGFN-----PELTGRENI----YlngRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAF 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489310645 165 ARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHEMGFARQVSSEVVFLHQGLVEEQG 235
Cdd:cd03220 154 AIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
8-236 |
1.08e-21 |
|
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: 93.65 E-value: 1.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRYG-ELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKlkaakngelvaadg 86
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLK-------------- 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 87 kQINR--LRSEIGFVFQNfnlwPHM---SVLDNIIEAPRRVLGQSKA-EATEIAEAllaKVGISDKRHAYPAQL------ 154
Cdd:TIGR01193 540 -DIDRhtLRQFINYLPQE----PYIfsgSILENLLLGAKENVSQDEIwAACEIAEI---KDDIENMPLGYQTELseegss 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 155 -SGGQQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEegRTMLLVTHEMGFARQvSSEVVFLHQGLVEE 233
Cdd:TIGR01193 612 iSGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQD--KTIIFVAHRLSVAKQ-SDKIIVLDHGKIIE 688
|
...
gi 489310645 234 QGS 236
Cdd:TIGR01193 689 QGS 691
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
19-212 |
2.56e-21 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 92.64 E-value: 2.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 19 ELEVLKGISLTARDGDVISILGSSGSGKSTFLrciNLLENPHQGQILVageelklkaaknGELVAADGKQINRLRSEIGF 98
Cdd:PLN03211 80 ERTILNGVTGMASPGEILAVLGPSGSGKSTLL---NALAGRIQGNNFT------------GTILANNRKPTKQILKRTGF 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 99 VFQNFNLWPHMSVLDNII-----EAPRRVLGQSKAEATE--IAEALLAKVGISDKRHAYPAQLSGGQQQRAAIARTLAMQ 171
Cdd:PLN03211 145 VTQDDILYPHLTVRETLVfcsllRLPKSLTKQEKILVAEsvISELGLTKCENTIIGNSFIRGISGGERKRVSIAHEMLIN 224
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489310645 172 PKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHE 212
Cdd:PLN03211 225 PSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQ 265
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
22-244 |
3.51e-21 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 89.46 E-value: 3.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 22 VLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKlkaakngelvAADGKQINRlrsEIGFVFQ 101
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLE----------SWSSKAFAR---KVAYLPQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 102 NFNLWPHMSV--LDNIIEAP-RRVLGQSKAEATEIAEALLAKVGISDKRHAYPAQLSGGQQQRAAIARTLAMQPKVILFD 178
Cdd:PRK10575 93 QLPAAEGMTVreLVAIGRYPwHGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLD 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489310645 179 EPTSALDPEMVQEVLNVIRALAEE-GRTMLLVTHEMGFARQVSSEVVFLHQGLVEEQGSPQQVFENP 244
Cdd:PRK10575 173 EPTSALDIAHQVDVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGE 239
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
6-237 |
4.01e-21 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 92.38 E-value: 4.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 6 PALEIRNLHK---RYGELEVLKgISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKlkaakngelv 82
Cdd:TIGR01257 927 PGVCVKNLVKifePSGRPAVDR-LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIE---------- 995
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 83 aadgKQINRLRSEIGFVFQNFNLWPHMSVLDNIIEAPRrVLGQSKAEATEIAEALLAKVGISDKRHAYPAQLSGGQQQRA 162
Cdd:TIGR01257 996 ----TNLDAVRQSLGMCPQHNILFHHLTVAEHILFYAQ-LKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKL 1070
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489310645 163 AIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALaEEGRTMLLVTHEMGFARQVSSEVVFLHQGLVEEQGSP 237
Cdd:TIGR01257 1071 SVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKY-RSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
6-236 |
7.49e-21 |
|
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: 91.42 E-value: 7.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 6 PALEIRNLHKRY-GELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKlkaakngelvaa 84
Cdd:COG5265 356 GEVRFENVSFGYdPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIR------------ 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 85 DGKQiNRLRSEIGFVFQN---FNlwphMSVLDNIIEAprrvlgqsKAEAT--EIAEAL-LAKVG--ISDKRHAYPAQ--- 153
Cdd:COG5265 424 DVTQ-ASLRAAIGIVPQDtvlFN----DTIAYNIAYG--------RPDASeeEVEAAArAAQIHdfIESLPDGYDTRvge 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 154 ----LSGGQQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAeEGRTMLLVTHEMgfarqvSS-----EVV 224
Cdd:COG5265 491 rglkLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVA-RGRTTLVIAHRL------STivdadEIL 563
|
250
....*....|..
gi 489310645 225 FLHQGLVEEQGS 236
Cdd:COG5265 564 VLEAGRIVERGT 575
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
5-213 |
8.96e-21 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 90.83 E-value: 8.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 5 TPALEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKLKAAKNGElvaa 84
Cdd:PRK10762 2 QALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQ---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 85 dgkqinrlRSEIGFVFQNFNLWPHMSVLDNII---EAPRRVLGQSKAEATEIAEALLAKVGISDKRHAYPAQLSGGQQQR 161
Cdd:PRK10762 78 --------EAGIGIIHQELNLIPQLTIAENIFlgrEFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQM 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489310645 162 AAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHEM 213
Cdd:PRK10762 150 VEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRL 201
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
22-229 |
9.50e-21 |
|
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: 86.75 E-value: 9.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 22 VLKGISLTARDGDVISILGSSGSGKSTFLRCInLLE-NPHQGQILVAGEelklkaakngelvaadgkqinrlrseIGFVF 100
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSAL-LGElEKLSGSVSVPGS--------------------------IAYVS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 101 QN---FNlwphMSVLDNII-----EAPR--RVLgqsKA-------------EATEIAEAllakvGISdkrhaypaqLSGG 157
Cdd:cd03250 73 QEpwiQN----GTIRENILfgkpfDEERyeKVI---KAcalepdleilpdgDLTEIGEK-----GIN---------LSGG 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489310645 158 QQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVL-NVIRALAEEGRTMLLVTHEMGFARQVSSeVVFLHQG 229
Cdd:cd03250 132 QKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFeNCILGLLLNNKTRILVTHQLQLLPHADQ-IVVLDNG 203
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
23-247 |
1.24e-20 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 87.59 E-value: 1.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 23 LKGISLTARDGDVISILGSSGSGKSTFLRCI-NLLenPHQGQILVAGEELKlkaakngelvAADGKQINRLRseiGFVFQ 101
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMaGLL--PGQGEILLNGRPLS----------DWSAAELARHR---AYLSQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 102 NFNLWPHMSV---LDniieaprrvLGQSKAEATEIAEALLAKV----GISDKRHAYPAQLSGGQQQRAAIARTLAM---- 170
Cdd:COG4138 77 QQSPPFAMPVfqyLA---------LHQPAGASSEAVEQLLAQLaealGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwpt 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 171 ---QPKVILFDEPTSALDpeMVQEV--LNVIRALAEEGRTMLLVTHEMGFARQVSSEVVFLHQGLVEEQGSPQQVF-ENP 244
Cdd:COG4138 148 inpEGQLLLLDEPMNSLD--VAQQAalDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMtPEN 225
|
...
gi 489310645 245 LSA 247
Cdd:COG4138 226 LSE 228
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
23-214 |
1.75e-20 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 87.63 E-value: 1.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 23 LKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKLKAAKNgeLVAadgkqinrlrseigFVFQN 102
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKN--LVA--------------YVPQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 103 FNL-WPHMSVLDNIIEAPRR----VLGQSKAEATEIAEALLAKVGISDKRHAYPAQLSGGQQQRAAIARTLAMQPKVILF 177
Cdd:PRK15056 87 EEVdWSFPVLVEDVVMMGRYghmgWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILL 166
|
170 180 190
....*....|....*....|....*....|....*..
gi 489310645 178 DEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHEMG 214
Cdd:PRK15056 167 DEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLG 203
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
6-236 |
1.90e-20 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 86.86 E-value: 1.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 6 PALEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELklkaakngelvaAD 85
Cdd:PRK11614 4 VMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDI------------TD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 86 GKQINRLRSEIGFVFQNFNLWPHMSVLDNIIEAPRRVLGQSKAEATEIAEALLAKvgISDKRHAYPAQLSGGQQQRAAIA 165
Cdd:PRK11614 72 WQTAKIMREAVAIVPEGRRVFSRMTVEENLAMGGFFAERDQFQERIKWVYELFPR--LHERRIQRAGTMSGGEQQMLAIG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489310645 166 RTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHEMGFARQVSSEVVFLHQGLV--EEQGS 236
Cdd:PRK11614 150 RALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVvlEDTGD 222
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
8-211 |
4.39e-20 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 85.24 E-value: 4.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEelklkaakngelvaADGK 87
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGG--------------PLDF 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 88 QINRLRSEIGFVFQNFNLWPHMSVLDNIieaprRVLgqSKAEATEIAEALLAKVGISDKRHAYPAQLSGGQQQRAAIART 167
Cdd:cd03231 67 QRDSIARGLLYLGHAPGIKTTLSVLENL-----RFW--HADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARL 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489310645 168 LAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTH 211
Cdd:cd03231 140 LLSGRPLWILDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTH 183
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
18-240 |
5.18e-20 |
|
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: 88.56 E-value: 5.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 18 GELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQIlvageelklkaakngELVAADGKQINR--LRSE 95
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSV---------------RLDGADLKQWDRetFGKH 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 96 IGFVFQNFNLWPHmSVLDNIIEAPRRVLGQSKAEATEIAEA--LLAKV--GISDKRHAYPAQLSGGQQQRAAIARTLAMQ 171
Cdd:TIGR01842 394 IGYLPQDVELFPG-TVAENIARFGENADPEKIIEAAKLAGVheLILRLpdGYDTVIGPGGATLSGGQRQRIALARALYGD 472
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489310645 172 PKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHEMGfARQVSSEVVFLHQGLVEEQGSPQQV 240
Cdd:TIGR01842 473 PKLVVLDEPNSNLDEEGEQALANAIKALKARGITVVVITHRPS-LLGCVDKILVLQDGRIARFGERDEV 540
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
6-237 |
6.73e-20 |
|
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: 84.85 E-value: 6.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 6 PALEIRNLHKRYGELE--VLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKlkaakngelva 83
Cdd:cd03244 1 GDIEFKNVSLRYRPNLppVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDIS----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 84 adgkQI--NRLRSEIGFVFQN---------FNLWPHMSVLD-NIIEAPRRVlgQSKAEATEIAEALLAKVgisdkrHAYP 151
Cdd:cd03244 70 ----KIglHDLRSRISIIPQDpvlfsgtirSNLDPFGEYSDeELWQALERV--GLKEFVESLPGGLDTVV------EEGG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 152 AQLSGGQQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIR-ALAeeGRTMLLVTHE----MGFARqvsseVVFL 226
Cdd:cd03244 138 ENLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIReAFK--DCTVLTIAHRldtiIDSDR-----ILVL 210
|
250
....*....|.
gi 489310645 227 HQGLVEEQGSP 237
Cdd:cd03244 211 DKGRVVEFDSP 221
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
6-213 |
2.53e-19 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 86.76 E-value: 2.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 6 PALEIRNLHKRygELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELK----LKAAKNGEL 81
Cdd:PRK09700 264 TVFEVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISprspLDAVKKGMA 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 82 VaadgkqINRLRSEIGFvFQNFNLWPHMSVLDNIIEAPRRV---LGQSKAEAtEIAEALLAKVGIsdKRHAYP---AQLS 155
Cdd:PRK09700 342 Y------ITESRRDNGF-FPNFSIAQNMAISRSLKDGGYKGamgLFHEVDEQ-RTAENQRELLAL--KCHSVNqniTELS 411
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489310645 156 GGQQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHEM 213
Cdd:PRK09700 412 GGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSEL 469
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
10-229 |
4.25e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 84.75 E-value: 4.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 10 IRNL-HKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKlkaakngelvaadgKQ 88
Cdd:COG4586 24 LKGLfRREYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPF--------------KR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 89 INRLRSEIGFVF-QNFNLWPHMSVLDN------IIEAPRRVLGQSKAEATEiaeaLLakvGISDKRHAyPA-QLSGGQQQ 160
Cdd:COG4586 90 RKEFARRIGVVFgQRSQLWWDLPAIDSfrllkaIYRIPDAEYKKRLDELVE----LL---DLGELLDT-PVrQLSLGQRM 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 161 RAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRAL-AEEGRTMLLVTHEMGFARQVSSEVVFLHQG 229
Cdd:COG4586 162 RCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYnRERGTTILLTSHDMDDIEALCDRVIVIDHG 231
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
10-229 |
6.30e-19 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 85.55 E-value: 6.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 10 IRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKLKAAKNGelvaadgkqi 89
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEA---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 90 nrLRSEIGFVFQNFNLWPHMSVLDNII--EAPRRVLGQSKAEATEIAEALLAKVGISDKRHAYPAQLSGGQQQRAAIART 167
Cdd:PRK10982 71 --LENGISMVHQELNLVLQRSVMDNMWlgRYPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489310645 168 LAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHEMGFARQVSSEVVFLHQG 229
Cdd:PRK10982 149 FSYNAKIVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDG 210
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
22-252 |
9.86e-19 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 82.95 E-value: 9.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 22 VLKGISLTARDGDVISILGSSGSGKSTFLRCI--NLLENPHQGQILVAGEelklkAAKNGE-LVAADGKQINRLR----- 93
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALagDLTGGGAPRGARVTGD-----VTLNGEpLAAIDAPRLARLRavlpq 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 94 -SEIGFVFQNFNL-----WPHMsvldniieaprRVLGQSKAEATEIAEALLAKVGISDKRHAYPAQLSGGQQQRAAIART 167
Cdd:PRK13547 91 aAQPAFAFSAREIvllgrYPHA-----------RRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 168 LAM---------QPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRT-MLLVTHEMGFARQVSSEVVFLHQGLVEEQGSP 237
Cdd:PRK13547 160 LAQlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLgVLAIVHDPNLAARHADRIAMLADGAIVAHGAP 239
|
250
....*....|....*
gi 489310645 238 QQVFENPLSARCKQF 252
Cdd:PRK13547 240 ADVLTPAHIARCYGF 254
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
6-212 |
1.70e-18 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 84.31 E-value: 1.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 6 PALEIRNLH-KRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELklkaakngelVAA 84
Cdd:COG3845 256 VVLEVENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDI----------TGL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 85 DGKQINRL--------RSEIGFVfqnfnlwPHMSVLDNII-----EAPRRVLG-QSKAEATEIAEALLAKVGISDKRHAY 150
Cdd:COG3845 326 SPRERRRLgvayipedRLGRGLV-------PDMSVAENLIlgryrRPPFSRGGfLDRKAIRAFAEELIEEFDVRTPGPDT 398
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489310645 151 PA-QLSGGQQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHE 212
Cdd:COG3845 399 PArSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISED 461
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
26-240 |
1.56e-17 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 81.50 E-value: 1.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 26 ISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKLKAAKNG-----ELVAADgkqinrlRSEIGFVf 100
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAiragiMLCPED-------RKAEGII- 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 101 qnfnlwPHMSVLDNI-IEAPR-----RVLGQSKAEAtEIAEALLAKVGISDKRHAYP-AQLSGGQQQRAAIARTLAMQPK 173
Cdd:PRK11288 344 ------PVHSVADNInISARRhhlraGCLINNRWEA-ENADRFIRSLNIKTPSREQLiMNLSGGNQQKAILGRWLSEDMK 416
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489310645 174 VILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHEMGFARQVSSEVVFLHQG-----LVEEQGSPQQV 240
Cdd:PRK11288 417 VILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGriageLAREQATERQA 488
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-211 |
2.59e-17 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 78.53 E-value: 2.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 1 MAEATPALEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCI------NLLEnphqGQILVAGEELKLK 74
Cdd:CHL00131 1 MNKNKPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIaghpayKILE----GDILFKGESILDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 75 AAKngelvaadgkqinrLRSEIGfVFQNFNlWP-------HMSVLDNIIEAPRRVLGQSKAEATEIAEALLAKVGISDKR 147
Cdd:CHL00131 77 EPE--------------ERAHLG-IFLAFQ-YPieipgvsNADFLRLAYNSKRKFQGLPELDPLEFLEIINEKLKLVGMD 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489310645 148 HAYPAQ-----LSGGQQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTH 211
Cdd:CHL00131 141 PSFLSRnvnegFSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITH 209
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
8-236 |
2.65e-17 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 80.83 E-value: 2.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRYGELEV--LKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKLKAAKNgelvaad 85
Cdd:PRK11176 342 IEFRNVTFTYPGKEVpaLRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLAS------- 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 86 gkqinrLRSEIGFVFQNFNLWpHMSVLDNIIEAPRRVLgqSKAEATEIAEALLAKVGISDKRHAYP-------AQLSGGQ 158
Cdd:PRK11176 415 ------LRNQVALVSQNVHLF-NDTIANNIAYARTEQY--SREQIEEAARMAYAMDFINKMDNGLDtvigengVLLSGGQ 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 159 QQRAAIARTLAMQPKVILFDEPTSALDPE---MVQEVLNVIRalaeEGRTMLLVTHEMGFARQvSSEVVFLHQGLVEEQG 235
Cdd:PRK11176 486 RQRIAIARALLRDSPILILDEATSALDTEserAIQAALDELQ----KNRTSLVIAHRLSTIEK-ADEILVVEDGEIVERG 560
|
.
gi 489310645 236 S 236
Cdd:PRK11176 561 T 561
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
8-229 |
3.69e-17 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 80.22 E-value: 3.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLrciNLLEN--PH---QGQILVAGEELKLKAAKNGElv 82
Cdd:NF040905 2 LEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLM---KVLSGvyPHgsyEGEILFDGEVCRFKDIRDSE-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 83 aADGkqinrlrseIGFVFQNFNLWPHMSVLDNIIeaprrvLGQSKA--------EATEIAEALLAKVGISDKRHAYPAQL 154
Cdd:NF040905 77 -ALG---------IVIIHQELALIPYLSIAENIF------LGNERAkrgvidwnETNRRARELLAKVGLDESPDTLVTDI 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489310645 155 SGGQQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHEMGFARQVSSEVVFLHQG 229
Cdd:NF040905 141 GVGKQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDG 215
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
4-235 |
9.45e-17 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 78.62 E-value: 9.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 4 ATPALEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKStflrcinllenphQGQI--LVAGEELKLKAAKNGEL 81
Cdd:NF000106 10 ARNAVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**-------------RGALpaHV*GPDAGRRPWRF*TW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 82 VAadgkqiNR--LRSEIGF-------VFQNFNLWPHMSVLDniieaprRVLGQSKAEATEIAEALLAKVGISDKRHAYPA 152
Cdd:NF000106 77 CA------NRraLRRTIG*hrpvr*gRRESFSGRENLYMIG-------R*LDLSRKDARARADELLERFSLTEAAGRAAA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 153 QLSGGQQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHEMGFARQVSSEVVFLHQGLVE 232
Cdd:NF000106 144 KYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVI 223
|
...
gi 489310645 233 EQG 235
Cdd:NF000106 224 ADG 226
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
8-211 |
1.40e-16 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 75.61 E-value: 1.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVageelklkaakngelvaaDGK 87
Cdd:PRK13538 2 LEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLW------------------QGE 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 88 QINRLRSEigfvFQNFNLW--------PHMSVLDNIIEApRRVLGQSKAEAteIAEALlAKVGISDKRHAYPAQLSGGQQ 159
Cdd:PRK13538 64 PIRRQRDE----YHQDLLYlghqpgikTELTALENLRFY-QRLHGPGDDEA--LWEAL-AQVGLAGFEDVPVRQLSAGQQ 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489310645 160 QRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTH 211
Cdd:PRK13538 136 RRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALLAQHAEQGGMVILTTH 187
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
7-244 |
4.04e-16 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 77.45 E-value: 4.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 7 ALEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEEL-KLkaakngelvaad 85
Cdd:PRK10789 315 DVNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLtKL------------ 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 86 gkQINRLRSEIGFVFQNFNLWPHmSVLDNIieaprrVLGQSKAEATEIAE-ALLAKV--GISDKRHAYPAQ-------LS 155
Cdd:PRK10789 383 --QLDSWRSRLAVVSQTPFLFSD-TVANNI------ALGRPDATQQEIEHvARLASVhdDILRLPQGYDTEvgergvmLS 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 156 GGQQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAeEGRTMLLVTHEMGfARQVSSEVVFLHQGLVEEQG 235
Cdd:PRK10789 454 GGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWG-EGRTVIISAHRLS-ALTEASEILVMQHGHIAQRG 531
|
....*....
gi 489310645 236 SPQQVFENP 244
Cdd:PRK10789 532 NHDQLAQQS 540
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
15-239 |
8.72e-16 |
|
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: 74.37 E-value: 8.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 15 KRYGE--LEVLKGislTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKLKAAKngelVAADGKqinrl 92
Cdd:cd03237 8 KTLGEftLEVEGG---SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQY----IKADYE----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 93 rseigfvfqnfnlwphMSVLDNIIEAPRRVLGQSKAEaTEIAEALLAKvGISDKRhayPAQLSGGQQQRAAIARTLAMQP 172
Cdd:cd03237 76 ----------------GTVRDLLSSITKDFYTHPYFK-TEIAKPLQIE-QILDRE---VPELSGGELQRVAIAACLSKDA 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489310645 173 KVILFDEPTSALDPEMVQEVLNVIRALAEEG-RTMLLVTHEMGFARQVSSEV-VFLHQGLVEEQGSPQQ 239
Cdd:cd03237 135 DIYLLDEPSAYLDVEQRLMASKVIRRFAENNeKTAFVVEHDIIMIDYLADRLiVFEGEPSVNGVANPPQ 203
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
8-245 |
1.19e-15 |
|
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: 76.02 E-value: 1.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNL---HKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCI-NLLENPHQGQILVAGEELKLKAAKNGelVA 83
Cdd:TIGR02633 258 LEARNLtcwDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALfGAYPGKFEGNVFINGKPVDIRNPAQA--IR 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 84 ADGKQINRLRSEIGFVfqnfnlwPHMSVLDNI-IEAPRRVLGQSKAEATEIAEALLAKVGISDKRHAYP----AQLSGGQ 158
Cdd:TIGR02633 336 AGIAMVPEDRKRHGIV-------PILGVGKNItLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASPflpiGRLSGGN 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 159 QQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHEMGFARQVSSEVVFLHQG-----LVEE 233
Cdd:TIGR02633 409 QQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGklkgdFVNH 488
|
250
....*....|..
gi 489310645 234 QGSPQQVFENPL 245
Cdd:TIGR02633 489 ALTQEQVLAAAL 500
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
6-244 |
1.50e-15 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 74.84 E-value: 1.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 6 PALEIRNLHKRY----GELEVLKGISLTARDGDVISILGSSGSGKSTFLRCInllenphqgqILVAGEELKLKAAK---- 77
Cdd:PRK15093 2 PLLDIRNLTIEFktsdGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAI----------CGVTKDNWRVTADRmrfd 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 78 NGELVAADGKQINRL-RSEIGFVFQNFN--LWPHMSVLDNIIEA-P--------RRVLGQSKAEATEiaeaLLAKVGISD 145
Cdd:PRK15093 72 DIDLLRLSPRERRKLvGHNVSMIFQEPQscLDPSERVGRQLMQNiPgwtykgrwWQRFGWRKRRAIE----LLHRVGIKD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 146 KR---HAYPAQLSGGQQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAE-EGRTMLLVTHEMGFARQVSS 221
Cdd:PRK15093 148 HKdamRSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnNNTTILLISHDLQMLSQWAD 227
|
250 260
....*....|....*....|...
gi 489310645 222 EVVFLHQGLVEEQGSPQQVFENP 244
Cdd:PRK15093 228 KINVLYCGQTVETAPSKELVTTP 250
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
2-211 |
2.40e-15 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 75.23 E-value: 2.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 2 AEATPALEIRNL---HKRYGELevLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILV-AGEELklkaak 77
Cdd:COG4178 357 TSEDGALALEDLtlrTPDGRPL--LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARV------ 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 78 ngelvaadgkqinrLrseigFVFQNfnlwPHMsVLDNIIEA---PRRVLGQSKAEATEIaealLAKVGIS------DKRH 148
Cdd:COG4178 429 --------------L-----FLPQR----PYL-PLGTLREAllyPATAEAFSDAELREA----LEAVGLGhlaerlDEEA 480
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489310645 149 AYPAQLSGGQQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRAlAEEGRTMLLVTH 211
Cdd:COG4178 481 DWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLRE-ELPGTTVISVGH 542
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
8-229 |
4.48e-15 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 74.20 E-value: 4.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNL---HKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCI-NLLENPHQGQILVAGEELKLK----AAKNG 79
Cdd:PRK13549 260 LEVRNLtawDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLfGAYPGRWEGEIFIDGKPVKIRnpqqAIAQG 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 80 -ELVAADgkqinrlRSEIGFVfqnfnlwPHMSVLDNI-IEAPRRVLGQSK----AEATEIAEALLA-KVGISDKRHAYpA 152
Cdd:PRK13549 340 iAMVPED-------RKRDGIV-------PVMGVGKNItLAALDRFTGGSRiddaAELKTILESIQRlKVKTASPELAI-A 404
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489310645 153 QLSGGQQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHEMGFARQVSSEVVFLHQG 229
Cdd:PRK13549 405 RLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEG 481
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
8-212 |
5.73e-15 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 73.85 E-value: 5.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRYGELEV-LKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELklkaakngelvaaDG 86
Cdd:PRK10522 323 LELRNVTFAYQDNGFsVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPV-------------TA 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 87 KQINRLRSEIGFVFQNFNLWphmsvldniieapRRVLGQSKAEA-TEIAEALLAKVGISDKRH-----AYPAQLSGGQQQ 160
Cdd:PRK10522 390 EQPEDYRKLFSAVFTDFHLF-------------DQLLGPEGKPAnPALVEKWLERLKMAHKLEledgrISNLKLSKGQKK 456
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489310645 161 RAAIARTLAMQPKVILFDEPTSALDP----EMVQEVLNVIRalaEEGRTMLLVTHE 212
Cdd:PRK10522 457 RLALLLALAEERDILLLDEWAADQDPhfrrEFYQVLLPLLQ---EMGKTIFAISHD 509
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
2-225 |
1.02e-14 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 73.28 E-value: 1.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 2 AEATPALEIRNLHKRYGE--LEVLKGislTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQIlvageELKLKAAKNG 79
Cdd:COG1245 336 KEEETLVEYPDLTKSYGGfsLEVEGG---EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV-----DEDLKISYKP 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 80 ELVAADGkqinrlrseigfvfqnfnlwpHMSVLDNIIEAPRRVLGQSKAEaTEIAEALlakvGISDKRHAYPAQLSGGQQ 159
Cdd:COG1245 408 QYISPDY---------------------DGTVEEFLRSANTDDFGSSYYK-TEIIKPL----GLEKLLDKNVKDLSGGEL 461
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489310645 160 QRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEE-GRTMLLVTHEMGFARQVSSEV-VF 225
Cdd:COG1245 462 QRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENrGKTAMVVDHDIYLIDYISDRLmVF 529
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
8-237 |
1.09e-14 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 70.52 E-value: 1.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRYG-EL-EVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKlkaakngelvaad 85
Cdd:cd03369 7 IEVENLSVRYApDLpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDIS------------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 86 GKQINRLRSEIGFVFQNFNLwphmsvLDNIIEAPRRVLGQSKAEatEIAEALLAKVGISDkrhaypaqLSGGQQQRAAIA 165
Cdd:cd03369 74 TIPLEDLRSSLTIIPQDPTL------FSGTIRSNLDPFDEYSDE--EIYGALRVSEGGLN--------LSQGQRQLLCLA 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489310645 166 RTLAMQPKVILFDEPTSALDPEMVQEVLNVIRalaEE--GRTMLLVTHEMG----FARqvsseVVFLHQGLVEEQGSP 237
Cdd:cd03369 138 RALLKRPRVLVLDEATASIDYATDALIQKTIR---EEftNSTILTIAHRLRtiidYDK-----ILVMDAGEVKEYDHP 207
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
2-211 |
2.66e-14 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 72.15 E-value: 2.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 2 AEATPALEIRNLHKRYGE--LEVLKGislTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQIlvageELKLKAAKNG 79
Cdd:PRK13409 335 SERETLVEYPDLTKKLGDfsLEVEGG---EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV-----DPELKISYKP 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 80 ELVAADgkqinrlrseigfvfqnfnlwPHMSVLDNIIEAPRRVlgQSKAEATEIAEAL-LAKvgISDKrhaYPAQLSGGQ 158
Cdd:PRK13409 407 QYIKPD---------------------YDGTVEDLLRSITDDL--GSSYYKSEIIKPLqLER--LLDK---NVKDLSGGE 458
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489310645 159 QQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEE-GRTMLLVTH 211
Cdd:PRK13409 459 LQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEErEATALVVDH 512
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
26-244 |
2.78e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 70.35 E-value: 2.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 26 ISLTARDGDVISILGSSGSGKSTFLRCI-NLLenPHQGQILVAGEELK-LKAAKNGELVAADGKQINRLrseigF---VF 100
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMaGLL--PGSGSIQFAGQPLEaWSAAELARHRAYLSQQQTPP-----FampVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 101 QNFNLwpHMsvldniieAPRRVLGQSKAEATEIAEALlakvGISDKRHAYPAQLSGGQQQR---AA----IARTLAMQPK 173
Cdd:PRK03695 88 QYLTL--HQ--------PDKTRTEAVASALNEVAEAL----GLDDKLGRSVNQLSGGEWQRvrlAAvvlqVWPDINPAGQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489310645 174 VILFDEPTSALDpeMVQEVL--NVIRALAEEGRTMLLVTHEMGFARQVSSEVVFLHQGLVEEQGSPQQVFENP 244
Cdd:PRK03695 154 LLLLDEPMNSLD--VAQQAAldRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPE 224
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
8-217 |
4.86e-14 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 71.60 E-value: 4.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRYG---ELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAG----EELKLK------ 74
Cdd:PTZ00265 383 IQFKNVRFHYDtrkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDshnlKDINLKwwrski 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 75 ------------AAKNG-------------------ELVAADGKQINRLRSEIGFVFQNFNLWPHMSVLDNIIEAPRRVL 123
Cdd:PTZ00265 463 gvvsqdpllfsnSIKNNikyslyslkdlealsnyynEDGNDSQENKNKRNSCRAKCAGDLNDMSNTTDSNELIEMRKNYQ 542
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 124 GQSKAEATEIAEallaKVGISDKRHAYP-----------AQLSGGQQQRAAIARTLAMQPKVILFDEPTSALDPE---MV 189
Cdd:PTZ00265 543 TIKDSEVVDVSK----KVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKseyLV 618
|
250 260
....*....|....*....|....*...
gi 489310645 190 QEVLNVIRalAEEGRTMLLVTHEMGFAR 217
Cdd:PTZ00265 619 QKTINNLK--GNENRITIIIAHRLSTIR 644
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
6-243 |
6.80e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 71.31 E-value: 6.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 6 PALEIRNLHKRY---GELEVLKGISLTARDGDVISILGSSGSGKSTFLrcinllenphqgqilvageelklkAAKNGELV 82
Cdd:PLN03130 613 PAISIKNGYFSWdskAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLI------------------------SAMLGELP 668
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 83 A-ADGKQInrLRSEIGFVFQN---FNlwphMSVLDNII-----EAPR-----RVLGQSK-------AEATEIAEAllakv 141
Cdd:PLN03130 669 PrSDASVV--IRGTVAYVPQVswiFN----ATVRDNILfgspfDPERyeraiDVTALQHdldllpgGDLTEIGER----- 737
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 142 GISdkrhaypaqLSGGQQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNviRALAEE--GRTMLLVTHEMGFARQV 219
Cdd:PLN03130 738 GVN---------ISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFD--KCIKDElrGKTRVLVTNQLHFLSQV 806
|
250 260
....*....|....*....|....
gi 489310645 220 sSEVVFLHQGLVEEQGSPQQVFEN 243
Cdd:PLN03130 807 -DRIILVHEGMIKEEGTYEELSNN 829
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
16-213 |
7.71e-14 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 68.93 E-value: 7.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 16 RYGELE-VLKGISlTARDGDVISILGSSGSGKSTFLRCI------NL---LENPHQGQIL--VAGEELK--LKAAKNGEL 81
Cdd:cd03236 9 RYGPNSfKLHRLP-VPREGQVLGLVGPNGIGKSTALKILagklkpNLgkfDDPPDWDEILdeFRGSELQnyFTKLLEGDV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 82 VAADGKQinrlrseigfvfqnfnlwphmsVLDNIieaPRRVLGQ-----SKAEATEIAEALLAKVGISDKRHAYPAQLSG 156
Cdd:cd03236 88 KVIVKPQ----------------------YVDLI---PKAVKGKvgellKKKDERGKLDELVDQLELRHVLDRNIDQLSG 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489310645 157 GQQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHEM 213
Cdd:cd03236 143 GELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLIRELAEDDNYVLVVEHDL 199
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
10-210 |
1.22e-13 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 67.67 E-value: 1.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 10 IRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPH---QGQILVAGEELKlkaakngelvaadg 86
Cdd:cd03233 10 SFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYK-------------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 87 KQINRLRSEIGFVFQNFNLWPHMSVLDnIIEAPRRVLGqskaeateiaeallakvgisdkrHAYPAQLSGGQQQRAAIAR 166
Cdd:cd03233 76 EFAEKYPGEIIYVSEEDVHFPTLTVRE-TLDFALRCKG-----------------------NEFVRGISGGERKRVSIAE 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489310645 167 TLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVT 210
Cdd:cd03233 132 ALVSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVS 175
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
31-240 |
2.14e-12 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 66.58 E-value: 2.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 31 RDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELklkaakngelvaadgkqinrlRSEIGFVFQNFNLWPHMS 110
Cdd:TIGR01257 1963 RPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI---------------------LTNISDVHQNMGYCPQFD 2021
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 111 VLDNIIEAPR------RVLGQSKAEATEIAEALLAKVGISDKRHAYPAQLSGGQQQRAAIARTLAMQPKVILFDEPTSAL 184
Cdd:TIGR01257 2022 AIDDLLTGREhlylyaRLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGM 2101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489310645 185 DPEMVQEVLNVIRALAEEGRTMLLVTHEMGFARQVSSEVVFLHQGLVEEQGSPQQV 240
Cdd:TIGR01257 2102 DPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHL 2157
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
5-243 |
2.16e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 66.54 E-value: 2.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 5 TPALEIRNLHKRYG---ELEVLKGISLTARDGDVISILGSSGSGKSTFLrcinllenphqgqilvageelklkAAKNGEL 81
Cdd:PLN03232 612 APAISIKNGYFSWDsktSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLI------------------------SAMLGEL 667
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 82 VAADGKQINrLRSEIGFVFQN---FNlwphMSVLDNIieaprrvLGQSKAEATEIAEALLAkVGISDKRHAYPAQ----- 153
Cdd:PLN03232 668 SHAETSSVV-IRGSVAYVPQVswiFN----ATVRENI-------LFGSDFESERYWRAIDV-TALQHDLDLLPGRdltei 734
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 154 ------LSGGQQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHEMGFARQVsSEVVFLH 227
Cdd:PLN03232 735 gergvnISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLM-DRIILVS 813
|
250
....*....|....*.
gi 489310645 228 QGLVEEQGSPQQVFEN 243
Cdd:PLN03232 814 EGMIKEEGTFAELSKS 829
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
5-244 |
2.64e-12 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 64.75 E-value: 2.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 5 TPALEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQIlvageelklkaakngelvaa 84
Cdd:PRK09544 2 TSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI-------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 85 dgKQINRLRseIGFVFQNFNLWPHMSvldniIEAPRRVLGQSKAEATEIAEALlaKVGISDKRHAYPAQ-LSGGQQQRAA 163
Cdd:PRK09544 62 --KRNGKLR--IGYVPQKLYLDTTLP-----LTVNRFLRLRPGTKKEDILPAL--KRVQAGHLIDAPMQkLSGGETQRVL 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 164 IARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEE-GRTMLLVTHEMGFARQVSSEVVFLHQGLVeEQGSPQQVFE 242
Cdd:PRK09544 131 LARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCLNHHIC-CSGTPEVVSL 209
|
..
gi 489310645 243 NP 244
Cdd:PRK09544 210 HP 211
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
7-213 |
2.78e-12 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 65.96 E-value: 2.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 7 ALEIRNL---------HkRYGElevlKGISL----TARDGDVISILGSSGSGKSTFLRCI------NL--LEN-PHQGQI 64
Cdd:COG1245 65 AISIVNLpeeleedpvH-RYGE----NGFRLyglpVPKKGKVTGILGPNGIGKSTALKILsgelkpNLgdYDEePSWDEV 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 65 L--VAGEELK--LKAAKNGELVAADGKQinrlrseigFVfqnfnlwphmsvlDNIieaPRRVLGQ-----SKAEATEIAE 135
Cdd:COG1245 140 LkrFRGTELQdyFKKLANGEIKVAHKPQ---------YV-------------DLI---PKVFKGTvrellEKVDERGKLD 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 136 ALLAKVGISDKRHAYPAQLSGGQQQRAAIARTLAMQPKVILFDEPTSALDpemVQEVLNV---IRALAEEGRTMLLVTHE 212
Cdd:COG1245 195 ELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLD---IYQRLNVarlIRELAEEGKYVLVVEHD 271
|
.
gi 489310645 213 M 213
Cdd:COG1245 272 L 272
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
21-215 |
3.95e-12 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 65.34 E-value: 3.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 21 EVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVA--------GEELKLKAAKN-GELVAADGKQINR 91
Cdd:TIGR03719 19 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQpgikvgylPQEPQLDPTKTvRENVEEGVAEIKD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 92 LRSEIGFVFQNFN--------LWPHMSVLDNIIEAprrVLGQSKAEATEIA-EALLAKVGISDKRHaypaqLSGGQQQRA 162
Cdd:TIGR03719 99 ALDRFNEISAKYAepdadfdkLAAEQAELQEIIDA---ADAWDLDSQLEIAmDALRCPPWDADVTK-----LSGGERRRV 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489310645 163 AIARTLAMQPKVILFDEPTSALDPEMVQ--EvlnviRALAEEGRTMLLVTHEMGF 215
Cdd:TIGR03719 171 ALCRLLLSKPDMLLLDEPTNHLDAESVAwlE-----RHLQEYPGTVVAVTHDRYF 220
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
22-211 |
4.46e-12 |
|
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: 62.56 E-value: 4.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 22 VLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGeelklkaakngelvaadgkqinrlRSEIGFVFQ 101
Cdd:cd03223 16 LLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPE------------------------GEDLLFLPQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 102 NfnlwPHMsvldniieaPRRVLgqskaeateiAEALlakvgisdkrhAYP--AQLSGGQQQRAAIARTLAMQPKVILFDE 179
Cdd:cd03223 72 R----PYL---------PLGTL----------REQL-----------IYPwdDVLSGGEQQRLAFARLLLHKPKFVFLDE 117
|
170 180 190
....*....|....*....|....*....|..
gi 489310645 180 PTSALDPEMVQEVLNVIRalaEEGRTMLLVTH 211
Cdd:cd03223 118 ATSALDEESEDRLYQLLK---ELGITVISVGH 146
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
18-229 |
6.95e-12 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 62.65 E-value: 6.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 18 GELEVLKGISLTARDGDVISILGSSGSGKSTFLRCinLLENPHQGqiLVAGEelklkaakngelVAADGKQINR-LRSEI 96
Cdd:cd03232 18 GKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDV--LAGRKTAG--VITGE------------ILINGRPLDKnFQRST 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 97 GFVFQNFNLWPHMSVLdniieaprrvlgqskaeateiaEALLAkvgisdkrHAYPAQLSGGQQQRAAIARTLAMQPKVIL 176
Cdd:cd03232 82 GYVEQQDVHSPNLTVR----------------------EALRF--------SALLRGLSVEQRKRLTIGVELAAKPSILF 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 177 FDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHemgfarQVSS-------EVVFLHQG 229
Cdd:cd03232 132 LDEPTSGLDSQAAYNIVRFLKKLADSGQAILCTIH------QPSAsifekfdRLLLLKRG 185
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
8-235 |
9.15e-12 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 63.27 E-value: 9.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHqgqilVAGEELKLKAAKNGELVAADgk 87
Cdd:PRK09580 2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYE-----VTGGTVEFKGKDLLELSPED-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 88 qinRLRSEIGFVFQNFNLWPHMS---VLDNIIEAPRRVLGQSKAEATEIAEALLAKVGISDkrhaYPAQL---------S 155
Cdd:PRK09580 75 ---RAGEGIFMAFQYPVEIPGVSnqfFLQTALNAVRSYRGQEPLDRFDFQDLMEEKIALLK----MPEDLltrsvnvgfS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 156 GGQQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHEMGFARQVSSEVV-FLHQGLVEEQ 234
Cdd:PRK09580 148 GGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYQRILDYIKPDYVhVLYQGRIVKS 227
|
.
gi 489310645 235 G 235
Cdd:PRK09580 228 G 228
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
8-242 |
1.02e-11 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 64.58 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRYGE-LE-VLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGeelkLKAAKNGelvaad 85
Cdd:TIGR00957 1285 VEFRNYCLRYREdLDlVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDG----LNIAKIG------ 1354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 86 gkqINRLRSEIGFVFQN---------FNLWPHMSVLDNIIEAPRRVlgqskAEATEIAEALLAKVgisDKRHAYPAQ-LS 155
Cdd:TIGR00957 1355 ---LHDLRFKITIIPQDpvlfsgslrMNLDPFSQYSDEEVWWALEL-----AHLKTFVSALPDKL---DHECAEGGEnLS 1423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 156 GGQQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGrTMLLVTHE----MGFARqvsseVVFLHQGLV 231
Cdd:TIGR00957 1424 VGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDC-TVLTIAHRlntiMDYTR-----VIVLDKGEV 1497
|
250
....*....|.
gi 489310645 232 EEQGSPQQVFE 242
Cdd:TIGR00957 1498 AEFGAPSNLLQ 1508
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
7-242 |
1.03e-11 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 64.35 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 7 ALEIRNLHKRYGELE-VLKGISLTARDGDVISILGSSGSGKSTFlrcINLLEN---PHQGQILVAGEELklkaakngelv 82
Cdd:PRK10790 340 RIDIDNVSFAYRDDNlVLQNINLSVPSRGFVALVGHTGSGKSTL---ASLLMGyypLTEGEIRLDGRPL----------- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 83 AADGKQInrLRSEIGFVFQNfnlwPHM---SVLDNII-------EAPRRVLgqskaEATEIAEalLAKvGISDKRHAYPA 152
Cdd:PRK10790 406 SSLSHSV--LRQGVAMVQQD----PVVladTFLANVTlgrdiseEQVWQAL-----ETVQLAE--LAR-SLPDGLYTPLG 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 153 Q----LSGGQQQRAAIARTLAMQPKVILFDEPTSALDP---EMVQEVLNVIRalaeEGRTMLLVTHEMGFARQVSSEVVf 225
Cdd:PRK10790 472 EqgnnLSVGQKQLLALARVLVQTPQILILDEATANIDSgteQAIQQALAAVR----EHTTLVVIAHRLSTIVEADTILV- 546
|
250
....*....|....*..
gi 489310645 226 LHQGLVEEQGSPQQVFE 242
Cdd:PRK10790 547 LHRGQAVEQGTHQQLLA 563
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
8-212 |
1.14e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 62.27 E-value: 1.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKlkaakngelvaadgK 87
Cdd:PRK13540 2 LDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIK--------------K 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 88 QINRLRSEIGFVFQNFNLWPHMSVLDNIIEAPrrvlgQSKAEATEIAEalLAKVGISDKRHAYP-AQLSGGQQQRAAIAR 166
Cdd:PRK13540 68 DLCTYQKQLCFVGHRSGINPYLTLRENCLYDI-----HFSPGAVGITE--LCRLFSLEHLIDYPcGLLSSGQKRQVALLR 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489310645 167 TLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHE 212
Cdd:PRK13540 141 LWMSKAKLWLLDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
7-213 |
1.20e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 64.06 E-value: 1.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 7 ALEIRNL---------HkRYGElevlKGISL----TARDGDVISILGSSGSGKSTFLRCI---------NLLENPHQGQI 64
Cdd:PRK13409 65 AISIVNLpeeleeepvH-RYGV----NGFKLyglpIPKEGKVTGILGPNGIGKTTAVKILsgelipnlgDYEEEPSWDEV 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 65 L--VAGEELK--LKAAKNGELVAADGKQInrlrseigfvfqnfnlwphmsvldnIIEAPRRVLGQ-----SKAEATEIAE 135
Cdd:PRK13409 140 LkrFRGTELQnyFKKLYNGEIKVVHKPQY-------------------------VDLIPKVFKGKvrellKKVDERGKLD 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 136 ALLAKVGIS---DKRhayPAQLSGGQQQRAAIARTLAMQPKVILFDEPTSALDpemVQEVLNV---IRALAeEGRTMLLV 209
Cdd:PRK13409 195 EVVERLGLEnilDRD---ISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD---IRQRLNVarlIRELA-EGKYVLVV 267
|
....
gi 489310645 210 THEM 213
Cdd:PRK13409 268 EHDL 271
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
9-252 |
2.04e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 63.59 E-value: 2.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 9 EIRNLHKRYgELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINllENPHQGQILVAGEelklkaakngelVAADG-- 86
Cdd:TIGR00956 64 KLKKFRDTK-TFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIA--SNTDGFHIGVEGV------------ITYDGit 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 87 --KQINRLRSEIGFVFQNFNLWPHMSVLDNIIEAPR------RVLGQSKAE-ATEIAEALLAKVGISdkrHAYPAQ---- 153
Cdd:TIGR00956 129 peEIKKHYRGDVVYNAETDVHFPHLTVGETLDFAARcktpqnRPDGVSREEyAKHIADVYMATYGLS---HTRNTKvgnd 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 154 ----LSGGQQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVThemgfARQVSSE------- 222
Cdd:TIGR00956 206 fvrgVSGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVA-----IYQCSQDayelfdk 280
|
250 260 270
....*....|....*....|....*....|
gi 489310645 223 VVFLHQGlveeqgspQQVFENPlSARCKQF 252
Cdd:TIGR00956 281 VIVLYEG--------YQIYFGP-ADKAKQY 301
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
8-225 |
3.21e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 63.12 E-value: 3.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRY---GELEVLKGISLTARDGDVISILGSSGSGKSTFLRCIN-----------LLENPHQGQI----LVAGE 69
Cdd:PTZ00265 1166 IEIMDVNFRYisrPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMrfydlkndhhiVFKNEHTNDMtneqDYQGD 1245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 70 E---LKLKAA------------------KNGELVAADGKQI-----NRLRSEIGFVFQNFNLWpHMSVLDNI-------- 115
Cdd:PTZ00265 1246 EeqnVGMKNVnefsltkeggsgedstvfKNSGKILLDGVDIcdynlKDLRNLFSIVSQEPMLF-NMSIYENIkfgkedat 1324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 116 IEAPRRVlgqSK-AEATEIAEALLAK----VGisdkrhAYPAQLSGGQQQRAAIARTLAMQPKVILFDEPTSALDP---E 187
Cdd:PTZ00265 1325 REDVKRA---CKfAAIDEFIESLPNKydtnVG------PYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSnseK 1395
|
250 260 270
....*....|....*....|....*....|....*...
gi 489310645 188 MVQEVLNVIRALAEegRTMLLVTHEMGFARQVSSEVVF 225
Cdd:PTZ00265 1396 LIEKTIVDIKDKAD--KTIITIAHRIASIKRSDKIVVF 1431
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
7-221 |
3.24e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 62.60 E-value: 3.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 7 ALEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRC-INLLEnPHQGQIlvageelklKAAKNgelvaad 85
Cdd:PRK15064 319 ALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTlVGELE-PDSGTV---------KWSEN------- 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 86 gkqinrlrSEIGFVFQNfnlwpH-------MSVLDNI---------IEAPRRVLGQSKAEATEIAEAllAKVgisdkrha 149
Cdd:PRK15064 382 --------ANIGYYAQD-----HaydfendLTLFDWMsqwrqegddEQAVRGTLGRLLFSQDDIKKS--VKV-------- 438
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489310645 150 ypaqLSGGQQQRAAIARTLAMQPKVILFDEPTSALDPEMVqEVLNVirALAEEGRTMLLVTHEMGFarqVSS 221
Cdd:PRK15064 439 ----LSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESI-ESLNM--ALEKYEGTLIFVSHDREF---VSS 500
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1-211 |
4.47e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 62.34 E-value: 4.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 1 MAEATPALEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLrciNLLENPH-QGQilvaGEELKLKAAKNG 79
Cdd:PRK10938 254 LPANEPRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLL---SLITGDHpQGY----SNDLTLFGRRRG 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 80 ElvaadGKQINRLRSEIGFVFQNFnlwpHM------SVLDNIIEAPRRVLG--QSKAEATEI-AEALLAKVGISDKRHAY 150
Cdd:PRK10938 327 S-----GETIWDIKKHIGYVSSSL----HLdyrvstSVRNVILSGFFDSIGiyQAVSDRQQKlAQQWLDILGIDKRTADA 397
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489310645 151 PAQ-LSGGQQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLL-VTH 211
Cdd:PRK10938 398 PFHsLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLfVSH 460
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
154-229 |
8.17e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 61.56 E-value: 8.17e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489310645 154 LSGGQQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHEMGFARQVSSEVVFLHQG 229
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEG 471
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
8-211 |
1.20e-10 |
|
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: 60.97 E-value: 1.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRYGELE-----VLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVageelklkaakNGELV 82
Cdd:COG4615 328 LELRGVTYRYPGEDgdegfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILL-----------DGQPV 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 83 AADgkQINRLRSEIGFVFQNFNLWphmsvldniieapRRVLGQSKAEATEIAEALLA------KVGISDKRHAYPAqLSG 156
Cdd:COG4615 397 TAD--NREAYRQLFSAVFSDFHLF-------------DRLLGLDGEADPARARELLErleldhKVSVEDGRFSTTD-LSQ 460
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489310645 157 GQQQRAAIARTLAMQPKVILFDEPTSALDPE----MVQEVLNVIRAlaeEGRTMLLVTH 211
Cdd:COG4615 461 GQRKRLALLVALLEDRPILVFDEWAADQDPEfrrvFYTELLPELKA---RGKTVIAISH 516
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
18-242 |
2.56e-10 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 60.34 E-value: 2.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 18 GELEVLKGISLTARDGDVISILGSSGSGKSTFLrcinllenphqGQILVAGEELKLKAAKNGELVAADGK---QINRLRS 94
Cdd:TIGR00957 649 DLPPTLNGITFSIPEGALVAVVGQVGCGKSSLL-----------SALLAEMDKVEGHVHMKGSVAYVPQQawiQNDSLRE 717
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 95 EIGF-----------VFQNFNLWPHMSVLDNiieaprrvlgqskAEATEIAEAllakvGISdkrhaypaqLSGGQQQRAA 163
Cdd:TIGR00957 718 NILFgkalnekyyqqVLEACALLPDLEILPS-------------GDRTEIGEK-----GVN---------LSGGQKQRVS 770
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 164 IARTLAMQPKVILFDEPTSALDPEMVQEVL-NVIRALAE-EGRTMLLVTHEMGFARQVSSeVVFLHQGLVEEQGSPQQVF 241
Cdd:TIGR00957 771 LARAVYSNADIYLFDDPLSAVDAHVGKHIFeHVIGPEGVlKNKTRILVTHGISYLPQVDV-IIVMSGGKISEMGSYQELL 849
|
.
gi 489310645 242 E 242
Cdd:TIGR00957 850 Q 850
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
23-240 |
3.12e-10 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 59.06 E-value: 3.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 23 LKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGE--ELKLKAAKNGELVAADGkqinrlrseigfvf 100
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEvsVIAISAGLSGQLTGIEN-------------- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 101 qnfnlwphmsvldniIEAPRRVLGQSKAEATEIAEALLAKVGISDKRHAYPAQLSGGQQQRAAIARTLAMQPKVILFDEP 180
Cdd:PRK13546 106 ---------------IEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 181 TSALDPEMVQEVLNVIRALAEEGRTMLLVTHEMGFARQVSSEVVFLHQGLVEEQGSPQQV 240
Cdd:PRK13546 171 LSVGDQTFAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDV 230
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
2-229 |
3.26e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 59.68 E-value: 3.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 2 AEATPALEIRNLHKrygelEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKLKAAKN--- 78
Cdd:PRK15439 263 AAGAPVLTVEDLTG-----EGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQrla 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 79 -GELVAADGKQINRLRSE-------IGFVFQNFNLWPHMSVLDNIIEAPRRVLGQSKAEATEIAEALlakvgisdkrhay 150
Cdd:PRK15439 338 rGLVYLPEDRQSSGLYLDaplawnvCALTHNRRGFWIKPARENAVLERYRRALNIKFNHAEQAARTL------------- 404
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489310645 151 paqlSGGQQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHEMGFARQVSSEVVFLHQG 229
Cdd:PRK15439 405 ----SGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQG 479
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
33-211 |
6.04e-10 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 57.55 E-value: 6.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 33 GDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGeelklKAAKNGElvaadgkqinRLRsEIGFVFQNFNLWPHMSVL 112
Cdd:PRK13543 37 GEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDG-----KTATRGD----------RSR-FMAYLGHLPGLKADLSTL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 113 DNIieapRRVLGQSKAEATEIAEALLAKVGISDKRHAYPAQLSGGQQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEV 192
Cdd:PRK13543 101 ENL----HFLCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLV 176
|
170
....*....|....*....
gi 489310645 193 LNVIRALAEEGRTMLLVTH 211
Cdd:PRK13543 177 NRMISAHLRGGGAALVTTH 195
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2-238 |
7.56e-10 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 58.98 E-value: 7.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 2 AEATPALEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELklkaakngel 81
Cdd:NF033858 261 DDDEPAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV---------- 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 82 vaaDGKQINrLRSEIGFVFQNFNLWPHMSVLDNIiEAPRRVLGQSKAEATEIAEALLAKVGISDKRHAYPAQLSGGQQQR 161
Cdd:NF033858 331 ---DAGDIA-TRRRVGYMSQAFSLYGELTVRQNL-ELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQR 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 162 AAIArtLAM--QPKVILFDEPTSALDP---EMVQEVLnvIRALAEEGRTMLLVTHEMGFA----RqVSsevvFLHQGLVE 232
Cdd:NF033858 406 LSLA--VAVihKPELLILDEPTSGVDPvarDMFWRLL--IELSREDGVTIFISTHFMNEAercdR-IS----LMHAGRVL 476
|
....*.
gi 489310645 233 EQGSPQ 238
Cdd:NF033858 477 ASDTPA 482
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
21-211 |
7.97e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 58.59 E-value: 7.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 21 EVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHqgqilvageelklkaakNGELVAADGKQInrlrseiGFVF 100
Cdd:PRK11819 21 QILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEF-----------------EGEARPAPGIKV-------GYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 101 QNFNLWPHMSVLDNIIEAPRRVLgQSKAEATEIAE----------ALLAKVG----ISDKRHAY---------------P 151
Cdd:PRK11819 77 QEPQLDPEKTVRENVEEGVAEVK-AALDRFNEIYAayaepdadfdALAAEQGelqeIIDAADAWdldsqleiamdalrcP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489310645 152 ------AQLSGGQQQRAAIARTLAMQPKVILFDEPTSALDPEMVQ--EvlnviRALAEEGRTMLLVTH 211
Cdd:PRK11819 156 pwdakvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAwlE-----QFLHDYPGTVVAVTH 218
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
23-243 |
8.64e-10 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 58.75 E-value: 8.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 23 LKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEE--LKLKAAKNGELVAadgkqinrlrseigfvf 100
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAalIAISSGLNGQLTG----------------- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 101 qnfnlwphmsvLDNIiEAPRRVLGQSKAEATEIAEALLAKVGISDKRHAYPAQLSGGQQQRAAIARTLAMQPKVILFDEP 180
Cdd:PRK13545 103 -----------IENI-ELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489310645 181 TSALDPEMVQEVLNVIRALAEEGRTMLLVTHEMGFARQVSSEVVFLHQGLVEEQGSPQQVFEN 243
Cdd:PRK13545 171 LSVGDQTFTKKCLDKMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDH 233
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
18-212 |
1.17e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 58.58 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 18 GELEVLKGISLTARDGDVISILGSSGSGKSTFLRCinLLENPHQGqILVAGEELklkaakngelVAADGKQINRLRSeIG 97
Cdd:TIGR00956 774 EKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNV--LAERVTTG-VITGGDRL----------VNGRPLDSSFQRS-IG 839
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 98 FVFQNFNLWPHMSVLDNIIEAPRrvLGQSKA-----------------EATEIAEALLAKVGISdkrhaypaqLSGGQQQ 160
Cdd:TIGR00956 840 YVQQQDLHLPTSTVRESLRFSAY--LRQPKSvsksekmeyveevikllEMESYADAVVGVPGEG---------LNVEQRK 908
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489310645 161 RAAIARTLAMQPKVILF-DEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHE 212
Cdd:TIGR00956 909 RLTIGVELVAKPKLLLFlDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQ 961
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
20-215 |
2.83e-09 |
|
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: 55.80 E-value: 2.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 20 LEVLKGISLTARDGDVISILGSSGSGKSTFLRCI-----NLLENPHQGQILVAGEELKLKAAKNGELVAADGKQINRLRS 94
Cdd:cd03290 14 LATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAIlgemqTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPWLLNA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 95 --EIGFVFQN-FNLWPHMSVLDNIIEAPRRVLgQSKAEATEIAEAllakvGISdkrhaypaqLSGGQQQRAAIARTLAMQ 171
Cdd:cd03290 94 tvEENITFGSpFNKQRYKAVTDACSLQPDIDL-LPFGDQTEIGER-----GIN---------LSGGQRQRICVARALYQN 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489310645 172 PKVILFDEPTSALDPEMVQEVLN--VIRALAEEGRTMLLVTHEMGF 215
Cdd:cd03290 159 TNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQY 204
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
154-212 |
3.53e-09 |
|
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: 54.64 E-value: 3.53e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489310645 154 LSGGQQQRAAIARTLAMQPK--VILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHE 212
Cdd:cd03238 88 LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHN 148
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
5-232 |
6.25e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 55.95 E-value: 6.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 5 TPALEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQI-LVAGEELKLKAAKNGELVA 83
Cdd:PRK10636 310 NPLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLGYFAQHQLEFLR 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 84 ADGKQINrlrseigfvfqnfnlwpHMSVLdniieAPRrvlgqskaEATEIAEALLAKVGIS-DKRHAYPAQLSGGQQQRA 162
Cdd:PRK10636 390 ADESPLQ-----------------HLARL-----APQ--------ELEQKLRDYLGGFGFQgDKVTEETRRFSGGEKARL 439
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 163 AIARTLAMQPKVILFDEPTSALDPEMVQEvlnVIRALAEEGRTMLLVTHEMGFARQVSSEVVFLHQGLVE 232
Cdd:PRK10636 440 VLALIVWQRPNLLLLDEPTNHLDLDMRQA---LTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGKVE 506
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
8-201 |
7.45e-09 |
|
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: 55.71 E-value: 7.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVageelklkaaknGELVaadgk 87
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI------------GETV----- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 88 qinrlrsEIGFVFQNfnlwphmsvldniieapRRVLGQSKAEATEIAEAL----LAKVGISDKrhAYPA----------- 152
Cdd:TIGR03719 386 -------KLAYVDQS-----------------RDALDPNKTVWEEISGGLdiikLGKREIPSR--AYVGrfnfkgsdqqk 439
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489310645 153 ---QLSGGQQQRAAIARTLAMQPKVILFDEPTSALDpemvqevLNVIRALAE 201
Cdd:TIGR03719 440 kvgQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLD-------VETLRALEE 484
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
23-213 |
1.02e-08 |
|
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: 54.54 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 23 LKGISLTARDGDVISILGSSGSGKSTFlrcINllenphqgQILVAG--EELKLKAAKNGELVAADG-KQINRL----RSE 95
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSL---IN--------DTLYPAlaRRLHLKKEQPGNHDRIEGlEHIDKVividQSP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 96 IGFVfQNFNLWPHMSVLDNIIE------APRR-----------------VLGQSKAEATEIAEA---------LLAKVGI 143
Cdd:cd03271 80 IGRT-PRSNPATYTGVFDEIRElfcevcKGKRynretlevrykgksiadVLDMTVEEALEFFENipkiarklqTLCDVGL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489310645 144 SDKRHAYPA-QLSGGQQQRAAIARTLAMQ---PKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHEM 213
Cdd:cd03271 159 GYIKLGQPAtTLSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNL 232
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
152-243 |
1.73e-08 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 54.83 E-value: 1.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 152 AQLSGGQQQRAAIARTLAMQPKVILF--DEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHE---MGFARQV------- 219
Cdd:PRK00635 475 ATLSGGEQERTALAKHLGAELIGITYilDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDeqmISLADRIidigpga 554
|
90 100
....*....|....*....|....*..
gi 489310645 220 ---SSEVVFlhqglveeQGSPQQVFEN 243
Cdd:PRK00635 555 gifGGEVLF--------NGSPREFLAK 573
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
153-236 |
1.74e-08 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 52.36 E-value: 1.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 153 QLSGGQQQRAAIARTLAMQPK----VILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHemgFARQVSSEVVFLHQ 228
Cdd:cd03227 77 QLSGGEKELSALALILALASLkprpLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITH---LPELAELADKLIHI 153
|
....*...
gi 489310645 229 GLVEEQGS 236
Cdd:cd03227 154 KKVITGVY 161
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
154-248 |
2.28e-08 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 52.57 E-value: 2.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 154 LSGGQQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEG-RTMLLVTHEMGFARQVSSEVVflhqgLVE 232
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGkKTALVVEHDLAVLDYLSDRIH-----VFE 146
|
90
....*....|....*.
gi 489310645 233 EQGSPQQVFENPLSAR 248
Cdd:cd03222 147 GEPGVYGIASQPKGTR 162
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
7-255 |
6.68e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 53.06 E-value: 6.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 7 ALEIRNLHKRY--GELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELklkaAKNGelvaa 84
Cdd:PLN03232 1234 SIKFEDVHLRYrpGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDV----AKFG----- 1304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 85 dgkqINRLRSEIGFVFQN---------FNLWPHMSvldniieaprrvlgQSKAEATEIAEALLAKVGISDKRHAYPAQL- 154
Cdd:PLN03232 1305 ----LTDLRRVLSIIPQSpvlfsgtvrFNIDPFSE--------------HNDADLWEALERAHIKDVIDRNPFGLDAEVs 1366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 155 ------SGGQQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRalaEEGR--TMLLVTHEMGFARQVsSEVVFL 226
Cdd:PLN03232 1367 eggenfSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIR---EEFKscTMLVIAHRLNTIIDC-DKILVL 1442
|
250 260
....*....|....*....|....*....
gi 489310645 227 HQGLVEEQGSPQQVFENPLSARCKQFMSS 255
Cdd:PLN03232 1443 SSGQVLEYDSPQELLSRDTSAFFRMVHST 1471
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
19-211 |
1.04e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 50.64 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 19 ELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVageelklkaaKNgelvaadgKQINRL-RSEIG 97
Cdd:PRK13541 12 EQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYY----------KN--------CNINNIaKPYCT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 98 FVFQNFNLWPHMSVLDNIieaprrVLGQSKAEATEIAEALLAKVGISDKRHAYPAQLSGGQQQRAAIARTLAMQPKVILF 177
Cdd:PRK13541 74 YIGHNLGLKLEMTVFENL------KFWSEIYNSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLL 147
|
170 180 190
....*....|....*....|....*....|....
gi 489310645 178 DEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTH 211
Cdd:PRK13541 148 DEVETNLSKENRDLLNNLIVMKANSGGIVLLSSH 181
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
8-213 |
1.22e-07 |
|
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: 51.39 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRYGE--LEVLKGISLTARDGDVISILGSSGSGKST----FLRCINLlenphQGQILVAGeelklkaakngel 81
Cdd:cd03289 3 MTVKDLTAKYTEggNAVLENISFSISPGQRVGLLGRTGSGKSTllsaFLRLLNT-----EGDIQIDG------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 82 VAADGKQINRLRSEIGFVFQNF---------NLWPHmsvldniieaprrvlGQ-SKAEATEIAEallaKVGISDKRHAYP 151
Cdd:cd03289 65 VSWNSVPLQKWRKAFGVIPQKVfifsgtfrkNLDPY---------------GKwSDEEIWKVAE----EVGLKSVIEQFP 125
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489310645 152 AQ-----------LSGGQQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRAlAEEGRTMLLVTHEM 213
Cdd:cd03289 126 GQldfvlvdggcvLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQ-AFADCTVILSEHRI 197
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
7-255 |
1.41e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 52.05 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 7 ALEIRNLHKRY-GELE-VLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELklkaAKNGelvaa 84
Cdd:PLN03130 1237 SIKFEDVVLRYrPELPpVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDI----SKFG----- 1307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 85 dgkqINRLRSEIGFVFQN---------FNLWPHMSVLD-NIIEAPRR------VLGQSKAEATEIAEAllakvgisdkrh 148
Cdd:PLN03130 1308 ----LMDLRKVLGIIPQApvlfsgtvrFNLDPFNEHNDaDLWESLERahlkdvIRRNSLGLDAEVSEA------------ 1371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 149 ayPAQLSGGQQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRalaEEGR--TMLLVTHEMGFARQvSSEVVFL 226
Cdd:PLN03130 1372 --GENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIR---EEFKscTMLIIAHRLNTIID-CDRILVL 1445
|
250 260
....*....|....*....|....*....
gi 489310645 227 HQGLVEEQGSPQQVFENPLSARCKQFMSS 255
Cdd:PLN03130 1446 DAGRVVEFDTPENLLSNEGSAFSKMVQST 1474
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
20-212 |
1.51e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 52.16 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 20 LEVLKGISLTARDGDVISILGSSGSGKSTFLrciNLLENPH-----QGQILVAGeelklkAAKNGELVAadgkqinRLRs 94
Cdd:PLN03140 893 LQLLREVTGAFRPGVLTALMGVSGAGKTTLM---DVLAGRKtggyiEGDIRISG------FPKKQETFA-------RIS- 955
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 95 eiGFVFQNFNLWPHMSVLDNIIEA-----PRRVlgqSKAEATEIAEALLAKVGISDKRHA---YPA--QLSGGQQQRAAI 164
Cdd:PLN03140 956 --GYCEQNDIHSPQVTVRESLIYSaflrlPKEV---SKEEKMMFVDEVMELVELDNLKDAivgLPGvtGLSTEQRKRLTI 1030
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489310645 165 ARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHE 212
Cdd:PLN03140 1031 AVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQ 1078
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
128-235 |
1.67e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 51.78 E-value: 1.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 128 AEATeiAEALLAKVGIS-DKRHAYPAQLSGGQQQRAAIARTLAMQPKVILFDEPTSALDpemVQEVLNVIRALAEEGRTM 206
Cdd:PLN03073 320 AEAR--AASILAGLSFTpEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD---LHAVLWLETYLLKWPKTF 394
|
90 100 110
....*....|....*....|....*....|
gi 489310645 207 LLVTHEMGFARQVSSEVVFLH-QGLVEEQG 235
Cdd:PLN03073 395 IVVSHAREFLNTVVTDILHLHgQKLVTYKG 424
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
21-247 |
2.17e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 51.70 E-value: 2.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 21 EVLKGISLTARDGDVISILGSSGSGKSTFLrcinllenphqgQILVAGEELKlkaakNGELVAAdgkqinrlRSeIGFVF 100
Cdd:PTZ00243 674 VLLRDVSVSVPRGKLTVVLGATGSGKSTLL------------QSLLSQFEIS-----EGRVWAE--------RS-IAYVP 727
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 101 QNfnLW-PHMSVLDNII----EAPRRVlgqskAEATEIA--EALLAKVG------ISDKrhayPAQLSGGQQQRAAIART 167
Cdd:PTZ00243 728 QQ--AWiMNATVRGNILffdeEDAARL-----ADAVRVSqlEADLAQLGggleteIGEK----GVNLSGGQKARVSLARA 796
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 168 LAMQPKVILFDEPTSALDPE----MVQEVLnvIRALAeeGRTMLLVTHEMGFARQvSSEVVFLHQGLVEEQGSPQQVFEN 243
Cdd:PTZ00243 797 VYANRDVYLLDDPLSALDAHvgerVVEECF--LGALA--GKTRVLATHQVHVVPR-ADYVVALGDGRVEFSGSSADFMRT 871
|
....
gi 489310645 244 PLSA 247
Cdd:PTZ00243 872 SLYA 875
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
7-213 |
2.83e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 50.94 E-value: 2.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 7 ALEIRNL---HKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCI-------NllenpHQGQILVAGEELKL--- 73
Cdd:NF040905 257 VFEVKNWtvyHPLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVfgrsygrN-----ISGTVFKDGKEVDVstv 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 74 -KAAKNG-ELVAADGKQ-----INRLRSEIGfvfqnfnlwphMSVLDNIieAPRRVLgqSKAEATEIAEALLAKVGI-SD 145
Cdd:NF040905 332 sDAIDAGlAYVTEDRKGyglnlIDDIKRNIT-----------LANLGKV--SRRGVI--DENEEIKVAEEYRKKMNIkTP 396
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489310645 146 KRHAYPAQLSGGQQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHEM 213
Cdd:NF040905 397 SVFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSEL 464
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
8-190 |
3.23e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 51.06 E-value: 3.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRYGE--LEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPhQGQILVAGeelklkaakngelVAAD 85
Cdd:TIGR01271 1218 MDVQGLTAKYTEagRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLST-EGEIQIDG-------------VSWN 1283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 86 GKQINRLRSEIGFVFQNF---------NLWPHMSVLDNiieaprrvlgqskaEATEIAEallaKVGISDKRHAYPAQL-- 154
Cdd:TIGR01271 1284 SVTLQTWRKAFGVIPQKVfifsgtfrkNLDPYEQWSDE--------------EIWKVAE----EVGLKSVIEQFPDKLdf 1345
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489310645 155 ---------SGGQQQRAAIARTLAMQPKVILFDEPTSALDPEMVQ 190
Cdd:TIGR01271 1346 vlvdggyvlSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQ 1390
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
154-213 |
3.23e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 50.88 E-value: 3.23e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 154 LSGGQQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHEM 213
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEM 451
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
8-246 |
6.02e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 50.16 E-value: 6.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRY--GELEVLKGISLTARDGDVISILGSSGSGKST----FLRCINllenphqgqilVAGEELKLkaakNGEL 81
Cdd:PTZ00243 1309 LVFEGVQMRYreGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTllltFMRMVE-----------VCGGEIRV----NGRE 1373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 82 VAADG-KQINRLRSEI--------GFVFQNfnlwphmsvLDNIIEAprrvlgqSKAE---ATEIAeALLAKV-----GIS 144
Cdd:PTZ00243 1374 IGAYGlRELRRQFSMIpqdpvlfdGTVRQN---------VDPFLEA-------SSAEvwaALELV-GLRERVaseseGID 1436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 145 DKRHAYPAQLSGGQQQRAAIARTLAMQ-PKVILFDEPTSALDPEMVQEVLNVIRAlAEEGRTMLLVTHEMGFARQVSSEV 223
Cdd:PTZ00243 1437 SRVLEGGSNYSVGQRQLMCMARALLKKgSGFILMDEATANIDPALDRQIQATVMS-AFSAYTVITIAHRLHTVAQYDKII 1515
|
250 260
....*....|....*....|...
gi 489310645 224 VFLHqGLVEEQGSPQQVFENPLS 246
Cdd:PTZ00243 1516 VMDH-GAVAEMGSPRELVMNRQS 1537
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
22-229 |
6.32e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 50.29 E-value: 6.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 22 VLKGISLTARDGDVISILGSSGSGKSTFLRCInllenphqgqilvageelklkaakNGELVAADGKQinRLRSEIGFVFQ 101
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMI------------------------MGELEPSEGKI--KHSGRISFSPQ 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 102 NFNLWPHmSVLDNIIeaprrvLGQSKAE--------ATEIAEAlLAKVGISDKRHAYPA--QLSGGQQQRAAIARTLAMQ 171
Cdd:TIGR01271 495 TSWIMPG-TIKDNII------FGLSYDEyrytsvikACQLEED-IALFPEKDKTVLGEGgiTLSGGQRARISLARAVYKD 566
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489310645 172 PKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHEMGFARQvSSEVVFLHQG 229
Cdd:TIGR01271 567 ADLYLLDSPFTHLDVVTEKEIFESCLCKLMSNKTRILVTSKLEHLKK-ADKILLLHEG 623
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
8-211 |
6.44e-07 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 48.47 E-value: 6.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLhKRYGELEVlkgISLtarDGDVISILGSSGSGKSTFLRCINL-LENPHQG------QILVAGE---ELKLKAAK 77
Cdd:COG0419 5 LRLENF-RSYRDTET---IDF---DDGLNLIVGPNGAGKSTILEAIRYaLYGKARSrsklrsDLINVGSeeaSVELEFEH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 78 NGE---LVAADGKQINRLR---SEIGFVFQN-FNLwphmSVLDNIIEAPRRVLGQSKAEATEIAEALLAKVGISDKRHAY 150
Cdd:COG0419 78 GGKryrIERRQGEFAEFLEakpSERKEALKRlLGL----EIYEELKERLKELEEALESALEELAELQKLKQEILAQLSGL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489310645 151 --PAQLSGGQQQRAAIARTLAMqpkviLFDepTSALDPEMVQEVLNVIRALAeegrtmlLVTH 211
Cdd:COG0419 154 dpIETLSGGERLRLALADLLSL-----ILD--FGSLDEERLERLLDALEELA-------IITH 202
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
9-215 |
6.49e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 49.95 E-value: 6.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 9 EIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCinLLE--NPHQGQILVAgeeLKLKAAkngelvaadg 86
Cdd:PRK11147 321 EMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKL--MLGqlQADSGRIHCG---TKLEVA---------- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 87 kQINRLRSEigfvfqnfnLWPHMSVLDNIIEA---------PRRVLGqskaeateiaeaLLAKVGISDKRHAYPAQ-LSG 156
Cdd:PRK11147 386 -YFDQHRAE---------LDPEKTVMDNLAEGkqevmvngrPRHVLG------------YLQDFLFHPKRAMTPVKaLSG 443
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489310645 157 GQQQRAAIARTLAMQPKVILFDEPTSALDPEMVqEVLNVIraLAEEGRTMLLVTHEMGF 215
Cdd:PRK11147 444 GERNRLLLARLFLKPSNLLILDEPTNDLDVETL-ELLEEL--LDSYQGTVLLVSHDRQF 499
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
7-186 |
7.41e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 49.74 E-value: 7.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 7 ALEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFL------RCInllenpHQGQILVAGEELklkaaknge 80
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLsliagaRKI------QQGRVEVLGGDM--------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 81 lvaADGKQINRLRSEIGFVFQNF--NLWPHMSVLDNiIEAPRRVLGQSKAE-ATEIAEaLLAKVGISD--KRhayPA-QL 154
Cdd:NF033858 66 ---ADARHRRAVCPRIAYMPQGLgkNLYPTLSVFEN-LDFFGRLFGQDAAErRRRIDE-LLRATGLAPfaDR---PAgKL 137
|
170 180 190
....*....|....*....|....*....|..
gi 489310645 155 SGGQQQRAAIARTLAMQPKVILFDEPTSALDP 186
Cdd:NF033858 138 SGGMKQKLGLCCALIHDPDLLILDEPTTGVDP 169
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
122-240 |
8.45e-07 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 49.63 E-value: 8.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 122 VLGQSKAEATEIAEA---------LLAKVGISDKRHAYPA-QLSGGQQQRAAIARTL---AMQPKVILFDEPTSALDPEM 188
Cdd:TIGR00630 788 VLDMTVEEAYEFFEAvpsisrklqTLCDVGLGYIRLGQPAtTLSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDD 867
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 489310645 189 VQEVLNVIRALAEEGRTMLLVTHEMGFARQvSSEVVFL------HQGLVEEQGSPQQV 240
Cdd:TIGR00630 868 IKKLLEVLQRLVDKGNTVVVIEHNLDVIKT-ADYIIDLgpeggdGGGTVVASGTPEEV 924
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
8-203 |
1.35e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 48.96 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVageelklkaaknGELVaadgk 87
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI------------GETV----- 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 88 qinrlrsEIGFVFQ-------NFNLWPHMSV-LDNI----IEAPRRV-LG--------QSKaeateiaeallaKVGisdk 146
Cdd:PRK11819 388 -------KLAYVDQsrdaldpNKTVWEEISGgLDIIkvgnREIPSRAyVGrfnfkggdQQK------------KVG---- 444
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489310645 147 rhaypaQLSGGQQQRAAIARTLAMQPKVILFDEPTSALDpemvqevLNVIRALaEEG 203
Cdd:PRK11819 445 ------VLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLD-------VETLRAL-EEA 487
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
152-229 |
1.54e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 48.79 E-value: 1.54e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489310645 152 AQLSGGQQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNViraLAEEGRTMLLVTHEMGFARQVSSEVVFLHQG 229
Cdd:PRK11147 155 SSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGF---LKTFQGSIIFISHDRSFIRNMATRIVDLDRG 229
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
22-229 |
1.56e-06 |
|
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: 48.31 E-value: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 22 VLKGISLTARDGDVISILGSSGSGKSTFLRCINllenphqgqilvageelklkaaknGELVAADGKQINRLRseIGFVFQ 101
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLIL------------------------GELEPSEGKIKHSGR--ISFSSQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 102 NFNLWPHmSVLDNIIEAPR--RVLGQSKAEATEIAEALLAkvgISDKRHAYPAQ----LSGGQQQRAAIARTLAMQPKVI 175
Cdd:cd03291 106 FSWIMPG-TIKENIIFGVSydEYRYKSVVKACQLEEDITK---FPEKDNTVLGEggitLSGGQRARISLARAVYKDADLY 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489310645 176 LFDEPTSALDPEMVQEVLN--VIRALAEegRTMLLVTHEMGFARQvSSEVVFLHQG 229
Cdd:cd03291 182 LLDSPFGYLDVFTEKEIFEscVCKLMAN--KTRILVTSKMEHLKK-ADKILILHEG 234
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
33-217 |
4.04e-06 |
|
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: 45.44 E-value: 4.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 33 GDVISILGSSGSGKSTFLRCI-NLLENPHQGQILVAGEELKLKAAKNGELVAADGKqinrlrseigfvfqnfnlwphmsv 111
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALaRELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGK------------------------ 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 112 ldniieaprrvlgqskaeateiaeallakvgisdkrhayPAQLSGGQQQRAAIARTLAMQPKVILFDEPTSALDPEMVQE 191
Cdd:smart00382 58 ---------------------------------------KASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEAL 98
|
170 180 190
....*....|....*....|....*....|..
gi 489310645 192 VL------NVIRALAEEGRTMLLVTHEMGFAR 217
Cdd:smart00382 99 LLlleelrLLLLLKSEKNLTVILTTNDEKDLG 130
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
8-227 |
4.37e-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: 46.92 E-value: 4.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNlHKRYGELEvlkgISLtarDGDVISILGSSGSGKSTFLRCINLL-----------------ENPHQGQILVAGE- 69
Cdd:COG3593 6 IKIKN-FRSIKDLS----IEL---SDDLTVLVGENNSGKSSILEALRLLlgpsssrkfdeedfylgDDPDLPEIEIELTf 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 70 --------ELKLKAAKNGELVAAdgkqINRLRSEIGFVFQNFNlwphmSVLDNIIEAPRRV----LGQSKAEATEIAEAL 137
Cdd:COG3593 78 gsllsrllRLLLKEEDKEELEEA----LEELNEELKEALKALN-----ELLSEYLKELLDGldleLELSLDELEDLLKSL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 138 laKVGISDKRHAYPAQLSGGQQQRAAIARTLAM-------QPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVT 210
Cdd:COG3593 149 --SLRIEDGKELPLDRLGSGFQRLILLALLSALaelkrapANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITT 226
|
250
....*....|....*...
gi 489310645 211 HEMGFARQVS-SEVVFLH 227
Cdd:COG3593 227 HSPHLLSEVPlENIRRLR 244
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
6-211 |
5.33e-06 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 46.61 E-value: 5.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 6 PALEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCINLLENPHQGQILVAGEELKLKAAKNGELVAAD 85
Cdd:pfam13304 92 TLLEKRLLLREDSEEREPKFPPEAEELRLGLDVEERIELSLSELSDLISGLLLLSIISPLSFLLLLDEGLLLEDWAVLDL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 86 GKQINRLRSEIGFVFQnfnLWPHMSVLDNIIEAPRRVLGQSKAEATEIAEALLAKVGISDKRHAYPAQLSGGQQQ---RA 162
Cdd:pfam13304 172 AADLALFPDLKELLQR---LVRGLKLADLNLSDLGEGIEKSLLVDDRLRERGLILLENGGGGELPAFELSDGTKRllaLL 248
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489310645 163 AIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTH 211
Cdd:pfam13304 249 AALLSALPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTH 297
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
154-211 |
6.07e-06 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 47.05 E-value: 6.07e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 489310645 154 LSGGQQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRalaEEGRTMLLVTH 211
Cdd:TIGR00954 583 LSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCR---EFGITLFSVSH 637
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
8-209 |
7.85e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 46.55 E-value: 7.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRYGELEVLKGISLTARDGDVISILGSSGSGKSTFLRCI----NLLENPHQGQ----ILVAGEEL-KLKAAK- 77
Cdd:PRK10938 4 LQISQGTFRLSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALagelPLLSGERQSQfshiTRLSFEQLqKLVSDEw 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 78 ---NGELVAADGKQINRLRSEIgfvfqnfnlwphmsvldniIeaprrvlgQSKAEATEIAEALLAKVGIS---DKRHAYp 151
Cdd:PRK10938 84 qrnNTDMLSPGEDDTGRTTAEI-------------------I--------QDEVKDPARCEQLAQQFGITallDRRFKY- 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489310645 152 aqLSGGQQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLV 209
Cdd:PRK10938 136 --LSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLV 191
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
154-212 |
1.03e-05 |
|
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: 45.33 E-value: 1.03e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489310645 154 LSGGQQQRAAIARTLAMQPKVIL--FDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHE 212
Cdd:cd03270 138 LSGGEAQRIRLATQIGSGLTGVLyvLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHD 198
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
8-241 |
2.26e-05 |
|
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: 44.51 E-value: 2.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRYGEL--EVLKGISLTARDGDVISILGSSGSGKST----FLRCINLLEnphqGQILVAGEEL-KLKaaknge 80
Cdd:cd03288 20 IKIHDLCVRYENNlkPVLKHVKAYIKPGQKVGICGRTGSGKSSlslaFFRMVDIFD----GKIVIDGIDIsKLP------ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 81 lvaadgkqINRLRSEIGFVFQN---------FNLWPHMSVLDNIIeaprrvlgqskAEATEIAEALLAKVGISDKRHAYP 151
Cdd:cd03288 90 --------LHTLRSRLSIILQDpilfsgsirFNLDPECKCTDDRL-----------WEALEIAQLKNMVKSLPGGLDAVV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 152 AQ----LSGGQQQRAAIARTLAMQPKVILFDEPTSALD---PEMVQEVlnVIRALAEegRTMLLVTHEMGFARQvSSEVV 224
Cdd:cd03288 151 TEggenFSVGQRQLFCLARAFVRKSSILIMDEATASIDmatENILQKV--VMTAFAD--RTVVTIAHRVSTILD-ADLVL 225
|
250
....*....|....*..
gi 489310645 225 FLHQGLVEEQGSPQQVF 241
Cdd:cd03288 226 VLSRGILVECDTPENLL 242
|
|
| Rad50_Sulf |
NF041034 |
DNA double-strand break repair ATPase Rad50; |
153-212 |
2.81e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 468963 [Multi-domain] Cd Length: 872 Bit Score: 45.09 E-value: 2.81e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489310645 153 QLSGGQQ------QRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHE 212
Cdd:NF041034 779 ALSGGERisialaLRLAIAKSLMDEIGFMILDEPTVHLDEERKKELIDIIRSSMEIVPQIIVVTHD 844
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
26-219 |
4.96e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 44.11 E-value: 4.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 26 ISLTARDGDVISILGSSGSGKSTFLRcinllenphqgqILvaGEELklkAAKNGELVAADGKQINRLRSEiGFVFQNFN- 104
Cdd:PRK15064 20 ISVKFGGGNRYGLIGANGCGKSTFMK------------IL--GGDL---EPSAGNVSLDPNERLGKLRQD-QFAFEEFTv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 105 ----------LWPHMSVLDNIIeaprrvlgqSKAEATE-------------------IAEA----LLAKVGISDKRHAYP 151
Cdd:PRK15064 82 ldtvimghteLWEVKQERDRIY---------ALPEMSEedgmkvadlevkfaemdgyTAEArageLLLGVGIPEEQHYGL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489310645 152 -AQLSGGQQQRAAIARTLAMQPKVILFDEPTSALDpemvqevLNVIRALAEE--GR--TMLLVTHEMGFARQV 219
Cdd:PRK15064 153 mSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLD-------INTIRWLEDVlnERnsTMIIISHDRHFLNSV 218
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
10-212 |
7.50e-05 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 42.59 E-value: 7.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 10 IRNLHKRyGELEVLKGISLtardgdvisILGSSGSGKSTFLRCI----------NLLENPHQGQILVAGE---ELKLkaa 76
Cdd:cd03240 9 IRSFHER-SEIEFFSPLTL---------IVGQNGAGKTTIIEALkyaltgelppNSKGGAHDPKLIREGEvraQVKL--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 77 kngELVAADGKQINRLRSeigfvfqnfnlwphMSVLDNIIEAPRrvlGQSKAEATEIaeallakvgisdkrhayPAQLSG 156
Cdd:cd03240 76 ---AFENANGKKYTITRS--------------LAILENVIFCHQ---GESNWPLLDM-----------------RGRCSG 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489310645 157 GQQQ------RAAIARTLAMQPKVILFDEPTSALDPEMVQEVL-NVIRA-LAEEGRTMLLVTHE 212
Cdd:cd03240 119 GEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEESLaEIIEErKSQKNFQLIVITHD 182
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
154-213 |
8.72e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 43.66 E-value: 8.72e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489310645 154 LSGGQQQRAAIARTL---AMQPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHEM 213
Cdd:PRK00635 810 LSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNM 872
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
8-211 |
3.41e-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: 40.72 E-value: 3.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 8 LEIRNLHKRYGELEvlkgISLTARDGDVI-SILGSSGSGKSTFLRCINLLenphqgqilVAGEELKLKAAKNGELVAADG 86
Cdd:cd03279 6 LELKNFGPFREEQV----IDFTGLDNNGLfLICGPTGAGKSTILDAITYA---------LYGKTPRYGRQENLRSVFAPG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 87 KQinrlRSEIGFVFQnfnlwphmsvLDNIIEAPRRVLGQSKAEATEIAeaLLAKVGISD--KRHAypAQLSGGQQQRAAI 164
Cdd:cd03279 73 ED----TAEVSFTFQ----------LGGKKYRVERSRGLDYDQFTRIV--LLPQGEFDRflARPV--STLSGGETFLASL 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489310645 165 ARTLAMQpKVI----------LF-DEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTH 211
Cdd:cd03279 135 SLALALS-EVLqnrggarleaLFiDEGFGTLDPEALEAVATALELIRTENRMVGVISH 191
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
154-212 |
3.75e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.38 E-value: 3.75e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 489310645 154 LSGGQQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEvlnVIRALAEEGRTMLLVTHE 212
Cdd:PLN03073 628 LSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEA---LIQGLVLFQGGVLMVSHD 683
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
154-213 |
4.33e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 41.17 E-value: 4.33e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489310645 154 LSGGQQQRAAIARTLAM---QPKVILFDEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHEM 213
Cdd:COG0178 827 LSGGEAQRVKLASELSKrstGKTLYILDEPTTGLHFHDIRKLLEVLHRLVDKGNTVVVIEHNL 889
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
154-246 |
6.42e-04 |
|
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: 40.77 E-value: 6.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489310645 154 LSGGQQQRAAIARTLAMQPKVILF--DEPTSALDPEMVQEVLNVIRALAEEGRTMLLVTHEmgfaRQVSSEVVFL----- 226
Cdd:TIGR00630 489 LSGGEAQRIRLATQIGSGLTGVLYvlDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHD----EDTIRAADYVidigp 564
|
90 100
....*....|....*....|....
gi 489310645 227 ----HQGLVEEQGSPQQVFENPLS 246
Cdd:TIGR00630 565 gageHGGEVVASGTPEEILANPDS 588
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
153-202 |
4.48e-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: 4.48e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 489310645 153 QLSGGQQQRAAIARTLAMQ-----PKViLFDEPTSALDPEMVQEVLNVIRALAEE 202
Cdd:cd03272 158 QLSGGQKSLVALALIFAIQkcdpaPFY-LFDEIDAALDAQYRTAVANMIKELSDG 211
|
|
| |
