|
Name |
Accession |
Description |
Interval |
E-value |
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
24-262 |
3.43e-158 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 439.04 E-value: 3.43e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 24 VEFRHVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGrLSGSGLRQLRSRVG 103
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLT-DSKKDINKLRRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 104 FVFQQFNLYAHLTASQNITLALEHVHGWKPLPAQERALALLEKVGMLEKAHHYPAELSGGQQQRVAIARALASSPQIILF 183
Cdd:COG1126 81 MVFQQFNLFPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 544825118 184 DEPTSALDPEMIGEVLFVMKALAHSGITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQFFSQPAHPRAQRFLQKV 262
Cdd:COG1126 161 DEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHERTRAFLSKV 239
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
24-237 |
1.27e-125 |
|
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: 355.68 E-value: 1.27e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 24 VEFRHVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGrLSGSGLRQLRSRVG 103
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLT-DDKKNINELRQKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 104 FVFQQFNLYAHLTASQNITLALEHVHGWKPLPAQERALALLEKVGMLEKAHHYPAELSGGQQQRVAIARALASSPQIILF 183
Cdd:cd03262 80 MVFQQFNLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 544825118 184 DEPTSALDPEMIGEVLFVMKALAHSGITMIVVTHEMQFAREIADRIVFIDGGHI 237
Cdd:cd03262 160 DEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
24-262 |
4.61e-115 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 330.13 E-value: 4.61e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 24 VEFRHVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVD----NKPTgrlsgSGLRQLR 99
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDglkvNDPK-----VDERLIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 100 SRVGFVFQQFNLYAHLTASQNITLALEHVHGWKPLPAQERALALLEKVGMLEKAHHYPAELSGGQQQRVAIARALASSPQ 179
Cdd:PRK09493 77 QEAGMVFQQFYLFPHLTALENVMFGPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 180 IILFDEPTSALDPEMIGEVLFVMKALAHSGITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQFFSQPAHPRAQRFL 259
Cdd:PRK09493 157 LMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEFL 236
|
...
gi 544825118 260 QKV 262
Cdd:PRK09493 237 QHV 239
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
17-263 |
7.73e-109 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 315.20 E-value: 7.73e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 17 SHLEQASVEFRHVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKP-------TGR 89
Cdd:COG4598 2 TDTAPPALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEirlkpdrDGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 90 LSGSGLRQL---RSRVGFVFQQFNLYAHLTASQNITLALEHVHGWKPLPAQERALALLEKVGMLEKAHHYPAELSGGQQQ 166
Cdd:COG4598 82 LVPADRRQLqriRTRLGMVFQSFNLWSHMTVLENVIEAPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 167 RVAIARALASSPQIILFDEPTSALDPEMIGEVLFVMKALAHSGITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQF 246
Cdd:COG4598 162 RAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEV 241
|
250
....*....|....*..
gi 544825118 247 FSQPAHPRAQRFLQKVL 263
Cdd:COG4598 242 FGNPKSERLRQFLSSSL 258
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
24-265 |
3.28e-101 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 298.53 E-value: 3.28e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 24 VEFRHVDKRY----GDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSGSGLRQLR 99
Cdd:COG1135 2 IELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 100 SRVGFVFQQFNLYAHLTASQNITLALEhVHGWKPLPAQERALALLEKVGMLEKAHHYPAELSGGQQQRVAIARALASSPQ 179
Cdd:COG1135 82 RKIGMIFQHFNLLSSRTVAENVALPLE-IAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 180 IILFDEPTSALDPEMIGEVLFVMKALAHS-GITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQFFSQPAHPRAQRF 258
Cdd:COG1135 161 VLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQSELTRRF 240
|
....*..
gi 544825118 259 LQKVLDP 265
Cdd:COG1135 241 LPTVLND 247
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
22-263 |
1.63e-91 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 270.85 E-value: 1.63e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 22 ASVEFRHVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLE-PLSG----GEILVD-NKPTGRLSGSgL 95
Cdd:PRK11264 2 SAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEqPEAGtirvGDITIDtARSLSQQKGL-I 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 96 RQLRSRVGFVFQQFNLYAHLTASQNITLALEHVHGWKPLPAQERALALLEKVGMLEKAHHYPAELSGGQQQRVAIARALA 175
Cdd:PRK11264 81 RQLRQHVGFVFQNFNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 176 SSPQIILFDEPTSALDPEMIGEVLFVMKALAHSGITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQFFSQPAHPRA 255
Cdd:PRK11264 161 MRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPRT 240
|
....*...
gi 544825118 256 QRFLQKVL 263
Cdd:PRK11264 241 RQFLEKFL 248
|
|
| ectoine_ehuA |
TIGR03005 |
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ... |
24-263 |
4.17e-90 |
|
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding protein of a conserved four gene ABC transporter operon found next to ectoine unilization operons and ectoine biosynthesis operons. Ectoine is a compatible solute that protects enzymes from high osmolarity. It is released by some species in response to hypoosmotic shock, and it is taken up by a number of bacteria as a compatible solute or for consumption. This family shows strong sequence similiarity to a number of amino acid ABC transporter ATP-binding proteins.
Pssm-ID: 132050 [Multi-domain] Cd Length: 252 Bit Score: 267.47 E-value: 4.17e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 24 VEFRHVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVD----------NKPTGRLSGS 93
Cdd:TIGR03005 1 VRFSDVTKRFGILTVLDGLNFSVAAGEKVALIGPSGSGKSTILRILMTLEPIDEGQIQVEgeqlyhmpgrNGPLVPADEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 94 GLRQLRSRVGFVFQQFNLYAHLTASQNITLALEHVHGWKPLPAQERALALLEKVGMLEKAHHYPAELSGGQQQRVAIARA 173
Cdd:TIGR03005 81 HLRQMRNKIGMVFQSFNLFPHKTVLDNVTEAPVLVLGMARAEAEKRAMELLDMVGLADKADHMPAQLSGGQQQRVAIARA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 174 LASSPQIILFDEPTSALDPEMIGEVLFVMKALAH-SGITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQFFSQPAH 252
Cdd:TIGR03005 161 LAMRPKVMLFDEVTSALDPELVGEVLNVIRRLASeHDLTMLLVTHEMGFAREFADRVCFFDKGRIVEQGKPDEIFRQPKE 240
|
250
....*....|.
gi 544825118 253 PRAQRFLQKVL 263
Cdd:TIGR03005 241 ERTREFLSKVI 251
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
24-239 |
8.20e-90 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 265.75 E-value: 8.20e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 24 VEFRHVDKRYGD----HQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSGSGLRQLR 99
Cdd:COG1136 5 LELRNLTKSYGTgegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELARLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 100 SR-VGFVFQQFNLYAHLTASQNITLALEhVHGWKPLPAQERALALLEKVGMLEKAHHYPAELSGGQQQRVAIARALASSP 178
Cdd:COG1136 85 RRhIGFVFQFFNLLPELTALENVALPLL-LAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 544825118 179 QIILFDEPTSALDPEMIGEVLFVMKALAH-SGITMIVVTHEMQFArEIADRIVFIDGGHILE 239
Cdd:COG1136 164 KLILADEPTGNLDSKTGEEVLELLRELNReLGTTIVMVTHDPELA-ARADRVIRLRDGRIVS 224
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
24-237 |
5.82e-89 |
|
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: 263.20 E-value: 5.82e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 24 VEFRHVDKRYGD----HQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSGSGLRQLR 99
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 100 SR-VGFVFQQFNLYAHLTASQNITLALeHVHGWKPLPAQERALALLEKVGMLEKAHHYPAELSGGQQQRVAIARALASSP 178
Cdd:cd03255 81 RRhIGFVFQSFNLLPDLTALENVELPL-LLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 179 QIILFDEPTSALDPEMIGEVLFVMKALAH-SGITMIVVTHEMQFArEIADRIVFIDGGHI 237
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVMELLRELNKeAGTTIVVVTHDPELA-EYADRIIELRDGKI 218
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
24-246 |
3.51e-88 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 262.30 E-value: 3.51e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 24 VEFRHVDKRY-GDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSGSGLRQLRSRV 102
Cdd:COG3638 3 LELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLRRRI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 103 GFVFQQFNLYAHLTASQNITL-ALEHVHGWKPL----PAQER--ALALLEKVGMLEKAHHYPAELSGGQQQRVAIARALA 175
Cdd:COG3638 83 GMIFQQFNLVPRLSVLTNVLAgRLGRTSTWRSLlglfPPEDRerALEALERVGLADKAYQRADQLSGGQQQRVAIARALV 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 544825118 176 SSPQIILFDEPTSALDPEMIGEVLFVMKALAHS-GITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQF 246
Cdd:COG3638 163 QEPKLILADEPVASLDPKTARQVMDLLRRIAREdGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAEL 234
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
24-259 |
2.90e-87 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 259.53 E-value: 2.90e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 24 VEFRHVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLI-NQLEPLSgGEILVDNKPTGRLSGSGLRQLRSRV 102
Cdd:COG1127 6 IEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIiGLLRPDS-GEILVDGQDITGLSEKELYELRRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 103 GFVFQQFNLYAHLTASQNITLAL-EHVHgwkpLP---AQERALALLEKVGMLEKAHHYPAELSGGQQQRVAIARALASSP 178
Cdd:COG1127 85 GMLFQGGALFDSLTVFENVAFPLrEHTD----LSeaeIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 179 QIILFDEPTSALDPEMIGEVLFVMKALAHS-GITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQFFSQPaHPRAQR 257
Cdd:COG1127 161 EILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASD-DPWVRQ 239
|
..
gi 544825118 258 FL 259
Cdd:COG1127 240 FL 241
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
24-250 |
3.69e-86 |
|
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: 256.74 E-value: 3.69e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 24 VEFRHVDKRYGDH----QVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSGSGLRQLR 99
Cdd:cd03258 2 IELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 100 SRVGFVFQQFNLYAHLTASQNITLALEhVHGWKPLPAQERALALLEKVGMLEKAHHYPAELSGGQQQRVAIARALASSPQ 179
Cdd:cd03258 82 RRIGMIFQHFNLLSSRTVFENVALPLE-IAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 544825118 180 IILFDEPTSALDPEMIGEVLFVMKALAHS-GITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQFFSQP 250
Cdd:cd03258 161 VLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANP 232
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
24-239 |
1.25e-85 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 254.98 E-value: 1.25e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 24 VEFRHVDKRY-GDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSGSGLRQLRSRV 102
Cdd:COG2884 2 IRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 103 GFVFQQFNLYAHLTASQNITLALEhVHGWKPLPAQERALALLEKVGMLEKAHHYPAELSGGQQQRVAIARALASSPQIIL 182
Cdd:COG2884 82 GVVFQDFRLLPDRTVYENVALPLR-VTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 544825118 183 FDEPTSALDPEMIGEVLFVMKALAHSGITMIVVTHEMQFAREIADRIVFIDGGHILE 239
Cdd:COG2884 161 ADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLVR 217
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
24-271 |
2.65e-82 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 250.49 E-value: 2.65e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 24 VEFRHVDKRY----GDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSGSGLRQLR 99
Cdd:PRK11153 2 IELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 100 SRVGFVFQQFNLYAHLTASQNITLALEhVHGWKPLPAQERALALLEKVGMLEKAHHYPAELSGGQQQRVAIARALASSPQ 179
Cdd:PRK11153 82 RQIGMIFQHFNLLSSRTVFDNVALPLE-LAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 180 IILFDEPTSALDPEMIGEVLFVMKAL-AHSGITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQFFSQPAHPRAQRF 258
Cdd:PRK11153 161 VLLCDEATSALDPATTRSILELLKDInRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTREF 240
|
250
....*....|...
gi 544825118 259 LQKVLDPLHQEHL 271
Cdd:PRK11153 241 IQSTLHLDLPEDY 253
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
23-258 |
1.27e-81 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 245.31 E-value: 1.27e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 23 SVEFRHVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLE-PLSGGEILVDNK--PTGRLSGSGLRQLR 99
Cdd:COG4161 2 SIQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLEtPDSGQLNIAGHQfdFSQKPSEKAIRLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 100 SRVGFVFQQFNLYAHLTASQNITLALEHVHGWKPLPAQERALALLEKVGMLEKAHHYPAELSGGQQQRVAIARALASSPQ 179
Cdd:COG4161 82 QKVGMVFQQYNLWPHLTVMENLIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 544825118 180 IILFDEPTSALDPEMIGEVLFVMKALAHSGITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQFfsqpAHPRAQRF 258
Cdd:COG4161 162 VLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDASHF----TQPQTEAF 236
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
25-246 |
1.34e-81 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 245.17 E-value: 1.34e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 25 EFRHVDKRYGD-HQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSGSGLRQLRSRVG 103
Cdd:cd03256 2 EVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLRRQIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 104 FVFQQFNLYAHLTASQNITL-ALEHVHGWKPLP------AQERALALLEKVGMLEKAHHYPAELSGGQQQRVAIARALAS 176
Cdd:cd03256 82 MIFQQFNLIERLSVLENVLSgRLGRRSTWRSLFglfpkeEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQ 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 544825118 177 SPQIILFDEPTSALDPEMIGEVLFVMKALAHS-GITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQF 246
Cdd:cd03256 162 QPKLILADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
23-259 |
1.86e-80 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 242.61 E-value: 1.86e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 23 SVEFRHVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLE-PLSGGEILVDNK--PTGRLSGSGLRQLR 99
Cdd:PRK11124 2 SIQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEmPRSGTLNIAGNHfdFSKTPSDKAIRELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 100 SRVGFVFQQFNLYAHLTASQNITLALEHVHGWKPLPAQERALALLEKVGMLEKAHHYPAELSGGQQQRVAIARALASSPQ 179
Cdd:PRK11124 82 RNVGMVFQQYNLWPHLTVQQNLIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 180 IILFDEPTSALDPEMIGEVLFVMKALAHSGITMIVVTHEMQFAREIADRIVFIDGGHILETApPAQFFSQPAHPRAQRFL 259
Cdd:PRK11124 162 VLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQG-DASCFTQPQTEAFKNYL 240
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
24-258 |
2.05e-80 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 242.02 E-value: 2.05e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 24 VEFRHVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLI-NQLEPLSgGEILVDNKPTGRLSGSGLRQLRSRV 102
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIvGLLRPDS-GEVLIDGEDISGLSEAELYRLRRRM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 103 GFVFQQFNLYAHLTASQNITLALeHVHGWKPLPA-QERALALLEKVGMLEKAHHYPAELSGGQQQRVAIARALASSPQII 181
Cdd:cd03261 80 GMLFQSGALFDSLTVFENVAFPL-REHTRLSEEEiREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 544825118 182 LFDEPTSALDPEMIGEVLFVMKAL-AHSGITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQFFsQPAHPRAQRF 258
Cdd:cd03261 159 LYDEPTAGLDPIASGVIDDLIRSLkKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELR-ASDDPLVRQF 235
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
31-263 |
2.14e-80 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 242.95 E-value: 2.14e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 31 KRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNK-------PTGRLS---GSGLRQLRS 100
Cdd:PRK10619 13 KRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQtinlvrdKDGQLKvadKNQLRLLRT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 101 RVGFVFQQFNLYAHLTASQNITLALEHVHGWKPLPAQERALALLEKVGMLEKAH-HYPAELSGGQQQRVAIARALASSPQ 179
Cdd:PRK10619 93 RLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQgKYPVHLSGGQQQRVSIARALAMEPE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 180 IILFDEPTSALDPEMIGEVLFVMKALAHSGITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQFFSQPAHPRAQRFL 259
Cdd:PRK10619 173 VLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSPRLQQFL 252
|
....
gi 544825118 260 QKVL 263
Cdd:PRK10619 253 KGSL 256
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
24-265 |
1.57e-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: 248.66 E-value: 1.57e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 24 VEFRHVDKRY-----GDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSGSGLRQL 98
Cdd:COG1123 261 LEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 99 RSRVGFVFQ----QFNlyAHLTASQNITLALeHVHGWKPLP-AQERALALLEKVGMLEK-AHHYPAELSGGQQQRVAIAR 172
Cdd:COG1123 341 RRRVQMVFQdpysSLN--PRMTVGDIIAEPL-RLHGLLSRAeRRERVAELLERVGLPPDlADRYPHELSGGQRQRVAIAR 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 173 ALASSPQIILFDEPTSALDPEMIGEVLFVMKALAHS-GITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQFFSQPA 251
Cdd:COG1123 418 ALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQ 497
|
250
....*....|....*.
gi 544825118 252 HPRAQRFLQKV--LDP 265
Cdd:COG1123 498 HPYTRALLAAVpsLDP 513
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
20-259 |
1.80e-79 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 243.85 E-value: 1.80e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 20 EQASVEFRHVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSgSGLRqlr 99
Cdd:COG3842 2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLP-PEKR--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 100 sRVGFVFQQFNLYAHLTASQNITLALEhVHGWKPLPAQERALALLEKVGMLEKAHHYPAELSGGQQQRVAIARALASSPQ 179
Cdd:COG3842 78 -NVGMVFQDYALFPHLTVAENVAFGLR-MRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 180 IILFDEPTSALDPEMIGEVLFVMKAL-AHSGITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQFFSQPAHPRAQRF 258
Cdd:COG3842 156 VLLLDEPLSALDAKLREEMREELRRLqRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADF 235
|
.
gi 544825118 259 L 259
Cdd:COG3842 236 I 236
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
24-250 |
1.71e-78 |
|
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: 236.85 E-value: 1.71e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 24 VEFRHVDKRY-GDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSgsgLRQLRSRV 102
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKN---LRELRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 103 GFVFQ----QFnlyAHLTASQNITLALEHvHGWKPLPAQERALALLEKVGMLEKAHHYPAELSGGQQQRVAIARALASSP 178
Cdd:COG1122 78 GLVFQnpddQL---FAPTVEEDVAFGPEN-LGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEP 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 544825118 179 QIILFDEPTSALDPEMIGEVLFVMKALAHSGITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQFFSQP 250
Cdd:COG1122 154 EVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
24-246 |
9.29e-78 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 235.34 E-value: 9.29e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 24 VEFRHVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSgsglRQLRSRVG 103
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDP----AEVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 104 FVFQQFNLYAHLTASQNITLALEhVHGWKPLPAQERALALLEKVGMLEKAHHYPAELSGGQQQRVAIARALASSPQIILF 183
Cdd:COG1131 77 YVPQEPALYPDLTVRENLRFFAR-LYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLIL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 544825118 184 DEPTSALDPEMIGEVLFVMKALAHSGITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQF 246
Cdd:COG1131 156 DEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
24-270 |
1.10e-76 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 233.44 E-value: 1.10e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 24 VEFRHVDKRY----GDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPtgrlsgsgLRQLR 99
Cdd:COG1116 8 LELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKP--------VTGPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 100 SRVGFVFQQFNLYAHLTASQNITLALEhVHGWKPLPAQERALALLEKVGMLEKAHHYPAELSGGQQQRVAIARALASSPQ 179
Cdd:COG1116 80 PDRGVVFQEPALLPWLTVLDNVALGLE-LRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 180 IILFDEPTSALDP---EMIGEVLfvMKALAHSGITMIVVTHEMQFAREIADRIVFIDG--GHILET----APPAQFFSQP 250
Cdd:COG1116 159 VLLMDEPFGALDAltrERLQDEL--LRLWQETGKTVLFVTHDVDEAVFLADRVVVLSArpGRIVEEidvdLPRPRDRELR 236
|
250 260
....*....|....*....|
gi 544825118 251 AHPRAQRFLQKVLDPLHQEH 270
Cdd:COG1116 237 TSPEFAALRAEILDLLREEA 256
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
24-241 |
5.67e-75 |
|
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: 227.40 E-value: 5.67e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 24 VEFRHVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTgrlsgSGLRQLRSRVG 103
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV-----TGVPPERRNIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 104 FVFQQFNLYAHLTASQNITLALEhVHGWKPLPAQERALALLEKVGMLEKAHHYPAELSGGQQQRVAIARALASSPQIILF 183
Cdd:cd03259 76 MVFQDYALFPHLTVAENIAFGLK-LRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 544825118 184 DEPTSALDP----EMIGEVLFVMKALahsGITMIVVTHEMQFAREIADRIVFIDGGHILETA 241
Cdd:cd03259 155 DEPLSALDAklreELREELKELQREL---GITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
24-246 |
1.42e-73 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 224.87 E-value: 1.42e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 24 VEFRHVDKRYG-DHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSGSGLRQLRSRV 102
Cdd:TIGR02315 2 LEVENLSKVYPnGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 103 GFVFQQFNLYAHLTASQNI-------TLALEHVHGWKPLPAQERALALLEKVGMLEKAHHYPAELSGGQQQRVAIARALA 175
Cdd:TIGR02315 82 GMIFQHYNLIERLTVLENVlhgrlgyKPTWRSLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARALA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 544825118 176 SSPQIILFDEPTSALDPEMIGEVLFVMKALA-HSGITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQF 246
Cdd:TIGR02315 162 QQPDLILADEPIASLDPKTSKQVMDYLKRINkEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSEL 233
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
24-236 |
1.46e-73 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 222.45 E-value: 1.46e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 24 VEFRHVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSGSgLRQLRSRVG 103
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDE-LPPLRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 104 FVFQQFNLYAHLTASQNITLAlehvhgwkplpaqeralallekvgmlekahhypaeLSGGQQQRVAIARALASSPQIILF 183
Cdd:cd03229 80 MVFQDFALFPHLTVLENIALG-----------------------------------LSGGQQQRVALARALAMDPDVLLL 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 544825118 184 DEPTSALDPEMIGEVLFVMKAL-AHSGITMIVVTHEMQFAREIADRIVFIDGGH 236
Cdd:cd03229 125 DEPTSALDPITRREVRALLKSLqAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
24-240 |
3.68e-73 |
|
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: 223.12 E-value: 3.68e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 24 VEFRHVDKRYGD----HQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPtgrlsgsgLRQLR 99
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEP--------VTGPG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 100 SRVGFVFQQFNLYAHLTASQNITLALEhVHGWKPLPAQERALALLEKVGMLEKAHHYPAELSGGQQQRVAIARALASSPQ 179
Cdd:cd03293 73 PDRGYVFQQDALLPWLTVLDNVALGLE-LQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPD 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 544825118 180 IILFDEPTSALDP---EMIGEVLfvMKALAHSGITMIVVTHEMQFAREIADRIVFIDG--GHILET 240
Cdd:cd03293 152 VLLLDEPFSALDAltrEQLQEEL--LDIWRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIVAE 215
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
24-263 |
4.70e-72 |
|
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: 221.40 E-value: 4.70e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 24 VEFRHVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSG-----GEILVDNKP--TGRLSgsgLR 96
Cdd:TIGR00972 2 IEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMNDLVPgvrieGKVLFDGQDiyDKKID---VV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 97 QLRSRVGFVFQQFNLYAhLTASQNITLALEhVHGWKPLP-AQERALALLEKVGMLE----KAHHYPAELSGGQQQRVAIA 171
Cdd:TIGR00972 79 ELRRRVGMVFQKPNPFP-MSIYDNIAYGPR-LHGIKDKKeLDEIVEESLKKAALWDevkdRLHDSALGLSGGQQQRLCIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 172 RALASSPQIILFDEPTSALDPEMIGEVLFVMKALAHSgITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQFFSQPA 251
Cdd:TIGR00972 157 RALAVEPEVLLLDEPTSALDPIATGKIEELIQELKKK-YTIVIVTHNMQQAARISDRTAFFYDGELVEYGPTEQIFTNPK 235
|
250
....*....|..
gi 544825118 252 HPRAQRFLQKVL 263
Cdd:TIGR00972 236 EKRTEDYISGRF 247
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
22-252 |
6.58e-72 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 224.18 E-value: 6.58e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 22 ASVEFRHVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSGSglrqlRSR 101
Cdd:COG3839 2 ASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPK-----DRN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 102 VGFVFQQFNLYAHLTASQNITLALEhVHGWKPLPAQERALALLEKVGMLEKAHHYPAELSGGQQQRVAIARALASSPQII 181
Cdd:COG3839 77 IAMVFQSYALYPHMTVYENIAFPLK-LRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVF 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 544825118 182 LFDEPTSALDP----EMIGEvlfvMKAL-AHSGITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQFFSQPAH 252
Cdd:COG3839 156 LLDEPLSNLDAklrvEMRAE----IKRLhRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPAN 227
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
23-259 |
1.79e-71 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 223.10 E-value: 1.79e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 23 SVEFRHVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDnkptGRLSGSGLRQLRSRV 102
Cdd:COG1118 2 SIEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLN----GRDLFTNLPPRERRV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 103 GFVFQQFNLYAHLTASQNITLALEHvhgwKPLP---AQERALALLEKVGMLEKAHHYPAELSGGQQQRVAIARALASSPQ 179
Cdd:COG1118 78 GFVFQHYALFPHMTVAENIAFGLRV----RPPSkaeIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 180 IILFDEPTSALDPemigevlFVMKAL--------AHSGITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQFFSQPA 251
Cdd:COG1118 154 VLLLDEPFGALDA-------KVRKELrrwlrrlhDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPA 226
|
....*...
gi 544825118 252 HPRAQRFL 259
Cdd:COG1118 227 TPFVARFL 234
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
25-259 |
4.05e-70 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 218.42 E-value: 4.05e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 25 EFRHVDKRYGD-HQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSgsgLRQLRSRVG 103
Cdd:COG1125 3 EFENVTKRYPDgTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLD---PVELRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 104 FVFQQFNLYAHLTASQNITL--ALEhvhGWKPLPAQERALALLEKVGMLEK--AHHYPAELSGGQQQRVAIARALASSPQ 179
Cdd:COG1125 80 YVIQQIGLFPHMTVAENIATvpRLL---GWDKERIRARVDELLELVGLDPEeyRDRYPHELSGGQQQRVGVARALAADPP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 180 IILFDEPTSALDP----EMIGEVLFVMKALahsGITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQFFSQPAHPRA 255
Cdd:COG1125 157 ILLMDEPFGALDPitreQLQDELLRLQREL---GKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFV 233
|
....
gi 544825118 256 QRFL 259
Cdd:COG1125 234 ADFV 237
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
25-236 |
1.14e-69 |
|
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: 213.87 E-value: 1.14e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 25 EFRHVDKRYGDH--QVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSgsgLRQLRSRV 102
Cdd:cd03225 1 ELKNLSFSYPDGarPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLS---LKELRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 103 GFVFQ----QFnlyAHLTASQNITLALEHvHGWKPLPAQERALALLEKVGMLEKAHHYPAELSGGQQQRVAIARALASSP 178
Cdd:cd03225 78 GLVFQnpddQF---FGPTVEEEVAFGLEN-LGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 544825118 179 QIILFDEPTSALDPEMIGEVLFVMKALAHSGITMIVVTHEMQFAREIADRIVFIDGGH 236
Cdd:cd03225 154 DILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
24-261 |
5.64e-69 |
|
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: 213.32 E-value: 5.64e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 24 VEFRHVDKRYGD-HQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQL-EPLSGgEILVDNKPTGRLSGSglrQLRSR 101
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLiEPTSG-EIFIDGEDIREQDPV---ELRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 102 VGFVFQQFNLYAHLTASQNITLALEhVHGWKPLPAQERALALLEKVGM--LEKAHHYPAELSGGQQQRVAIARALASSPQ 179
Cdd:cd03295 77 IGYVIQQIGLFPHMTVEENIALVPK-LLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 180 IILFDEPTSALDP----EMIGEVLFVMKALahsGITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQFFSQPAHPRA 255
Cdd:cd03295 156 LLLMDEPFGALDPitrdQLQEEFKRLQQEL---GKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFV 232
|
....*.
gi 544825118 256 QRFLQK 261
Cdd:cd03295 233 AEFVGA 238
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
24-235 |
8.62e-67 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 206.72 E-value: 8.62e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 24 VEFRHVDKRY-GDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSGSGLRQLRSRV 102
Cdd:TIGR02673 2 IEFHNVSKAYpGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 103 GFVFQQFNLYAHLTASQNITLALEhVHGWKPLPAQERALALLEKVGMLEKAHHYPAELSGGQQQRVAIARALASSPQIIL 182
Cdd:TIGR02673 82 GVVFQDFRLLPDRTVYENVALPLE-VRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 544825118 183 FDEPTSALDPEMIGEVLFVMKALAHSGITMIVVTHEMQFAREIADRIVFIDGG 235
Cdd:TIGR02673 161 ADEPTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLSLVDRVAHRVIILDDG 213
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
24-264 |
3.02e-66 |
|
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: 206.58 E-value: 3.02e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 24 VEFRHVDKRYG----DHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPtgrLSGSGLRQLR 99
Cdd:COG1124 2 LEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRP---VTRRRRKAFR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 100 SRVGFVFQQFnlYAHLTASQNITLALE---HVHGWkpLPAQERALALLEKVGMLEK-AHHYPAELSGGQQQRVAIARALA 175
Cdd:COG1124 79 RRVQMVFQDP--YASLHPRHTVDRILAeplRIHGL--PDREERIAELLEQVGLPPSfLDRYPHQLSGGQRQRVAIARALI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 176 SSPQIILFDEPTSALDPEMIGEVLFVMKAL-AHSGITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQFFSQPAHPR 254
Cdd:COG1124 155 LEPELLLLDEPTSALDVSVQAEILNLLKDLrEERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKHPY 234
|
250
....*....|
gi 544825118 255 AQRFLQKVLD 264
Cdd:COG1124 235 TRELLAASLA 244
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
24-246 |
4.92e-66 |
|
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: 205.11 E-value: 4.92e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 24 VEFRHVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPL-----SGGEILVDNKPTGRLSGSGLRqL 98
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVDVLE-L 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 99 RSRVGFVFQQFNLYaHLTASQNITLALEhVHGWKP-LPAQERALALLEKVGMLE--KAHHYPAELSGGQQQRVAIARALA 175
Cdd:cd03260 80 RRRVGMVFQKPNPF-PGSIYDNVAYGLR-LHGIKLkEELDERVEEALRKAALWDevKDRLHALGLSGGQQQRLCLARALA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 544825118 176 SSPQIILFDEPTSALDPEMIGEVLFVMKALAHSgITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQF 246
Cdd:cd03260 158 NEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
24-244 |
9.53e-66 |
|
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: 204.59 E-value: 9.53e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 24 VEFRHVDKRYGDH----QVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSGSGLRQLR 99
Cdd:COG4181 9 IELRGLTKTVGTGagelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARARLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 100 SR-VGFVFQQFNLYAHLTASQNITLALEhvhgwkpL----PAQERALALLEKVGMLEKAHHYPAELSGGQQQRVAIARAL 174
Cdd:COG4181 89 ARhVGFVFQSFQLLPTLTALENVMLPLE-------LagrrDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAF 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 544825118 175 ASSPQIILFDEPTSALDP---EMIGEVLFVMKalAHSGITMIVVTHEMQFAREiADRIVFIDGGHILETAPPA 244
Cdd:COG4181 162 ATEPAILFADEPTGNLDAatgEQIIDLLFELN--RERGTTLVLVTHDPALAAR-CDRVLRLRAGRLVEDTAAT 231
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
24-255 |
1.48e-65 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 204.55 E-value: 1.48e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 24 VEFRHVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPtgrlsgsgLRQLRSRVG 103
Cdd:COG1121 7 IELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKP--------PRRARRRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 104 FVFQQFNLYAH--LTASQNITLALEHVHGWKPLPAQ---ERALALLEKVGMLEKAHHYPAELSGGQQQRVAIARALASSP 178
Cdd:COG1121 79 YVPQRAEVDWDfpITVRDVVLMGRYGRRGLFRRPSRadrEAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 544825118 179 QIILFDEPTSALDPEMIGEVLFVMKALAHSGITMIVVTHEMQFAREIADRIVFIDGGHILEtAPPAQFFSQPAHPRA 255
Cdd:COG1121 159 DLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLVAH-GPPEEVLTPENLSRA 234
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
24-241 |
2.13e-65 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 203.51 E-value: 2.13e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 24 VEFRHVDKRY----GDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSGSGLRQLR 99
Cdd:cd03257 2 LEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 100 SRVGFVFQ--QFNLYAHLTASQNITLALE-HVHGWKPLPAQERALALLEKVGMLEK-AHHYPAELSGGQQQRVAIARALA 175
Cdd:cd03257 82 KEIQMVFQdpMSSLNPRMTIGEQIAEPLRiHGKLSKKEARKEAVLLLLVGVGLPEEvLNRYPHELSGGQRQRVAIARALA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 544825118 176 SSPQIILFDEPTSALDPEMIGEVLFVMKAL-AHSGITMIVVTHEMQFAREIADRIVFIDGGHILETA 241
Cdd:cd03257 162 LNPKLLIADEPTSALDVSVQAQILDLLKKLqEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
25-246 |
1.73e-64 |
|
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: 201.62 E-value: 1.73e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 25 EFRHVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSgsglRQLRSRVGF 104
Cdd:COG4555 3 EVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEP----REARRQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 105 VFQQFNLYAHLTASQNITLALEhVHGWKPLPAQERALALLEKVGMLEKAHHYPAELSGGQQQRVAIARALASSPQIILFD 184
Cdd:COG4555 79 LPDERGLYDRLTVRENIRYFAE-LYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 544825118 185 EPTSALDPEMIGEVLFVMKALAHSGITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQF 246
Cdd:COG4555 158 EPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
20-259 |
2.81e-64 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 201.80 E-value: 2.81e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 20 EQASVEFRHVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLIN---QLEPlsG----GEILVDNKPtgrLSG 92
Cdd:COG1117 8 LEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNrmnDLIP--GarveGEILLDGED---IYD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 93 SGLR--QLRSRVGFVFQQFNLYAHltaS--QNITLALEhVHGWKPlPAQ-----ERAL---ALLEKVGmlEKAHHYPAEL 160
Cdd:COG1117 83 PDVDvvELRRRVGMVFQKPNPFPK---SiyDNVAYGLR-LHGIKS-KSEldeivEESLrkaALWDEVK--DRLKKSALGL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 161 SGGQQQRVAIARALASSPQIILFDEPTSALDP-------EMIGEvlfvmkaLAHSgITMIVVTHEMQFAREIADRIVFID 233
Cdd:COG1117 156 SGGQQQRLCIARALAVEPEVLLMDEPTSALDPistakieELILE-------LKKD-YTIVIVTHNMQQAARVSDYTAFFY 227
|
250 260
....*....|....*....|....*.
gi 544825118 234 GGHILETAPPAQFFSQPAHPRAQRFL 259
Cdd:COG1117 228 LGELVEFGPTEQIFTNPKDKRTEDYI 253
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
24-245 |
4.80e-64 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 201.04 E-value: 4.80e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 24 VEFRHVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSGsglRQLRSRVG 103
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSR---RELARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 104 FVFQQFNLYAHLTASQNITLA-LEHVHGWKPLPAQERALAL--LEKVGMLEKAHHYPAELSGGQQQRVAIARALASSPQI 180
Cdd:COG1120 79 YVPQEPPAPFGLTVRELVALGrYPHLGLFGRPSAEDREAVEeaLERTGLEHLADRPVDELSGGERQRVLIARALAQEPPL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 544825118 181 ILFDEPTSALDPEMIGEVLFVMKALAHS-GITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQ 245
Cdd:COG1120 159 LLLDEPTSHLDLAHQLEVLELLRRLARErGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEE 224
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
39-262 |
3.35e-63 |
|
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: 199.41 E-value: 3.35e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 39 LNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSGSGLRQLRS-RVGFVFQQFNLYAHLTA 117
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRkKISMVFQSFALLPHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 118 SQNITLALEhVHGWKPLPAQERALALLEKVGMLEKAHHYPAELSGGQQQRVAIARALASSPQIILFDEPTSALDP----E 193
Cdd:cd03294 120 LENVAFGLE-VQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPlirrE 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 544825118 194 MIGEVLfvmKALAHSGITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQFFSQPAHPRAQRFLQKV 262
Cdd:cd03294 199 MQDELL---RLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFFRGV 264
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
24-237 |
4.65e-63 |
|
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: 195.69 E-value: 4.65e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 24 VEFRHVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSgsglRQLRSRVG 103
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEP----EEVKRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 104 FVFQQFNLYAHLTASQNItlalehvhgwkplpaqeralallekvgmlekahhypaELSGGQQQRVAIARALASSPQIILF 183
Cdd:cd03230 77 YLPEEPSLYENLTVRENL-------------------------------------KLSGGMKQRLALAQALLHDPELLIL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 544825118 184 DEPTSALDPEMIGEVLFVMKALAHSGITMIVVTHEMQFAREIADRIVFIDGGHI 237
Cdd:cd03230 120 DEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
27-253 |
1.92e-62 |
|
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: 200.26 E-value: 1.92e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 27 RHVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSgSGLRQLrsrvGFVF 106
Cdd:TIGR03265 8 DNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLP-PQKRDY----GIVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 107 QQFNLYAHLTASQNITLALeHVHGWKPLPAQERALALLEKVGMLEKAHHYPAELSGGQQQRVAIARALASSPQIILFDEP 186
Cdd:TIGR03265 83 QSYALFPNLTVADNIAYGL-KNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 544825118 187 TSALDPEMIGEVLFVMKAL-AHSGITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQFFSQPAHP 253
Cdd:TIGR03265 162 LSALDARVREHLRTEIRQLqRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATP 229
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
24-251 |
2.79e-62 |
|
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: 195.92 E-value: 2.79e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 24 VEFRHVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTgrlsgSGLRQLRSRVG 103
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI-----TNLPPHKRPVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 104 FVFQQFNLYAHLTASQNITLALEhvhgWKPLPAQE---RALALLEKVGMLEKAHHYPAELSGGQQQRVAIARALASSPQI 180
Cdd:cd03300 76 TVFQNYALFPHLTVFENIAFGLR----LKKLPKAEikeRVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 544825118 181 ILFDEPTSALDPEMIGEVLFVMKALAHS-GITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQFFSQPA 251
Cdd:cd03300 152 LLLDEPLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPA 223
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
28-232 |
1.10e-61 |
|
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: 193.22 E-value: 1.10e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 28 HVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSGSGLRQL-RSRVGFVF 106
Cdd:TIGR03608 3 NISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKFrREKLGYLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 107 QQFNLYAHLTASQNITLALEHVHGWKPlPAQERALALLEKVGMLEKAHHYPAELSGGQQQRVAIARALASSPQIILFDEP 186
Cdd:TIGR03608 83 QNFALIENETVEENLDLGLKYKKLSKK-EKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADEP 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 544825118 187 TSALDPEMIGEVLFVMKALAHSGITMIVVTHEMQFArEIADRIVFI 232
Cdd:TIGR03608 162 TGSLDPKNRDEVLDLLLELNDEGKTIIIVTHDPEVA-KQADRVIEL 206
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
23-259 |
4.44e-61 |
|
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: 192.94 E-value: 4.44e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 23 SVEFRHVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSgsglrqLRSR- 101
Cdd:cd03296 2 SIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVP------VQERn 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 102 VGFVFQQFNLYAHLTASQNITLALEHVHGWKPLPAQE---RALALLEKVGMLEKAHHYPAELSGGQQQRVAIARALASSP 178
Cdd:cd03296 76 VGFVFQHYALFRHMTVFDNVAFGLRVKPRSERPPEAEiraKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 179 QIILFDEPTSALDPEMIGEVLFVMKALAHS-GITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQFFSQPAHPRAQR 257
Cdd:cd03296 156 KVLLLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYS 235
|
..
gi 544825118 258 FL 259
Cdd:cd03296 236 FL 237
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
24-249 |
7.60e-61 |
|
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: 193.42 E-value: 7.60e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 24 VEFRHVDKRY--GDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLIN-QLEPLSGgEILVDNKPTgrLSGSGLRQLRS 100
Cdd:TIGR04520 1 IEVENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNgLLLPTSG-KVTVDGLDT--LDEENLWEIRK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 101 RVGFVFQ----QFnlyAHLTASQNITLALEHvhgwKPLPAQE---RALALLEKVGMLEKAHHYPAELSGGQQQRVAIARA 173
Cdd:TIGR04520 78 KVGMVFQnpdnQF---VGATVEDDVAFGLEN----LGVPREEmrkRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 544825118 174 LASSPQIILFDEPTSALDPEMIGEVLFVMKALAHS-GITMIVVTHEMQFAREiADRIVFIDGGHILETAPPAQFFSQ 249
Cdd:TIGR04520 151 LAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEeGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGTPREIFSQ 226
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
21-255 |
9.08e-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: 200.13 E-value: 9.08e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 21 QASVEFRHVDKRY--GDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSG---GEILVDNKPTGRLSgsgL 95
Cdd:COG1123 2 TPLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELS---E 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 96 RQLRSRVGFVFQ----QFNLyahLTASQNITLALEhVHGWKPLPAQERALALLEKVGMLEKAHHYPAELSGGQQQRVAIA 171
Cdd:COG1123 79 ALRGRRIGMVFQdpmtQLNP---VTVGDQIAEALE-NLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 172 RALASSPQIILFDEPTSALDPEMIGEVLFVMKAL-AHSGITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQFFSQP 250
Cdd:COG1123 155 MALALDPDLLIADEPTTALDVTTQAEILDLLRELqRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAP 234
|
....*
gi 544825118 251 AHPRA 255
Cdd:COG1123 235 QALAA 239
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
24-228 |
2.10e-60 |
|
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: 190.31 E-value: 2.10e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 24 VEFRHVDKRY-GDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSGSGLRQLRSRV 102
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 103 GFVFQQFNLYAHLTASQNITLALEhVHGWKPLPAQERALALLEKVGMLEKAHHYPAELSGGQQQRVAIARALASSPQIIL 182
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALE-VTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILI 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 544825118 183 FDEPTSALDPEMIGEVLFVMKALAHSGITMIVVTHemqfAREIADR 228
Cdd:cd03292 160 ADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATH----AKELVDT 201
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
24-253 |
2.93e-60 |
|
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: 193.35 E-value: 2.93e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 24 VEFRHVDKRY----GDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEP---LSGGEILVDNKPTGRLSGSGLR 96
Cdd:COG0444 2 LEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 97 QLR-SRVGFVFQqfNLYAHL----TASQNITLALEHVHGWKPLPAQERALALLEKVGMLEKAHH---YPAELSGGQQQRV 168
Cdd:COG0444 82 KIRgREIQMIFQ--DPMTSLnpvmTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPDPERRldrYPHELSGGMRQRV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 169 AIARALASSPQIILFDEPTSALDPEMIGEVLFVMKALAHS-GITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQFF 247
Cdd:COG0444 160 MIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELF 239
|
....*.
gi 544825118 248 SQPAHP 253
Cdd:COG0444 240 ENPRHP 245
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
31-262 |
4.15e-60 |
|
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: 194.30 E-value: 4.15e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 31 KRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSGSGLRQLRSR-VGFVFQQF 109
Cdd:TIGR01186 1 KKTGGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPVELREVRRKkIGMVFQQF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 110 NLYAHLTASQNITLALEhVHGWKPLPAQERALALLEKVGMLEKAHHYPAELSGGQQQRVAIARALASSPQIILFDEPTSA 189
Cdd:TIGR01186 81 ALFPHMTILQNTSLGPE-LLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 544825118 190 LDP----EMIGEVLFVMKALahsGITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQFFSQPAHPRAQRFLQKV 262
Cdd:TIGR01186 160 LDPlirdSMQDELKKLQATL---QKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIGKV 233
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
24-267 |
6.16e-60 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 194.55 E-value: 6.16e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 24 VEFRHVDKRYGDH----------------------QVL--NDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGE 79
Cdd:COG4175 4 IEVRNLYKIFGKRperalklldqgkskdeilektgQTVgvNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 80 ILVDNKPTGRLSGSGLRQLR-SRVGFVFQQFNLYAHLTASQNITLALEhVHGwkpLPAQER---ALALLEKVGMLEKAHH 155
Cdd:COG4175 84 VLIDGEDITKLSKKELRELRrKKMSMVFQHFALLPHRTVLENVAFGLE-IQG---VPKAERrerAREALELVGLAGWEDS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 156 YPAELSGGQQQRVAIARALASSPQIILFDEPTSALDP----EMIGEVLfvmkALAHS-GITMIVVTHEMQFAREIADRIV 230
Cdd:COG4175 160 YPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPlirrEMQDELL----ELQAKlKKTIVFITHDLDEALRLGDRIA 235
|
250 260 270
....*....|....*....|....*....|....*..
gi 544825118 231 FIDGGHILETAPPAQFFSQPAHPRAQRFLQKVlDPLH 267
Cdd:COG4175 236 IMKDGRIVQIGTPEEILTNPANDYVADFVEDV-DRSK 271
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
25-259 |
1.41e-59 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 188.81 E-value: 1.41e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 25 EFRHVDKRYGdHQVLNdINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSgSGLRQlrsrVGF 104
Cdd:COG3840 3 RLDDLTYRYG-DFPLR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALP-PAERP----VSM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 105 VFQQFNLYAHLTASQNITLALEHvhGWKPLPAQERALA-LLEKVGMLEKAHHYPAELSGGQQQRVAIARALASSPQIILF 183
Cdd:COG3840 76 LFQENNLFPHLTVAQNIGLGLRP--GLKLTAEQRAQVEqALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 544825118 184 DEPTSALDPEMIGEVLFVMKALAHS-GITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQFFSQPAHPRAQRFL 259
Cdd:COG3840 154 DEPFSALDPALRQEMLDLVDELCRErGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYL 230
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
25-237 |
5.03e-58 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 184.25 E-value: 5.03e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 25 EFRHVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPtgrLSGSGLRQLRSRVGF 104
Cdd:COG4619 2 ELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKP---LSAMPPPEWRRQVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 105 VFQQFNLYAHlTASQNITLALEHVHgwkPLPAQERALALLEKVG----MLEKAHHypaELSGGQQQRVAIARALASSPQI 180
Cdd:COG4619 79 VPQEPALWGG-TVRDNLPFPFQLRE---RKFDRERALELLERLGlppdILDKPVE---RLSGGERQRLALIRALLLQPDV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 544825118 181 ILFDEPTSALDPEMIGEVL-FVMKALAHSGITMIVVTHEMQFAREIADRIVFIDGGHI 237
Cdd:COG4619 152 LLLDEPTSALDPENTRRVEeLLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
23-262 |
1.08e-57 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 187.98 E-value: 1.08e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 23 SVEFRHVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSGsglrqlRSR- 101
Cdd:PRK10851 2 SIEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHA------RDRk 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 102 VGFVFQQFNLYAHLTASQNITLALehvhgwKPLPAQER---------ALALLEKVGMLEKAHHYPAELSGGQQQRVAIAR 172
Cdd:PRK10851 76 VGFVFQHYALFRHMTVFDNIAFGL------TVLPRRERpnaaaikakVTQLLEMVQLAHLADRYPAQLSGGQKQRVALAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 173 ALASSPQIILFDEPTSALDPEMIGEVLFVMKALaHSGI--TMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQFFSQP 250
Cdd:PRK10851 150 ALAVEPQILLLDEPFGALDAQVRKELRRWLRQL-HEELkfTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREP 228
|
250
....*....|..
gi 544825118 251 AHPRAQRFLQKV 262
Cdd:PRK10851 229 ATRFVLEFMGEV 240
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
25-235 |
3.01e-57 |
|
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: 182.35 E-value: 3.01e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 25 EFRHVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPtgrlsgsgLRQLRSRVGF 104
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKP--------LEKERKRIGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 105 VFQQFNL--YAHLTASQNITLALE-HVHGWKPLPAQERALAL--LEKVGMLEKAHHYPAELSGGQQQRVAIARALASSPQ 179
Cdd:cd03235 73 VPQRRSIdrDFPISVRDVVLMGLYgHKGLFRRLSKADKAKVDeaLERVGLSELADRQIGELSGGQQQRVLLARALVQDPD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 544825118 180 IILFDEPTSALDPEMIGEVLFVMKALAHSGITMIVVTHEMQFAREIADRIVFIDGG 235
Cdd:cd03235 153 LLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLNRT 208
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
25-238 |
7.11e-57 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 179.94 E-value: 7.11e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 25 EFRHVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSgsgLRQLRSRVGF 104
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLS---PKELARKIAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 105 VFQqfnlyahltasqnitlalehvhgwkplpaqeralaLLEKVGMLEKAHHYPAELSGGQQQRVAIARALASSPQIILFD 184
Cdd:cd03214 78 VPQ-----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLD 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 544825118 185 EPTSALDPEMIGEVLFVMKALAHS-GITMIVVTHEMQFAREIADRIVFIDGGHIL 238
Cdd:cd03214 123 EPTSHLDIAHQIELLELLRRLARErGKTVVMVLHDLNLAARYADRVILLKDGRIV 177
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
27-245 |
2.56e-56 |
|
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: 180.71 E-value: 2.56e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 27 RHVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSgsglRQLRSRVGFV- 105
Cdd:cd03219 4 RGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLP----PHEIARLGIGr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 106 -FQQFNLYAHLTASQNITLALEHVHG-----WKPLP----AQERALALLEKVGMLEKAHHYPAELSGGQQQRVAIARALA 175
Cdd:cd03219 80 tFQIPRLFPELTVLENVMVAAQARTGsglllARARReereARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 176 SSPQIILFDEPTSALDPEMIGEVLFVMKALAHSGITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQ 245
Cdd:cd03219 160 TDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDE 229
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
25-251 |
1.55e-55 |
|
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: 179.08 E-value: 1.55e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 25 EFRHVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSGSglrqLRSRVGF 104
Cdd:COG0411 6 EVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPH----RIARLGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 105 V--FQQFNLYAHLTASQNITLALEHVHGWKPLP--------------AQERALALLEKVGMLEKAHHYPAELSGGQQQRV 168
Cdd:COG0411 82 ArtFQNPRLFPELTVLENVLVAAHARLGRGLLAallrlprarreereARERAEELLERVGLADRADEPAGNLSYGQQRRL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 169 AIARALASSPQIILFDEPTSALDPEMIGEVLFVMKAL-AHSGITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQFF 247
Cdd:COG0411 162 EIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLrDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAEVR 241
|
....
gi 544825118 248 SQPA 251
Cdd:COG0411 242 ADPR 245
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
21-245 |
5.00e-55 |
|
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: 188.50 E-value: 5.00e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 21 QASVEFRHVDKRYGDHQ--VLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSgsgLRQL 98
Cdd:COG2274 471 KGDIELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQID---PASL 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 99 RSRVGFVFQQFNLYaHLTASQNITLalehvhgWKPLPAQERALALLEKVGMLEKAHHYP-----------AELSGGQQQR 167
Cdd:COG2274 548 RRQIGVVLQDVFLF-SGTIRENITL-------GDPDATDEEIIEAARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQR 619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 168 VAIARALASSPQIILFDEPTSALDP--EMIgevlfVMKALAH--SGITMIVVTHEMQFAReIADRIVFIDGGHILETAPP 243
Cdd:COG2274 620 LAIARALLRNPRILILDEATSALDAetEAI-----ILENLRRllKGRTVIIIAHRLSTIR-LADRIIVLDKGRIVEDGTH 693
|
..
gi 544825118 244 AQ 245
Cdd:COG2274 694 EE 695
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
24-236 |
7.41e-55 |
|
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: 174.49 E-value: 7.41e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 24 VEFRHVDKRYGD--HQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPtgrLSGSGLRQLRSR 101
Cdd:cd03228 1 IEFKNVSFSYPGrpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVD---LRDLDLESLRKN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 102 VGFVFQQFNLYaHLTASQNItlalehvhgwkplpaqeralallekvgmlekahhypaeLSGGQQQRVAIARALASSPQII 181
Cdd:cd03228 78 IAYVPQDPFLF-SGTIRENI--------------------------------------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 544825118 182 LFDEPTSALDPEMIGEVLFVMKALAHsGITMIVVTHEMQFAReIADRIVFIDGGH 236
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALAK-GKTVIVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
39-253 |
2.04e-53 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 176.08 E-value: 2.04e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 39 LNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSGSGLRQLRSRVGFVFQqfNLYAHL--- 115
Cdd:COG4608 34 VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPLRRRMQMVFQ--DPYASLnpr 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 116 -TASQNITLALEhVHGWKPLPA-QERALALLEKVGML-EKAHHYPAELSGGQQQRVAIARALASSPQIILFDEPTSALDP 192
Cdd:COG4608 112 mTVGDIIAEPLR-IHGLASKAErRERVAELLELVGLRpEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDV 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 544825118 193 EMIGEVLFVMKAL-AHSGITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQFFSQPAHP 253
Cdd:COG4608 191 SIQAQVLNLLEDLqDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPRDELYARPLHP 252
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
24-241 |
2.81e-53 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 172.05 E-value: 2.81e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 24 VEFRHVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNK------PTGRlsgsglrq 97
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRdvtdlpPKDR-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 98 lrsRVGFVFQQFNLYAHLTASQNITLALEhVHGWKPLPAQERALALLEKVGMLEKAHHYPAELSGGQQQRVAIARALASS 177
Cdd:cd03301 73 ---DIAMVFQNYALYPHMTVYDNIAFGLK-LRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVRE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 544825118 178 PQIILFDEPTSALDP----EMIGEVLFVMKALahsGITMIVVTHEMQFAREIADRIVFIDGGHILETA 241
Cdd:cd03301 149 PKVFLMDEPLSNLDAklrvQMRAELKRLQQRL---GTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
25-236 |
3.22e-53 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 170.12 E-value: 3.22e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 25 EFRHVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSgsgLRQLRSRVGF 104
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLP---LEELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 105 VFQqfnlyahltasqnitlalehvhgwkplpaqeralallekvgmlekahhypaeLSGGQQQRVAIARALASSPQIILFD 184
Cdd:cd00267 78 VPQ----------------------------------------------------LSGGQRQRVALARALLLNPDLLLLD 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 544825118 185 EPTSALDPEMIGEVLFVMKALAHSGITMIVVTHEMQFAREIADRIVFIDGGH 236
Cdd:cd00267 106 EPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
24-261 |
3.98e-53 |
|
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: 173.79 E-value: 3.98e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 24 VEFRHVDKRYG-----DHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSGSGLRQL 98
Cdd:TIGR04521 1 IKLKNVSYIYQpgtpfEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 99 RSRVGFVFQqfnlYAhltASQnitLALEHVH----------GWKPLPAQERALALLEKVGMLEK-AHHYPAELSGGQQQR 167
Cdd:TIGR04521 81 RKKVGLVFQ----FP---EHQ---LFEETVYkdiafgpknlGLSEEEAEERVKEALELVGLDEEyLERSPFELSGGQMRR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 168 VAIARALASSPQIILFDEPTSALDPEMIGEVLFVMKALAHS-GITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQF 246
Cdd:TIGR04521 151 VAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEkGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREV 230
|
250 260
....*....|....*....|...
gi 544825118 247 FSQP--------AHPRAQRFLQK 261
Cdd:TIGR04521 231 FSDVdelekiglDVPEITELARK 253
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
24-251 |
1.82e-52 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 174.75 E-value: 1.82e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 24 VEFRHVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSGSglrqlRSRVG 103
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE-----NRHVN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 104 FVFQQFNLYAHLTASQNITLALEhvhgWKPLPAQE---RALALLEKVGMLEKAHHYPAELSGGQQQRVAIARALASSPQI 180
Cdd:PRK09452 90 TVFQSYALFPHMTVFENVAFGLR----MQKTPAAEitpRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKV 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 544825118 181 ILFDEPTSALDPEMIGEVLFVMKALAHS-GITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQFFSQPA 251
Cdd:PRK09452 166 LLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPK 237
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
21-239 |
2.59e-52 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 179.21 E-value: 2.59e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 21 QASVEFRHVDKRY-GDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSgsgLRQLR 99
Cdd:COG1132 337 RGEIEFENVSFSYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLT---LESLR 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 100 SRVGFVFQQFNLYaHLTASQNITLAlehvhgwKPLPAQERALALLEKVGMLEKAHHYP-----------AELSGGQQQRV 168
Cdd:COG1132 414 RQIGVVPQDTFLF-SGTIRENIRYG-------RPDATDEEVEEAAKAAQAHEFIEALPdgydtvvgergVNLSGGQRQRI 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 544825118 169 AIARALASSPQIILFDEPTSALDPEMigEVLfVMKALAH--SGITMIVVTHEMQFAREiADRIVFIDGGHILE 239
Cdd:COG1132 486 AIARALLKDPPILILDEATSALDTET--EAL-IQEALERlmKGRTTIVIAHRLSTIRN-ADRILVLDDGRIVE 554
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
37-237 |
1.49e-51 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 167.97 E-value: 1.49e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 37 QVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSGSGLRQLRSR-VGFVFQQFNLYAHL 115
Cdd:NF038007 19 KVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNLSYSQKIILRRElIGYIFQSFNLIPHL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 116 TASQNITLALEHvHGWKPLPAQERALALLEKVGMLEKAHHYPAELSGGQQQRVAIARALASSPQIILFDEPTSALDPEMI 195
Cdd:NF038007 99 SIFDNVALPLKY-RGVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSNPALLLADEPTGNLDSKNA 177
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 544825118 196 GEVLFVMKALAHSGITMIVVTHEMQfAREIADRIVFIDGGHI 237
Cdd:NF038007 178 RAVLQQLKYINQKGTTIIMVTHSDE-ASTYGNRIINMKDGKL 218
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
22-243 |
1.71e-51 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 177.99 E-value: 1.71e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 22 ASVEFRHVDKRY--GDHQ--VLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSGSGLRQ 97
Cdd:PRK10535 3 ALLELKDIRRSYpsGEEQveVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 98 LR-SRVGFVFQQFNLYAHLTASQNITLALEHVhGWKPLPAQERALALLEKVGMLEKAHHYPAELSGGQQQRVAIARALAS 176
Cdd:PRK10535 83 LRrEHFGFIFQRYHLLSHLTAAQNVEVPAVYA-GLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 544825118 177 SPQIILFDEPTSALDPEMIGEVLFVMKALAHSGITMIVVTHEMQFAREiADRIVFIDGGHILETAPP 243
Cdd:PRK10535 162 GGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEIVRNPPA 227
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
24-246 |
3.78e-51 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 174.44 E-value: 3.78e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 24 VEFRHVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPtgrLSGSGLRQ-LRSRV 102
Cdd:COG1129 5 LEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEP---VRFRSPRDaQAAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 103 GFVFQQFNLYAHLTASQNITLALEHVHG----WKPLpaQERALALLEKVGMLEKAHHYPAELSGGQQQRVAIARALASSP 178
Cdd:COG1129 82 AIIHQELNLVPNLSVAENIFLGREPRRGglidWRAM--RRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 179 QIILFDEPTSALDPEMIgEVLF-VMKALAHSGITMIVVTHEMQFAREIADRI-VFIDGGHIlETAPPAQF 246
Cdd:COG1129 160 RVLILDEPTASLTEREV-ERLFrIIRRLKAQGVAIIYISHRLDEVFEIADRVtVLRDGRLV-GTGPVAEL 227
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
27-235 |
3.81e-51 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 166.76 E-value: 3.81e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 27 RHVDKRYGDH----QVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSGSGLRQLRSR- 101
Cdd:TIGR02211 5 ENLGKRYQEGkldtRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAKLRNKk 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 102 VGFVFQQFNLYAHLTASQNITLALeHVHGWKPLPAQERALALLEKVGMLEKAHHYPAELSGGQQQRVAIARALASSPQII 181
Cdd:TIGR02211 85 LGFIYQFHHLLPDFTALENVAMPL-LIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPSLV 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 544825118 182 LFDEPTSALDPEMIGEVLFVMKAL-AHSGITMIVVTHEMQFAREIADRIVFIDGG 235
Cdd:TIGR02211 164 LADEPTGNLDNNNAKIIFDLMLELnRELNTSFLVVTHDLELAKKLDRVLEMKDGQ 218
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
23-258 |
9.92e-51 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 169.90 E-value: 9.92e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 23 SVEFRHvdkRYGDHQVlnDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPtgrLSGSGLRQL---- 98
Cdd:COG4148 4 EVDFRL---RRGGFTL--DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEV---LQDSARGIFlpph 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 99 RSRVGFVFQQFNLYAHLTASQNITLalehvhGWKPLPAQERALALLEKVGMLEKAH---HYPAELSGGQQQRVAIARALA 175
Cdd:COG4148 76 RRRIGYVFQEARLFPHLSVRGNLLY------GRKRAPRAERRISFDEVVELLGIGHlldRRPATLSGGERQRVAIGRALL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 176 SSPQIILFDEPTSALDPEMIGEVLFVMKALAHS-GITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQFFSQPA-HP 253
Cdd:COG4148 150 SSPRLLLMDEPLAALDLARKAEILPYLERLRDElDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDlLP 229
|
....*
gi 544825118 254 RAQRF 258
Cdd:COG4148 230 LAGGE 234
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
25-246 |
1.09e-50 |
|
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: 165.69 E-value: 1.09e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 25 EFRHVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSGSglRQLRSRVGF 104
Cdd:cd03224 2 EVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPH--ERARAGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 105 VFQQFNLYAHLTASQNITLALEHVHGWKPLPAQERALALLEKVGmlEKAHHYPAELSGGQQQRVAIARALASSPQIILFD 184
Cdd:cd03224 80 VPEGRRIFPELTVEENLLLGAYARRRAKRKARLERVYELFPRLK--ERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 544825118 185 EPTSALDPEMIGEVLFVMKALAHSGITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQF 246
Cdd:cd03224 158 EPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
31-265 |
1.70e-50 |
|
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: 173.33 E-value: 1.70e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 31 KRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPlSGGEILVDNKPTGRLSGSGLRQLRSRVGFVFQqfN 110
Cdd:COG4172 294 RTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSRRALRPLRRRMQVVFQ--D 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 111 LYAHL----TASQNITLALeHVHGWKPLPAQ--ERALALLEKVGMLEKA-HHYPAELSGGQQQRVAIARALASSPQIILF 183
Cdd:COG4172 371 PFGSLsprmTVGQIIAEGL-RVHGPGLSAAErrARVAEALEEVGLDPAArHRYPHEFSGGQRQRIAIARALILEPKLLVL 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 184 DEPTSALDPEMIGEVLFVMKAL-AHSGITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQFFSQPAHPRAQRFLQKV 262
Cdd:COG4172 450 DEPTSALDVSVQAQILDLLRDLqREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDAPQHPYTRALLAAA 529
|
...
gi 544825118 263 LDP 265
Cdd:COG4172 530 PLL 532
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
39-188 |
3.40e-49 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 159.35 E-value: 3.40e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 39 LNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPtgrLSGSGLRQLRSRVGFVFQQFNLYAHLTAS 118
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQD---LTDDERKSLRKEIGYVFQDPQLFPRLTVR 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 544825118 119 QNITLALeHVHGWKPLPAQERALALLEKVGMLEKAHH----YPAELSGGQQQRVAIARALASSPQIILFDEPTS 188
Cdd:pfam00005 78 ENLRLGL-LLKGLSKREKDARAEEALEKLGLGDLADRpvgeRPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
24-249 |
6.92e-49 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 162.88 E-value: 6.92e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 24 VEFRHVDKRYGD--HQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPtgrLSGSGLRQLRSR 101
Cdd:PRK13635 6 IRVEHISFRYPDaaTYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMV---LSEETVWDVRRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 102 VGFVFQQ-FNLYAHLTASQNITLALEHvHGWKPLPAQERALALLEKVGMLEKAHHYPAELSGGQQQRVAIARALASSPQI 180
Cdd:PRK13635 83 VGMVFQNpDNQFVGATVQDDVAFGLEN-IGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDI 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 181 ILFDEPTSALDPEMIGEVLFVMKAL-AHSGITMIVVTHEMQFAREiADRIVFIDGGHILETAPPAQFFSQ 249
Cdd:PRK13635 162 IILDEATSMLDPRGRREVLETVRQLkEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFKS 230
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
20-260 |
3.67e-48 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 167.64 E-value: 3.67e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 20 EQASVEFRHVDKRY--GDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSGSglrQ 97
Cdd:COG4987 330 GGPSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDED---D 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 98 LRSRVGFVFQQfnlyAHL---TASQNITLAlehvhgwKPLPAQERALALLEKVGMLEKAHHYP-----------AELSGG 163
Cdd:COG4987 407 LRRRIAVVPQR----PHLfdtTLRENLRLA-------RPDATDEELWAALERVGLGDWLAALPdgldtwlgeggRRLSGG 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 164 QQQRVAIARALASSPQIILFDEPTSALDPEMIGEVLFVMKALAHsGITMIVVTHEMQfAREIADRIVFIDGGHILETAPP 243
Cdd:COG4987 476 ERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA-GRTVLLITHRLA-GLERMDRILVLEDGRIVEQGTH 553
|
250
....*....|....*..
gi 544825118 244 AQFFSQpaHPRAQRFLQ 260
Cdd:COG4987 554 EELLAQ--NGRYRQLYQ 568
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
23-237 |
1.71e-47 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 159.89 E-value: 1.71e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 23 SVEFRHVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGrlsgsglRQLRSRV 102
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD-------PEDRRRI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 103 GFVFQQFNLYAHLTASQNIT-LA-LehvHGWKPLPAQERALALLEKVGMLEKAHHYPAELSGGQQQRVAIARALASSPQI 180
Cdd:COG4152 74 GYLPEERGLYPKMKVGEQLVyLArL---KGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPEL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 181 ILFDEPTSALDP---EMIGEVLfvmKALAHSGITMIVVTHEMQFAREIADRIVFIDGGHI 237
Cdd:COG4152 151 LILDEPFSGLDPvnvELLKDVI---RELAAKGTTVIFSSHQMELVEELCDRIVIINKGRK 207
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
22-251 |
5.17e-47 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 160.58 E-value: 5.17e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 22 ASVEFRHVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNK------PTGRlsgsgl 95
Cdd:PRK11000 2 ASVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKrmndvpPAER------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 96 rqlrsRVGFVFQQFNLYAHLTASQNITLALEhVHGWKPLPAQERALALLEkvgMLEKAH---HYPAELSGGQQQRVAIAR 172
Cdd:PRK11000 76 -----GVGMVFQSYALYPHLSVAENMSFGLK-LAGAKKEEINQRVNQVAE---VLQLAHlldRKPKALSGGQRQRVAIGR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 173 ALASSPQIILFDEPTSALDP----EMIGEVLFVMKALahsGITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQFFS 248
Cdd:PRK11000 147 TLVAEPSVFLLDEPLSNLDAalrvQMRIEISRLHKRL---GRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYH 223
|
...
gi 544825118 249 QPA 251
Cdd:PRK11000 224 YPA 226
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
28-237 |
2.21e-46 |
|
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: 153.95 E-value: 2.21e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 28 HVDKRYGDHQ-VLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRlsgsglRQLRSRVGFVF 106
Cdd:cd03226 4 NISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA------KERRKSIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 107 QqfNLYAHLTASqniTLALEHVHGWKPLPA-QERALALLEKVGMLEKAHHYPAELSGGQQQRVAIARALASSPQIILFDE 185
Cdd:cd03226 78 Q--DVDYQLFTD---SVREELLLGLKELDAgNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 544825118 186 PTSALDPEMIGEVLFVMKALAHSGITMIVVTHEMQFAREIADRIVFIDGGHI 237
Cdd:cd03226 153 PTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
8-245 |
2.28e-46 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 163.01 E-value: 2.28e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 8 HSAAGAADFSHLEQASVEFRHVDKRYGD-HQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKP 86
Cdd:COG4988 321 AAPAGTAPLPAAGPPSIELEDVSFSYPGgRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVD 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 87 TGRLSgsgLRQLRSRVGFVFQQFNLYaHLTASQNITLAlehvhgwKPLPAQERALALLEKVGMLEKAHHYP--------- 157
Cdd:COG4988 401 LSDLD---PASWRRQIAWVPQNPYLF-AGTIRENLRLG-------RPDASDEELEAALEAAGLDEFVAALPdgldtplge 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 158 --AELSGGQQQRVAIARALASSPQIILFDEPTSALDPEMIGEVLFVMKALAHsGITMIVVTHEMQFAREiADRIVFIDGG 235
Cdd:COG4988 470 ggRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK-GRTVILITHRLALLAQ-ADRILVLDDG 547
|
250
....*....|
gi 544825118 236 HILETAPPAQ 245
Cdd:COG4988 548 RIVEQGTHEE 557
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
21-246 |
2.84e-46 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 155.94 E-value: 2.84e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 21 QASVEFRHVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQL-----EPLSGGEILVDN-KPTGRLSGSg 94
Cdd:PRK09984 2 QTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgdkSAGSHIELLGRTvQREGRLARD- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 95 LRQLRSRVGFVFQQFNLYAHLTASQNITL-ALEHVHGWKPL-----PAQ-ERALALLEKVGMLEKAHHYPAELSGGQQQR 167
Cdd:PRK09984 81 IRKSRANTGYIFQQFNLVNRLSVLENVLIgALGSTPFWRTCfswftREQkQRALQALTRVGMVHFAHQRVSTLSGGQQQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 168 VAIARALASSPQIILFDEPTSALDPEMIGEVLFVMKALAHS-GITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQF 246
Cdd:PRK09984 161 VAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQF 240
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
33-252 |
3.02e-46 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 155.32 E-value: 3.02e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 33 YGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGgEILVdnkpTGRLSGSGLR---------QLRSRVG 103
Cdd:PRK14239 15 YNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNP-EVTI----TGSIVYNGHNiysprtdtvDLRKEIG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 104 FVFQQFNLYAhLTASQNIT--LALEHVHGWKPL-PAQERAL---ALLEKVGmlEKAHHYPAELSGGQQQRVAIARALASS 177
Cdd:PRK14239 90 MVFQQPNPFP-MSIYENVVygLRLKGIKDKQVLdEAVEKSLkgaSIWDEVK--DRLHDSALGLSGGQQQRVCIARVLATS 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 544825118 178 PQIILFDEPTSALDP---EMIGEVLFVMKalahSGITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQFFSQPAH 252
Cdd:PRK14239 167 PKIILLDEPTSALDPisaGKIEETLLGLK----DDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPKH 240
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
24-237 |
3.67e-46 |
|
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: 152.20 E-value: 3.67e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 24 VEFRHVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSGSglRQLRSRVG 103
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPR--DARRAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 104 FVFQqfnlyahltasqnitlalehvhgwkplpaqeralallekvgmlekahhypaeLSGGQQQRVAIARALASSPQIILF 183
Cdd:cd03216 79 MVYQ----------------------------------------------------LSVGERQMVEIARALARNARLLIL 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 544825118 184 DEPTSALDPEMIGEVLFVMKALAHSGITMIVVTHEMQFAREIADRIVFIDGGHI 237
Cdd:cd03216 107 DEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
24-245 |
3.77e-46 |
|
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: 154.86 E-value: 3.77e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 24 VEFRHVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLIN-QLEPLSGGEILVDNKPTGRLSgsgLRQLRSRV 102
Cdd:COG1119 4 LELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITgDLPPTYGNDVRLFGERRGGED---VWELRKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 103 GFV--FQQFNLYAHLTASQNITLALEHVHG-WKPLPAQ--ERALALLEKVGMLEKAHHYPAELSGGQQQRVAIARALASS 177
Cdd:COG1119 81 GLVspALQLRFPRDETVLDVVLSGFFDSIGlYREPTDEqrERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 544825118 178 PQIILFDEPTSALDPEMIGEVLFVMKALAHSG-ITMIVVTHEMQfarEIAD---RIVFIDGGHILETAPPAQ 245
Cdd:COG1119 161 PELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHHVE---EIPPgitHVLLLKDGRVVAAGPKEE 229
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-259 |
6.77e-46 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 154.30 E-value: 6.77e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 21 QASVEFRHVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQL-----EPLSGGEILVDNKPTGRLSgsgL 95
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMD---V 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 96 RQLRSRVGFVFQQFNLYAHLTASQNITLALEH---VHGWKPLpaQERALALLEKVGMLEKAHHY---PA-ELSGGQQQRV 168
Cdd:PRK14247 78 IELRRRVQMVFQIPNPIPNLSIFENVALGLKLnrlVKSKKEL--QERVRWALEKAQLWDEVKDRldaPAgKLSGGQQQRL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 169 AIARALASSPQIILFDEPTSALDPEMIGEVLFVMKALAHSgITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQFFS 248
Cdd:PRK14247 156 CIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFT 234
|
250
....*....|.
gi 544825118 249 QPAHPRAQRFL 259
Cdd:PRK14247 235 NPRHELTEKYV 245
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
23-259 |
9.67e-46 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 160.62 E-value: 9.67e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 23 SVEFRHVDkryGDHQVLNDINLTITPGEVVAILGPSGSGKS----TLIRLINQLEPLSGGEILVDNKPTGRLSGSGLRQL 98
Cdd:COG4172 13 SVAFGQGG---GTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRRI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 99 R-SRVGFVFQQ----FN-LYahlTASQNITLALEHVHGWKPLPAQERALALLEKVGMLE---KAHHYPAELSGGQQQRVA 169
Cdd:COG4172 90 RgNRIAMIFQEpmtsLNpLH---TIGKQIAEVLRLHRGLSGAAARARALELLERVGIPDperRLDAYPHQLSGGQRQRVM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 170 IARALASSPQIILFDEPTSALDPEMIGEVLFVMKAL-AHSGITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQFFS 248
Cdd:COG4172 167 IAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLqRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAELFA 246
|
250
....*....|.
gi 544825118 249 QPAHPRAQRFL 259
Cdd:COG4172 247 APQHPYTRKLL 257
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
22-225 |
9.72e-46 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 152.63 E-value: 9.72e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 22 ASVEFRHVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSgsglRQLRSR 101
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAR----EDYRRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 102 VGFVFQQFNLYAHLTASQNITLaleHVHGWKPLPAQERALALLEKVGMLEKAHHYPAELSGGQQQRVAIARALASSPQII 181
Cdd:COG4133 77 LAYLGHADGLKPELTVRENLRF---WAALYGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLW 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 544825118 182 LFDEPTSALDPEMIGEVLFVMKALAHSGITMIVVTH---EMQFAREI 225
Cdd:COG4133 154 LLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHqplELAAARVL 200
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
24-241 |
2.06e-45 |
|
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: 151.60 E-value: 2.06e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 24 VEFRHVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSGSglrqlRSRVG 103
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEA-----LRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 104 FVFQQFNLYAHLTASQNI-TLALehVHGWKplpaQERALALLEKVGMLEKAHHYPAELSGGQQQRVAIARALASSPQIIL 182
Cdd:cd03268 76 ALIEAPGFYPNLTARENLrLLAR--LLGIR----KKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 544825118 183 FDEPTSALDPEMIGEVLFVMKALAHSGITMIVVTH---EMQfarEIADRIVFIDGGHILETA 241
Cdd:cd03268 150 LDEPTNGLDPDGIKELRELILSLRDQGITVLISSHllsEIQ---KVADRIGIINKGKLIEEG 208
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
24-249 |
2.47e-45 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 153.70 E-value: 2.47e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 24 VEFRHVDKRYG-DHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSGsgLRQLRSRV 102
Cdd:PRK13633 10 VSYKYESNEEStEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEN--LWDIRNKA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 103 GFVFQqfNLYAHLTAS---QNITLALEHVhGWKPLPAQERALALLEKVGMLEKAHHYPAELSGGQQQRVAIARALASSPQ 179
Cdd:PRK13633 88 GMVFQ--NPDNQIVATiveEDVAFGPENL-GIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPE 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 544825118 180 IILFDEPTSALDPEMIGEVLFVMKAL-AHSGITMIVVTHEMQFAREiADRIVFIDGGHILETAPPAQFFSQ 249
Cdd:PRK13633 165 CIIFDEPTAMLDPSGRREVVNTIKELnKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
19-247 |
3.38e-45 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 153.22 E-value: 3.38e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 19 LEQASVEFRHVDKRYGDHQ--VLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKptgRLSGSGLR 96
Cdd:PRK13632 3 NKSVMIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGI---TISKENLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 97 QLRSRVGFVFQ----QFnlyAHLTASQNITLALEHvhgwKPLPAQERA---LALLEKVGMLEKAHHYPAELSGGQQQRVA 169
Cdd:PRK13632 80 EIRKKIGIIFQnpdnQF---IGATVEDDIAFGLEN----KKVPPKKMKdiiDDLAKKVGMEDYLDKEPQNLSGGQKQRVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 170 IARALASSPQIILFDEPTSALDPEMIGEVLFVMKALAHSGI-TMIVVTHEMQfarEI--ADRIVFIDGGHILETAPPAQF 246
Cdd:PRK13632 153 IASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLISITHDMD---EAilADKVIVFSEGKLIAQGKPKEI 229
|
.
gi 544825118 247 F 247
Cdd:PRK13632 230 L 230
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
31-238 |
3.53e-45 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 151.29 E-value: 3.53e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 31 KRYGDHQVlnDINLTiTPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDnkptGRLSGSGLRQL-----RSRVGFV 105
Cdd:cd03297 8 KRLPDFTL--KIDFD-LNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLN----GTVLFDSRKKInlppqQRKIGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 106 FQQFNLYAHLTASQNITLALEhvhGWKPLPAQERALALLEKVGMLEKAHHYPAELSGGQQQRVAIARALASSPQIILFDE 185
Cdd:cd03297 81 FQQYALFPHLNVRENLAFGLK---RKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 544825118 186 PTSALDPEMIGEVL-FVMKALAHSGITMIVVTHEMQFAREIADRIVFIDGGHIL 238
Cdd:cd03297 158 PFSALDRALRLQLLpELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQ 211
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
31-238 |
4.55e-45 |
|
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: 153.70 E-value: 4.55e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 31 KRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGeilvdnkpTGRLSG----SGLRQLRSRVGFVF 106
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSG--------TARVAGydvvREPRKVRRSIGIVP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 107 QQFNLYAHLTASQNITLALEhVHGWKPLPAQERALALLEKVGMLEKAHHYPAELSGGQQQRVAIARALASSPQIILFDEP 186
Cdd:TIGR01188 73 QYASVDEDLTGRENLEMMGR-LYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEP 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 544825118 187 TSALDPEMIGEVLFVMKALAHSGITMIVVTHEMQFAREIADRIVFIDGGHIL 238
Cdd:TIGR01188 152 TTGLDPRTRRAIWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRII 203
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
18-260 |
7.00e-45 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 151.94 E-value: 7.00e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 18 HLEQASVEFrhvDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPtgrLSGSGLRQ 97
Cdd:COG4525 5 TVRHVSVRY---PGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVP---VTGPGADR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 98 lrsrvGFVFQQFNLYAHLTASQNITLALEhvhgWKPLPAQER---ALALLEKVGMLEKAHHYPAELSGGQQQRVAIARAL 174
Cdd:COG4525 79 -----GVVFQKDALLPWLNVLDNVAFGLR----LRGVPKAERrarAEELLALVGLADFARRRIWQLSGGMRQRVGIARAL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 175 ASSPQIILFDEPTSALDP---EMIGEVLFVMKALAHSGITMIvvTHEMQFAREIADRIVFIDG--GHILETAPPaqffsq 249
Cdd:COG4525 150 AADPRFLLMDEPFGALDAltrEQMQELLLDVWQRTGKGVFLI--THSVEEALFLATRLVVMSPgpGRIVERLEL------ 221
|
250
....*....|.
gi 544825118 250 pahPRAQRFLQ 260
Cdd:COG4525 222 ---DFSRRFLA 229
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
24-264 |
9.63e-45 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 151.84 E-value: 9.63e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 24 VEFRHVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLI-NQLEPLSgGEILVDNKPTGRLSGSGLRQLRSRV 102
Cdd:PRK11831 8 VDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIgGQIAPDH-GEILFDGENIPAMSRSRLYTVRKRM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 103 GFVFQQFNLYAHLTASQNITLAL-EHVHGWKPLpAQERALALLEKVGMLEKAHHYPAELSGGQQQRVAIARALASSPQII 181
Cdd:PRK11831 87 SMLFQSGALFTDMNVFDNVAYPLrEHTQLPAPL-LHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 182 LFDEPTSALDPEMIGEVLFVMKALAHS-GITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQFFSQPaHPRAQRFLQ 260
Cdd:PRK11831 166 MFDEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANP-DPRVRQFLD 244
|
....
gi 544825118 261 KVLD 264
Cdd:PRK11831 245 GIAD 248
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
25-251 |
1.05e-44 |
|
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: 150.90 E-value: 1.05e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 25 EFRHVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSGSglRQLRSRVGF 104
Cdd:COG0410 5 EVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPH--RIARLGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 105 VFQQFNLYAHLTASQNITLALEHVHGWKPLPAQ-ERALAL---LEkvgmlEKAHHYPAELSGGQQQRVAIARALASSPQI 180
Cdd:COG0410 83 VPEGRRIFPSLTVEENLLLGAYARRDRAEVRADlERVYELfprLK-----ERRRQRAGTLSGGEQQMLAIGRALMSRPKL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 544825118 181 ILFDEPTSALDPEMIGEVLFVMKALAHSGITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQFFSQPA 251
Cdd:COG0410 158 LLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPE 228
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
24-251 |
1.49e-44 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 153.72 E-value: 1.49e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 24 VEFRHVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRlsgsglRQLRSR-V 102
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTH------RSIQQRdI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 103 GFVFQQFNLYAHLTASQNITLALEHVHgwkpLPAQER------ALALLEKVGMLEKahhYPAELSGGQQQRVAIARALAS 176
Cdd:PRK11432 81 CMVFQSYALFPHMSLGENVGYGLKMLG----VPKEERkqrvkeALELVDLAGFEDR---YVDQISGGQQQRVALARALIL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 544825118 177 SPQIILFDEPTSALDPEMIGEVLFVMKALAHS-GITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQFFSQPA 251
Cdd:PRK11432 154 KPKVLLFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPA 229
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
23-270 |
1.73e-44 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 153.73 E-value: 1.73e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 23 SVEFRHvdkRYGDHQVlnDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDnkptGRLSGSGLRQL---- 98
Cdd:TIGR02142 2 SARFSK---RLGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLN----GRTLFDSRKGIflpp 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 99 -RSRVGFVFQQFNLYAHLTASQNITLALEHVHGWKPLPAQERALALLEKVGMLEKahhYPAELSGGQQQRVAIARALASS 177
Cdd:TIGR02142 73 eKRRIGYVFQEARLFPHLSVRGNLRYGMKRARPSERRISFERVIELLGIGHLLGR---LPGRLSGGEKQRVAIGRALLSS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 178 PQIILFDEPTSALDPEMIGEVLFVMKAL-AHSGITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQFFSQPAHPRAQ 256
Cdd:TIGR02142 150 PRLLLMDEPLAALDDPRKYEILPYLERLhAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPWLA 229
|
250
....*....|....*....
gi 544825118 257 R-----FLQKVLDPLHQEH 270
Cdd:TIGR02142 230 RedqgsLIEGVVAEHDQHY 248
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
29-237 |
2.08e-44 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 150.60 E-value: 2.08e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 29 VDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPtgrlsgsgLRQLRSRVGFVFQQ 108
Cdd:PRK11247 18 VSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAP--------LAEAREDTRLMFQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 109 FNLYAHLTASQNITLALEHvhGWKPlpaqeRALALLEKVGMLEKAHHYPAELSGGQQQRVAIARALASSPQIILFDEPTS 188
Cdd:PRK11247 90 ARLLPWKKVIDNVGLGLKG--QWRD-----AALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLG 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 544825118 189 ALDP----EMIGevLFVMKALAHsGITMIVVTHEMQFAREIADRIVFIDGGHI 237
Cdd:PRK11247 163 ALDAltriEMQD--LIESLWQQH-GFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
24-245 |
4.10e-44 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 155.96 E-value: 4.10e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 24 VEFRHVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTgRLSGSglRQ-LRSRV 102
Cdd:COG3845 6 LELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPV-RIRSP--RDaIALGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 103 GFVFQQFNLYAHLTASQNITLALEHVHGWKPLPAQERA--LALLEKVGMLEKAHHYPAELSGGQQQRVAIARALASSPQI 180
Cdd:COG3845 83 GMVHQHFMLVPNLTVAENIVLGLEPTKGGRLDRKAARAriRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARI 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 544825118 181 ILFDEPTSALDPEMIGEVLFVMKALAHSGITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQ 245
Cdd:COG3845 163 LILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAE 227
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
27-251 |
4.16e-44 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 150.22 E-value: 4.16e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 27 RHVDKRYGDH---------QVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSGSGLRQ 97
Cdd:PRK10419 7 SGLSHHYAHGglsgkhqhqTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 98 LRSRVGFVFQQ----FNlyAHLTASQNITLALEHVHGWKPLPAQERALALLEKVGM-LEKAHHYPAELSGGQQQRVAIAR 172
Cdd:PRK10419 87 FRRDIQMVFQDsisaVN--PRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLdDSVLDKRPPQLSGGQLQRVCLAR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 173 ALASSPQIILFDEPTSALDPEMIGEVLFVMKALAH-SGITMIVVTHEMQFAREIADRIVFIDGGHILETAP--PAQFFSQ 249
Cdd:PRK10419 165 ALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQqFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPvgDKLTFSS 244
|
..
gi 544825118 250 PA 251
Cdd:PRK10419 245 PA 246
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
31-234 |
6.97e-44 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 148.81 E-value: 6.97e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 31 KRYGDHQ----VLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSGSGLRQLRSR-VGFV 105
Cdd:PRK11629 13 KRYQEGSvqtdVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRNQkLGFI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 106 FQQFNLYAHLTASQNITLALeHVHGWKPLPAQERALALLEKVGMLEKAHHYPAELSGGQQQRVAIARALASSPQIILFDE 185
Cdd:PRK11629 93 YQFHHLLPDFTALENVAMPL-LIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 544825118 186 PTSALDPEMIGEVLFVMKAL-AHSGITMIVVTHEMQFAREIADRIVFIDG 234
Cdd:PRK11629 172 PTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDLQLAKRMSRQLEMRDG 221
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
24-235 |
9.95e-44 |
|
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: 147.43 E-value: 9.95e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 24 VEFRHVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSgsglrqlRSRVG 103
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA-------RNRIG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 104 FVFQQFNLYAHLTAsQNITLALEHVHGWKPLPAQERALALLEKVGMLEKAHHYPAELSGGQQQRVAIARALASSPQIILF 183
Cdd:cd03269 74 YLPEERGLYPKMKV-IDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLIL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 544825118 184 DEPTSALDPEMIGEVLFVMKALAHSGITMIVVTHEMQFAREIADRIVFIDGG 235
Cdd:cd03269 153 DEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKG 204
|
|
| PhnT |
TIGR03258 |
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ... |
24-259 |
1.09e-43 |
|
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding component of an ABC transport system is found in Salmonella and Burkholderia lineages in the vicinity of enzymes for the breakdown of 2-aminoethylphosphonate.
Pssm-ID: 132302 [Multi-domain] Cd Length: 362 Bit Score: 151.69 E-value: 1.09e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 24 VEFRHVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSG--GEILVDNKPTGRLSgsglrQLRSR 101
Cdd:TIGR03258 6 IRIDHLRVAYGANTVLDDLSLEIEAGELLALIGKSGCGKTTLLRAIAGFVKAAGltGRIAIADRDLTHAP-----PHKRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 102 VGFVFQQFNLYAHLTASQNITLALEHVHGWKPLPAqERALALLEKVGMLEKAHHYPAELSGGQQQRVAIARALASSPQII 181
Cdd:TIGR03258 81 LALLFQNYALFPHLKVEDNVAFGLRAQKMPKADIA-ERVADALKLVGLGDAAAHLPAQLSGGMQQRIAIARAIAIEPDVL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 182 LFDEPTSALDPEMIGEVLFVMKALAHS--GITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQFFSQPAHPRAQRFL 259
Cdd:TIGR03258 160 LLDEPLSALDANIRANMREEIAALHEElpELTILCVTHDQDDALTLADKAGIMKDGRLAAHGEPQALYDAPADGFAAEFL 239
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
24-259 |
1.52e-43 |
|
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: 147.87 E-value: 1.52e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 24 VEFRHVDKRYGDHQvLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTgrlsgSGLRQLRSRVG 103
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDI-----TNLPPEKRDIS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 104 FVFQQFNLYAHLTASQNITLALEHVHGWKPlPAQERALALLEKVGMLEKAHHYPAELSGGQQQRVAIARALASSPQIILF 183
Cdd:cd03299 75 YVPQNYALFPHMTVYKNIAYGLKKRKVDKK-EIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 544825118 184 DEPTSALDPEmIGEVLFVMKALAH--SGITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQFFSQPAHPRAQRFL 259
Cdd:cd03299 154 DEPFSALDVR-TKEKLREELKKIRkeFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFL 230
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
27-245 |
1.64e-43 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 148.34 E-value: 1.64e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 27 RHVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSGSGLRQLR------S 100
Cdd:COG4559 5 ENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRavlpqhS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 101 RVGFVFqqfnlyahlTASQNITLALeHVHGWKPLPAQERALALLEKVGMLEKAH-HYPaELSGGQQQRVAIARALA---- 175
Cdd:COG4559 85 SLAFPF---------TVEEVVALGR-APHGSSAAQDRQIVREALALVGLAHLAGrSYQ-TLSGGEQQRVQLARVLAqlwe 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 544825118 176 ---SSPQIILFDEPTSALDpemIGEVLFVM---KALAHSGITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQ 245
Cdd:COG4559 154 pvdGGPRWLFLDEPTSALD---LAHQHAVLrlaRQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEE 226
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
28-238 |
1.69e-43 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 146.95 E-value: 1.69e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 28 HVDKRYGDHQVLNDINLTITPGeVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRlsgsGLRQLRSRVGFVFQ 107
Cdd:cd03264 5 NLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK----QPQKLRRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 108 QFNLYAHLTASQnitlALEHV---HGWKPLPAQERALALLEKVGMLEKAHHYPAELSGGQQQRVAIARALASSPQIILFD 184
Cdd:cd03264 80 EFGVYPNFTVRE----FLDYIawlKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 544825118 185 EPTSALDPEMIGEVLFVMKALAhSGITMIVVTHEMQFAREIADRIVFIDGGHIL 238
Cdd:cd03264 156 EPTAGLDPEERIRFRNLLSELG-EDRIVILSTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
41-237 |
3.11e-43 |
|
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: 146.10 E-value: 3.11e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 41 DINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSGSglrqlRSRVGFVFQQFNLYAHLTASQN 120
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA-----DRPVSMLFQENNLFAHLTVEQN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 121 ITLALehVHGWKPLPAQERAL-ALLEKVGMLEKAHHYPAELSGGQQQRVAIARALASSPQIILFDEPTSALDPEMIGEVL 199
Cdd:cd03298 91 VGLGL--SPGLKLTAEDRQAIeVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEML 168
|
170 180 190
....*....|....*....|....*....|....*....
gi 544825118 200 -FVMKALAHSGITMIVVTHEMQFAREIADRIVFIDGGHI 237
Cdd:cd03298 169 dLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
54-259 |
8.30e-43 |
|
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: 148.41 E-value: 8.30e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 54 ILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSGsglrQLRSrVGFVFQQFNLYAHLTASQNITLALEHvhgwKP 133
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPP----HLRH-INMVFQSYALFPHMTVEENVAFGLKM----RK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 134 LPAQE---RALALLEKVGMLEKAHHYPAELSGGQQQRVAIARALASSPQIILFDEPTSALDPEMIGEVLFVMKALAHS-G 209
Cdd:TIGR01187 72 VPRAEikpRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQlG 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 544825118 210 ITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQFFSQPAHPRAQRFL 259
Cdd:TIGR01187 152 ITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFI 201
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
24-235 |
1.00e-42 |
|
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: 145.34 E-value: 1.00e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 24 VEFRHVDKRYGD--HQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDnkptGRLSGSGLRQLRSR 101
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYIN----GYSIRTDRKAARQS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 102 VGFVFQQFNLYAHLTASQNITL-ALehVHGWKPLPAQERALALLEKVGMLEKAHHYPAELSGGQQQRVAIARALASSPQI 180
Cdd:cd03263 77 LGYCPQFDALFDELTVREHLRFyAR--LKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 544825118 181 ILFDEPTSALDPEMIGEVLFVMKALAhSGITMIVVTHEMQFAREIADRIVFIDGG 235
Cdd:cd03263 155 LLLDEPTSGLDPASRRAIWDLILEVR-KGRSIILTTHSMDEAEALCDRIAIMSDG 208
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
24-234 |
1.30e-42 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 145.31 E-value: 1.30e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 24 VEFRHVDKRYG--DHQ--VLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSGSGLRQLR 99
Cdd:PRK10584 7 VEVHHLKKSVGqgEHElsILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 100 SR-VGFVFQQFNLYAHLTASQNITL-ALehVHGWKPLPAQERALALLEKVGMLEKAHHYPAELSGGQQQRVAIARALASS 177
Cdd:PRK10584 87 AKhVGFVFQSFMLIPTLNALENVELpAL--LRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGR 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 178 PQIILFDEPTSALDP---EMIGEVLFVMKalAHSGITMIVVTHEMQFAREIADRIVFIDG 234
Cdd:PRK10584 165 PDVLFADEPTGNLDRqtgDKIADLLFSLN--REHGTTLILVTHDLQLAARCDRRLRLVNG 222
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
24-237 |
1.66e-42 |
|
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: 144.82 E-value: 1.66e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 24 VEFRHVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSgsglRQLRSRVG 103
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREP----REVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 104 FVFQQFNLYAHLTASQNITLaLEHVHGWKPLPAQERALALLEKVGMLEKAHHYPAELSGGQQQRVAIARALASSPQIILF 183
Cdd:cd03265 77 IVFQDLSVDDELTGWENLYI-HARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 544825118 184 DEPTSALDPEMIGEVLFVMKAL-AHSGITMIVVTHEMQFAREIADRIVFIDGGHI 237
Cdd:cd03265 156 DEPTIGLDPQTRAHVWEYIEKLkEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRI 210
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
26-262 |
1.72e-42 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 149.41 E-value: 1.72e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 26 FRHVDKRYGDHQVLN---------DINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSGSGLR 96
Cdd:PRK10070 22 FKYIEQGLSKEQILEktglslgvkDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 97 QLR-SRVGFVFQQFNLYAHLTASQNITLALEhVHGWKPLPAQERALALLEKVGMLEKAHHYPAELSGGQQQRVAIARALA 175
Cdd:PRK10070 102 EVRrKKIAMVFQSFALMPHMTVLDNTAFGME-LAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 176 SSPQIILFDEPTSALDP----EMIGEVLfvmKALAHSGITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQFFSQPA 251
Cdd:PRK10070 181 INPDILLMDEAFSALDPlirtEMQDELV---KLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPA 257
|
250
....*....|.
gi 544825118 252 HPRAQRFLQKV 262
Cdd:PRK10070 258 NDYVRTFFRGV 268
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
43-251 |
7.16e-42 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 143.18 E-value: 7.16e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 43 NLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSGSglrqlRSRVGFVFQQFNLYAHLTASQNIT 122
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS-----RRPVSMLFQENNLFSHLTVAQNIG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 123 LALEHvhGWKPLPAQERAL-ALLEKVGMLEKAHHYPAELSGGQQQRVAIARALASSPQIILFDEPTSALDPEMIGEVLFV 201
Cdd:PRK10771 94 LGLNP--GLKLNAAQREKLhAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 544825118 202 MKALAHS-GITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQFFSQPA 251
Cdd:PRK10771 172 VSQVCQErQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLSGKA 222
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
24-262 |
1.15e-41 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 146.90 E-value: 1.15e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 24 VEFRHVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDnkptgrlsGSGLRQL---RS 100
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLD--------GVDLSHVppyQR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 101 RVGFVFQQFNLYAHLTASQNITLALEHvhgwKPLPAQE---RALALLEKVGMLEKAHHYPAELSGGQQQRVAIARALASS 177
Cdd:PRK11607 92 PINMMFQSYALFPHMTVEQNIAFGLKQ----DKLPKAEiasRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 178 PQIILFDEPTSALDPEMIGEV-LFVMKALAHSGITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQFFSQPAHPRAQ 256
Cdd:PRK11607 168 PKLLLLDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSA 247
|
....*.
gi 544825118 257 RFLQKV 262
Cdd:PRK11607 248 EFIGSV 253
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
23-263 |
1.24e-41 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 143.44 E-value: 1.24e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 23 SVEFRHVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSG-----GEIlvdnkptgRLSGSGLR- 96
Cdd:PRK14267 4 AIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEearveGEV--------RLFGRNIYs 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 97 ------QLRSRVGFVFQQFNLYAHLTASQNITLALEH---VHGWKPLPaqERALALLEKVGMLE----KAHHYPAELSGG 163
Cdd:PRK14267 76 pdvdpiEVRREVGMVFQYPNPFPHLTIYDNVAIGVKLnglVKSKKELD--ERVEWALKKAALWDevkdRLNDYPSNLSGG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 164 QQQRVAIARALASSPQIILFDEPTSALDP---EMIGEVLFVMKalahSGITMIVVTHEMQFAREIADRIVFIDGGHILET 240
Cdd:PRK14267 154 QRQRLVIARALAMKPKILLMDEPTANIDPvgtAKIEELLFELK----KEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEV 229
|
250 260
....*....|....*....|...
gi 544825118 241 APPAQFFSQPAHPRAQRFLQKVL 263
Cdd:PRK14267 230 GPTRKVFENPEHELTEKYVTGAL 252
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
24-252 |
1.36e-41 |
|
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: 142.68 E-value: 1.36e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 24 VEFRHVDKRY---GDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSgsgLRQLRS 100
Cdd:cd03249 1 IEFKNVSFRYpsrPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLN---LRWLRS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 101 RVGFVFQQFNLYAhLTASQNITLALEHVHgwkpLPAQERA--LALLEKVGM-LEKAHH-----YPAELSGGQQQRVAIAR 172
Cdd:cd03249 78 QIGLVSQEPVLFD-GTIAENIRYGKPDAT----DEEVEEAakKANIHDFIMsLPDGYDtlvgeRGSQLSGGQKQRIAIAR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 173 ALASSPQIILFDEPTSALDPEMIGEvlfVMKAL--AHSGITMIVVTHEMQFAREiADRIVFIDGGHILETAPPAQFFSQP 250
Cdd:cd03249 153 ALLRNPKILLLDEATSALDAESEKL---VQEALdrAMKGRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGTHDELMAQK 228
|
..
gi 544825118 251 AH 252
Cdd:cd03249 229 GV 230
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
25-260 |
1.64e-41 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 143.44 E-value: 1.64e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 25 EFRHVDKRYGDH---------QVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPtgrLSgSGL 95
Cdd:COG4167 6 EVRNLSKTFKYRtglfrrqqfEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHK---LE-YGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 96 RQLRSR-VGFVFQQFN--LYAHLTASQNITLALEHVHGWKPLPAQERALALLEKVGML-EKAHHYPAELSGGQQQRVAIA 171
Cdd:COG4167 82 YKYRCKhIRMIFQDPNtsLNPRLNIGQILEEPLRLNTDLTAEEREERIFATLRLVGLLpEHANFYPHMLSSGQKQRVALA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 172 RALASSPQIILFDEPTSALDPEMIGEVLFVMKAL-AHSGITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQFFSQP 250
Cdd:COG4167 162 RALILQPKIIIADEALAALDMSVRSQIINLMLELqEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAEVFANP 241
|
250
....*....|
gi 544825118 251 AHPRAQRFLQ 260
Cdd:COG4167 242 QHEVTKRLIE 251
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
24-249 |
4.22e-41 |
|
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: 141.21 E-value: 4.22e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 24 VEFRHVDKRY-GDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSgsgLRQLRSRV 102
Cdd:cd03254 3 IEFENVNFSYdEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDIS---RKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 103 GFVFQQFNLYAHlTASQNITLAlehvhgwKPLPAQERALALLEKVGM------LEKA-HHYPAE----LSGGQQQRVAIA 171
Cdd:cd03254 80 GVVLQDTFLFSG-TIMENIRLG-------RPNATDEEVIEAAKEAGAhdfimkLPNGyDTVLGEnggnLSQGERQLLAIA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 172 RALASSPQIILFDEPTSALDPEMigEVLfVMKALAH--SGITMIVVTHEMQFAREiADRIVFIDGGHILETAPPAQFFSQ 249
Cdd:cd03254 152 RAMLRDPKILILDEATSNIDTET--EKL-IQEALEKlmKGRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDELLAK 227
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
37-259 |
7.37e-41 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 143.57 E-value: 7.37e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 37 QVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSGSGLRQLRSRVGFVFQqfNLYAHLT 116
Cdd:PRK11308 29 KALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLLRQKIQIVFQ--NPYGSLN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 117 ASQNITLALEhvhgwKPL------PAQER---ALALLEKVGML-EKAHHYPAELSGGQQQRVAIARALASSPQIILFDEP 186
Cdd:PRK11308 107 PRKKVGQILE-----EPLlintslSAAERrekALAMMAKVGLRpEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEP 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 544825118 187 TSALDPEMIGEVLFVMKALAHS-GITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQFFSQPAHPRAQRFL 259
Cdd:PRK11308 182 VSALDVSVQAQVLNLMMDLQQElGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPRHPYTQALL 255
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
24-250 |
7.91e-41 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 142.14 E-value: 7.91e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 24 VEFRHVDKRYGD-HQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQ-LEPLSGgEILVDNKPTgRLSGSGLRQLRSR 101
Cdd:PRK13639 2 LETRDLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGiLKPTSG-EVLIKGEPI-KYDKKSLLEVRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 102 VGFVFQQFN--LYAHlTASQ-------NITLALEHVhgwkplpaQERALALLEKVGMLEKAHHYPAELSGGQQQRVAIAR 172
Cdd:PRK13639 80 VGIVFQNPDdqLFAP-TVEEdvafgplNLGLSKEEV--------EKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 544825118 173 ALASSPQIILFDEPTSALDPEMIGEVLFVMKALAHSGITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQFFSQP 250
Cdd:PRK13639 151 ILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDI 228
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
27-245 |
9.50e-41 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 141.06 E-value: 9.50e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 27 RHVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSGsglRQLRSRVGFVF 106
Cdd:PRK13548 6 RNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSP---AELARRRAVLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 107 QQFNLYAHLTASQNITLALehvHGWKPLPAQERAL--ALLEKVGMLEKAHHYPAELSGGQQQRVAIARALA------SSP 178
Cdd:PRK13548 83 QHSSLSFPFTVEEVVAMGR---APHGLSRAEDDALvaAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 544825118 179 QIILFDEPTSALDPEMIGEVLFVMKALAHS-GITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQ 245
Cdd:PRK13548 160 RWLLLDEPTSALDLAHQHHVLRLARQLAHErGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAE 227
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
23-237 |
9.56e-41 |
|
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: 140.03 E-value: 9.56e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 23 SVEFRHVDKRYGDHQ--VLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSGSGLRQlrs 100
Cdd:cd03245 2 RIEFRNVSFSYPNQEipALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRR--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 101 RVGFVFQQFNLYAHlTASQNITLAlehvhgwKPLPAQERALALLEKVGMLEKAHHYP-----------AELSGGQQQRVA 169
Cdd:cd03245 79 NIGYVPQDVTLFYG-TLRDNITLG-------APLADDERILRAAELAGVTDFVNKHPngldlqigergRGLSGGQRQAVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 170 IARALASSPQIILFDEPTSALDpeMIGEVLFV--MKALAhSGITMIVVTHEMQFArEIADRIVFIDGGHI 237
Cdd:cd03245 151 LARALLNDPPILLLDEPTSAMD--MNSEERLKerLRQLL-GDKTLIIITHRPSLL-DLVDRIIVMDSGRI 216
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
24-250 |
1.01e-40 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 141.86 E-value: 1.01e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 24 VEFRHVDKRYGDHQ--VLNDINLTITPGEVVAILGPSGSGKSTLIRLINqleplsgGEILVDNKPTGRLSGSGLR----- 96
Cdd:PRK13640 6 VEFKHVSFTYPDSKkpALNDISFSIPRGSWTALIGHNGSGKSTISKLIN-------GLLLPDDNPNSKITVDGITltakt 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 97 --QLRSRVGFVFQQ-FNLYAHLTASQNITLALEHvhgwKPLPAQER---ALALLEKVGMLEKAHHYPAELSGGQQQRVAI 170
Cdd:PRK13640 79 vwDIREKVGIVFQNpDNQFVGATVGDDVAFGLEN----RAVPRPEMikiVRDVLADVGMLDYIDSEPANLSGGQKQRVAI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 171 ARALASSPQIILFDEPTSALDPEMIGEVLFVMKALAH-SGITMIVVTHEMQFArEIADRIVFIDGGHILETAPPAQFFSQ 249
Cdd:PRK13640 155 AGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKkNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSK 233
|
.
gi 544825118 250 P 250
Cdd:PRK13640 234 V 234
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
15-217 |
3.22e-40 |
|
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: 138.07 E-value: 3.22e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 15 DFSHLEQASVEFRHVDKRygdhQVLNDINLTITPGEVVAILGPSGSGKSTLIR-LINQLEPLS-GGEILVDNKPtgrlsg 92
Cdd:cd03213 5 SFRNLTVTVKSSPSKSGK----QLLKNVSGKAKPGELTAIMGPSGAGKSTLLNaLAGRRTGLGvSGEVLINGRP------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 93 SGLRQLRSRVGFVFQQFNLYAHLTASQNITLAlehvhgwkplpaqeralALLEKvgmlekahhypaeLSGGQQQRVAIAR 172
Cdd:cd03213 75 LDKRSFRKIIGYVPQDDILHPTLTVRETLMFA-----------------AKLRG-------------LSGGERKRVSIAL 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 544825118 173 ALASSPQIILFDEPTSALDPEMIGEVLFVMKALAHSGITMIVVTH 217
Cdd:cd03213 125 ELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIH 169
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
23-262 |
5.33e-40 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 140.35 E-value: 5.33e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 23 SVEFRHVDKRYG-----DHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEI-LVDNKPTGRLSGSGLR 96
Cdd:PRK13641 2 SIKFENVDYIYSpgtpmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTItIAGYHITPETGNKNLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 97 QLRSRVGFVFQ--QFNLYAHlTASQNITLALEHVhGWKPLPAQERALALLEKVGMLEK-AHHYPAELSGGQQQRVAIARA 173
Cdd:PRK13641 82 KLRKKVSLVFQfpEAQLFEN-TVLKDVEFGPKNF-GFSEDEAKEKALKWLKKVGLSEDlISKSPFELSGGQMRRVAIAGV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 174 LASSPQIILFDEPTSALDPEMIGEVLFVMKALAHSGITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQFFSQP--- 250
Cdd:PRK13641 160 MAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKewl 239
|
250
....*....|....*..
gi 544825118 251 -----AHPRAQRFLQKV 262
Cdd:PRK13641 240 kkhylDEPATSRFASKL 256
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
24-245 |
5.36e-40 |
|
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: 138.52 E-value: 5.36e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 24 VEFRHVDKRYGDH-QVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPtgrLSGSGLRQLRSRV 102
Cdd:cd03253 1 IEFENVTFAYDPGrPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQD---IREVTLDSLRRAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 103 GFVFQQ---FN-------LYAHLTAS--QNITLA-LEHVHgwkplpaqERALALLE----KVGmlEKAhhypAELSGGQQ 165
Cdd:cd03253 78 GVVPQDtvlFNdtigyniRYGRPDATdeEVIEAAkAAQIH--------DKIMRFPDgydtIVG--ERG----LKLSGGEK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 166 QRVAIARALASSPQIILFDEPTSALDPEMIGEVLFVMKALAhSGITMIVVTHEMqfaREI--ADRIVFIDGGHILETAPP 243
Cdd:cd03253 144 QRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVS-KGRTTIVIAHRL---STIvnADKIIVLKDGRIVERGTH 219
|
..
gi 544825118 244 AQ 245
Cdd:cd03253 220 EE 221
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
24-239 |
7.23e-40 |
|
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: 138.39 E-value: 7.23e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 24 VEFRHVDKRYG--DHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPtgrLSGSGLRQLRSR 101
Cdd:cd03252 1 ITFEHVRFRYKpdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHD---LALADPAWLRRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 102 VGFVFQQfNLYAHLTASQNITLAlehvhgwKPLPAQERalalLEKVGMLEKAHHYPAE---------------LSGGQQQ 166
Cdd:cd03252 78 VGVVLQE-NVLFNRSIRDNIALA-------DPGMSMER----VIEAAKLAGAHDFISElpegydtivgeqgagLSGGQRQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 544825118 167 RVAIARALASSPQIILFDEPTSALDPEMIGEVLFVMKALAhSGITMIVVTHEMQFAREiADRIVFIDGGHILE 239
Cdd:cd03252 146 RIAIARALIHNPRILIFDEATSALDYESEHAIMRNMHDIC-AGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVE 216
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
30-237 |
1.05e-39 |
|
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: 137.30 E-value: 1.05e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 30 DKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKptgrlSGSGLRQLRSRVGFVFQQF 109
Cdd:TIGR01277 5 KVRYEYEHLPMEFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQ-----SHTGLAPYQRPVSMLFQEN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 110 NLYAHLTASQNITLALehvHGWKPLPA--QERALALLEKVGMLEKAHHYPAELSGGQQQRVAIARALASSPQIILFDEPT 187
Cdd:TIGR01277 80 NLFAHLTVRQNIGLGL---HPGLKLNAeqQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPF 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 544825118 188 SALDPEMIGEVLFVMKALA-HSGITMIVVTHEMQFAREIADRIVFIDGGHI 237
Cdd:TIGR01277 157 SALDPLLREEMLALVKQLCsERQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
21-249 |
1.05e-39 |
|
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: 146.16 E-value: 1.05e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 21 QASVEFRHVDKRYGDHQ--VLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDnkptgrlsGSGLRQ- 97
Cdd:TIGR03375 461 QGEIEFRNVSFAYPGQEtpALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLD--------GVDIRQi 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 98 ----LRSRVGFVFQQFNLYaHLTASQNITLAlehvhgwKPLPAQERALALLEKVGMLEKAHHYP-----------AELSG 162
Cdd:TIGR03375 533 dpadLRRNIGYVPQDPRLF-YGTLRDNIALG-------APYADDEEILRAAELAGVTEFVRRHPdgldmqigergRSLSG 604
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 163 GQQQRVAIARALASSPQIILFDEPTSALDpeMIGEVLFvMKALAH--SGITMIVVTHEMQFArEIADRIVFIDGGHILET 240
Cdd:TIGR03375 605 GQRQAVALARALLRDPPILLLDEPTSAMD--NRSEERF-KDRLKRwlAGKTLVLVTHRTSLL-DLVDRIIVMDNGRIVAD 680
|
....*....
gi 544825118 241 APPAQFFSQ 249
Cdd:TIGR03375 681 GPKDQVLEA 689
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
25-240 |
1.27e-39 |
|
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: 137.27 E-value: 1.27e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 25 EFRHVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSGSglRQLRSRVGF 104
Cdd:TIGR03410 2 EVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPH--ERARAGIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 105 VFQQFNLYAHLTASQNITLALEhvhgwkPLPAQERALA--LLEKVGMLEKAHHYPA-ELSGGQQQRVAIARALASSPQII 181
Cdd:TIGR03410 80 VPQGREIFPRLTVEENLLTGLA------ALPRRSRKIPdeIYELFPVLKEMLGRRGgDLSGGQQQQLAIARALVTRPKLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 182 LFDEPTSALDPEMIGEVLFVMKALAHS-GITMIVVTHEMQFAREIADRIVFIDGGHILET 240
Cdd:TIGR03410 154 LLDEPTEGIQPSIIKDIGRVIRRLRAEgGMAILLVEQYLDFARELADRYYVMERGRVVAS 213
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
22-251 |
1.96e-39 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 140.36 E-value: 1.96e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 22 ASVEFRHVDKRY-GDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSGsglrqlRS 100
Cdd:PRK11650 2 AGLKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEP------AD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 101 R-VGFVFQQFNLYAHLTASQNITLALEhVHGwkpLPAQER------ALALLEKVGMLEKAhhyPAELSGGQQQRVAIARA 173
Cdd:PRK11650 76 RdIAMVFQNYALYPHMSVRENMAYGLK-IRG---MPKAEIeervaeAARILELEPLLDRK---PRELSGGQRQRVAMGRA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 174 LASSPQIILFDEPTSALDP----EMIGEVLFVMKALahsGITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQFFSQ 249
Cdd:PRK11650 149 IVREPAVFLFDEPLSNLDAklrvQMRLEIQRLHRRL---KTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEK 225
|
..
gi 544825118 250 PA 251
Cdd:PRK11650 226 PA 227
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
32-234 |
7.09e-39 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 134.92 E-value: 7.09e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 32 RYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIR-LINQLEPL--SGGEILVDNKptgRLSGsgLRQLRSRVGFVFQQ 108
Cdd:COG4136 10 TLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAaIAGTLSPAfsASGEVLLNGR---RLTA--LPAEQRRIGILFQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 109 FNLYAHLTASQNITLALehVHGWKPLPAQERALALLEKVGMLEKAHHYPAELSGGQQQRVAIARALASSPQIILFDEPTS 188
Cdd:COG4136 85 DLLFPHLSVGENLAFAL--PPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFS 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 544825118 189 ALDPEMIGEVL-FVMKALAHSGITMIVVTHEMQFAREiADRIVFIDG 234
Cdd:COG4136 163 KLDAALRAQFReFVFEQIRQRGIPALLVTHDEEDAPA-AGRVLDLGN 208
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
24-249 |
7.61e-39 |
|
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: 135.44 E-value: 7.61e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 24 VEFRHVDKRYGDHQ--VLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPtgrLSGSGLRQLRSR 101
Cdd:cd03251 1 VEFKNVTFRYPGDGppVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHD---VRDYTLASLRRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 102 VGFVFQQFNLYaHLTASQNITLAlehvhgwKPLPAQERALALLEKVGMLEKAHHYP-----------AELSGGQQQRVAI 170
Cdd:cd03251 78 IGLVSQDVFLF-NDTVAENIAYG-------RPGATREEVEEAARAANAHEFIMELPegydtvigergVKLSGGQRQRIAI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 171 ARALASSPQIILFDEPTSALDPEmiGEVLfVMKALAH--SGITMIVVTHEMQFAREiADRIVFIDGGHILETAPPAQFFS 248
Cdd:cd03251 150 ARALLKDPPILILDEATSALDTE--SERL-VQAALERlmKNRTTFVIAHRLSTIEN-ADRIVVLEDGKIVERGTHEELLA 225
|
.
gi 544825118 249 Q 249
Cdd:cd03251 226 Q 226
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
24-237 |
1.61e-38 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 134.62 E-value: 1.61e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 24 VEFRHVDKRY-GDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSGSGLRQLRSRV 102
Cdd:PRK10908 2 IRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 103 GFVFQQFNLYAHLTASQNITLALEhVHGWKPLPAQERALALLEKVGMLEKAHHYPAELSGGQQQRVAIARALASSPQIIL 182
Cdd:PRK10908 82 GMIFQDHHLLMDRTVYDNVAIPLI-IAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 544825118 183 FDEPTSALDPEMIGEVLFVMKALAHSGITMIVVTHEMQFAREIADRIVFIDGGHI 237
Cdd:PRK10908 161 ADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
24-238 |
1.87e-38 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 134.03 E-value: 1.87e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 24 VEFRHVDKRYGD----HQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDnkptGRLSGSGLRQLR 99
Cdd:cd03266 2 ITADALTKRFRDvkktVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVD----GFDVVKEPAEAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 100 SRVGFVFQQFNLYAHLTASQNItLALEHVHGWKPLPAQERALALLEKVGMLEKAHHYPAELSGGQQQRVAIARALASSPQ 179
Cdd:cd03266 78 RRLGFVSDSTGLYDRLTARENL-EYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 544825118 180 IILFDEPTSALDPEMIGEVLFVMKALAHSGITMIVVTHEMQFAREIADRIVFIDGGHIL 238
Cdd:cd03266 157 VLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVV 215
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
24-264 |
2.16e-38 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 135.63 E-value: 2.16e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 24 VEFRHVDKRYGDHQ---VLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKptgRLSGSGLRQLRS 100
Cdd:PRK13650 5 IEVKNLTFKYKEDQekyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGD---LLTEENVWDIRH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 101 RVGFVFQQ-FNLYAHLTASQNITLALEHvhgwKPLPAQE---RALALLEKVGMLEKAHHYPAELSGGQQQRVAIARALAS 176
Cdd:PRK13650 82 KIGMVFQNpDNQFVGATVEDDVAFGLEN----KGIPHEEmkeRVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 177 SPQIILFDEPTSALDPEMIGEVLFVMKALAHS-GITMIVVTHEMQfarEIA--DRIVFIDGGHILETAPPAQFFSqpahp 253
Cdd:PRK13650 158 RPKIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLD---EVAlsDRVLVMKNGQVESTSTPRELFS----- 229
|
250
....*....|.
gi 544825118 254 RAQRFLQKVLD 264
Cdd:PRK13650 230 RGNDLLQLGLD 240
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
27-251 |
2.49e-38 |
|
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: 134.21 E-value: 2.49e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 27 RHVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSGSGlrqlRSRVGFVF 106
Cdd:cd03218 4 ENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHK----RARLGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 107 --QQFNLYAHLTASQNITLALEhVHGWKPLPAQERALALLEKVGMLEKAHHYPAELSGGQQQRVAIARALASSPQIILFD 184
Cdd:cd03218 80 lpQEASIFRKLTVEENILAVLE-IRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 185 EPTSALDPEMIGEVLFVMKALAHSGITMIVVTHEmqfARE---IADRIVFIDGGHILETAPPAQFFSQPA 251
Cdd:cd03218 159 EPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHN---VREtlsITDRAYIIYEGKVLAEGTPEEIAANEL 225
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
34-260 |
6.06e-38 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 139.46 E-value: 6.06e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 34 GDHQVLNDINLTITPGEVVAILGPSGSGKST----LIRLINqleplSGGEILVDNKPTGRLSGSGLRQLRSRVGFVFQQF 109
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPLHNLNRRQLLPVRHRIQVVFQDP 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 110 N--LYAHLTASQNITLALEhVHgWKPLPAQER---ALALLEKVGM-LEKAHHYPAELSGGQQQRVAIARALASSPQIILF 183
Cdd:PRK15134 372 NssLNPRLNVLQIIEEGLR-VH-QPTLSAAQReqqVIAVMEEVGLdPETRHRYPAEFSGGQRQRIAIARALILKPSLIIL 449
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 544825118 184 DEPTSALDPEMIGEVLFVMKALAHS-GITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQFFSQPAHPRAQRFLQ 260
Cdd:PRK15134 450 DEPTSSLDKTVQAQILALLKSLQQKhQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEYTRQLLA 527
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
39-235 |
1.78e-37 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 131.82 E-value: 1.78e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 39 LNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRlsgSGLRQLrsrvgFVFQQFNLYAHLTAS 118
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITE---PGPDRM-----VVFQNYSLLPWLTVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 119 QNITLALEHVHGWKPLPAQERAL-ALLEKVGMLEKAHHYPAELSGGQQQRVAIARALASSPQIILFDEPTSALDPEMIGE 197
Cdd:TIGR01184 73 ENIALAVDRVLPDLSKSERRAIVeEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGN 152
|
170 180 190
....*....|....*....|....*....|....*....
gi 544825118 198 VL-FVMKALAHSGITMIVVTHEMQFAREIADRIVFIDGG 235
Cdd:TIGR01184 153 LQeELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
18-252 |
2.48e-37 |
|
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: 138.31 E-value: 2.48e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 18 HLEQAS--VEFRHVDKRYG--DHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSgs 93
Cdd:TIGR02203 323 AIERARgdVEFRNVTFRYPgrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYT-- 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 94 gLRQLRSRVGFVFQQFNLYAHlTASQNITL-ALEHVhgwkPLPAQERALA---LLEKVGMLEKAHHYP-----AELSGGQ 164
Cdd:TIGR02203 401 -LASLRRQVALVSQDVVLFND-TIANNIAYgRTEQA----DRAEIERALAaayAQDFVDKLPLGLDTPigengVLLSGGQ 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 165 QQRVAIARALASSPQIILFDEPTSALDPEmiGEVLfVMKALAH--SGITMIVVTHEMQfAREIADRIVFIDGGHILETAP 242
Cdd:TIGR02203 475 RQRLAIARALLKDAPILILDEATSALDNE--SERL-VQAALERlmQGRTTLVIAHRLS-TIEKADRIVVMDDGRIVERGT 550
|
250
....*....|
gi 544825118 243 PAQFFSQPAH 252
Cdd:TIGR02203 551 HNELLARNGL 560
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
25-237 |
2.52e-37 |
|
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: 129.64 E-value: 2.52e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 25 EFRHVDKRYGDHQ--VLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLsgsGLRQLRSRV 102
Cdd:cd03246 2 EVENVSFRYPGAEppVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQW---DPNELGDHV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 103 GFVFQQFNLYAHlTASQNItlalehvhgwkplpaqeralallekvgmlekahhypaeLSGGQQQRVAIARALASSPQIIL 182
Cdd:cd03246 79 GYLPQDDELFSG-SIAENI--------------------------------------LSGGQRQRLGLARALYGNPRILV 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 544825118 183 FDEPTSALDPE---MIGEVLFVMKAlahSGITMIVVTHEMQfAREIADRIVFIDGGHI 237
Cdd:cd03246 120 LDEPNSHLDVEgerALNQAIAALKA---AGATRIVIAHRPE-TLASADRILVLEDGRV 173
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
39-249 |
2.71e-37 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 133.25 E-value: 2.71e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 39 LNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDN-KPTGRlsGSGLRQLRSRVGFVFQ--QFNLYAHL 115
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvDITDK--KVKLSDIRKKVGLVFQypEYQLFEET 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 116 TAS------QNITLALEHVHgwkplpaqERALALLEKVG-----MLEKAhhyPAELSGGQQQRVAIARALASSPQIILFD 184
Cdd:PRK13637 101 IEKdiafgpINLGLSEEEIE--------NRVKRAMNIVGldyedYKDKS---PFELSGGQKRRVAIAGVVAMEPKILILD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 544825118 185 EPTSALDPEMIGEVLFVMKALaHS--GITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQFFSQ 249
Cdd:PRK13637 170 EPTAGLDPKGRDEILNKIKEL-HKeyNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKE 235
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
37-238 |
4.83e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 132.90 E-value: 4.83e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 37 QVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEIL------VDNKPTGRLSGSG---------------L 95
Cdd:PRK13651 21 KALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEwifkdeKNKKKTKEKEKVLeklviqktrfkkikkI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 96 RQLRSRVGFVFQ--QFNLYAHlTASQNITLALEHVhGWKPLPAQERALALLEKVGM----LEKAhhyPAELSGGQQQRVA 169
Cdd:PRK13651 101 KEIRRRVGVVFQfaEYQLFEQ-TIEKDIIFGPVSM-GVSKEEAKKRAAKYIELVGLdesyLQRS---PFELSGGQKRRVA 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 544825118 170 IARALASSPQIILFDEPTSALDPEMIGEVLFVMKALAHSGITMIVVTHEMQFAREIADRIVFIDGGHIL 238
Cdd:PRK13651 176 LAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKII 244
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
7-244 |
4.86e-37 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 133.80 E-value: 4.86e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 7 SHSAAGAADFSHLEQASVEFRHVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKP 86
Cdd:PRK13536 25 GISEAKASIPGSMSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 87 TGRLSgsglRQLRSRVGFVFQQFNLYAHLTASQNItLALEHVHGWKPLPAQERALALLEKVGMLEKAHHYPAELSGGQQQ 166
Cdd:PRK13536 105 VPARA----RLARARIGVVPQFDNLDLEFTVRENL-LVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKR 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 167 RVAIARALASSPQIILFDEPTSALDP---EMIGEVLfvmKALAHSGITMIVVTHEMQFAREIADRIVFIDGGH-ILETAP 242
Cdd:PRK13536 180 RLTLARALINDPQLLILDEPTTGLDPharHLIWERL---RSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRkIAEGRP 256
|
..
gi 544825118 243 PA 244
Cdd:PRK13536 257 HA 258
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
28-243 |
7.90e-37 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 130.98 E-value: 7.90e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 28 HVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPtgrLSGSGLRQlrsrvGFVFQ 107
Cdd:PRK11248 6 HLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKP---VEGPGAER-----GVVFQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 108 QFNLYAHLTASQNITLALEhVHGWKPLPAQERALALLEKVGMLEKAHHYPAELSGGQQQRVAIARALASSPQIILFDEPT 187
Cdd:PRK11248 78 NEGLLPWRNVQDNVAFGLQ-LAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPF 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 544825118 188 SALDP---EMIGEVLfvMKALAHSGITMIVVTHEMQFAREIADRIVFI--DGGHILETAPP 243
Cdd:PRK11248 157 GALDAftrEQMQTLL--LKLWQETGKQVLLITHDIEEAVFMATELVLLspGPGRVVERLPL 215
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
23-245 |
8.36e-37 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 137.78 E-value: 8.36e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 23 SVEFRHVDKRYGDH--QVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLE-PLSGGeILVDNKPtgrLSGSGLRQLR 99
Cdd:TIGR03797 451 AIEVDRVTFRYRPDgpLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFEtPESGS-VFYDGQD---LAGLDVQAVR 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 100 SRVGFVFQQFNLyahLTAS--QNITlalehvhGWKPLPaQERALALLEKVGMLE--KA-----HHYPAE----LSGGQQQ 166
Cdd:TIGR03797 527 RQLGVVLQNGRL---MSGSifENIA-------GGAPLT-LDEAWEAARMAGLAEdiRAmpmgmHTVISEgggtLSGGQRQ 595
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 544825118 167 RVAIARALASSPQIILFDEPTSALDPEMIGevlFVMKALAHSGITMIVVTHEMQFAREiADRIVFIDGGHILETAPPAQ 245
Cdd:TIGR03797 596 RLLIARALVRKPRILLFDEATSALDNRTQA---IVSESLERLKVTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQGTYDE 670
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
24-251 |
1.01e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 131.68 E-value: 1.01e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 24 VEFRHVDKRYG-----DHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQL-EPLSGGEILVDNKPTGRLSGSGLRQ 97
Cdd:PRK13634 3 ITFQKVEHRYQyktpfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLlQPTSGTVTIGERVITAGKKNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 98 LRSRVGFVFQ--QFNLYAHlTASQNITLALEHVhGWKPLPAQERALALLEKVGMLEKA-HHYPAELSGGQQQRVAIARAL 174
Cdd:PRK13634 83 LRKKVGIVFQfpEHQLFEE-TVEKDICFGPMNF-GVSEEDAKQKAREMIELVGLPEELlARSPFELSGGQMRRVAIAGVL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 544825118 175 ASSPQIILFDEPTSALDPEMIGEVLFVMKALAH-SGITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQFFSQPA 251
Cdd:PRK13634 161 AMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKeKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
18-237 |
1.15e-36 |
|
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: 129.90 E-value: 1.15e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 18 HLEqASVEFRHVDKRY---GDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPtgrLSGSG 94
Cdd:cd03248 7 HLK-GIVKFQNVTFAYptrPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKP---ISQYE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 95 LRQLRSRVGFVFQQFNLYAHlTASQNITLALEHVHGWKPLPAQERALA-----LLEKvGMLEKAHHYPAELSGGQQQRVA 169
Cdd:cd03248 83 HKYLHSKVSLVGQEPVLFAR-SLQDNIAYGLQSCSFECVKEAAQKAHAhsfisELAS-GYDTEVGEKGSQLSGGQKQRVA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 170 IARALASSPQIILFDEPTSALDPEmigEVLFVMKAL--AHSGITMIVVTHEMQFArEIADRIVFIDGGHI 237
Cdd:cd03248 161 IARALIRNPQVLILDEATSALDAE---SEQQVQQALydWPERRTVLVIAHRLSTV-ERADQILVLDGGRI 226
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
24-248 |
1.16e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 131.03 E-value: 1.16e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 24 VEFRHVDKRY-GDHQ-VLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPtgrLSGSGLRQLRSR 101
Cdd:PRK13648 8 IVFKNVSFQYqSDASfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQA---ITDDNFEKLRKH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 102 VGFVFQQ-FNLYAHLTASQNITLALEHvHGWKPLPAQERALALLEKVGMLEKAHHYPAELSGGQQQRVAIARALASSPQI 180
Cdd:PRK13648 85 IGIVFQNpDNQFVGSIVKYDVAFGLEN-HAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSV 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 544825118 181 ILFDEPTSALDPEMIGEVL-FVMKALAHSGITMIVVTHEMQFAREiADRIVFIDGGHILETAPPAQFFS 248
Cdd:PRK13648 164 IILDEATSMLDPDARQNLLdLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFD 231
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
18-262 |
1.90e-36 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 136.11 E-value: 1.90e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 18 HLEQASVEFRHVDKRYGD--HQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSGSGL 95
Cdd:PRK11160 333 AADQVSLTLNNVSFTYPDqpQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAAL 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 96 RQLRSrvgFVFQQFNLYAHlTASQNITLAlehvhgwKPLPAQERALALLEKVGM---LEKAHHYPA-------ELSGGQQ 165
Cdd:PRK11160 413 RQAIS---VVSQRVHLFSA-TLRDNLLLA-------APNASDEALIEVLQQVGLeklLEDDKGLNAwlgeggrQLSGGEQ 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 166 QRVAIARALASSPQIILFDEPTSALDPEMIGEVLFVMKALAhSGITMIVVTHEMQfAREIADRIVFIDGGHILETAPPAQ 245
Cdd:PRK11160 482 RRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHA-QNKTVLMITHRLT-GLEQFDRICVMDNGQIIEQGTHQE 559
|
250
....*....|....*..
gi 544825118 246 FFSQpaHPRAQRFLQKV 262
Cdd:PRK11160 560 LLAQ--QGRYYQLKQRL 574
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
24-265 |
2.58e-36 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 134.93 E-value: 2.58e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 24 VEFRHVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLI---RLINQLEPLSG------------GEILVDNKpTG 88
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMhvlRGMDQYEPTSGriiyhvalcekcGYVERPSK-VG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 89 R------------------LSGSGLRQLRSRVGFVFQQ-FNLYAHLTASQNITLALEHVhGWKPLPAQERALALLEKVGM 149
Cdd:TIGR03269 80 EpcpvcggtlepeevdfwnLSDKLRRRIRKRIAIMLQRtFALYGDDTVLDNVLEALEEI-GYEGKEAVGRAVDLIEMVQL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 150 LEKAHHYPAELSGGQQQRVAIARALASSPQIILFDEPTSALDPE---MIGEVLfvMKALAHSGITMIVVTHEMQFAREIA 226
Cdd:TIGR03269 159 SHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQtakLVHNAL--EEAVKASGISMVLTSHWPEVIEDLS 236
|
250 260 270
....*....|....*....|....*....|....*....
gi 544825118 227 DRIVFIDGGHILETAPPAQFFSqpahpraqRFLQKVLDP 265
Cdd:TIGR03269 237 DKAIWLENGEIKEEGTPDEVVA--------VFMEGVSEV 267
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
22-244 |
2.62e-36 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 131.08 E-value: 2.62e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 22 ASVEFRHVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIR-LINQLEPLSGGEILVDNKPTGRlsgsgLRQLRS 100
Cdd:PRK13537 6 APIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRmLLGLTHPDAGSISLCGEPVPSR-----ARHARQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 101 RVGFVFQQFNLYAHLTASQNItLALEHVHGWKPLPAQERALALLEKVGMLEKAHHYPAELSGGQQQRVAIARALASSPQI 180
Cdd:PRK13537 81 RVGVVPQFDNLDPDFTVRENL-LVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 544825118 181 ILFDEPTSALDPE---MIGEVLfvmKALAHSGITMIVVTHEMQFAREIADRIVFIDGGH-ILETAPPA 244
Cdd:PRK13537 160 LVLDEPTTGLDPQarhLMWERL---RSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRkIAEGAPHA 224
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
23-243 |
2.64e-36 |
|
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: 128.77 E-value: 2.64e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 23 SVEFRHVDKRYGDHQ--VLNDINLTITPGEVVAILGPSGSGKSTLI----RLInqlePLSGGEILVDNKPTGRLsgsGLR 96
Cdd:cd03244 2 DIEFKNVSLRYRPNLppVLKNISFSIKPGEKVGIVGRTGSGKSSLLlalfRLV----ELSSGSILIDGVDISKI---GLH 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 97 QLRSRVGFVFQ---------QFNLYAHLTAS-QNITLALEHVHGWKPLPAQERALALLEKVGmlekahhyPAELSGGQQQ 166
Cdd:cd03244 75 DLRSRISIIPQdpvlfsgtiRSNLDPFGEYSdEELWQALERVGLKEFVESLPGGLDTVVEEG--------GENLSVGQRQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 167 RVAIARALASSPQIILFDEPTSALDPE---MIGEVLfvMKALAHSgiTMIVVTHE----MQFareiaDRIVFIDGGHILE 239
Cdd:cd03244 147 LLCLARALLRKSKILVLDEATASVDPEtdaLIQKTI--REAFKDC--TVLTIAHRldtiIDS-----DRILVLDKGRVVE 217
|
....
gi 544825118 240 TAPP 243
Cdd:cd03244 218 FDSP 221
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
24-239 |
3.45e-36 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 134.81 E-value: 3.45e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 24 VEFRHVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLI-NQLEPLSgGEILVdnkptgrlsGSGLrqlrsRV 102
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLaGELEPDS-GTVKL---------GETV-----KI 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 103 GFVFQQfnlYAHLTASQNItlaLEHVHGWKPLPAQERALALLEKvgML---EKAHHYPAELSGGQQQRVAIARALASSPQ 179
Cdd:COG0488 381 GYFDQH---QEELDPDKTV---LDELRDGAPGGTEQEVRGYLGR--FLfsgDDAFKPVGVLSGGEKARLALAKLLLSPPN 452
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 544825118 180 IILFDEPTSALDPEMIgEVLfvMKALAH-SGiTMIVVTHEMQFAREIADRIVFIDGGHILE 239
Cdd:COG0488 453 VLLLDEPTNHLDIETL-EAL--EEALDDfPG-TVLLVSHDRYFLDRVATRILEFEDGGVRE 509
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
38-251 |
3.91e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 130.74 E-value: 3.91e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 38 VLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILV------DNKPTGRLSGSGL-------RQLRSRVGF 104
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigDKKNNHELITNPYskkiknfKELRRRVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 105 VFQ--QFNLYAHlTASQNIT---LALehvhGWKPLPAQERALALLEKVGM----LEKAhhyPAELSGGQQQRVAIARALA 175
Cdd:PRK13631 121 VFQfpEYQLFKD-TIEKDIMfgpVAL----GVKKSEAKKLAKFYLNKMGLddsyLERS---PFGLSGGQKRRVAIAGILA 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 544825118 176 SSPQIILFDEPTSALDPEMIGEVLFVMKALAHSGITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQFFSQPA 251
Cdd:PRK13631 193 IQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQH 268
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
32-230 |
4.21e-36 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 127.35 E-value: 4.21e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 32 RYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPlsggeilvdnkPTgrlSGSGLRQLRSRVGFVFQQFNL 111
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLR-----------PT---SGTVRRAGGARVAYVPQRSEV 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 112 YAHL--TASQNITLAL-EHVHGWKPLPAQERAL--ALLEKVGMLEKAHHYPAELSGGQQQRVAIARALASSPQIILFDEP 186
Cdd:NF040873 67 PDSLplTVRDLVAMGRwARRGLWRRLTRDDRAAvdDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEP 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 544825118 187 TSALDPEMIGEVLFVMKALAHSGITMIVVTHEMQFAREiADRIV 230
Cdd:NF040873 147 TTGLDAESRERIIALLAEEHARGATVVVVTHDLELVRR-ADPCV 189
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
34-222 |
8.18e-36 |
|
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: 126.38 E-value: 8.18e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 34 GDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGrLSGSGLRQLRSRVGFVFQQFN--L 111
Cdd:TIGR01166 3 GGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLD-YSRKGLLERRQRVGLVFQDPDdqL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 112 YAHlTASQNITLALEHVhGWKPLPAQERALALLEKVGMLEKAHHYPAELSGGQQQRVAIARALASSPQIILFDEPTSALD 191
Cdd:TIGR01166 82 FAA-DVDQDVAFGPLNL-GLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLD 159
|
170 180 190
....*....|....*....|....*....|.
gi 544825118 192 PEMIGEVLFVMKALAHSGITMIVVTHEMQFA 222
Cdd:TIGR01166 160 PAGREQMLAILRRLRAEGMTVVISTHDVDLA 190
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
24-245 |
2.25e-35 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 127.12 E-value: 2.25e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 24 VEFRHVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSG-------SGLR 96
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSrelakrlAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 97 Q---LRSR------VGFvfqqfNLYAHltaSQ-NITLA-LEHVhgwkplpaqERALALLEkvgMLEKAHHYPAELSGGQQ 165
Cdd:COG4604 82 QenhINSRltvrelVAF-----GRFPY---SKgRLTAEdREII---------DEAIAYLD---LEDLADRYLDELSGGQR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 166 QRVAIARALASSPQIILFDEPTSALDP----EMigevlfvMKALAH----SGITMIVVTHEMQFAREIADRIVFIDGGHI 237
Cdd:COG4604 142 QRAFIAMVLAQDTDYVLLDEPLNNLDMkhsvQM-------MKLLRRladeLGKTVVIVLHDINFASCYADHIVAMKDGRV 214
|
....*...
gi 544825118 238 LETAPPAQ 245
Cdd:COG4604 215 VAQGTPEE 222
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
35-259 |
4.42e-35 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 126.70 E-value: 4.42e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 35 DHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTgrLSGSGLRQ-----LRSRVGFVFQQF 109
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVL--YFGKDIFQidaikLRKEVGMVFQQP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 110 NLYAHLTASQNITLALEHvHGWKPLPAQERALA-LLEKVGMLEKAH---HYPA-ELSGGQQQRVAIARALASSPQIILFD 184
Cdd:PRK14246 100 NPFPHLSIYDNIAYPLKS-HGIKEKREIKKIVEeCLRKVGLWKEVYdrlNSPAsQLSGGQQQRLTIARALALKPKVLLMD 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 544825118 185 EPTSALDPEMIGEVLFVMKALAHSgITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQFFSQPAHPRAQRFL 259
Cdd:PRK14246 179 EPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKYV 252
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
27-258 |
6.27e-35 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 125.53 E-value: 6.27e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 27 RHVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSgsgLRQlRSR--VGF 104
Cdd:COG1137 7 ENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLP---MHK-RARlgIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 105 VFQQFNLYAHLTASQNITLALEHVhgwkPLPAQERAL---ALLEKVGMLEKAHHYPAELSGGQQQRVAIARALASSPQII 181
Cdd:COG1137 83 LPQEASIFRKLTVEDNILAVLELR----KLSKKEREErleELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 182 LFDEPTSALDPEMIGEVLFVMKALAHSGITmIVVT-HEmqfARE---IADRIVFIDGGHILETAPPAQFFsqpAHPRAQR 257
Cdd:COG1137 159 LLDEPFAGVDPIAVADIQKIIRHLKERGIG-VLITdHN---VREtlgICDRAYIISEGKVLAEGTPEEIL---NNPLVRK 231
|
.
gi 544825118 258 F 258
Cdd:COG1137 232 V 232
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
26-237 |
9.23e-35 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 130.57 E-value: 9.23e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 26 FRHVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNkptgrlsgsglrqlRSRVGFV 105
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK--------------GLRIGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 106 FQQFNLYAHLTASQNI----------------------------------TLALEHVHGWKplpAQERALALLEKVGMLE 151
Cdd:COG0488 67 PQEPPLDDDLTVLDTVldgdaelraleaeleeleaklaepdedlerlaelQEEFEALGGWE---AEARAEEILSGLGFPE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 152 KAHHYP-AELSGGQQQRVAIARALASSPQIILFDEPTSALDPEMIG--EvlfvmKALAHSGITMIVVTHEMQFAREIADR 228
Cdd:COG0488 144 EDLDRPvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEwlE-----EFLKNYPGTVLVVSHDRYFLDRVATR 218
|
....*....
gi 544825118 229 IVFIDGGHI 237
Cdd:COG0488 219 ILELDRGKL 227
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
36-268 |
1.16e-34 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 131.52 E-value: 1.16e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 36 HQVLNdINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSGSGLRQLRSRVGFVFQqfNLYAHL 115
Cdd:PRK10261 338 HAVEK-VSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRRDIQFIFQ--DPYASL 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 116 TASQNITLALEH---VHGWKP-LPAQERALALLEKVGML-EKAHHYPAELSGGQQQRVAIARALASSPQIILFDEPTSAL 190
Cdd:PRK10261 415 DPRQTVGDSIMEplrVHGLLPgKAAAARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSAL 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 191 DPEMIGEVLFVMKALAHS-GITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQFFSQPAHPRAQRFLQK--VLDPLH 267
Cdd:PRK10261 495 DVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLMAAvpVADPSR 574
|
.
gi 544825118 268 Q 268
Cdd:PRK10261 575 Q 575
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
24-249 |
2.58e-34 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 129.54 E-value: 2.58e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 24 VEFRHVDKRY-----GDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLI-NQLEPLSG------GEILVD-NKPTGRL 90
Cdd:TIGR03269 280 IKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIaGVLEPTSGevnvrvGDEWVDmTKPGPDG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 91 SGSGLRQLrsrvGFVFQQFNLYAHLTASQNITLA--LEhvhgwkpLP---AQERALALLEKVGMLEKA-----HHYPAEL 160
Cdd:TIGR03269 360 RGRAKRYI----GILHQEYDLYPHRTVLDNLTEAigLE-------LPdelARMKAVITLKMVGFDEEKaeeilDKYPDEL 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 161 SGGQQQRVAIARALASSPQIILFDEPTSALDP-EMIGEVLFVMKALAHSGITMIVVTHEMQFAREIADRIVFIDGGHILE 239
Cdd:TIGR03269 429 SEGERHRVALAQVLIKEPRIVILDEPTGTMDPiTKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVK 508
|
250
....*....|
gi 544825118 240 TAPPAQFFSQ 249
Cdd:TIGR03269 509 IGDPEEIVEE 518
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
19-249 |
2.93e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 124.96 E-value: 2.93e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 19 LEQASVEFRHVDKRYGD-HQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGrLSGSGLRQ 97
Cdd:PRK13636 1 MEDYILKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPID-YSRKGLMK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 98 LRSRVGFVFQQFNlYAHLTAS--QNITLALEHVHgwkpLP---AQERALALLEKVGMLEKAHHYPAELSGGQQQRVAIAR 172
Cdd:PRK13636 80 LRESVGMVFQDPD-NQLFSASvyQDVSFGAVNLK----LPedeVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 544825118 173 ALASSPQIILFDEPTSALDPEMIGEVLFVMKALAHS-GITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQFFSQ 249
Cdd:PRK13636 155 VLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAE 232
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
27-265 |
5.59e-34 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 123.50 E-value: 5.59e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 27 RHVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNK-----PTGRLSGSGLRQL-RS 100
Cdd:PRK11701 10 RGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrDLYALSEAERRRLlRT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 101 RVGFVFQ--QFNLYAHLTASQNITLALEHVhGWKPLPA-QERALALLEKVGM-LEKAHHYPAELSGGQQQRVAIARALAS 176
Cdd:PRK11701 90 EWGFVHQhpRDGLRMQVSAGGNIGERLMAV-GARHYGDiRATAGDWLERVEIdAARIDDLPTTFSGGMQQRLQIARNLVT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 177 SPQIILFDEPTSALDPEMIGEVLFVMKALAHS-GITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQFFSQPAHPRA 255
Cdd:PRK11701 169 HPRLVFMDEPTGGLDVSVQARLLDLLRGLVRElGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLTDQVLDDPQHPYT 248
|
250
....*....|
gi 544825118 256 QRFLQKVLDP 265
Cdd:PRK11701 249 QLLVSSVLQV 258
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
9-217 |
1.50e-33 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 127.48 E-value: 1.50e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 9 SAAGAADfSHLEQASVEFRHVDKRY-GDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPT 87
Cdd:TIGR02868 321 SAPAAGA-VGLGKPTLELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPV 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 88 GRLSGSglrQLRSRVGFVFQQfnlyAHL---TASQNITLAlehvhgwKPLPAQERALALLEKVGMLEKAHHYP------- 157
Cdd:TIGR02868 400 SSLDQD---EVRRRVSVCAQD----AHLfdtTVRENLRLA-------RPDATDEELWAALERVGLADWLRALPdgldtvl 465
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 544825118 158 ----AELSGGQQQRVAIARALASSPQIILFDEPTSALDPEMIGEVLFVMKAlAHSGITMIVVTH 217
Cdd:TIGR02868 466 geggARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLA-ALSGRTVVLITH 528
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
39-249 |
2.11e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 122.55 E-value: 2.11e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 39 LNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKP-TGRLSGSGLRQLRSRVGFVFQ--QFNLYAHl 115
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLiTSTSKNKDIKQIRKKVGLVFQfpESQLFEE- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 116 TASQNITLALEHVhGWKPLPAQERALALLEKVGMLEKA-HHYPAELSGGQQQRVAIARALASSPQIILFDEPTSALDPEM 194
Cdd:PRK13649 102 TVLKDVAFGPQNF-GVSQEEAEALAREKLALVGISESLfEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKG 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 544825118 195 IGEVLFVMKALAHSGITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQFFSQ 249
Cdd:PRK13649 181 RKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
25-237 |
2.68e-33 |
|
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: 120.97 E-value: 2.68e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 25 EFRHVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRlsgsglRQLRSrVGF 104
Cdd:TIGR03740 2 ETKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWTR------KDLHK-IGS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 105 VFQQFNLYAHLTASQNITLALEHVHgwkpLPAQeRALALLEKVGMLEKAHHYPAELSGGQQQRVAIARALASSPQIILFD 184
Cdd:TIGR03740 75 LIESPPLYENLTARENLKVHTTLLG----LPDS-RIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILD 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 544825118 185 EPTSALDPEMIGEVLFVMKALAHSGITMIVVTHEMQFAREIADRIVFIDGGHI 237
Cdd:TIGR03740 150 EPTNGLDPIGIQELRELIRSFPEQGITVILSSHILSEVQQLADHIGIISEGVL 202
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
24-250 |
2.73e-33 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 127.92 E-value: 2.73e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 24 VEFRHVDKRY---GDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPtgrLSGSGLRQLRS 100
Cdd:TIGR00958 479 IEFQDVSFSYpnrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVP---LVQYDHHYLHR 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 101 RVGFVFQQFNLYAHlTASQNITLALEHVHGWKPLPAQERALALLEKVGMLEKAHHYPAE----LSGGQQQRVAIARALAS 176
Cdd:TIGR00958 556 QVALVGQEPVLFSG-SVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEkgsqLSGGQKQRIAIARALVR 634
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 544825118 177 SPQIILFDEPTSALDPEMIGEVLFVMKAlahSGITMIVVTHEMQFAREiADRIVFIDGGHILETAPPAQFFSQP 250
Cdd:TIGR00958 635 KPRVLILDEATSALDAECEQLLQESRSR---ASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
33-264 |
2.75e-33 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 121.66 E-value: 2.75e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 33 YGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIR-LINQLEPLSgGEILVDNKPtgrLSGSGLRQLRSRVGFVFQQfnl 111
Cdd:PRK11231 12 YGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKcFARLLTPQS-GTVFLGDKP---ISMLSSRQLARRLALLPQH--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 112 yaHLTaSQNITLA-------LEHVHGWKPLPAQERALA--LLEKVGMLEKAHHYPAELSGGQQQRVAIARALASSPQIIL 182
Cdd:PRK11231 85 --HLT-PEGITVRelvaygrSPWLSLWGRLSAEDNARVnqAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 183 FDEPTSALDPEMIGEVLFVMKALAHSGITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQFFSqpahpraQRFLQKV 262
Cdd:PRK11231 162 LDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMT-------PGLLRTV 234
|
..
gi 544825118 263 LD 264
Cdd:PRK11231 235 FD 236
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
39-251 |
2.76e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 122.40 E-value: 2.76e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 39 LNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSGsgLRQLRSRVGFVFQ----QFnlyAH 114
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSK--LQGIRKLVGIVFQnpetQF---VG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 115 LTASQNITLALEHVhGWKPLPAQERALALLEKVGMLEKAHHYPAELSGGQQQRVAIARALASSPQIILFDEPTSALDPEM 194
Cdd:PRK13644 93 RTVEEDLAFGPENL-CLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDS 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 544825118 195 IGEVLFVMKALAHSGITMIVVTHEMQfAREIADRIVFIDGGHILETAPPAQFFSQPA 251
Cdd:PRK13644 172 GIAVLERIKKLHEKGKTIVYITHNLE-ELHDADRIIVMDRGKIVLEGEPENVLSDVS 227
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
10-239 |
3.13e-33 |
|
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: 127.24 E-value: 3.13e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 10 AAGAADFsHLEQASVEFRHVDKRY-GDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDnkptg 88
Cdd:COG5265 345 APDAPPL-VVGGGEVRFENVSFGYdPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILID----- 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 89 rlsGSGLRQ-----LRSRVGFVFQQ---FN-------LYAHLTASQN-----ITLAleHVHGW-KPLPAQ------ERAL 141
Cdd:COG5265 419 ---GQDIRDvtqasLRAAIGIVPQDtvlFNdtiayniAYGRPDASEEeveaaARAA--QIHDFiESLPDGydtrvgERGL 493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 142 allekvgmlekahhypaELSGGQQQRVAIARALASSPQIILFDEPTSALDPEMIGEVLFVMKALAHsGITMIVVTHEMQF 221
Cdd:COG5265 494 -----------------KLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVAR-GRTTLVIAHRLST 555
|
250
....*....|....*...
gi 544825118 222 AREiADRIVFIDGGHILE 239
Cdd:COG5265 556 IVD-ADEILVLEAGRIVE 572
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
33-259 |
3.67e-33 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 122.13 E-value: 3.67e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 33 YGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQL-EPLSG----GEILVDNKPTgrLSGSGLRQLRSRVGFVFQ 107
Cdd:PRK14271 31 FAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMnDKVSGyrysGDVLLGGRSI--FNYRDVLEFRRRVGMLFQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 108 QFNLYAhLTASQNItlaLEHVHGWKPLPAQE---RALALLEKVGMLE----KAHHYPAELSGGQQQRVAIARALASSPQI 180
Cdd:PRK14271 109 RPNPFP-MSIMDNV---LAGVRAHKLVPRKEfrgVAQARLTEVGLWDavkdRLSDSPFRLSGGQQQLLCLARTLAVNPEV 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 544825118 181 ILFDEPTSALDPEMIGEVLFVMKALAHSgITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQFFSQPAHPRAQRFL 259
Cdd:PRK14271 185 LLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETARYV 262
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
11-230 |
4.22e-33 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 126.25 E-value: 4.22e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 11 AGAADFSHLEQASVEFRHVDKRygdhQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRL 90
Cdd:TIGR02857 314 VTAAPASSLEFSGVSVAYPGRR----PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADA 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 91 SGSGLRQlrsRVGFVFQQFNLYAHlTASQNITLALEHVHGWKPLPAQERAlALLEKVGMLEKAHHYP-----AELSGGQQ 165
Cdd:TIGR02857 390 DADSWRD---QIAWVPQHPFLFAG-TIAENIRLARPDASDAEIREALERA-GLDEFVAALPQGLDTPigeggAGLSGGQA 464
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 544825118 166 QRVAIARALASSPQIILFDEPTSALDPEMIGEVLFVMKALAhSGITMIVVTHEMQFAREiADRIV 230
Cdd:TIGR02857 465 QRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALA-QGRTVLLVTHRLALAAL-ADRIV 527
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
40-253 |
4.83e-33 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 122.89 E-value: 4.83e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 40 NDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSGSGLRQLRSRVGFVFQqfNLYAHLTASQ 119
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVRSDIQMIFQ--DPLASLNPRM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 120 NI-TLALEHVHGWKP-LPAQE---RALALLEKVGMLEKA-HHYPAELSGGQQQRVAIARALASSPQIILFDEPTSALDPE 193
Cdd:PRK15079 116 TIgEIIAEPLRTYHPkLSRQEvkdRVKAMMLKVGLLPNLiNRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVS 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 544825118 194 MIGEVLFVMKAL-AHSGITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQFFSQPAHP 253
Cdd:PRK15079 196 IQAQVVNLLQQLqREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHP 256
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
19-248 |
9.71e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 120.97 E-value: 9.71e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 19 LEQASVEFRHvdKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKptgRLSGSGLRQL 98
Cdd:PRK13642 5 LEVENLVFKY--EKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGE---LLTAENVWNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 99 RSRVGFVFQQ-FNLYAHLTASQNITLALEHvhgwKPLPAQE---RALALLEKVGMLEKAHHYPAELSGGQQQRVAIARAL 174
Cdd:PRK13642 80 RRKIGMVFQNpDNQFVGATVEDDVAFGMEN----QGIPREEmikRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGII 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 544825118 175 ASSPQIILFDEPTSALDPEMIGEVLFVMKALAHS-GITMIVVTHEMQFAREiADRIVFIDGGHILETAPPAQFFS 248
Cdd:PRK13642 156 ALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKyQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFA 229
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
17-252 |
1.05e-32 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 120.66 E-value: 1.05e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 17 SHLEQASVEFR--HVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPL-----SGGEILVDNKptgR 89
Cdd:PRK14243 2 STLNGTETVLRteNLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLipgfrVEGKVTFHGK---N 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 90 LSGSGLR--QLRSRVGFVFQQFNLYAHlTASQNITLALEhVHGWKPLPAQ--ERAL---ALLEKVGmlEKAHHYPAELSG 162
Cdd:PRK14243 79 LYAPDVDpvEVRRRIGMVFQKPNPFPK-SIYDNIAYGAR-INGYKGDMDElvERSLrqaALWDEVK--DKLKQSGLSLSG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 163 GQQQRVAIARALASSPQIILFDEPTSALDPEMIGEVLFVMKALAHSgITMIVVTHEMQFAREIADRIVFIDG-------- 234
Cdd:PRK14243 155 GQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHNMQQAARVSDMTAFFNVeltegggr 233
|
250
....*....|....*....
gi 544825118 235 -GHILETAPPAQFFSQPAH 252
Cdd:PRK14243 234 yGYLVEFDRTEKIFNSPQQ 252
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
37-235 |
3.89e-32 |
|
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: 117.92 E-value: 3.89e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 37 QVLNDINLTITPGEVVAILGPSGSGKSTLIRLI--NQLEplSGGEILVDNKPTG-RLSGSGLRQL----RSRVGFVFQqf 109
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIygNYLP--DSGSILVRHDGGWvDLAQASPREIlalrRRTIGYVSQ-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 110 nlyaHLTASQNITlALEHV------HGWKPLPAQERALALLEKVGMLEKAHH-YPAELSGGQQQRVAIARALASSPQIIL 182
Cdd:COG4778 101 ----FLRVIPRVS-ALDVVaeplleRGVDREEARARARELLARLNLPERLWDlPPATFSGGEQQRVNIARGFIADPPLLL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 544825118 183 FDEPTSALDPEMIGEVLFVMKALAHSGITMIVVTHEMQFAREIADRIVFIDGG 235
Cdd:COG4778 176 LDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
23-249 |
4.39e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 119.50 E-value: 4.39e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 23 SVEFRHVDKRYG-----DHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDN-KPTGRLSGSGLR 96
Cdd:PRK13646 2 TIRFDNVSYTYQkgtpyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDiTITHKTKDKYIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 97 QLRSRVGFVFQ--QFNLYAH------LTASQNITLALEHVhgwkplpaQERALALLEKVG----MLEKAhhyPAELSGGQ 164
Cdd:PRK13646 82 PVRKRIGMVFQfpESQLFEDtvereiIFGPKNFKMNLDEV--------KNYAHRLLMDLGfsrdVMSQS---PFQMSGGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 165 QQRVAIARALASSPQIILFDEPTSALDPEMIGEVLFVMKALA-HSGITMIVVTHEMQFAREIADRIVFIDGGHILETAPP 243
Cdd:PRK13646 151 MRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSP 230
|
....*.
gi 544825118 244 AQFFSQ 249
Cdd:PRK13646 231 KELFKD 236
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
24-235 |
4.75e-32 |
|
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: 117.19 E-value: 4.75e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 24 VEFRHVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIR-LINQLEPLSGgeilvdnkptgrlsgsgLRQLRSRV 102
Cdd:cd03250 6 ASFTWDSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSaLLGELEKLSG-----------------SVSVPGSI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 103 GFVFQQ---FNLyahlTASQNITLALEHVHGW--KPLPA--QERALALLEK-----VGmlEKAhhypAELSGGQQQRVAI 170
Cdd:cd03250 69 AYVSQEpwiQNG----TIRENILFGKPFDEERyeKVIKAcaLEPDLEILPDgdlteIG--EKG----INLSGGQKQRISL 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 544825118 171 ARALASSPQIILFDEPTSALDPEmIGEVLF---VMKALAHSGiTMIVVTHEMQFAREiADRIVFIDGG 235
Cdd:cd03250 139 ARAVYSDADIYLLDDPLSAVDAH-VGRHIFencILGLLLNNK-TRILVTHQLQLLPH-ADQIVVLDNG 203
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
37-238 |
1.50e-31 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 116.22 E-value: 1.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 37 QVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQL---EPLSGGEILVDNKPTGRlsgsglRQLRSRVGFVFQQFNLYA 113
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRvegGGTTSGQILFNGQPRKP------DQFQKCVAYVRQDDILLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 114 HLTASQNITLALE---HVHGWKPLPAQERALALLEKVGMLEKAHHYPAELSGGQQQRVAIARALASSPQIILFDEPTSAL 190
Cdd:cd03234 95 GLTVRETLTYTAIlrlPRKSSDAIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 544825118 191 DPEMIGEVLFVMKALAHSGITMIVVTH----EMqFarEIADRIVFIDGGHIL 238
Cdd:cd03234 175 DSFTALNLVSTLSQLARRNRIVILTIHqprsDL-F--RLFDRILLLSSGEIV 223
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
32-255 |
1.57e-31 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 117.01 E-value: 1.57e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 32 RYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSGsglrQLRSRVGFV--FQQF 109
Cdd:PRK11300 14 RFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPG----HQIARMGVVrtFQHV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 110 NLYAHLTASQNITLAlEHVH-------GWKPLP--------AQERALALLEKVGMLEKAHHYPAELSGGQQQRVAIARAL 174
Cdd:PRK11300 90 RLFREMTVIENLLVA-QHQQlktglfsGLLKTPafrraeseALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCM 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 175 ASSPQIILFDEPTSALDPEMIGEVLFVMKALAHS-GITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQFFSQPAHP 253
Cdd:PRK11300 169 VTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNPDVI 248
|
..
gi 544825118 254 RA 255
Cdd:PRK11300 249 KA 250
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
21-249 |
1.60e-31 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 122.12 E-value: 1.60e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 21 QASVEFRHVDKRYG---DHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSGsglRQ 97
Cdd:TIGR02204 335 RGEIEFEQVNFAYParpDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDP---AE 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 98 LRSRVGFVFQQFNLYAHlTASQNITLALEHVHGWKPLPAQERALAlLEKVGMLEKAHHYP-----AELSGGQQQRVAIAR 172
Cdd:TIGR02204 412 LRARMALVPQDPVLFAA-SVMENIRYGRPDATDEEVEAAARAAHA-HEFISALPEGYDTYlgergVTLSGGQRQRIAIAR 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 544825118 173 ALASSPQIILFDEPTSALDPEmiGEVLfVMKALAH--SGITMIVVTHEMQFAREiADRIVFIDGGHILETAPPAQFFSQ 249
Cdd:TIGR02204 490 AILKDAPILLLDEATSALDAE--SEQL-VQQALETlmKGRTTLIIAHRLATVLK-ADRIVVMDQGRIVAQGTHAELIAK 564
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
33-259 |
1.85e-31 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 117.06 E-value: 1.85e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 33 YGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGgEILVDnkptGRLSGSG---------LRQLRSRVG 103
Cdd:PRK14258 17 YDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELES-EVRVE----GRVEFFNqniyerrvnLNRLRRQVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 104 FVFQQFNLYAhLTASQNITLALEHVhGWKP-------LPAQERALALLEKVGmlEKAHHYPAELSGGQQQRVAIARALAS 176
Cdd:PRK14258 92 MVHPKPNLFP-MSVYDNVAYGVKIV-GWRPkleiddiVESALKDADLWDEIK--HKIHKSALDLSGGQQQRLCIARALAV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 177 SPQIILFDEPTSALDPEMIGEVLFVMKALA-HSGITMIVVTHEMQFAREIADRIVFIDG-----GHILETAPPAQFFSQP 250
Cdd:PRK14258 168 KPKVLLMDEPCFGLDPIASMKVESLIQSLRlRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKKIFNSP 247
|
....*....
gi 544825118 251 AHPRAQRFL 259
Cdd:PRK14258 248 HDSRTREYV 256
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
24-238 |
1.91e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 117.53 E-value: 1.91e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 24 VEFRHVDKRYGD-HQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKptgRLSGSGLRQLRSRV 102
Cdd:PRK13647 5 IEVEDLHFRYKDgTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGR---EVNAENEKWVRSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 103 GFVFQQFN--LYAhLTASQNITLALEHVhGWKPLPAQERALALLEKVGMLEKAHHYPAELSGGQQQRVAIARALASSPQI 180
Cdd:PRK13647 82 GLVFQDPDdqVFS-STVWDDVAFGPVNM-GLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 544825118 181 ILFDEPTSALDPEMIGEVLFVMKALAHSGITMIVVTHEMQFAREIADRIVFIDGGHIL 238
Cdd:PRK13647 160 IVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVL 217
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
31-263 |
2.33e-31 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 116.47 E-value: 2.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 31 KRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTG-----RLSGSGLRQL-RSRVGF 104
Cdd:TIGR02323 11 KSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAelelyQLSEAERRRLmRTEWGF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 105 VFQQF--NLYAHLTASQNIT---LALEHVHGWKplpAQERALALLEKVGM-LEKAHHYPAELSGGQQQRVAIARALASSP 178
Cdd:TIGR02323 91 VHQNPrdGLRMRVSAGANIGerlMAIGARHYGN---IRATAQDWLEEVEIdPTRIDDLPRAFSGGMQQRLQIARNLVTRP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 179 QIILFDEPTSALDPEMIGEVLFVMKALAHS-GITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQFFSQPAHPRAQR 257
Cdd:TIGR02323 168 RLVFMDEPTGGLDVSVQARLLDLLRGLVRDlGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVLDDPQHPYTQL 247
|
....*.
gi 544825118 258 FLQKVL 263
Cdd:TIGR02323 248 LVSSIL 253
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
23-239 |
4.25e-31 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 121.39 E-value: 4.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 23 SVEFRHVDKRYGDHQ--VLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSGSGLRQlrs 100
Cdd:TIGR01846 455 AITFENIRFRYAPDSpeVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRR--- 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 101 RVGFVFQQfNLYAHLTASQNITLA-----LEHV-HGWKPLPAQERALALLEkvGMLEKAHHYPAELSGGQQQRVAIARAL 174
Cdd:TIGR01846 532 QMGVVLQE-NVLFSRSIRDNIALCnpgapFEHViHAAKLAGAHDFISELPQ--GYNTEVGEKGANLSGGQRQRIAIARAL 608
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 544825118 175 ASSPQIILFDEPTSALDPEMIGEVLFVMKALAhSGITMIVVTHEMQFAREiADRIVFIDGGHILE 239
Cdd:TIGR01846 609 VGNPRILIFDEATSALDYESEALIMRNMREIC-RGRTVIIIAHRLSTVRA-CDRIIVLEKGQIAE 671
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
24-250 |
9.93e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 115.67 E-value: 9.93e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 24 VEFRHVDKRY-GDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPtgrLSGSGLRQLRSRV 102
Cdd:PRK13652 4 IETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEP---ITKENIREVRKFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 103 GFVFQQFN-LYAHLTASQNITLALEHVhGWKPLPAQERALALLEKVGMLEKAHHYPAELSGGQQQRVAIARALASSPQII 181
Cdd:PRK13652 81 GLVFQNPDdQIFSPTVEQDIAFGPINL-GLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 182 LFDEPTSALDPEMIGEVLFVMKALAHS-GITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQFFSQP 250
Cdd:PRK13652 160 VLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
19-259 |
1.64e-30 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 119.04 E-value: 1.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 19 LEQASVEFRHVDKrygDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLS-----GGEILVDNKPTGRLSGS 93
Cdd:PRK15134 8 IENLSVAFRQQQT---VRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPpvvypSGDIRFHGESLLHASEQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 94 GLRQLR-SRVGFVFQQfnLYAHLTASQNITLALEHV----HGWKPLPAQERALALLEKVGMLEKA---HHYPAELSGGQQ 165
Cdd:PRK15134 85 TLRGVRgNKIAMIFQE--PMVSLNPLHTLEKQLYEVlslhRGMRREAARGEILNCLDRVGIRQAAkrlTDYPHQLSGGER 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 166 QRVAIARALASSPQIILFDEPTSALDPEMIGEVLFVMKALAHS-GITMIVVTHEMQFAREIADRIVFIDGGHILETAPPA 244
Cdd:PRK15134 163 QRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAA 242
|
250
....*....|....*
gi 544825118 245 QFFSQPAHPRAQRFL 259
Cdd:PRK15134 243 TLFSAPTHPYTQKLL 257
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
24-239 |
1.69e-30 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 112.41 E-value: 1.69e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 24 VEFRHVDKRYG--DHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLI-NQLEPLSGgEILVDNKPTGRLSGsglrQLRS 100
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLtGDLKPQQG-EITLDGVPVSDLEK----ALSS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 101 RVGFVFQQFNLYAHltasqnitlalehvhgwkplpaqeralALLEKVGmlekahhypAELSGGQQQRVAIARALASSPQI 180
Cdd:cd03247 76 LISVLNQRPYLFDT---------------------------TLRNNLG---------RRFSGGERQRLALARILLQDAPI 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 181 ILFDEPTSALDPEMIGEVL-FVMKALahSGITMIVVTHEMQfAREIADRIVFIDGGHILE 239
Cdd:cd03247 120 VLLDEPTVGLDPITERQLLsLIFEVL--KDKTLIWITHHLT-GIEHMDKILFLENGKIIM 176
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
24-237 |
4.95e-30 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 117.58 E-value: 4.95e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 24 VEFRHVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSGSGLRQLRsrVG 103
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLG--IG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 104 FVFQQFNLYAHLTASQNI---TLALEHVHG-----WKPLpaQERALALLEKVGMLEKAHHYPAELSGGQQQRVAIARALA 175
Cdd:PRK09700 84 IIYQELSVIDELTVLENLyigRHLTKKVCGvniidWREM--RVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 544825118 176 SSPQIILFDEPTSALDPEMIGEVLFVMKALAHSGITMIVVTHEMQFAREIADRI-VFIDGGHI 237
Cdd:PRK09700 162 LDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYtVMKDGSSV 224
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
11-240 |
7.73e-30 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 117.75 E-value: 7.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 11 AGAADFSHLEQAsVEFRHVDKRY-GDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGR 89
Cdd:PRK13657 323 PGAIDLGRVKGA-VEFDDVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRT 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 90 LSgsgLRQLRSRVGFVFQQFNLYAHlTASQNITLALEHVHGWKPLPAQERALALlekVGMLEKAHHYPA-------ELSG 162
Cdd:PRK13657 402 VT---RASLRRNIAVVFQDAGLFNR-SIEDNIRVGRPDATDEEMRAAAERAQAH---DFIERKPDGYDTvvgergrQLSG 474
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 544825118 163 GQQQRVAIARALASSPQIILFDEPTSALDPEMIGEVLFVMKALAHsGITMIVVTHEMQFAREiADRIVFIDGGHILET 240
Cdd:PRK13657 475 GERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMK-GRTTFIIAHRLSTVRN-ADRILVFDNGRVVES 550
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
38-237 |
1.35e-29 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 109.83 E-value: 1.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 38 VLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSGSGLRQL--------RSRVGfVFQQF 109
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgiayvpedRKREG-LVLDL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 110 NLYahltasQNITLalehvhgwkplpaqeralallekvgmlekahhyPAELSGGQQQRVAIARALASSPQIILFDEPTSA 189
Cdd:cd03215 94 SVA------ENIAL---------------------------------SSLLSGGNQQKVVLARWLARDPRVLILDEPTRG 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 544825118 190 LDPEMIGEVLFVMKALAHSGITMIVVTHEMQFAREIADRIVFIDGGHI 237
Cdd:cd03215 135 VDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
37-261 |
2.27e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 112.52 E-value: 2.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 37 QVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQL-EPLSGGEILVDNKPTGRLSGSGLRQLRSRVGFVFQ--QFNLYA 113
Cdd:PRK13643 20 RALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLlQPTEGKVTVGDIVVSSTSKQKEIKPVRKKVGVVFQfpESQLFE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 114 HlTASQNITLALEHVhGWKPLPAQERALALLEKVGMLEKA-HHYPAELSGGQQQRVAIARALASSPQIILFDEPTSALDP 192
Cdd:PRK13643 100 E-TVLKDVAFGPQNF-GIPKEKAEKIAAEKLEMVGLADEFwEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 193 EMIGEVLFVMKALAHSGITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQFFSQ----PAH----PRAQRF---LQK 261
Cdd:PRK13643 178 KARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQEvdflKAHelgvPKATHFadqLQK 257
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
37-253 |
2.40e-29 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 116.30 E-value: 2.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 37 QVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEP---LSGGEILVDNKPTGRlsgsglRQLRSRVGFVfQQFNLY- 112
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPkgvKGSGSVLLNGMPIDA------KEMRAISAYV-QQDDLFi 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 113 AHLTASQNITLAlEHVHGWKPLPAQERAL---ALLEKVGMLEKAH------HYPAELSGGQQQRVAIARALASSPQIILF 183
Cdd:TIGR00955 112 PTLTVREHLMFQ-AHLRMPRRVTKKEKRErvdEVLQALGLRKCANtrigvpGRVKGLSGGERKRLAFASELLTDPPLLFC 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 544825118 184 DEPTSALDPEMIGEVLFVMKALAHSGITMIVVTHemQFAREIA---DRIVFIDGGHILETAPP---AQFFSQPAHP 253
Cdd:TIGR00955 191 DEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIH--QPSSELFelfDKIILMAEGRVAYLGSPdqaVPFFSDLGHP 264
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
24-236 |
4.46e-29 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 107.53 E-value: 4.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 24 VEFRHVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLI-NQLEPLSGgeilvdnkptgrlsgsglrqlrsrv 102
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIaGELEPDEG------------------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 103 gfvfqqfnlyaHLTASQNITLAlehvhgwkplpaqeralallekvgmlekahhYPAELSGGQQQRVAIARALASSPQIIL 182
Cdd:cd03221 56 -----------IVTWGSTVKIG-------------------------------YFEQLSGGEKMRLALAKLLLENPNLLL 93
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 544825118 183 FDEPTSALDPEMIgevLFVMKALAHSGITMIVVTHEMQFAREIADRIVFIDGGH 236
Cdd:cd03221 94 LDEPTNHLDLESI---EALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
36-237 |
4.55e-29 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 110.95 E-value: 4.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 36 HQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSgsglRQLRSR-VGFVFQ--QFNLY 112
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLP----EYKRAKyIGRVFQdpMMGTA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 113 AHLTASQNITLALE--HVHGWKP-LPAQERAL--ALLEKVGM-LEKAHHYPAE-LSGGQQQRVAIARALASSPQIILFDE 185
Cdd:COG1101 95 PSMTIEENLALAYRrgKRRGLRRgLTKKRRELfrELLATLGLgLENRLDTKVGlLSGGQRQALSLLMATLTKPKLLLLDE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 544825118 186 PTSALDPEMIGEVL-FVMKALAHSGITMIVVTHEMQFAREIADRIVFIDGGHI 237
Cdd:COG1101 175 HTAALDPKTAALVLeLTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRI 227
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
25-246 |
6.33e-29 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 114.26 E-value: 6.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 25 EFRHVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLinqlepLSG--------GEILVDNKPtgrLSGSGLR 96
Cdd:PRK13549 7 EMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKV------LSGvyphgtyeGEIIFEGEE---LQASNIR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 97 QL-RSRVGFVFQQFNLYAHLTASQNITLALEHVHG----WKPLPAqeRALALLEKVGMLEKAHHYPAELSGGQQQRVAIA 171
Cdd:PRK13549 78 DTeRAGIAIIHQELALVKELSVLENIFLGNEITPGgimdYDAMYL--RAQKLLAQLKLDINPATPVGNLGLGQQQLVEIA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 544825118 172 RALASSPQIILFDEPTSALDPEMIGEVLFVMKALAHSGITMIVVTHEMQFAREIADRIVFI-DGGHIlETAPPAQF 246
Cdd:PRK13549 156 KALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIrDGRHI-GTRPAAGM 230
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
21-239 |
2.74e-28 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 113.19 E-value: 2.74e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 21 QASVEFRHVDKRY--GDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKptgRLSGSGLRQL 98
Cdd:PRK11176 339 KGDIEFRNVTFTYpgKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGH---DLRDYTLASL 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 99 RSRVGFVFQQFNLYAHlTASQNITLALEHVHGWKPLpaqERALALLEKVGMLEKAHH--------YPAELSGGQQQRVAI 170
Cdd:PRK11176 416 RNQVALVSQNVHLFND-TIANNIAYARTEQYSREQI---EEAARMAYAMDFINKMDNgldtvigeNGVLLSGGQRQRIAI 491
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 544825118 171 ARALASSPQIILFDEPTSALDPEmigEVLFVMKALA--HSGITMIVVTHEMQfAREIADRIVFIDGGHILE 239
Cdd:PRK11176 492 ARALLRDSPILILDEATSALDTE---SERAIQAALDelQKNRTSLVIAHRLS-TIEKADEILVVEDGEIVE 558
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
26-245 |
3.53e-28 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 107.86 E-value: 3.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 26 FRHVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDnkptGRLS-----GSGlrqlrs 100
Cdd:COG1134 29 LRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVN----GRVSallelGAG------ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 101 rvgfvfqqFNlyAHLTASQNITL-ALehVHGWKPLPAQER-----ALALLEKVgMLEKAHHYpaelSGGQQQRVAIARAL 174
Cdd:COG1134 99 --------FH--PELTGRENIYLnGR--LLGLSRKEIDEKfdeivEFAELGDF-IDQPVKTY----SSGMRARLAFAVAT 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 544825118 175 ASSPQIILFDEPTSALDPEmigevlF------VMKALAHSGITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQ 245
Cdd:COG1134 162 AVDPDILLVDEVLAVGDAA------FqkkclaRIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEE 232
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
24-250 |
7.26e-28 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 110.32 E-value: 7.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 24 VEFRHVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSGsglRQLRSRVG 103
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSA---RAASRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 104 FVFQQFNLYAHLTASQNITLAlEHVH-----GWKPL--PAQERALallEKVGMLEKAHHYPAELSGGQQQRVAIARALAS 176
Cdd:PRK09536 81 SVPQDTSLSFEFDVRQVVEMG-RTPHrsrfdTWTETdrAAVERAM---ERTGVAQFADRPVTSLSGGERQRVLLARALAQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 544825118 177 SPQIILFDEPTSALDPEMIGEVLFVMKALAHSGITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQFFSQP 250
Cdd:PRK09536 157 ATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTAD 230
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
23-265 |
7.93e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 108.17 E-value: 7.93e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 23 SVEFRHVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNK--PTGRLSGSGLRQLRS 100
Cdd:PRK13645 11 NVSYTYAKKTPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYaiPANLKKIKEVKRLRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 101 RVGFVFQ--QFNLYAHlTASQNITLALEHVhGWKPLPAQERALALLEKVGMLEK-AHHYPAELSGGQQQRVAIARALASS 177
Cdd:PRK13645 91 EIGLVFQfpEYQLFQE-TIEKDIAFGPVNL-GENKQEAYKKVPELLKLVQLPEDyVKRSPFELSGGQKRRVALAGIIAMD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 178 PQIILFDEPTSALDPEmiGEVLFV---MKALAHSGITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQFFSQpahpr 254
Cdd:PRK13645 169 GNTLVLDEPTGGLDPK--GEEDFInlfERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN----- 241
|
250
....*....|..
gi 544825118 255 aQRFLQKV-LDP 265
Cdd:PRK13645 242 -QELLTKIeIDP 252
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
31-245 |
1.21e-27 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 106.52 E-value: 1.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 31 KRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSGSglRQLRSRVGFVFQQFN 110
Cdd:PRK10895 11 KAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLH--ARARRGIGYLPQEAS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 111 LYAHLTASQNITLALEHVHGWKPLPAQERALALLEKVGMLEKAHHYPAELSGGQQQRVAIARALASSPQIILFDEPTSAL 190
Cdd:PRK10895 89 IFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGV 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 544825118 191 DPEMIGEVLFVMKALAHSGITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQ 245
Cdd:PRK10895 169 DPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTE 223
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
21-237 |
4.78e-27 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 109.23 E-value: 4.78e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 21 QASVEFRHVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPtgRLSGSGLRQLRS 100
Cdd:PRK11288 2 SPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQE--MRFASTTAALAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 101 RVGFVFQQFNLYAHLTASQNITL-ALEHVHGW-KPLPAQERALALLEKVGMLEKAHHYPAELSGGQQQRVAIARALASSP 178
Cdd:PRK11288 80 GVAIIYQELHLVPEMTVAENLYLgQLPHKGGIvNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 544825118 179 QIILFDEPTSALDPEMIgEVLF-VMKALAHSGITMIVVTHEMQFAREIADRI-VFIDGGHI 237
Cdd:PRK11288 160 RVIAFDEPTSSLSAREI-EQLFrVIRELRAEGRVILYVSHRMEEIFALCDAItVFKDGRYV 219
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
28-237 |
5.28e-27 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 107.27 E-value: 5.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 28 HVDKRYGDHQVlnDINLTITPGEVVAILGPSGSGKSTLIRLINQL-EPLSG-----GEILVDNKptgrlSGSGLRQLRSR 101
Cdd:PRK11144 5 NFKQQLGDLCL--TVNLTLPAQGITAIFGRSGAGKTSLINAISGLtRPQKGrivlnGRVLFDAE-----KGICLPPEKRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 102 VGFVFQQFNLYAHLTASQNITLALEHVhgwkpLPAQERALallekVGMLEKAHH---YPAELSGGQQQRVAIARALASSP 178
Cdd:PRK11144 78 IGYVFQDARLFPHYKVRGNLRYGMAKS-----MVAQFDKI-----VALLGIEPLldrYPGSLSGGEKQRVAIGRALLTAP 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 544825118 179 QIILFDEPTSALDPEMIGEVLFVMKALAHS-GITMIVVTHEMQfarEI---ADRIVFIDGGHI 237
Cdd:PRK11144 148 ELLLMDEPLASLDLPRKRELLPYLERLAREiNIPILYVSHSLD---EIlrlADRVVVLEQGKV 207
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
18-238 |
8.57e-27 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 108.59 E-value: 8.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 18 HLEQASVEFRHVDkryGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEIlvdnkptgRLSGSGLRQ 97
Cdd:TIGR01842 316 HLSVENVTIVPPG---GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSV--------RLDGADLKQ 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 98 -----LRSRVGFVFQQFNLYAHlTASQNITLALEHVHGWKPLPAQeRALALLEKVGMLEKAHHYP-----AELSGGQQQR 167
Cdd:TIGR01842 385 wdretFGKHIGYLPQDVELFPG-TVAENIARFGENADPEKIIEAA-KLAGVHELILRLPDGYDTVigpggATLSGGQRQR 462
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 544825118 168 VAIARALASSPQIILFDEPTSALDPEmiGEVLFV--MKALAHSGITMIVVTHEMQfAREIADRIVFIDGGHIL 238
Cdd:TIGR01842 463 IALARALYGDPKLVVLDEPNSNLDEE--GEQALAnaIKALKARGITVVVITHRPS-LLGCVDKILVLQDGRIA 532
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
38-237 |
8.97e-27 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 108.18 E-value: 8.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 38 VLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPtgrLSGSGLRQ-LRSRVGFV---FQQFNLYA 113
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKP---VRIRSPRDaIRAGIAYVpedRKGEGLVL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 114 HLTASQNITLA-LEHVHGWKPL-PAQERALA--LLEKVGMleKAH--HYPA-ELSGGQQQRVAIARALASSPQIILFDEP 186
Cdd:COG1129 344 DLSIRENITLAsLDRLSRGGLLdRRRERALAeeYIKRLRI--KTPspEQPVgNLSGGNQQKVVLAKWLATDPKVLILDEP 421
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 544825118 187 TSALDpemIG---EVLFVMKALAHSGITMIVVTHEMQFAREIADRIVFIDGGHI 237
Cdd:COG1129 422 TRGID---VGakaEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRI 472
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
21-241 |
9.10e-27 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 108.17 E-value: 9.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 21 QASVEFRHVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTgRLSGSGLRQlRS 100
Cdd:PRK10762 2 QALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEV-TFNGPKSSQ-EA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 101 RVGFVFQQFNLYAHLTASQNITLALEHVHG-----WKPLPAQerALALLEKVGMLEKAHHYPAELSGGQQQRVAIARALA 175
Cdd:PRK10762 80 GIGIIHQELNLIPQLTIAENIFLGREFVNRfgridWKKMYAE--ADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLS 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 544825118 176 SSPQIILFDEPTSAL-DPEMigEVLF-VMKALAHSGITMIVVTHEMQFAREIADRI-VFIDGGHILETA 241
Cdd:PRK10762 158 FESKVIIMDEPTDALtDTET--ESLFrVIRELKSQGRGIVYISHRLKEIFEICDDVtVFRDGQFIAERE 224
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
18-260 |
1.27e-26 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 105.59 E-value: 1.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 18 HLEQASVEFRHVDKrygdhqvlndINLTITPGEVVAILGPSGSGKS----TLIRLINQLEPLSGGEILVDNKPTGRLSGS 93
Cdd:PRK11022 12 HFGDESAPFRAVDR----------ISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDLQRISEK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 94 GLRQL-RSRVGFVFQQ--FNLYAHLTASQNITLALEHVHGWKPLPAQERALALLEKVGMLEKAHH---YPAELSGGQQQR 167
Cdd:PRK11022 82 ERRNLvGAEVAMIFQDpmTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASRldvYPHQLSGGMSQR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 168 VAIARALASSPQIILFDEPTSALDPEMIGEVLFVMKALAH-SGITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQF 246
Cdd:PRK11022 162 VMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQkENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDI 241
|
250
....*....|....
gi 544825118 247 FSQPAHPRAQRFLQ 260
Cdd:PRK11022 242 FRAPRHPYTQALLR 255
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
38-256 |
1.70e-26 |
|
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: 107.91 E-value: 1.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 38 VLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSGsglRQLRSRVGFVFQQFNLYAHlTA 117
Cdd:COG4618 347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDR---EELGRHIGYLPQDVELFDG-TI 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 118 SQNITLALEhvhgwkplPAQERALALLEKVGMLEKAHHYP-----------AELSGGQQQRVAIARALASSPQIILFDEP 186
Cdd:COG4618 423 AENIARFGD--------ADPEKVVAAAKLAGVHEMILRLPdgydtrigeggARLSGGQRQRIGLARALYGDPRLVVLDEP 494
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 544825118 187 TSALDPEmiGEVLfVMKALAH---SGITMIVVTHEMQfAREIADRIVFIDGGHILETAPPAQFFSQPAHPRAQ 256
Cdd:COG4618 495 NSNLDDE--GEAA-LAAAIRAlkaRGATVVVITHRPS-LLAAVDKLLVLRDGRVQAFGPRDEVLARLARPAAA 563
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
41-259 |
1.93e-26 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 104.10 E-value: 1.93e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 41 DINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPtgrLSGSGLRQLRSRVGFVFQ--QFNLYAHLTAS 118
Cdd:PRK15112 31 PLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHP---LHFGDYSYRSQRIRMIFQdpSTSLNPRQRIS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 119 QNITLALEHVHGWKPLPAQERALALLEKVGML-EKAHHYPAELSGGQQQRVAIARALASSPQIILFDEPTSALDPEMIGE 197
Cdd:PRK15112 108 QILDFPLRLNTDLEPEQREKQIIETLRQVGLLpDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQ 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 544825118 198 VLFVMKALAHS-GITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQFFSQPAHPRAQRFL 259
Cdd:PRK15112 188 LINLMLELQEKqGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASPLHELTKRLI 250
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
24-246 |
2.95e-26 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 107.06 E-value: 2.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 24 VEFRHVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSGSGLRQLrsRVG 103
Cdd:PRK15439 12 LCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQL--GIY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 104 FVFQQFNLYAHLTASQNITLALEhvhgwKPLPAQERALALLEKVGMLEKAHHYPAELSGGQQQRVAIARALASSPQIILF 183
Cdd:PRK15439 90 LVPQEPLLFPNLSVKENILFGLP-----KRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILIL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 544825118 184 DEPTSALDPemiGEV--LFV-MKALAHSGITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQF 246
Cdd:PRK15439 165 DEPTASLTP---AETerLFSrIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADL 227
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
23-240 |
4.42e-26 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 107.13 E-value: 4.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 23 SVEFRHVDKRYG-DHQVLNDINLTITPGEVVAILGPSGSGKSTLIRL-INQLEPLSGgEILVDNKPTGRLSGSGLRQLrs 100
Cdd:TIGR01193 473 DIVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLlVGFFQARSG-EILLNGFSLKDIDRHTLRQF-- 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 101 rVGFVFQQFNLYAHlTASQNITLalehvhGWKPLPAQERALALLEKVGMLEKAHHYP-----------AELSGGQQQRVA 169
Cdd:TIGR01193 550 -INYLPQEPYIFSG-SILENLLL------GAKENVSQDEIWAACEIAEIKDDIENMPlgyqtelseegSSISGGQKQRIA 621
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 544825118 170 IARALASSPQIILFDEPTSALDpeMIGEVLFVMKALAHSGITMIVVTHEMQFAREiADRIVFIDGGHILET 240
Cdd:TIGR01193 622 LARALLTDSKVLILDESTSNLD--TITEKKIVNNLLNLQDKTIIFVAHRLSVAKQ-SDKIIVLDHGKIIEQ 689
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
27-238 |
4.72e-26 |
|
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: 102.03 E-value: 4.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 27 RHVDKR-YGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVdnkpTGRLSGSGLRQLRSRVGFV 105
Cdd:cd03267 24 KSLFKRkYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV----AGLVPWKRRKKFLRRIGVV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 106 FQQFN-LYAHLTASQNITLaLEHVHGWKPLPAQERalaLLEKVGMLEKAH--HYPA-ELSGGQQQRVAIARALASSPQII 181
Cdd:cd03267 100 FGQKTqLWWDLPVIDSFYL-LAAIYDLPPARFKKR---LDELSELLDLEEllDTPVrQLSLGQRMRAEIAAALLHEPEIL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 182 LFDEPTSALD---PEMIGEvlFVMKALAHSGITMIVVTHEMQFAREIADRIVFIDGGHIL 238
Cdd:cd03267 176 FLDEPTIGLDvvaQENIRN--FLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
24-237 |
1.27e-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: 105.29 E-value: 1.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 24 VEFRHVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSG--GEILVDNKPtgrLSGSGLRQL-RS 100
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSP---LKASNIRDTeRA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 101 RVGFVFQQFNLYAHLTASQNITLALEHVH--GWKPLPAQ-ERALALLEKVGMLEKAHHYP-AELSGGQQQRVAIARALAS 176
Cdd:TIGR02633 79 GIVIIHQELTLVPELSVAENIFLGNEITLpgGRMAYNAMyLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNK 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 544825118 177 SPQIILFDEPTSALDPEMIGEVLFVMKALAHSGITMIVVTHEMQFAREIADRIVFI-DGGHI 237
Cdd:TIGR02633 159 QARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIrDGQHV 220
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
32-269 |
1.48e-25 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 101.62 E-value: 1.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 32 RYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGrLSGSGLRQLRSRVGFVFQ---Q 108
Cdd:PRK13638 10 RYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLD-YSKRGLLALRQQVATVFQdpeQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 109 FNLYAHLTAsqNITLALEHVHgwkpLPAQERALALLEKVGMLEKAH--HYPAE-LSGGQQQRVAIARALASSPQIILFDE 185
Cdd:PRK13638 89 QIFYTDIDS--DIAFSLRNLG----VPEAEITRRVDEALTLVDAQHfrHQPIQcLSHGQKKRVAIAGALVLQARYLLLDE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 186 PTSALDPEMIGEVLFVMKALAHSGITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQFFSQPAHPRAQRFLQKVLDP 265
Cdd:PRK13638 163 PTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFACTEAMEQAGLTQPWLVK 242
|
....
gi 544825118 266 LHQE 269
Cdd:PRK13638 243 LHTQ 246
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
38-217 |
1.54e-25 |
|
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: 99.74 E-value: 1.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 38 VLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSGSGLRQLrsrvgfvfqqfnLYA-HLT 116
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENI------------LYLgHLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 117 ASQNITLALEHVHGWKPL--PAQERALALLEKVGMLEKAHHYPAELSGGQQQRVAIARALASSPQIILFDEPTSALDPEM 194
Cdd:TIGR01189 83 GLKPELSALENLHFWAAIhgGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAG 162
|
170 180
....*....|....*....|...
gi 544825118 195 IGEVLFVMKALAHSGITMIVVTH 217
Cdd:TIGR01189 163 VALLAGLLRAHLARGGIVLLTTH 185
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
24-264 |
4.54e-25 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 101.72 E-value: 4.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 24 VEFRHVDkryGDHQVLNDINLTITPGEVVAILGPSGSGKS-TLIRLINQLEP--LSGGEILVDNKPTGRLSGSGLRQLRS 100
Cdd:PRK09473 20 VTFSTPD---GDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAAngRIGGSATFNGREILNLPEKELNKLRA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 101 -RVGFVFQQ--FNLYAHLTASQNITLALEHVHGWKPLPAQERALALLEKVGMLE---KAHHYPAELSGGQQQRVAIARAL 174
Cdd:PRK09473 97 eQISMIFQDpmTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMPEarkRMKMYPHEFSGGMRQRVMIAMAL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 175 ASSPQIILFDEPTSALDPEMIGEVLFVMKALAHS-GITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQFFSQPAHP 253
Cdd:PRK09473 177 LCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQPSHP 256
|
250
....*....|...
gi 544825118 254 RAQRFLQKV--LD 264
Cdd:PRK09473 257 YSIGLLNAVprLD 269
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
19-238 |
5.22e-25 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 99.57 E-value: 5.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 19 LEQASVEFRHVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNK-----PTGRLsgs 93
Cdd:PRK11614 1 MEKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKditdwQTAKI--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 94 glrqLRSRVGFVFQQFNLYAHLTASQNITLALEHVHGWKPLPAQERALALLEKvgMLEKAHHYPAELSGGQQQRVAIARA 173
Cdd:PRK11614 78 ----MREAVAIVPEGRRVFSRMTVEENLAMGGFFAERDQFQERIKWVYELFPR--LHERRIQRAGTMSGGEQQMLAIGRA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 544825118 174 LASSPQIILFDEPTSALDPEMIGEVLFVMKALAHSGITMIVVTHEMQFAREIADRIVFIDGGHIL 238
Cdd:PRK11614 152 LMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVV 216
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
25-240 |
1.60e-24 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 101.79 E-value: 1.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 25 EFRHVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLinqlepLSG--------GEILVDNKPtgrlsgsglR 96
Cdd:NF040905 3 EMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKV------LSGvyphgsyeGEILFDGEV---------C 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 97 QLRS-----RVGFVF--QQFNLYAHLTASQNITLALEHVHG----WKplPAQERALALLEKVGMLEKAHHYPAELSGGQQ 165
Cdd:NF040905 68 RFKDirdseALGIVIihQELALIPYLSIAENIFLGNERAKRgvidWN--ETNRRARELLAKVGLDESPDTLVTDIGVGKQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 544825118 166 QRVAIARALASSPQIILFDEPTSALDPEMIGEVLFVMKALAHSGITMIVVTHEMQFAREIADRIVFIDGGHILET 240
Cdd:NF040905 146 QLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTIET 220
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
36-255 |
2.14e-24 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 98.80 E-value: 2.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 36 HQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRlsgsGLRQlrSRVGFVFQQFNL-YAH 114
Cdd:PRK15056 20 HTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ----ALQK--NLVAYVPQSEEVdWSF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 115 LTASQNITLALEHVH-GWKPLPA---QERALALLEKVGMLEKAHHYPAELSGGQQQRVAIARALASSPQIILFDEPTSAL 190
Cdd:PRK15056 94 PVLVEDVVMMGRYGHmGWLRRAKkrdRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 544825118 191 DPEMIGEVLFVMKALAHSGITMIVVTHEMQFAREIADRIVFIDGGhILETAPPAQFFSQPAHPRA 255
Cdd:PRK15056 174 DVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMVKGT-VLASGPTETTFTAENLELA 237
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
20-217 |
2.89e-24 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 101.42 E-value: 2.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 20 EQASVEFRHVDKRYGDHQVL-NDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNK------------P 86
Cdd:COG4178 359 EDGALALEDLTLRTPDGRPLlEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGarvlflpqrpylP 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 87 TGRLsgsgLRQLrsrvgfvfqqfnLYAHLTASqnitlalehvhgwkplPAQERALALLEKVG------MLEKAHHYPAEL 160
Cdd:COG4178 439 LGTL----REAL------------LYPATAEA----------------FSDAELREALEAVGlghlaeRLDEEADWDQVL 486
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 544825118 161 SGGQQQRVAIARALASSPQIILFDEPTSALDPEMIGEvlfVMKALAHS--GITMIVVTH 217
Cdd:COG4178 487 SLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAA---LYQLLREElpGTTVISVGH 542
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
19-249 |
3.01e-24 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 101.72 E-value: 3.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 19 LEQASVEFRHVDKRY-GDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSGSGLRQ 97
Cdd:PRK10790 336 LQSGRIDIDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQ 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 98 lrsRVGFVfQQFNLYAHLTASQNITLALEHvhgwkplpAQERALALLEKVGMLEKAHHYPA-----------ELSGGQQQ 166
Cdd:PRK10790 416 ---GVAMV-QQDPVVLADTFLANVTLGRDI--------SEEQVWQALETVQLAELARSLPDglytplgeqgnNLSVGQKQ 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 167 RVAIARALASSPQIILFDEPTSALDPemiGEVLFVMKALA--HSGITMIVVTHEMQFAREiADRIVFIDGGHILETAPPA 244
Cdd:PRK10790 484 LLALARVLVQTPQILILDEATANIDS---GTEQAIQQALAavREHTTLVVIAHRLSTIVE-ADTILVLHRGQAVEQGTHQ 559
|
....*
gi 544825118 245 QFFSQ 249
Cdd:PRK10790 560 QLLAA 564
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
41-260 |
3.33e-24 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 97.85 E-value: 3.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 41 DINLTITPGEVVAILGPSGSGKS-TLIRLINQLEP---LSGGEILVDNKPtgrLSGSGLRQlrSRVGFVFQQ----FNLY 112
Cdd:PRK10418 21 GVSLTLQRGRVLALVGGSGSGKSlTCAAALGILPAgvrQTAGRVLLDGKP---VAPCALRG--RKIATIMQNprsaFNPL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 113 AHLTASQNITLALEHVHGwkplpAQERALALLEKVGmLEKAHH----YPAELSGGQQQRVAIARALASSPQIILFDEPTS 188
Cdd:PRK10418 96 HTMHTHARETCLALGKPA-----DDATLTAALEAVG-LENAARvlklYPFEMSGGMLQRMMIALALLCEAPFIIADEPTT 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 544825118 189 ALDPEMIGEVL-FVMKALAHSGITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQFFSQPAHPRAQRFLQ 260
Cdd:PRK10418 170 DLDVVAQARILdLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLVS 242
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
25-230 |
5.34e-24 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 96.32 E-value: 5.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 25 EFRHVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSGSGLRQlrsRVGF 104
Cdd:PRK10247 9 QLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQ---QVSY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 105 VFQQFNLYAHlTASQNITLALEhVHGWKPLPAqeRALALLEKVG----MLEKAhhyPAELSGGQQQRVAIARALASSPQI 180
Cdd:PRK10247 86 CAQTPTLFGD-TVYDNLIFPWQ-IRNQQPDPA--IFLDDLERFAlpdtILTKN---IAELSGGEKQRISLIRNLQFMPKV 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 544825118 181 ILFDEPTSALDPEMIGEVLFVMKALA-HSGITMIVVTHEmqfAREI--ADRIV 230
Cdd:PRK10247 159 LLLDEITSALDESNKHNVNEIIHRYVrEQNIAVLWVTHD---KDEInhADKVI 208
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
15-245 |
6.50e-24 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 97.17 E-value: 6.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 15 DFSHLEQASVEFRHVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSGSG 94
Cdd:PRK10575 3 EYTNHSDTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 95 LRQlrsRVGFVFQQFNLYAHLTASQNITLALEHVHGWKPLPAQ------ERALALlekVGMLEKAHHYPAELSGGQQQRV 168
Cdd:PRK10575 83 FAR---KVAYLPQQLPAAEGMTVRELVAIGRYPWHGALGRFGAadrekvEEAISL---VGLKPLAHRLVDSLSGGERQRA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 544825118 169 AIARALASSPQIILFDEPTSALDPEMIGEVLFVMKALAHS-GITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQ 245
Cdd:PRK10575 157 WIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAE 234
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
36-239 |
2.32e-23 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 94.64 E-value: 2.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 36 HQVLNDINLTITPGEVVAILGPSGSGKSTLIRLInqleplsggeilvdnkpTGRLSGsglRQLRSRVGFVFQQFnlyahl 115
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLL-----------------AGALKG---TPVAGCVDVPDNQF------ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 116 taSQNITLaLEHVHGWKPLPAqerALALLEKVGmLEKAHHY---PAELSGGQQQRVAIARALASSPQIILFDEPTSALDP 192
Cdd:COG2401 97 --GREASL-IDAIGRKGDFKD---AVELLNAVG-LSDAVLWlrrFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDR 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 544825118 193 EMIGEVLFVMKALAHS-GITMIVVTHEMQFAREIA-DRIVFID-GGHILE 239
Cdd:COG2401 170 QTAKRVARNLQKLARRaGITLVVATHHYDVIDDLQpDLLIFVGyGGVPEE 219
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
37-262 |
2.61e-23 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 98.77 E-value: 2.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 37 QVLNDINLTITPGEVVAILGPSGSGKS----TLIRLINQleplSGGEILVDNKPTGR----------LSGSGLRQLR-SR 101
Cdd:PRK10261 30 AAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLEQ----AGGLVQCDKMLLRRrsrqvielseQSAAQMRHVRgAD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 102 VGFVFQQ--FNLYAHLTASQNITLALEHVHGWKPLPAQERALALLEKVGMLEKA---HHYPAELSGGQQQRVAIARALAS 176
Cdd:PRK10261 106 MAMIFQEpmTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQtilSRYPHQLSGGMRQRVMIAMALSC 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 177 SPQIILFDEPTSALDPEMIGEVLFVMKALAHS-GITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQFFSQPAHPRA 255
Cdd:PRK10261 186 RPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAPQHPYT 265
|
....*..
gi 544825118 256 QRFLQKV 262
Cdd:PRK10261 266 RALLAAV 272
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
37-264 |
2.92e-23 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 96.51 E-value: 2.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 37 QVLNDINLTITPGEVVAILGPSGSGKSTLIRLI-NQLEP----------LSGGEILvdnkptgRLSGSGLRQLRSR-VGF 104
Cdd:COG4170 21 KAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAIcGITKDnwhvtadrfrWNGIDLL-------KLSPRERRKIIGReIAM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 105 VFQqfNLYAHLTASQNITLALEHV-------------HGWKplpaQERALALLEKVGMleKAHH-----YPAELSGGQQQ 166
Cdd:COG4170 94 IFQ--EPSSCLDPSAKIGDQLIEAipswtfkgkwwqrFKWR----KKRAIELLHRVGI--KDHKdimnsYPHELTEGECQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 167 RVAIARALASSPQIILFDEPTSALDPEMIGEVLFVMKALAH-SGITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQ 245
Cdd:COG4170 166 KVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQlQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQ 245
|
250
....*....|....*....
gi 544825118 246 FFSQPAHPRAQRFLQKVLD 264
Cdd:COG4170 246 ILKSPHHPYTKALLRSMPD 264
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
9-244 |
2.94e-23 |
|
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: 98.72 E-value: 2.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 9 SAAGAADFSHLEQASVEFRHVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPtg 88
Cdd:COG4615 318 APPAPADFQTLELRGVTYRYPGEDGDEGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQP-- 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 89 rLSGSGLRQLRSRVGFVFQQFnlyaHLTasqnitlalEHVHGWKPLPAQERALALLEKVGMLEKAHHY-----PAELSGG 163
Cdd:COG4615 396 -VTADNREAYRQLFSAVFSDF----HLF---------DRLLGLDGEADPARARELLERLELDHKVSVEdgrfsTTDLSQG 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 164 QQQRVAIARALASSPQIILFDEPTSALDP--------EMIGEvlfvMKALahsGITMIVVTHEMQFArEIADRIVFIDGG 235
Cdd:COG4615 462 QRKRLALLVALLEDRPILVFDEWAADQDPefrrvfytELLPE----LKAR---GKTVIAISHDDRYF-DLADRVLKMDYG 533
|
....*....
gi 544825118 236 HILETAPPA 244
Cdd:COG4615 534 KLVELTGPA 542
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
31-237 |
4.20e-23 |
|
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: 94.14 E-value: 4.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 31 KRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLS-GSGLRqlrsrvgfvfqqf 109
Cdd:cd03220 30 GEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGlGGGFN------------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 110 nlyAHLTASQNITLALEhVHGWKPLPAQERALALLEKVGmLEKAHHYP-AELSGGQQQRVAIARALASSPQIILFDEPTS 188
Cdd:cd03220 97 ---PELTGRENIYLNGR-LLGLSRKEIDEKIDEIIEFSE-LGDFIDLPvKTYSSGMKARLAFAIATALEPDILLIDEVLA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 544825118 189 AldpemiGEVLFVMKALAH------SGITMIVVTHEMQFAREIADRIVFIDGGHI 237
Cdd:cd03220 172 V------GDAAFQEKCQRRlrellkQGKTVILVSHDPSSIKRLCDRALVLEKGKI 220
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
39-243 |
6.18e-23 |
|
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: 98.16 E-value: 6.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 39 LNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDnkptGRLSGSGLRQLRSRVGFVFQQFNLYAHLTAS 118
Cdd:TIGR01257 946 VDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVG----GKDIETNLDAVRQSLGMCPQHNILFHHLTVA 1021
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 119 QNItLALEHVHGWKPLPAQERALALLEKVGMLEKAHHYPAELSGGQQQRVAIARALASSPQIILFDEPTSALDP---EMI 195
Cdd:TIGR01257 1022 EHI-LFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPysrRSI 1100
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 544825118 196 GEVLFVMKalahSGITMIVVTHEMQFAREIADRIVFIDGGHILETAPP 243
Cdd:TIGR01257 1101 WDLLLKYR----SGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
42-240 |
7.30e-23 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 97.61 E-value: 7.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 42 INLTITPGEVVAILGPSGSGKSTLIRLinqlepLSG-----GEILVDNKPTGRLSgsgLRQLRSRVGFVFQQFNLYaHLT 116
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNA------LLGflpyqGSLKINGIELRELD---PESWRKHLSWVGQNPQLP-HGT 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 117 ASQNITLAlehvhgwKPLPAQERALALLEK------VGMLEKAHHYP-----AELSGGQQQRVAIARALASSPQIILFDE 185
Cdd:PRK11174 439 LRDNVLLG-------NPDASDEQLQQALENawvsefLPLLPQGLDTPigdqaAGLSVGQAQRLALARALLQPCQLLLLDE 511
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 544825118 186 PTSALDpeMIGEVLfVMKAL--AHSGITMIVVTHEMQFAREIaDRIVFIDGGHILET 240
Cdd:PRK11174 512 PTASLD--AHSEQL-VMQALnaASRRQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQQ 564
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
38-217 |
1.35e-22 |
|
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: 92.17 E-value: 1.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 38 VLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSGSGLRQLrsrvgfvfqqfnLY-AHLT 116
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGL------------LYlGHAP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 117 ASQNITLALEHVHGWKPLPAQERALALLEKVGMLEKAHHYPAELSGGQQQRVAIARALASSPQIILFDEPTSALDPEMIG 196
Cdd:cd03231 83 GIKTTLSVLENLRFWHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVA 162
|
170 180
....*....|....*....|.
gi 544825118 197 EVLFVMKALAHSGITMIVVTH 217
Cdd:cd03231 163 RFAEAMAGHCARGGMVVLTTH 183
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
35-250 |
1.69e-22 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 96.32 E-value: 1.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 35 DHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSgsgLRQLRSRVGFVFQQFNLYAH 114
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQ---LDSWRSRLAVVSQTPFLFSD 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 115 lTASQNITLAlehvhgwKPLPAQERalalLEKVGMLEKAHH--------YPAE-------LSGGQQQRVAIARALASSPQ 179
Cdd:PRK10789 404 -TVANNIALG-------RPDATQQE----IEHVARLASVHDdilrlpqgYDTEvgergvmLSGGQKQRISIARALLLNAE 471
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 544825118 180 IILFDEPTSALDPEMIGEVLFVMKALAHsGITMIVVTHEMQFAREiADRIVFIDGGHILETAPPAQFFSQP 250
Cdd:PRK10789 472 ILILDDALSAVDGRTEHQILHNLRQWGE-GRTVIISAHRLSALTE-ASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
26-238 |
3.87e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 93.23 E-value: 3.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 26 FRHVDKR-YGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLinqlepLSGgeILVdnkPT-GRLSGSGL------RQ 97
Cdd:COG4586 24 LKGLFRReYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKM------LTG--ILV---PTsGEVRVLGYvpfkrrKE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 98 LRSRVGFVFQQFN-LYAHLTASQNITLaLEHVHGwkpLPAQERALALLEKVGMLEKAH--HYPA-ELSGGQQQRVAIARA 173
Cdd:COG4586 93 FARRIGVVFGQRSqLWWDLPAIDSFRL-LKAIYR---IPDAEYKKRLDELVELLDLGEllDTPVrQLSLGQRMRCELAAA 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 544825118 174 LASSPQIILFDEPTSALDPEMIGEVL-FVMKALAHSGITMIVVTHEMQFAREIADRIVFIDGGHIL 238
Cdd:COG4586 169 LLHRPKILFLDEPTIGLDVVSKEAIReFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRII 234
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
24-239 |
4.78e-22 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 95.04 E-value: 4.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 24 VEFRHVDKRYGDHQV-LNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPtgrLSGSGLRQLRSRV 102
Cdd:PRK10522 323 LELRNVTFAYQDNGFsVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKP---VTAEQPEDYRKLF 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 103 GFVFQQFNLYAHLTASQNITLALEHVHGWkplpaqeralalLEKVGMLEKAHHYPAE-----LSGGQQQRVAIARALASS 177
Cdd:PRK10522 400 SAVFTDFHLFDQLLGPEGKPANPALVEKW------------LERLKMAHKLELEDGRisnlkLSKGQKKRLALLLALAEE 467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 544825118 178 PQIILFDEPTSALDP----EMIGEVLFVMKALahsGITMIVVTHEMQFArEIADRIVFIDGGHILE 239
Cdd:PRK10522 468 RDILLLDEWAADQDPhfrrEFYQVLLPLLQEM---GKTIFAISHDDHYF-IHADRLLEMRNGQLSE 529
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
33-237 |
5.12e-22 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 95.02 E-value: 5.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 33 YGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKptgrLSGSGLRQ--LRSRVGFVF---- 106
Cdd:PRK11147 13 FSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQD----LIVARLQQdpPRNVEGTVYdfva 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 107 ----------QQFNLYAHLTAS----QNIT-LA-----LEHVHGWKplpAQERALALLEKVGMleKAHHYPAELSGGQQQ 166
Cdd:PRK11147 89 egieeqaeylKRYHDISHLVETdpseKNLNeLAklqeqLDHHNLWQ---LENRINEVLAQLGL--DPDAALSSLSGGWLR 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 544825118 167 RVAIARALASSPQIILFDEPTSALDPEMIgEVL--FVmkaLAHSGiTMIVVTHEMQFAREIADRIVFIDGGHI 237
Cdd:PRK11147 164 KAALGRALVSNPDVLLLDEPTNHLDIETI-EWLegFL---KTFQG-SIIFISHDRSFIRNMATRIVDLDRGKL 231
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
36-245 |
5.95e-22 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 94.71 E-value: 5.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 36 HQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSGSGLRQL--------RSRVGFVfq 107
Cdd:COG3845 271 VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgvayipedRLGRGLV-- 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 108 qfnlyAHLTASQNitLALEHvHGWKPL---------PAQERALALLEKVGMLEKAHHYPAE-LSGGQQQRVAIARALASS 177
Cdd:COG3845 349 -----PDMSVAEN--LILGR-YRRPPFsrggfldrkAIRAFAEELIEEFDVRTPGPDTPARsLSGGNQQKVILARELSRD 420
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 544825118 178 PQIILFDEPTSALDpemIGEVLFV---MKALAHSGITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQ 245
Cdd:COG3845 421 PKLLIAAQPTRGLD---VGAIEFIhqrLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRIVGEVPAAE 488
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
23-264 |
8.56e-22 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 92.56 E-value: 8.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 23 SVEFRHVDkryGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEP----LSGGEILVDNKPTGRLSgsgLRQL 98
Cdd:PRK15093 10 TIEFKTSD---GWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKdnwrVTADRMRFDDIDLLRLS---PRER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 99 RSRVG----FVFQQFNlyAHLTASQNITLAL-EHVHGW--------KPLPAQERALALLEKVGMleKAHH-----YPAEL 160
Cdd:PRK15093 84 RKLVGhnvsMIFQEPQ--SCLDPSERVGRQLmQNIPGWtykgrwwqRFGWRKRRAIELLHRVGI--KDHKdamrsFPYEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 161 SGGQQQRVAIARALASSPQIILFDEPTSALDPEMIGEVLFVMKAL-AHSGITMIVVTHEMQFAREIADRIVFIDGGHILE 239
Cdd:PRK15093 160 TEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLnQNNNTTILLISHDLQMLSQWADKINVLYCGQTVE 239
|
250 260
....*....|....*....|....*
gi 544825118 240 TAPPAQFFSQPAHPRAQRFLQKVLD 264
Cdd:PRK15093 240 TAPSKELVTTPHHPYTQALIRAIPD 264
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
39-245 |
1.04e-21 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 90.67 E-value: 1.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 39 LNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPlSGGEILVDNKPTGRLSGSGLRQLRsrvGFVFQQFNLYAHLTAS 118
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPLSDWSAAELARHR---AYLSQQQSPPFAMPVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 119 QNITLaleHVHGWKPLPAQERALA-LLEKVGMLEKAHHYPAELSGGQQQRVAIARALA-------SSPQIILFDEPTSAL 190
Cdd:COG4138 88 QYLAL---HQPAGASSEAVEQLLAqLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLqvwptinPEGQLLLLDEPMNSL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 544825118 191 DPEMIGEVLFVMKALAHSGITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQ 245
Cdd:COG4138 165 DVAQQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAE 219
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
16-218 |
2.44e-21 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 93.02 E-value: 2.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 16 FSHLEQASVEFRHVDKRygdhQVLNDINLTITPGEVVAILGPSGSGKSTLIRLIN---QLEPLSGGEILVDNKPTgrlsg 92
Cdd:PLN03211 65 LGHKPKISDETRQIQER----TILNGVTGMASPGEILAVLGPSGSGKSTLLNALAgriQGNNFTGTILANNRKPT----- 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 93 sglRQLRSRVGFVFQQFNLYAHLTASQNITL-ALEHVHgwKPLPAQERALAL--------LEKVGMLEKAHHYPAELSGG 163
Cdd:PLN03211 136 ---KQILKRTGFVTQDDILYPHLTVRETLVFcSLLRLP--KSLTKQEKILVAesviselgLTKCENTIIGNSFIRGISGG 210
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 544825118 164 QQQRVAIARALASSPQIILFDEPTSALDPEMIGEVLFVMKALAHSGITMIVVTHE 218
Cdd:PLN03211 211 ERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQ 265
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
34-243 |
3.48e-21 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 88.35 E-value: 3.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 34 GDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLI--NQLEPLSGGEILVDNkptgrlsgsglrqlrsrvgfvfqqfnl 111
Cdd:cd03217 11 GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTImgHPKYEVTEGEILFKG--------------------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 112 yahltasQNITlalehvhgwkPLPAQERALAlleKVGMlekAHHYPAE----------------LSGGQQQRVAIARALA 175
Cdd:cd03217 64 -------EDIT----------DLPPEERARL---GIFL---AFQYPPEipgvknadflryvnegFSGGEKKRNEILQLLL 120
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 544825118 176 SSPQIILFDEPTSALDP---EMIGEVLfvmKALAHSGITMIVVTHEMQFAREI-ADRIVFIDGGHILETAPP 243
Cdd:cd03217 121 LEPDLAILDEPDSGLDIdalRLVAEVI---NKLREEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGDK 189
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
20-243 |
4.26e-21 |
|
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: 88.24 E-value: 4.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 20 EQASVEFRHVDKRYGDH--QVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTgrlSGSGLRQ 97
Cdd:cd03369 3 EHGEIEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDI---STIPLED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 98 LRSRVGFVFQQFNLYAHlTASQNITLALEHVHgwkplpAQERAlALLEKVGMLekahhypaELSGGQQQRVAIARALASS 177
Cdd:cd03369 80 LRSSLTIIPQDPTLFSG-TIRSNLDPFDEYSD------EEIYG-ALRVSEGGL--------NLSQGQRQLLCLARALLKR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 544825118 178 PQIILFDEPTSALDPEMIGEVLFVMKALaHSGITMIVVTHEMqfaREIA--DRIVFIDGGHILETAPP 243
Cdd:cd03369 144 PRVLVLDEATASIDYATDALIQKTIREE-FTNSTILTIAHRL---RTIIdyDKILVMDAGEVKEYDHP 207
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
35-217 |
9.20e-21 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 86.05 E-value: 9.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 35 DHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEIlvdNKPTGrlsgsglrqlrSRVGFVFQqfnlyah 114
Cdd:cd03223 13 GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI---GMPEG-----------EDLLFLPQ------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 115 ltasqnitlalehvhgwKP-LPAqeralallekvGMLEKAHHYP--AELSGGQQQRVAIARALASSPQIILFDEPTSALD 191
Cdd:cd03223 72 -----------------RPyLPL-----------GTLREQLIYPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALD 123
|
170 180
....*....|....*....|....*.
gi 544825118 192 PEMIGEVLFVMKALahsGITMIVVTH 217
Cdd:cd03223 124 EESEDRLYQLLKEL---GITVISVGH 146
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
34-217 |
9.39e-21 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 87.24 E-value: 9.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 34 GDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPtgrlsgSGLRQLRSRVGFVFQQFNLYA 113
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGD------IDDPDVAEACHYLGHRNAMKP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 114 HLTASQNITLalehvhgWKPLPAQE--RALALLEKVGMLEKAHHYPAELSGGQQQRVAIARALASSPQIILFDEPTSALD 191
Cdd:PRK13539 87 ALTVAENLEF-------WAAFLGGEelDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALD 159
|
170 180
....*....|....*....|....*.
gi 544825118 192 PEMIGEVLFVMKALAHSGITMIVVTH 217
Cdd:PRK13539 160 AAAVALFAELIRAHLAQGGIVIAATH 185
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
25-234 |
3.92e-20 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 89.46 E-value: 3.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 25 EFRHVDKRygDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKptgRLS-GSGLRQLRSRVG 103
Cdd:PRK09700 267 EVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGK---DISpRSPLDAVKKGMA 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 104 FV---------FQQFNLYAHLTASQNITLAlehvhGWKPL-----PAQERALALLEKVGMLEKAHHYP---AELSGGQQQ 166
Cdd:PRK09700 342 YItesrrdngfFPNFSIAQNMAISRSLKDG-----GYKGAmglfhEVDEQRTAENQRELLALKCHSVNqniTELSGGNQQ 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 544825118 167 RVAIARALASSPQIILFDEPTSALDPEMIGEVLFVMKALAHSGITMIVVTHEMQFAREIADRI-VFIDG 234
Cdd:PRK09700 417 KVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIaVFCEG 485
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
24-244 |
4.03e-20 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 89.80 E-value: 4.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 24 VEFRHVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVdnkpTGRLSGSGLRQLRSRVG 103
Cdd:NF033858 267 IEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWL----FGQPVDAGDIATRRRVG 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 104 FVFQQFNLYAHLTASQNITL--ALEHvhgwkpLPAQE---RALALLEKVGMLEKAHHYPAELSGGQQQRVAIARALASSP 178
Cdd:NF033858 343 YMSQAFSLYGELTVRQNLELhaRLFH------LPAAEiaaRVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKP 416
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 544825118 179 QIILFDEPTSALDP-------EMIGEvlfvmkaLA-HSGITMIVVTHEMQFArEIADRIVFIDGGHILETAPPA 244
Cdd:NF033858 417 ELLILDEPTSGVDPvardmfwRLLIE-------LSrEDGVTIFISTHFMNEA-ERCDRISLMHAGRVLASDTPA 482
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
34-243 |
6.85e-20 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 85.89 E-value: 6.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 34 GDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLI--NQLEPLSGGEILVDNK------PTGRlSGSGLrqlrsrvGFV 105
Cdd:COG0396 11 EGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmgHPKYEVTSGSILLDGEdilelsPDER-ARAGI-------FLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 106 FQQ---------FNLyahltasqnITLALEHVHGwKPLPAQE---RALALLEKVGMLEK-AHHYPAE-LSGGQQQRVAIA 171
Cdd:COG0396 83 FQYpveipgvsvSNF---------LRTALNARRG-EELSAREflkLLKEKMKELGLDEDfLDRYVNEgFSGGEKKRNEIL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 544825118 172 RALASSPQIILFDEPTSALDPEMIGEVLFVMKALAHSGITMIVVTHEMQFAREI-ADRIVFIDGGHILETAPP 243
Cdd:COG0396 153 QMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITHYQRILDYIkPDFVHVLVDGRIVKSGGK 225
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
19-191 |
1.25e-19 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 85.17 E-value: 1.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 19 LEQASVEFrhvdkryGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEplsggeilvdnKPTgrlSGSGLRQL 98
Cdd:PRK09544 7 LENVSVSF-------GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLV-----------APD---EGVIKRNG 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 99 RSRVGFVFQQFNLYAH--LTASQNITLAlEHVHGWKPLPAQERALAllekvgmlEKAHHYPAE-LSGGQQQRVAIARALA 175
Cdd:PRK09544 66 KLRIGYVPQKLYLDTTlpLTVNRFLRLR-PGTKKEDILPALKRVQA--------GHLIDAPMQkLSGGETQRVLLARALL 136
|
170
....*....|....*.
gi 544825118 176 SSPQIILFDEPTSALD 191
Cdd:PRK09544 137 NRPQLLVLDEPTQGVD 152
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
28-252 |
1.28e-19 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 85.65 E-value: 1.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 28 HVDKRYgdHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSG--------GEILVDNKPTGRLSGSGLRQLR 99
Cdd:PRK13547 8 HVARRH--RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGaprgarvtGDVTLNGEPLAAIDAPRLARLR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 100 ------SRVGFVFQQFNL-----YAHLTASQnitlALEHVHGwkplpaqERALALLEKVGMLEKAHHYPAELSGGQQQRV 168
Cdd:PRK13547 86 avlpqaAQPAFAFSAREIvllgrYPHARRAG----ALTHRDG-------EIAWQALALAGATALVGRDVTTLSGGELARV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 169 AIARALA---------SSPQIILFDEPTSALDPEMIGEVLFVMKALA---HSGITMIVvtHEMQFAREIADRIVFIDGGH 236
Cdd:PRK13547 155 QFARVLAqlwpphdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLArdwNLGVLAIV--HDPNLAARHADRIAMLADGA 232
|
250
....*....|....*.
gi 544825118 237 ILETAPPAQFFsQPAH 252
Cdd:PRK13547 233 IVAHGAPADVL-TPAH 247
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
34-191 |
4.43e-19 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 82.54 E-value: 4.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 34 GDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSGSGLRQLrsrvgfvfqqfnLY- 112
Cdd:PRK13538 12 DERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDL------------LYl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 113 AH-------LTASQNITLALeHVHGwkpLPAQERALALLEKVGmLEKAHHYPAE-LSGGQQQRVAIARALASSPQIILFD 184
Cdd:PRK13538 80 GHqpgikteLTALENLRFYQ-RLHG---PGDDEALWEALAQVG-LAGFEDVPVRqLSAGQQRRVALARLWLTRAPLWILD 154
|
....*..
gi 544825118 185 EPTSALD 191
Cdd:PRK13538 155 EPFTAID 161
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
33-248 |
8.40e-19 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 83.50 E-value: 8.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 33 YGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSGsglRQLRSRVGFVFQQFNLY 112
Cdd:PRK10253 17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYAS---KEVARRIGLLAQNATTP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 113 AHLTAsQNITLALEHVHgwKPL-----PAQERALA-LLEKVGMLEKAHHYPAELSGGQQQRVAIARALASSPQIILFDEP 186
Cdd:PRK10253 94 GDITV-QELVARGRYPH--QPLftrwrKEDEEAVTkAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 544825118 187 TSALDPEMIGEVLFVMKALAHS-GITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQFFS 248
Cdd:PRK10253 171 TTWLDISHQIDLLELLSELNREkGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVT 233
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
37-234 |
3.03e-18 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 81.30 E-value: 3.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 37 QVLNDINLTITPG-----EVVAILGPSGSGKSTLIRLI-NQLEPlSGGEILVDN-----KP---TGRLSGSgLRQLRSRV 102
Cdd:cd03237 8 KTLGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLaGVLKP-DEGDIEIELdtvsyKPqyiKADYEGT-VRDLLSSI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 103 gfvfqqfnLYAHLTASQNITLALehvhgwKPLPaqeralalLEKVgmLEKAhhyPAELSGGQQQRVAIARALASSPQIIL 182
Cdd:cd03237 86 --------TKDFYTHPYFKTEIA------KPLQ--------IEQI--LDRE---VPELSGGELQRVAIAACLSKDADIYL 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 544825118 183 FDEPTSALDPEMIGEVLFVMKALA-HSGITMIVVTHEMQFAREIADRIVFIDG 234
Cdd:cd03237 139 LDEPSAYLDVEQRLMASKVIRRFAeNNEKTAFVVEHDIIMIDYLADRLIVFEG 191
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
29-235 |
3.46e-18 |
|
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: 79.98 E-value: 3.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 29 VDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLS--GGEILVDNKPTGrlsgsglRQLRSRVGFVF 106
Cdd:cd03232 13 VPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGRPLD-------KNFQRSTGYVE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 107 QQfnlYAHLtASQNITLALEhvhgwkpLPAQERALALlekvgmlekahhypaelsgGQQQRVAIARALASSPQIILFDEP 186
Cdd:cd03232 86 QQ---DVHS-PNLTVREALR-------FSALLRGLSV-------------------EQRKRLTIGVELAAKPSILFLDEP 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 544825118 187 TSALDPEMIGEVLFVMKALAHSGITMIVVTHemQFAREIA---DRIVFIDGG 235
Cdd:cd03232 136 TSGLDSQAAYNIVRFLKKLADSGQAILCTIH--QPSASIFekfDRLLLLKRG 185
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
18-243 |
5.29e-18 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 83.67 E-value: 5.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 18 HLEQA-SVEFRHVDKRY--GDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGrlsGSG 94
Cdd:PTZ00243 1302 HPVQAgSLVFEGVQMRYreGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIG---AYG 1378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 95 LRQLRSRVGFVFQQFNLYAHlTASQNITLALEhvhgwkplPAQERALALLEKVGMLEkahHYPAELSG------------ 162
Cdd:PTZ00243 1379 LRELRRQFSMIPQDPVLFDG-TVRQNVDPFLE--------ASSAEVWAALELVGLRE---RVASESEGidsrvleggsny 1446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 163 --GQQQRVAIARA-LASSPQIILFDEPTSALDPEMIGEV-LFVMKALahSGITMIVVTHEMQFAREIaDRIVFIDGGHIL 238
Cdd:PTZ00243 1447 svGQRQLMCMARAlLKKGSGFILMDEATANIDPALDRQIqATVMSAF--SAYTVITIAHRLHTVAQY-DKIIVMDHGAVA 1523
|
....*
gi 544825118 239 ETAPP 243
Cdd:PTZ00243 1524 EMGSP 1528
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
34-239 |
7.46e-18 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 83.25 E-value: 7.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 34 GDHQVLNDINLTITPGEVVAILGPSGSGKSTLIR-LINQLEPLSGGEILvdnkptgrlsgsglrqLRSRVGFVFQQ---F 109
Cdd:PLN03130 628 AERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVV----------------IRGTVAYVPQVswiF 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 110 NLyahlTASQNITLAL--EHVHGWKPL--PAQERALALLEKvGMLEKAHHYPAELSGGQQQRVAIARALASSPQIILFDE 185
Cdd:PLN03130 692 NA----TVRDNILFGSpfDPERYERAIdvTALQHDLDLLPG-GDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDD 766
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 544825118 186 PTSALDPEMIGEVLFVMKALAHSGITMIVVTHEMQFAREIaDRIVFIDGGHILE 239
Cdd:PLN03130 767 PLSALDAHVGRQVFDKCIKDELRGKTRVLVTNQLHFLSQV-DRIILVHEGMIKE 819
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
28-236 |
6.31e-17 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 79.98 E-value: 6.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 28 HVDKRY-GDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVdnkptgrlsgsglrQLRSRVGFVF 106
Cdd:TIGR03719 9 RVSKVVpPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARP--------------QPGIKVGYLP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 107 QQFNLYAHLTASQNITLALEHVHGwkplpAQER------ALA--------LLEKVGMLE------KAHHY---------- 156
Cdd:TIGR03719 75 QEPQLDPTKTVRENVEEGVAEIKD-----ALDRfneisaKYAepdadfdkLAAEQAELQeiidaaDAWDLdsqleiamda 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 157 ---P------AELSGGQQQRVAIARALASSPQIILFDEPTSALDPEmigEVLFVMKALAHSGITMIVVTHEMQFAREIAD 227
Cdd:TIGR03719 150 lrcPpwdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAE---SVAWLERHLQEYPGTVVAVTHDRYFLDNVAG 226
|
....*....
gi 544825118 228 RIVFIDGGH 236
Cdd:TIGR03719 227 WILELDRGR 235
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
31-237 |
6.81e-17 |
|
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: 76.92 E-value: 6.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 31 KRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLI-NQLEPLSG--GEILVDNKPtgrlSGSGLRQLRSRVGFVFQ 107
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALaNRTEGNVSveGDIHYNGIP----YKEFAEKYPGEIIYVSE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 108 QFNLYAHLTASQNITLALEHvhgwkplpaqeralallekvgmleKAHHYPAELSGGQQQRVAIARALASSPQIILFDEPT 187
Cdd:cd03233 91 EDVHFPTLTVRETLDFALRC------------------------KGNEFVRGISGGERKRVSIAEALVSRASVLCWDNST 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 544825118 188 SALDPEMIGEVLFVMKALAHS--GITMIVVTHEMQFAREIADRIVFIDGGHI 237
Cdd:cd03233 147 RGLDSSTALEILKCIRTMADVlkTTTFVSLYQASDEIYDLFDKVLVLYEGRQ 198
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
41-237 |
6.92e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 79.71 E-value: 6.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 41 DINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKptgRLSGSGLRQlRSRVGFVF-----QQFNLYAHL 115
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGK---EINALSTAQ-RLARGLVYlpedrQSSGLYLDA 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 116 TASQNITLALEHVHGWKPLPAQERALallekvgmLEKAHH----------YPAE-LSGGQQQRVAIARALASSPQIILFD 184
Cdd:PRK15439 357 PLAWNVCALTHNRRGFWIKPARENAV--------LERYRRalnikfnhaeQAARtLSGGNQQKVLIAKCLEASPQLLIVD 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 544825118 185 EPTSALDPEMIGEVLFVMKALAHSGITMIVVTHEMQFAREIADRIVFIDGGHI 237
Cdd:PRK15439 429 EPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
34-242 |
8.37e-17 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 79.99 E-value: 8.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 34 GDHQVLNDINLTITPGEVVAILGPSGSGKSTLIR-LINQLEPLSGGEilvdnkptgrlsgsglrQLRSRVGFVFQQFNLy 112
Cdd:TIGR00957 649 DLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDKVEGHV-----------------HMKGSVAYVPQQAWI- 710
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 113 ahltasQNITLAlEHVHGWKPL-----PAQERALALLEKVGML---------EKAhhypAELSGGQQQRVAIARALASSP 178
Cdd:TIGR00957 711 ------QNDSLR-ENILFGKALnekyyQQVLEACALLPDLEILpsgdrteigEKG----VNLSGGQKQRVSLARAVYSNA 779
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 544825118 179 QIILFDEPTSALDPEmIGEVLFvMKALAHSGI----TMIVVTHEMQFAREIaDRIVFIDGGHILETAP 242
Cdd:TIGR00957 780 DIYLFDDPLSAVDAH-VGKHIF-EHVIGPEGVlknkTRILVTHGISYLPQV-DVIIVMSGGKISEMGS 844
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
24-249 |
8.53e-17 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 79.99 E-value: 8.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 24 VEFRHVDKRY--GDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLsgsGLRQLRSR 101
Cdd:TIGR00957 1285 VEFRNYCLRYreDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKI---GLHDLRFK 1361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 102 VGFVFQ---------QFNLYAHLTAS-QNITLALE--HVHGW-KPLPAqeralallekvgmleKAHHYPAE----LSGGQ 164
Cdd:TIGR00957 1362 ITIIPQdpvlfsgslRMNLDPFSQYSdEEVWWALElaHLKTFvSALPD---------------KLDHECAEggenLSVGQ 1426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 165 QQRVAIARALASSPQIILFDEPTSALDPEMIGEVLFVMKAlAHSGITMIVVTHEMQfarEIAD--RIVFIDGGHILETAP 242
Cdd:TIGR00957 1427 RQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRT-QFEDCTVLTIAHRLN---TIMDytRVIVLDKGEVAEFGA 1502
|
....*..
gi 544825118 243 PAQFFSQ 249
Cdd:TIGR00957 1503 PSNLLQQ 1509
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
20-236 |
2.47e-16 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 78.13 E-value: 2.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 20 EQASVEFRHVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSggeilVDNKPT--GRLSGSG--L 95
Cdd:PRK10938 257 NEPRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPQG-----YSNDLTlfGRRRGSGetI 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 96 RQLRSRVGFVFQQFNL-YAHLTASQNITLA--LEHVHGWKPLPAQERALAL--LEKVGMLEKAHHYP-AELSGGQQQRVA 169
Cdd:PRK10938 332 WDIKKHIGYVSSSLHLdYRVSTSVRNVILSgfFDSIGIYQAVSDRQQKLAQqwLDILGIDKRTADAPfHSLSWGQQRLAL 411
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 544825118 170 IARALASSPQIILFDEPTSALDPemIGEVL---FVMKALAHSGITMIVVTHEMQFARE-IADRIVFI-DGGH 236
Cdd:PRK10938 412 IVRALVKHPTLLILDEPLQGLDP--LNRQLvrrFVDVLISEGETQLLFVSHHAEDAPAcITHRLEFVpDGDI 481
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
24-234 |
3.23e-16 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 77.90 E-value: 3.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 24 VEFRHVDKRYGDHQvlndinLTITPG-----EVVAILGPSGSGKSTLIRLI-NQLEPLSG---GEILVDNKPtgrlsgsg 94
Cdd:COG1245 342 VEYPDLTKSYGGFS------LEVEGGeiregEVLGIVGPNGIGKTTFAKILaGVLKPDEGevdEDLKISYKP-------- 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 95 lrQ-LRSRVGFVFQQFnLYAHLTASQNITLALEHVhgWKPLpaqeralaLLEKvgMLEKahhYPAELSGGQQQRVAIARA 173
Cdd:COG1245 408 --QyISPDYDGTVEEF-LRSANTDDFGSSYYKTEI--IKPL--------GLEK--LLDK---NVKDLSGGELQRVAIAAC 469
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 544825118 174 LASSPQIILFDEPTSALDPEmigEVLFVMKALAH----SGITMIVVTHEMQFAREIADRIVFIDG 234
Cdd:COG1245 470 LSRDADLYLLDEPSAHLDVE---QRLAVAKAIRRfaenRGKTAMVVDHDIYLIDYISDRLMVFEG 531
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
23-238 |
1.41e-15 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 75.54 E-value: 1.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 23 SVEFRHVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGE-----ILVDNKPTGRLSGSGLRQ 97
Cdd:NF000106 13 AVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPDAGRRpwrf*TWCANRRALRRTIG*HRP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 98 LR--SRVGFVFQQfNLYahlTASQNITLALEHvhgwkplpAQERALALLEKVGMLEKAHHYPAELSGGQQQRVAIARALA 175
Cdd:NF000106 93 VR*gRRESFSGRE-NLY---MIGR*LDLSRKD--------ARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 544825118 176 SSPQIILFDEPTSALDPEMIGEVLFVMKALAHSGITMIVVTHEMQFAREIADRIVFIDGGHIL 238
Cdd:NF000106 161 GRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVI 223
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
39-247 |
2.22e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 75.78 E-value: 2.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 39 LNDINLTITPGEVVAILGPSGSGKSTLIR-LINQLEPLSGGEILVdnkptgrlsgsglrqlRSRVGFVfQQFNLYAHLTA 117
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVI----------------RGSVAYV-PQVSWIFNATV 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 118 SQNITLA--LEHVHGWKPL--PAQERALALLEKVGMLEKAHHyPAELSGGQQQRVAIARALASSPQIILFDEPTSALDPE 193
Cdd:PLN03232 696 RENILFGsdFESERYWRAIdvTALQHDLDLLPGRDLTEIGER-GVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAH 774
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 544825118 194 MIGEVLFVMKALAHSGITMIVVTHEMQFAREIaDRIVFIDGGHILETAPPAQFF 247
Cdd:PLN03232 775 VAHQVFDSCMKDELKGKTRVLVTNQLHFLPLM-DRIILVSEGMIKEEGTFAELS 827
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
27-242 |
2.66e-15 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 75.15 E-value: 2.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 27 RHVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSGSglRQLRSRVGFVF 106
Cdd:PRK10982 2 SNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSK--EALENGISMVH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 107 QQFNLYAHLTASQNITLALEHVHGW-----KPLPAQERALALLE-KVGMLEKAhhypAELSGGQQQRVAIARALASSPQI 180
Cdd:PRK10982 80 QELNLVLQRSVMDNMWLGRYPTKGMfvdqdKMYRDTKAIFDELDiDIDPRAKV----ATLSVSQMQMIEIAKAFSYNAKI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 544825118 181 ILFDEPTSALDPEMIGEVLFVMKALAHSGITMIVVTHEMQFAREIADRIVFIDGGHILETAP 242
Cdd:PRK10982 156 VIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQP 217
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
24-234 |
2.75e-15 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 75.23 E-value: 2.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 24 VEFRHVDKRYGDHQvLNDINLTITPGEVVAILGPSGSGKSTLIRLIN-QLEPLSG---GEILVDNKP-------TGRLSg 92
Cdd:PRK13409 341 VEYPDLTKKLGDFS-LEVEGGEIYEGEVIGIVGPNGIGKTTFAKLLAgVLKPDEGevdPELKISYKPqyikpdyDGTVE- 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 93 SGLRQLRSRVG--FVFQQFNlyahltasqnitlalehvhgwKPLpaqeralaLLEKvgMLEKahhYPAELSGGQQQRVAI 170
Cdd:PRK13409 419 DLLRSITDDLGssYYKSEII---------------------KPL--------QLER--LLDK---NVKDLSGGELQRVAI 464
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 544825118 171 ARALASSPQIILFDEPTSALDPEmigEVLFVMKALAH----SGITMIVVTHEMQFAREIADRIVFIDG 234
Cdd:PRK13409 465 AACLSRDADLYLLDEPSAHLDVE---QRLAVAKAIRRiaeeREATALVVDHDIYMIDYISDRLMVFEG 529
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
39-237 |
3.37e-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: 74.86 E-value: 3.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 39 LNDINLTITPGEVVAILGPSGSGKSTLIR-LINQLEPLSGGEILVDNKPTG-RLSGSGLRQL-------RSRVGFVFQqf 109
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQaLFGAYPGKFEGNVFINGKPVDiRNPAQAIRAGiamvpedRKRHGIVPI-- 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 110 nlyahLTASQNITLA-LEHVHGWKPLPAQERALALLEKVGMLEKAHHYP----AELSGGQQQRVAIARALASSPQIILFD 184
Cdd:TIGR02633 354 -----LGVGKNITLSvLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASPflpiGRLSGGNQQKAVLAKMLLTNPRVLILD 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 544825118 185 EPTSALDPEMIGEVLFVMKALAHSGITMIVVTHEMQFAREIADRIVFIDGGHI 237
Cdd:TIGR02633 429 EPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
24-245 |
4.07e-15 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 74.78 E-value: 4.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 24 VEFRHVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVdnkptgrLSGS-----GLRQL 98
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEV-------LGGDmadarHRRAV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 99 RSRVGFVFQQF--NLYAHLTASQNI----TLalehvHGwkpLPAQERA---LALLEKVGMLEKAHHyPA-ELSGGQQQRV 168
Cdd:NF033858 75 CPRIAYMPQGLgkNLYPTLSVFENLdffgRL-----FG---QDAAERRrriDELLRATGLAPFADR-PAgKLSGGMKQKL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 169 AIARALASSPQIILFDEPTSALDP-------EMIGEvlfvMKAlAHSGITMIVVTHEMQFArEIADRIVFIDGGHILETA 241
Cdd:NF033858 146 GLCCALIHDPDLLILDEPTTGVDPlsrrqfwELIDR----IRA-ERPGMSVLVATAYMEEA-ERFDWLVAMDAGRVLATG 219
|
....
gi 544825118 242 PPAQ 245
Cdd:NF033858 220 TPAE 223
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
18-250 |
6.51e-15 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 72.27 E-value: 6.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 18 HLEQASVEFRhvdkrygdhqvLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPlSGGEILVDNKPTGRLSGSGLRQ 97
Cdd:PRK03695 2 QLNDVAVSTR-----------LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQPLEAWSAAELAR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 98 LR------SRVGF---VFQQFNLyaHLTASQNITLALEHVHgwkplpaqeralALLEKVGMLEKAHHYPAELSGGQQQRV 168
Cdd:PRK03695 70 HRaylsqqQTPPFampVFQYLTL--HQPDKTRTEAVASALN------------EVAEALGLDDKLGRSVNQLSGGEWQRV 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 169 AIA-------RALASSPQIILFDEPTSALDPEMIGEVLFVMKALAHSGITMIVVTHEMQFAREIADRIVFIDGGHILETA 241
Cdd:PRK03695 136 RLAavvlqvwPDINPAGQLLLLDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASG 215
|
....*....
gi 544825118 242 PPAQFFSQP 250
Cdd:PRK03695 216 RRDEVLTPE 224
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
24-234 |
7.42e-15 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 73.82 E-value: 7.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 24 VEFRHVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVdnkptgrlsGSGLrqlrsRVG 103
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI---------GETV-----KLA 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 104 FVFQQfnlYAHLTASQN----ITLALEHVH-GWKPLPA-------------QERalalleKVGmlekahhypaELSGGQQ 165
Cdd:TIGR03719 389 YVDQS---RDALDPNKTvweeISGGLDIIKlGKREIPSrayvgrfnfkgsdQQK------KVG----------QLSGGER 449
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 544825118 166 QRVAIARALASSPQIILFDEPTSALDPEmigevlfVMKAL-----AHSGITMiVVTHEMQFAREIADRIVFIDG 234
Cdd:TIGR03719 450 NRVHLAKTLKSGGNVLLLDEPTNDLDVE-------TLRALeeallNFAGCAV-VISHDRWFLDRIATHILAFEG 515
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
38-217 |
1.22e-14 |
|
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: 73.24 E-value: 1.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 38 VLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKptGRL------SGSGLRQLRSRVGFVFQQFNL 111
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAK--GKLfyvpqrPYMTLGTLRDQIIYPDSSEDM 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 112 YAHLTASQNITLALEHVHgwkplpaqeraLA-LLEKVGMLEKAHHYPAELSGGQQQRVAIARALASSPQIILFDEPTSAL 190
Cdd:TIGR00954 545 KRRGLSDKDLEQILDNVQ-----------LThILEREGGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAV 613
|
170 180
....*....|....*....|....*..
gi 544825118 191 DPEMIGevlFVMKALAHSGITMIVVTH 217
Cdd:TIGR00954 614 SVDVEG---YMYRLCREFGITLFSVSH 637
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
35-217 |
1.28e-14 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 71.03 E-value: 1.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 35 DHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSgsglrqlRSR-VGFVFQQFNLYA 113
Cdd:PRK13543 23 EEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGD-------RSRfMAYLGHLPGLKA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 114 HLTASQNITLaLEHVHGWKPLPAQERALALlekVGMLEKAHHYPAELSGGQQQRVAIARALASSPQIILFDEPTSALDPE 193
Cdd:PRK13543 96 DLSTLENLHF-LCGLHGRRAKQMPGSALAI---VGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLE 171
|
170 180
....*....|....*....|....
gi 544825118 194 MIGEVLFVMKALAHSGITMIVVTH 217
Cdd:PRK13543 172 GITLVNRMISAHLRGGGAALVTTH 195
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
15-191 |
1.35e-14 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 73.52 E-value: 1.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 15 DFSHLEQASVEFrHVDKRyGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNkpTGRLSGSG 94
Cdd:PTZ00265 379 DIKKIQFKNVRF-HYDTR-KDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIND--SHNLKDIN 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 95 LRQLRSRVGFVFQQFNLYAHlTASQNITLALEHVHGWKPLPAQ----------------------ERALALLEKV----G 148
Cdd:PTZ00265 455 LKWWRSKIGVVSQDPLLFSN-SIKNNIKYSLYSLKDLEALSNYynedgndsqenknkrnscrakcAGDLNDMSNTtdsnE 533
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 544825118 149 MLEKAHHY-----------------------------------PAELSGGQQQRVAIARALASSPQIILFDEPTSALD 191
Cdd:PTZ00265 534 LIEMRKNYqtikdsevvdvskkvlihdfvsalpdkyetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
45-219 |
2.01e-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: 72.51 E-value: 2.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 45 TITPGEVVAILGPSGSGKSTLIRLinqlepLSGGEI----LVDNKPT-----GRLSGSGLrqlrsrvgfvfqqfnlYAHL 115
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKSTALKI------LSGELKpnlgDYDEEPSwdevlKRFRGTEL----------------QDYF 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 116 T--ASQNITLALehvhgwKP-----LP-------------AQERALA--LLEKVGMLEKAHHYPAELSGGQQQRVAIARA 173
Cdd:COG1245 153 KklANGEIKVAH------KPqyvdlIPkvfkgtvrellekVDERGKLdeLAEKLGLENILDRDISELSGGELQRVAIAAA 226
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 544825118 174 LASSPQIILFDEPTSALDpemIGEVLFVMKA---LAHSGITMIVVTHEM 219
Cdd:COG1245 227 LLRDADFYFFDEPSSYLD---IYQRLNVARLireLAEEGKYVLVVEHDL 272
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
39-235 |
3.12e-14 |
|
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: 70.05 E-value: 3.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 39 LNDINLTITPGEVVAILGPSGSGKSTLI-RLINQLEPLSGGEILVDNKPTGRLSGSGLRQLRSRVGFVFQQFNLYaHLTA 117
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPWLL-NATV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 118 SQNITLAlehvhgwKPLPAQeRALALLEKVGMLEKAHHYP-----------AELSGGQQQRVAIARALASSPQIILFDEP 186
Cdd:cd03290 96 EENITFG-------SPFNKQ-RYKAVTDACSLQPDIDLLPfgdqteigergINLSGGQRQRICVARALYQNTNIVFLDDP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 544825118 187 TSALDPEMIGEVL--FVMKALAHSGITMIVVTHEMQFAREiADRIVFIDGG 235
Cdd:cd03290 168 FSALDIHLSDHLMqeGILKFLQDDKRTLVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
23-249 |
3.28e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 72.32 E-value: 3.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 23 SVEFRHVDKRY--GDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLsgsGLRQLRS 100
Cdd:PLN03232 1234 SIKFEDVHLRYrpGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKF---GLTDLRR 1310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 101 RVGFVFQQFNLYAHlTASQNITLALEHVHG--WKPLP-AQERALALLEKVGMLEKAHHYPAELSGGQQQRVAIARALASS 177
Cdd:PLN03232 1311 VLSIIPQSPVLFSG-TVRFNIDPFSEHNDAdlWEALErAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRR 1389
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 544825118 178 PQIILFDEPTSALDPEMIGEVLFVMKALAHSgITMIVVTHEMQFAREiADRIVFIDGGHILETAPPAQFFSQ 249
Cdd:PLN03232 1390 SKILVLDEATASVDVRTDSLIQRTIREEFKS-CTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSR 1459
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
23-248 |
3.66e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 72.08 E-value: 3.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 23 SVEFRHVDKRYGDH--QVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLsgsGLRQLRS 100
Cdd:PLN03130 1237 SIKFEDVVLRYRPElpPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKF---GLMDLRK 1313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 101 RVGFVFQQFNLYAHlTASQNITLALEH--VHGWKPLpaqERA----------LALLEKVgmLEKAHHYpaelSGGQQQRV 168
Cdd:PLN03130 1314 VLGIIPQAPVLFSG-TVRFNLDPFNEHndADLWESL---ERAhlkdvirrnsLGLDAEV--SEAGENF----SVGQRQLL 1383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 169 AIARALASSPQIILFDEPTSALDpemIGEVLFVMKALAHS--GITMIVVTHEMQFAREiADRIVFIDGGHILETAPPAQF 246
Cdd:PLN03130 1384 SLARALLRRSKILVLDEATAAVD---VRTDALIQKTIREEfkSCTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPENL 1459
|
..
gi 544825118 247 FS 248
Cdd:PLN03130 1460 LS 1461
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
38-237 |
6.31e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 71.11 E-value: 6.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 38 VLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEP-LSGGEILVDNKP-TGRLSGSGLRQL-------RSRVGFVFQq 108
Cdd:PRK13549 277 RVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPvKIRNPQQAIAQGiamvpedRKRDGIVPV- 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 109 fnlyahLTASQNITLA-LEHVHGWKPLPAQERALALLEKVGMLE-KAHHyP----AELSGGQQQRVAIARALASSPQIIL 182
Cdd:PRK13549 356 ------MGVGKNITLAaLDRFTGGSRIDDAAELKTILESIQRLKvKTAS-PelaiARLSGGNQQKAVLAKCLLLNPKILI 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 544825118 183 FDEPTSALDpemIG---EVLFVMKALAHSGITMIVVTHEMQFAREIADRIVFIDGGHI 237
Cdd:PRK13549 429 LDEPTRGID---VGakyEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
39-239 |
6.40e-14 |
|
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: 68.12 E-value: 6.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 39 LNDINLTITPGEVVAILGPSGSGKSTLIrliNQLEPLSGGEILVDNKPTgrlsgsglrqlrsrvgfvfqqfnlyahltAS 118
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLV---NEGLYASGKARLISFLPK-----------------------------FS 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 119 QNITLALEHvhgwkplpaqeraLALLEKVGM----LEKAhhyPAELSGGQQQRVAIARALASSPQ--IILFDEPTSALDP 192
Cdd:cd03238 59 RNKLIFIDQ-------------LQFLIDVGLgyltLGQK---LSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQ 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 544825118 193 EMIGEVLFVMKALAHSGITMIVVTHEMQFAREiADRIVFI------DGGHILE 239
Cdd:cd03238 123 QDINQLLEVIKGLIDLGNTVILIEHNLDVLSS-ADWIIDFgpgsgkSGGKVVF 174
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
39-237 |
8.26e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 70.80 E-value: 8.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 39 LNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKP-TGRLSGSGLR-------QLRSRVGFVFQqfn 110
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEvVTRSPQDGLAngivyisEDRKRDGLVLG--- 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 111 lyahLTASQNITL-ALEHV-HGWKPLPAQERALALLEKVGM-------LEKAhhyPAELSGGQQQRVAIARALASSPQII 181
Cdd:PRK10762 345 ----MSVKENMSLtALRYFsRAGGSLKHADEQQAVSDFIRLfniktpsMEQA---IGLLSGGNQQKVAIARGLMTRPKVL 417
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 544825118 182 LFDEPTSALDPEMIGEVLFVMKALAHSGITMIVVTHEMQFAREIADRIVFIDGGHI 237
Cdd:PRK10762 418 ILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
34-220 |
1.12e-13 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 69.11 E-value: 1.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 34 GDHQVLNDINLTITPGEVVAILGPSGSGKSTL----IRLINqleplSGGEILVDNKPTGRLSgsgLRQLRSRVGFVFQQF 109
Cdd:cd03289 15 GGNAVLENISFSISPGQRVGLLGRTGSGKSTLlsafLRLLN-----TEGDIQIDGVSWNSVP---LQKWRKAFGVIPQKV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 110 NLYahltaSQNITLALEHVHGWKplpaQERALALLEKVGMLEKAHHYPAE-----------LSGGQQQRVAIARALASSP 178
Cdd:cd03289 87 FIF-----SGTFRKNLDPYGKWS----DEEIWKVAEEVGLKSVIEQFPGQldfvlvdggcvLSHGHKQLMCLARSVLSKA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 544825118 179 QIILFDEPTSALDPEMIGEVLFVMKAlAHSGITMIVVTHEMQ 220
Cdd:cd03289 158 KILLLDEPSAHLDPITYQVIRKTLKQ-AFADCTVILSEHRIE 198
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
24-193 |
1.30e-13 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 70.15 E-value: 1.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 24 VEFRHVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDnkPTGRLSgsglrqlrsrvg 103
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIG--ETVKLA------------ 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 104 FVFQQF-NLYAHLTASQNITLALEHVH-GWKPLPA-------------QERalalleKVGMlekahhypaeLSGGQQQRV 168
Cdd:PRK11819 391 YVDQSRdALDPNKTVWEEISGGLDIIKvGNREIPSrayvgrfnfkggdQQK------KVGV----------LSGGERNRL 454
|
170 180
....*....|....*....|....*
gi 544825118 169 AIARALASSPQIILFDEPTSALDPE 193
Cdd:PRK11819 455 HLAKTLKQGGNVLLLDEPTNDLDVE 479
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
39-243 |
2.08e-13 |
|
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: 68.02 E-value: 2.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 39 LNDINLTITPGEVVAILGPSGSGKSTLI----------RLINQLEP------LSGGE-----ILVDNKPTGRLSGSG--- 94
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLIndtlypalarRLHLKKEQpgnhdrIEGLEhidkvIVIDQSPIGRTPRSNpat 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 95 -------LRQLRSRV--GfvfQQFN------LYAHLTASQ--NITL--ALEHvhgWKPLPAQERALALLEKVGMlekahH 155
Cdd:cd03271 91 ytgvfdeIRELFCEVckG---KRYNretlevRYKGKSIADvlDMTVeeALEF---FENIPKIARKLQTLCDVGL-----G 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 156 Y-----PA-ELSGGQQQRVAIARAL---ASSPQIILFDEPTSALDPEMIGEVLFVMKALAHSGITMIVVTHEMQFAReIA 226
Cdd:cd03271 160 YiklgqPAtTLSGGEAQRIKLAKELskrSTGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIK-CA 238
|
250 260
....*....|....*....|....*
gi 544825118 227 DRIvfID--------GGHILETAPP 243
Cdd:cd03271 239 DWI--IDlgpeggdgGGQVVASGTP 261
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
29-236 |
2.55e-13 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 69.38 E-value: 2.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 29 VDKRYG-DHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEIlvdnkptgRLSgSGLRqlrsrVGFVFQ 107
Cdd:PRK11819 12 VSKVVPpKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEA--------RPA-PGIK-----VGYLPQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 108 QFNLYAHLTASQNITLALEHVHGwkplpAQER------ALA--------LLEKVGMLEK-------------------AH 154
Cdd:PRK11819 78 EPQLDPEKTVRENVEEGVAEVKA-----ALDRfneiyaAYAepdadfdaLAAEQGELQEiidaadawdldsqleiamdAL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 155 HYP------AELSGGQQQRVAIARALASSPQIILFDEPTSALDPEmigEVLFVMKALAHSGITMIVVTHEMQFAREIADR 228
Cdd:PRK11819 153 RCPpwdakvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAE---SVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGW 229
|
....*...
gi 544825118 229 IVFIDGGH 236
Cdd:PRK11819 230 ILELDRGR 237
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
38-235 |
2.85e-13 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 67.96 E-value: 2.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 38 VLNDINLTITPGEVVAILGPSGSGKSTLIRLI-NQLEPlSGGEIlvdnKPTGRLSGSglrqlrsrvgfvfQQFNLYAHLT 116
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLIlGELEP-SEGKI----KHSGRISFS-------------SQFSWIMPGT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 117 ASQNITLALEHvhgwkplpAQERALALLEKVGMLEKAHHYPAE-----------LSGGQQQRVAIARALASSPQIILFDE 185
Cdd:cd03291 114 IKENIIFGVSY--------DEYRYKSVVKACQLEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLDS 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 544825118 186 PTSALDPEMIGEVL--FVMKALAHSgiTMIVVTHEMQFAReIADRIVFIDGG 235
Cdd:cd03291 186 PFGYLDVFTEKEIFesCVCKLMANK--TRILVTSKMEHLK-KADKILILHEG 234
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
48-231 |
2.87e-13 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 65.86 E-value: 2.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 48 PGEVVAILGPSGSGKSTLIRLI-NQLEPLSGGEILVDnkptgrlsgsglrqlrsrvgfvfqqfnlyahltasqnitlale 126
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALaRELGPPGGGVIYID------------------------------------------- 37
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 127 hvhgwkplpaQERALALLEKVGMLEKAHHYPAELSGGQQQRVAIARALASSPQIILFDEPTSALDPEMIGEVLF------ 200
Cdd:smart00382 38 ----------GEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLleelrl 107
|
170 180 190
....*....|....*....|....*....|.
gi 544825118 201 VMKALAHSGITMIVVTHEMQFAREIADRIVF 231
Cdd:smart00382 108 LLLLKSEKNLTVILTTNDEKDLGPALLRRRF 138
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
24-237 |
2.98e-13 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 69.15 E-value: 2.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 24 VEFRHVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIR-LINQLEPLSGGEILVDNkptgrlsgsglrqlrSRV 102
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRtLVGELEPDSGTVKWSEN---------------ANI 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 103 GFvfqqfnlYAHLTAS---QNITLaLEHVHGWKPLPAQERALAllekvGML-------EKAHHYPAELSGGQQQRVAIAR 172
Cdd:PRK15064 385 GY-------YAQDHAYdfeNDLTL-FDWMSQWRQEGDDEQAVR-----GTLgrllfsqDDIKKSVKVLSGGEKGRMLFGK 451
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 544825118 173 ALASSPQIILFDEPTSALDPEMIgEVLFVmkALAHSGITMIVVTHEMQFAREIADRIVFIDGGHI 237
Cdd:PRK15064 452 LMMQKPNVLVMDEPTNHMDMESI-ESLNM--ALEKYEGTLIFVSHDREFVSSLATRIIEITPDGV 513
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
40-237 |
4.49e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 68.40 E-value: 4.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 40 NDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPtgrlsgsglRQLRS-----RVGFVF-----QQF 109
Cdd:PRK11288 270 EPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKP---------IDIRSprdaiRAGIMLcpedrKAE 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 110 NLYAHLTASQNITL-ALEHVHGWKPL--PAQERALALLEKVGMLEK---AHHYPAELSGGQQQRVAIARALASSPQIILF 183
Cdd:PRK11288 341 GIIPVHSVADNINIsARRHHLRAGCLinNRWEAENADRFIRSLNIKtpsREQLIMNLSGGNQQKAILGRWLSEDMKVILL 420
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 544825118 184 DEPTSALDPEMIGEVLFVMKALAHSGITMIVVTHEMQFAREIADRIVFIDGGHI 237
Cdd:PRK11288 421 DEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
34-240 |
1.59e-12 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 65.43 E-value: 1.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 34 GDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQlEP---LSGGEILVDNKPTGRLSGsglrQLRSRVGfVFQQFN 110
Cdd:CHL00131 18 NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG-HPaykILEGDILFKGESILDLEP----EERAHLG-IFLAFQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 111 LYAHLTASQNIT---LALEHVHGWKPLPAQErALALLE-------KVGMLEK-AHHYPAE-LSGGQQQRVAIARALASSP 178
Cdd:CHL00131 92 YPIEIPGVSNADflrLAYNSKRKFQGLPELD-PLEFLEiineklkLVGMDPSfLSRNVNEgFSGGEKKRNEILQMALLDS 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 544825118 179 QIILFDEPTSALDPEMIGEVLFVMKALAHSGITMIVVTHEMQFAREIA-DRIVFIDGGHILET 240
Cdd:CHL00131 171 ELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHYQRLLDYIKpDYVHVMQNGKIIKT 233
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
34-220 |
3.29e-12 |
|
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: 66.47 E-value: 3.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 34 GDHQVLNDINLTITPGEVVAILGPSGSGKSTL----IRLINqleplSGGEILVDNKPTGRLSgsgLRQLRSRVGFVFQQF 109
Cdd:TIGR01271 1230 AGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLlsalLRLLS-----TEGEIQIDGVSWNSVT---LQTWRKAFGVIPQKV 1301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 110 NLYahltaSQNITLALEHVHGWkplpAQERALALLEKVGMLEKAHHYPAE-----------LSGGQQQRVAIARALASSP 178
Cdd:TIGR01271 1302 FIF-----SGTFRKNLDPYEQW----SDEEIWKVAEEVGLKSVIEQFPDKldfvlvdggyvLSNGHKQLMCLARSILSKA 1372
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 544825118 179 QIILFDEPTSALDPEMIGEVLFVMKAlAHSGITMIVVTHEMQ 220
Cdd:TIGR01271 1373 KILLLDEPSAHLDPVTLQIIRKTLKQ-SFSNCTVILSEHRVE 1413
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
45-219 |
4.75e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 65.60 E-value: 4.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 45 TITPGEVVAILGPSGSGKSTLIR-LINQLEPLSGGeilVDNKPT-----GRLSGSGLRQLRSRVgfvfqqfnlyahltAS 118
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKiLSGELIPNLGD---YEEEPSwdevlKRFRGTELQNYFKKL--------------YN 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 119 QNITLALehvhgwKP-----LP-------------AQERALA--LLEKVGMLEKAHHYPAELSGGQQQRVAIARALASSP 178
Cdd:PRK13409 158 GEIKVVH------KPqyvdlIPkvfkgkvrellkkVDERGKLdeVVERLGLENILDRDISELSGGELQRVAIAAALLRDA 231
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 544825118 179 QIILFDEPTSALDpemIGEVLFVMKA---LAhSGITMIVVTHEM 219
Cdd:PRK13409 232 DFYFFDEPTSYLD---IRQRLNVARLireLA-EGKYVLVVEHDL 271
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
38-236 |
5.03e-12 |
|
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: 65.70 E-value: 5.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 38 VLNDINLTITPGEVVAILGPSGSGKSTLIRLI-NQLEPlSGGEIlvdnKPTGRLSGSglrqlrsrvgfvfQQFNLYAHLT 116
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMImGELEP-SEGKI----KHSGRISFS-------------PQTSWIMPGT 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 117 ASQNITLALEHVHgwKPLPAQERALALLEKVGMLEKAHHYP-----AELSGGQQQRVAIARALASSPQIILFDEPTSALD 191
Cdd:TIGR01271 503 IKDNIIFGLSYDE--YRYTSVIKACQLEEDIALFPEKDKTVlgeggITLSGGQRARISLARAVYKDADLYLLDSPFTHLD 580
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 544825118 192 PEMIGEVL--FVMKALAHSgiTMIVVTHEMQFAREiADRIVFIDGGH 236
Cdd:TIGR01271 581 VVTEKEIFesCLCKLMSNK--TRILVTSKLEHLKK-ADKILLLHEGV 624
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
32-257 |
6.90e-12 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 65.19 E-value: 6.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 32 RYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLI-NQLEPLSGGEILVD-------NKPTGRLSGSGL-------- 95
Cdd:PRK10636 10 RRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLkNEISADGGSYTFPGnwqlawvNQETPALPQPALeyvidgdr 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 96 --RQLRSRVgfvfQQFNlyahltaSQNITLALEHVHG-------WKplpAQERALALLEKVGMLEKAHHYP-AELSGGQQ 165
Cdd:PRK10636 90 eyRQLEAQL----HDAN-------ERNDGHAIATIHGkldaidaWT---IRSRAASLLHGLGFSNEQLERPvSDFSGGWR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 166 QRVAIARALASSPQIILFDEPTSALDpemIGEVLFVMKALAHSGITMIVVTHEMQFAREIADRIVFIDGGHILE-TAPPA 244
Cdd:PRK10636 156 MRLNLAQALICRSDLLLLDEPTNHLD---LDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEyTGNYS 232
|
250
....*....|...
gi 544825118 245 QFFSQPAHPRAQR 257
Cdd:PRK10636 233 SFEVQRATRLAQQ 245
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
39-238 |
1.92e-11 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 62.28 E-value: 1.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 39 LNDINLTITPGEVVAILGPSGSGKSTLI----------RLINQL-------------------EPLSGGeILVDNKPTGR 89
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLAfdtiyaegqrRYVESLsayarqflgqmdkpdvdsiEGLSPA-IAIDQKTTSR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 90 LSgsglrqlRSRVGFVFQQFNLYAHLTASQNITlalehvhgwkplpaqeRALALLEKVGM----LEKAhhyPAELSGGQQ 165
Cdd:cd03270 90 NP-------RSTVGTVTEIYDYLRLLFARVGIR----------------ERLGFLVDVGLgyltLSRS---APTLSGGEA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 166 QRVAIARALAS--SPQIILFDEPTSALDPEMIGEVLFVMKALAHSGITMIVVTHEMQFAREiADRIVFI------DGGHI 237
Cdd:cd03270 144 QRIRLATQIGSglTGVLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIRA-ADHVIDIgpgagvHGGEI 222
|
.
gi 544825118 238 L 238
Cdd:cd03270 223 V 223
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
28-237 |
2.11e-11 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 63.65 E-value: 2.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 28 HVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLI-NQLEPLSgGEIlvdnkptgrlsgsGLRQlRSRVGFvF 106
Cdd:PRK10636 317 KVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLaGELAPVS-GEI-------------GLAK-GIKLGY-F 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 107 QQFNLyAHLTASQNitlALEHVHGWKPLPAQERALALLEKVGML-EKAHHYPAELSGGQQQRVAIARALASSPQIILFDE 185
Cdd:PRK10636 381 AQHQL-EFLRADES---PLQHLARLAPQELEQKLRDYLGGFGFQgDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDE 456
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 544825118 186 PTSALDPEMigevlfvMKALAHSGI----TMIVVTHEMQFAREIADRIVFIDGGHI 237
Cdd:PRK10636 457 PTNHLDLDM-------RQALTEALIdfegALVVVSHDRHLLRSTTDDLYLVHDGKV 505
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
32-249 |
3.10e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 63.11 E-value: 3.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 32 RYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIR-LINQLEPLSGGEILVDNKPTgRLSgsgLRQLRSRVGFVFQQFN 110
Cdd:PRK10938 12 RLSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARaLAGELPLLSGERQSQFSHIT-RLS---FEQLQKLVSDEWQRNN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 111 ---LYAH-----LTASQNItlaLEHVHgwkplpAQERALALLEKVG---MLEKAHHYpaeLSGGQQQRVAIARALASSPQ 179
Cdd:PRK10938 88 tdmLSPGeddtgRTTAEII---QDEVK------DPARCEQLAQQFGitaLLDRRFKY---LSTGETRKTLLCQALMSEPD 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 180 IILFDEPTSALDPEMIGEVLFVMKALAHSGITMIVVTHEMQFAREIADRIVFIDGGHILETAPPAQFFSQ 249
Cdd:PRK10938 156 LLILDEPFDGLDVASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQQ 225
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
38-249 |
5.98e-11 |
|
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: 61.08 E-value: 5.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 38 VLNDINLTITPGEVVAILGPSGSGKSTL----IRLINQLEplsgGEILVDNKPTGRLSgsgLRQLRSRVGFVFQ------ 107
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIFD----GKIVIDGIDISKLP---LHTLRSRLSIILQdpilfs 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 108 ---QFNLYAHLTASQNiTLalehvhgWKPLPAQERALALLEKVGMLEKAHHYPAE-LSGGQQQRVAIARALASSPQIILF 183
Cdd:cd03288 109 gsiRFNLDPECKCTDD-RL-------WEALEIAQLKNMVKSLPGGLDAVVTEGGEnFSVGQRQLFCLARAFVRKSSILIM 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 544825118 184 DEPTSALDpeMIGEVLF---VMKALAHSgiTMIVVTHEMQFAREiADRIVFIDGGHILETAPPAQFFSQ 249
Cdd:cd03288 181 DEATASID--MATENILqkvVMTAFADR--TVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLAQ 244
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
35-217 |
9.81e-11 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 60.58 E-value: 9.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 35 DHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLE--PLSGGEILVDNKPTGRLSGSglrqlrSRVG-FVFQQFNL 111
Cdd:PRK09580 13 DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPE------DRAGeGIFMAFQY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 112 YAHLTASQN---ITLALEHVHGWKPLPAQER---ALALLEKVGMLEkahhYPAEL---------SGGQQQRVAIARALAS 176
Cdd:PRK09580 87 PVEIPGVSNqffLQTALNAVRSYRGQEPLDRfdfQDLMEEKIALLK----MPEDLltrsvnvgfSGGEKKRNDILQMAVL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 544825118 177 SPQIILFDEPTSALDPEMIGEVLFVMKALAHSGITMIVVTH 217
Cdd:PRK09580 163 EPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTH 203
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
31-234 |
9.97e-11 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 59.12 E-value: 9.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 31 KRYGDHQVLNDINlTITPGEVVAILGPSGSGKSTLIR-LINQLEPlSGGEILVDNkptgrlsgsglrqlrsrvgfvfqqf 109
Cdd:cd03222 8 KRYGVFFLLVELG-VVKEGEVIGIVGPNGTGKTTAVKiLAGQLIP-NGDNDEWDG------------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 110 nlyahltasqnITLAlehvhgWKPlpaqeralallEKVgmlekahhypaELSGGQQQRVAIARALASSPQIILFDEPTSA 189
Cdd:cd03222 61 -----------ITPV------YKP-----------QYI-----------DLSGGELQRVAIAAALLRNATFYLFDEPSAY 101
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 544825118 190 LDPEMIGEVLFVMKALA-HSGITMIVVTHEMQFAREIADRIVFIDG 234
Cdd:cd03222 102 LDIEQRLNAARAIRRLSeEGKKTALVVEHDLAVLDYLSDRIHVFEG 147
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
46-235 |
1.49e-10 |
|
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: 61.57 E-value: 1.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 46 ITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKptgrlsgsglrQLRSRVGFVFQQFNLYAHLTASQNITLAL 125
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGK-----------SILTNISDVHQNMGYCPQFDAIDDLLTGR 2030
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 126 EHVHGWKPL---PAQEralalLEKV--------GMLEKAHHYPAELSGGQQQRVAIARALASSPQIILFDEPTSALDPEM 194
Cdd:TIGR01257 2031 EHLYLYARLrgvPAEE-----IEKVanwsiqslGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQA 2105
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 544825118 195 IGEVLFVMKALAHSGITMIVVTHEMQFAREIADRIVFIDGG 235
Cdd:TIGR01257 2106 RRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
34-218 |
2.52e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 60.89 E-value: 2.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 34 GDHQVLNDINLTITPGEVVAILGPSGSGKSTLIrliNQL-EPLSGGEILVDNkptgRLSGSGLRQ--LRSRVGFVFQQ-- 108
Cdd:TIGR00956 774 EKRVILNNVDGWVKPGTLTALMGASGAGKTTLL---NVLaERVTTGVITGGD----RLVNGRPLDssFQRSIGYVQQQdl 846
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 109 ------------FNLYAHLTASQNITLALEHVhgwkplpaqERALALLEKVGMLEKAHHYPAE-LSGGQQQRVAIARALA 175
Cdd:TIGR00956 847 hlptstvreslrFSAYLRQPKSVSKSEKMEYV---------EEVIKLLEMESYADAVVGVPGEgLNVEQRKRLTIGVELV 917
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 544825118 176 SSPQIILF-DEPTSALDPEMIGEVLFVMKALAHSGITMIVVTHE 218
Cdd:TIGR00956 918 AKPKLLLFlDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQ 961
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
39-245 |
3.51e-10 |
|
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: 60.03 E-value: 3.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 39 LNDINLTITPGEVVAILGPSGSGKSTLI---------RLINQ--LEPLSGGEIL----------VDNKPTGRLSGSG--- 94
Cdd:TIGR00630 624 LKNITVSIPLGLFTCITGVSGSGKSTLIndtlypalaNRLNGakTVPGRYTSIEglehldkvihIDQSPIGRTPRSNpat 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 95 -------LRQL-------RSR---VG-FVF-----------------------------------QQFN------LYAHL 115
Cdd:TIGR00630 704 ytgvfdeIRELfaetpeaKVRgytPGrFSFnvkggrceacqgdgvikiemhflpdvyvpcevckgKRYNretlevKYKGK 783
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 116 TASQNITLALEHVHGW-KPLPAQERALALLEKVGMlekahHY-----PA-ELSGGQQQRVAIARAL---ASSPQIILFDE 185
Cdd:TIGR00630 784 NIADVLDMTVEEAYEFfEAVPSISRKLQTLCDVGL-----GYirlgqPAtTLSGGEAQRIKLAKELskrSTGRTLYILDE 858
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 544825118 186 PTSALDPEMIGEVLFVMKALAHSGITMIVVTHEMQFAReIADRIvfID--------GGHILETAPPAQ 245
Cdd:TIGR00630 859 PTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNLDVIK-TADYI--IDlgpeggdgGGTVVASGTPEE 923
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
48-250 |
3.94e-10 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 58.92 E-value: 3.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 48 PGEVVAILGPSGSGKSTLIR-LINQLEPLSGGEilvDNKPTGRlsgSGLRQLRsrvGFVFQQFnlyahLTASQNITLALE 126
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKiLAGKLKPNLGKF---DDPPDWD---EILDEFR---GSELQNY-----FTKLLEGDVKVI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 127 HvhgwKP-----LPAQ--ERALALLEKV---GMLEKA----------HHYPAELSGGQQQRVAIARALASSPQIILFDEP 186
Cdd:cd03236 91 V----KPqyvdlIPKAvkGKVGELLKKKderGKLDELvdqlelrhvlDRNIDQLSGGELQRVAIAAALARDADFYFFDEP 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 544825118 187 TSALDPEMIGEVLFVMKALAHSGITMIVVTHEMQFAREIADRIvfidggHILETAPPAQ-FFSQP 250
Cdd:cd03236 167 SSYLDIKQRLNAARLIRELAEDDNYVLVVEHDLAVLDYLSDYI------HCLYGEPGAYgVVTLP 225
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
28-218 |
5.01e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 57.65 E-value: 5.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 28 HVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSGSGLRQLrsrvGFVFQ 107
Cdd:PRK13540 6 ELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQL----CFVGH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 108 QFNLYAHLTASQNITLALEHVHGwkplpaqerALALLEKVGMLEKAHH--YPAEL-SGGQQQRVAIARALASSPQIILFD 184
Cdd:PRK13540 82 RSGINPYLTLRENCLYDIHFSPG---------AVGITELCRLFSLEHLidYPCGLlSSGQKRQVALLRLWMSKAKLWLLD 152
|
170 180 190
....*....|....*....|....*....|....
gi 544825118 185 EPTSALDPEMIGEVLFVMKALAHSGITMIVVTHE 218
Cdd:PRK13540 153 EPLVALDELSLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
19-230 |
8.72e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 59.27 E-value: 8.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 19 LEQASVEFRHVDKRygDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILV-DNKPTGRLS------ 91
Cdd:PTZ00265 1166 IEIMDVNFRYISRP--NVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKNDHHIVfKNEHTNDMTneqdyq 1243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 92 ---------------------GSG-----------------------LRQLRSRVGFVFQQFNLYaHLTASQNITLALEH 127
Cdd:PTZ00265 1244 gdeeqnvgmknvnefsltkegGSGedstvfknsgkilldgvdicdynLKDLRNLFSIVSQEPMLF-NMSIYENIKFGKED 1322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 128 VhgwkPLPAQERA---LALLEKVGMLEKAHH-----YPAELSGGQQQRVAIARALASSPQIILFDEPTSALDP---EMIG 196
Cdd:PTZ00265 1323 A----TREDVKRAckfAAIDEFIESLPNKYDtnvgpYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSnseKLIE 1398
|
250 260 270
....*....|....*....|....*....|....
gi 544825118 197 EVLFVMKALAHSgiTMIVVTHEMQFAREiADRIV 230
Cdd:PTZ00265 1399 KTIVDIKDKADK--TIITIAHRIASIKR-SDKIV 1429
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
41-218 |
8.73e-10 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 59.10 E-value: 8.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 41 DINLTITPGEVVAILGPSGSGKSTLIRLIN-QLEPLSGgeilvdnkptgrlsgSGLRQLRSRVGfVFQQFNLYAhLTASQ 119
Cdd:PLN03073 527 NLNFGIDLDSRIAMVGPNGIGKSTILKLISgELQPSSG---------------TVFRSAKVRMA-VFSQHHVDG-LDLSS 589
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 120 NITLALEHVHGWKPLPAQERALALLEKVGMLEKAHHYpaELSGGQQQRVAIARALASSPQIILFDEPTSALDPEMIgEVL 199
Cdd:PLN03073 590 NPLLYMMRCFPGVPEQKLRAHLGSFGVTGNLALQPMY--TLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAV-EAL 666
|
170
....*....|....*....
gi 544825118 200 FVMKALAHSGITMivVTHE 218
Cdd:PLN03073 667 IQGLVLFQGGVLM--VSHD 683
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
35-217 |
1.57e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 56.03 E-value: 1.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 35 DHQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVDNKPTGRLSgsglrqlRSRVGFVFQQFNLYAH 114
Cdd:PRK13541 12 EQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIA-------KPYCTYIGHNLGLKLE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 115 LTASQNITLALEHVHGWKPLPAqerALALLEKVGMLEKAHHypaELSGGQQQRVAIARALASSPQIILFDEPTSALDPEM 194
Cdd:PRK13541 85 MTVFENLKFWSEIYNSAETLYA---AIHYFKLHDLLDEKCY---SLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKEN 158
|
170 180
....*....|....*....|....*
gi 544825118 195 IGEV--LFVMKalAHSGITMIVVTH 217
Cdd:PRK13541 159 RDLLnnLIVMK--ANSGGIVLLSSH 181
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
160-245 |
1.62e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 57.82 E-value: 1.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 160 LSGGQQQRVAIARALASSPQIILFDEPTSALDPEMIGEVLFVMKALAHSGITMIVVTHEMQFAREIADRIVFIDGGH--- 236
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLvag 471
|
....*....
gi 544825118 237 ILETAPPAQ 245
Cdd:PRK10982 472 IVDTKTTTQ 480
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
38-250 |
2.00e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 57.87 E-value: 2.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 38 VLNDINLTITPGEVVAILGPSGSGKSTLIR-LINQLEpLSGGEILVDnkptgrlsgsglrqlRSrVGFVFQQFNLyAHLT 116
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQsLLSQFE-ISEGRVWAE---------------RS-IAYVPQQAWI-MNAT 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 117 ASQNI-------TLALEHVHGWKPLPAQERALA--LLEKVGmlEKAhhypAELSGGQQQRVAIARALASSPQIILFDEPT 187
Cdd:PTZ00243 737 VRGNIlffdeedAARLADAVRVSQLEADLAQLGggLETEIG--EKG----VNLSGGQKARVSLARAVYANRDVYLLDDPL 810
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 544825118 188 SALDP---EMIGEVLFvMKALAhsGITMIVVTHEMQFArEIADRIVFIDGGHILETAPPAQFFSQP 250
Cdd:PTZ00243 811 SALDAhvgERVVEECF-LGALA--GKTRVLATHQVHVV-PRADYVVALGDGRVEFSGSSADFMRTS 872
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
24-239 |
8.31e-09 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 55.67 E-value: 8.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 24 VEFRHVDKRY-----------------GD---HQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEPLSGGEILVD 83
Cdd:PRK13545 5 VKFEHVTKKYkmynkpfdklkdlffrsKDgeyHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 84 NKPTGRLSGSGLRqlrsrvgfvfqqfnlyAHLTASQNITLAlEHVHGWKPLPAQERALALLEKVGMLEKAHHYPAELSGG 163
Cdd:PRK13545 85 GSAALIAISSGLN----------------GQLTGIENIELK-GLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 544825118 164 QQQRVAIARALASSPQIILFDEPTSALDPEMIGEVLFVMKALAHSGITMIVVTHEMQFAREIADRIVFIDGGHILE 239
Cdd:PRK13545 148 MKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKE 223
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
26-265 |
9.93e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 55.89 E-value: 9.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 26 FRHVDKRygdhQVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQlePLSGGEILVDnkptGRLSGSGL------RQLR 99
Cdd:TIGR00956 68 FRDTKTF----DILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAS--NTDGFHIGVE----GVITYDGItpeeikKHYR 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 100 SRVGFVFQQFNLYAHLTASQNITLALehvhgwKPLPAQERALALLEKVGMLEKAHHYPAEL------------------S 161
Cdd:TIGR00956 138 GDVVYNAETDVHFPHLTVGETLDFAA------RCKTPQNRPDGVSREEYAKHIADVYMATYglshtrntkvgndfvrgvS 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 162 GGQQQRVAIARALASSPQIILFDEPTSALDPEMIGEVLFVMKALAHSGITMIVVT--HEMQFAREIADRIVFIDGGHILE 239
Cdd:TIGR00956 212 GGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVAiyQCSQDAYELFDKVIVLYEGYQIY 291
|
250 260 270
....*....|....*....|....*....|....
gi 544825118 240 TAP---PAQFFSQPAHPRAQR-----FLQKVLDP 265
Cdd:TIGR00956 292 FGPadkAKQYFEKMGFKCPDRqttadFLTSLTSP 325
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
39-239 |
1.04e-08 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 54.82 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 39 LNDINLTITPGEVVAILGPSGSGKSTLIRLInqleplsGGEIlvdnKPTgrlsgSGLRQLRSRVGFVFQQFNLYAHLTAS 118
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNII-------GGSL----SPT-----VGKVDRNGEVSVIAISAGLSGQLTGI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 119 QNITLALeHVHGWKPLPAQERALALLEKVGMLEKAHHYPAELSGGQQQRVAIARALASSPQIILFDEPTSALDPEMIGEV 198
Cdd:PRK13546 104 ENIEFKM-LCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKC 182
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 544825118 199 LFVMKALAHSGITMIVVTHEMQFAREIADRIVFIDGGHILE 239
Cdd:PRK13546 183 LDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKD 223
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
40-230 |
3.20e-08 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 51.98 E-value: 3.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 40 NDInlTITPGEVVAILGPSGSGKSTLIRLInqleplsggeilvdnkptgrlsgsglrqlrsRVGFVFQQFNLYAHLTASQ 119
Cdd:cd03227 14 NDV--TFGEGSLTIITGPNGSGKSTILDAI-------------------------------GLALGGAQSATRRRSGVKA 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 120 NITLALEHVhgwkplpaqERALALLEkvgmlekahhypaeLSGGQQQRVAIARALAS----SPQIILFDEPTSALDPEMI 195
Cdd:cd03227 61 GCIVAAVSA---------ELIFTRLQ--------------LSGGEKELSALALILALaslkPRPLYILDEIDRGLDPRDG 117
|
170 180 190
....*....|....*....|....*....|....*
gi 544825118 196 GEVLFVMKALAHSGITMIVVTHEMQFArEIADRIV 230
Cdd:cd03227 118 QALAEAILEHLVKGAQVIVITHLPELA-ELADKLI 151
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
35-237 |
9.98e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 52.48 E-value: 9.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 35 DHQVLNDINLTITPGEVVAILGPSGSGKSTLI---------RLInqleplsGGEILVDNKPTgRLS------GSGLRQL- 98
Cdd:NF040905 272 ERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAmsvfgrsygRNI-------SGTVFKDGKEV-DVStvsdaiDAGLAYVt 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 99 --RSRVGFVFQQfnlyahlTASQNITLA-LEHV--HGW-----KPLPAQE-------RALALLEKVGmlekahhypaELS 161
Cdd:NF040905 344 edRKGYGLNLID-------DIKRNITLAnLGKVsrRGVideneEIKVAEEyrkkmniKTPSVFQKVG----------NLS 406
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 544825118 162 GGQQQRVAIARALASSPQIILFDEPTSALDpemIG---EVLFVMKALAHSGITMIVVTHEMQFAREIADRIVFIDGGHI 237
Cdd:NF040905 407 GGNQQKVVLSKWLFTDPDVLILDEPTRGID---VGakyEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMNEGRI 482
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
51-232 |
1.78e-07 |
|
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: 50.30 E-value: 1.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 51 VVAILGPSGSGKSTLIRLINQleplsggeILVDNKPTGRLSGSGLRQLrSRVGFVFQQfnlyahltasqnITLALEHVHG 130
Cdd:cd03240 24 LTLIVGQNGAGKTTIIEALKY--------ALTGELPPNSKGGAHDPKL-IREGEVRAQ------------VKLAFENANG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 131 wKPLPAqERALALLEKV------GMLEKAHHYPAELSGGQQQ------RVAIARALASSPQIILFDEPTSALDPEMIGEV 198
Cdd:cd03240 83 -KKYTI-TRSLAILENVifchqgESNWPLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEES 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 544825118 199 LF-VMKALAHSGI-TMIVVTHEMQFaREIADRIVFI 232
Cdd:cd03240 161 LAeIIEERKSQKNfQLIVITHDEEL-VDAADHIYRV 195
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
56-221 |
1.89e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 51.82 E-value: 1.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 56 GPSGSGKSTLIR-LINQLEPlSGGEILVDnkPTGRLSGsgLRQLRsrvgFVFQQFN---------------------LYA 113
Cdd:PRK15064 34 GANGCGKSTFMKiLGGDLEP-SAGNVSLD--PNERLGK--LRQDQ----FAFEEFTvldtvimghtelwevkqerdrIYA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 114 HLTASQN--ITLA-LEHVHG-WKPLPAQERALALLEKVGMLEKAHHYP-AELSGGQQQRVAIARALASSPQIILFDEPTS 188
Cdd:PRK15064 105 LPEMSEEdgMKVAdLEVKFAeMDGYTAEARAGELLLGVGIPEEQHYGLmSEVAPGWKLRVLLAQALFSNPDILLLDEPTN 184
|
170 180 190
....*....|....*....|....*....|....*.
gi 544825118 189 ALDPEMI---GEVLFVMKAlahsgiTMIVVTHEMQF 221
Cdd:PRK15064 185 NLDINTIrwlEDVLNERNS------TMIIISHDRHF 214
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
158-246 |
3.36e-07 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 51.37 E-value: 3.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 158 AELSGGQQQRVAIARALASSPQIILF--DEPTSALDPEMIGEVLFVMKALAHSGITMIVVTHEMQFArEIADRIVFID-- 233
Cdd:PRK00635 475 ATLSGGEQERTALAKHLGAELIGITYilDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDEQMI-SLADRIIDIGpg 553
|
90
....*....|....*..
gi 544825118 234 ----GGHILETAPPAQF 246
Cdd:PRK00635 554 agifGGEVLFNGSPREF 570
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
37-218 |
7.31e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 50.23 E-value: 7.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 37 QVLNDINLTITPGEVVAILGPSGSGKSTLIRLINQLEplSGGEILVDNkptgRLSGSGLRQ-LRSRV-GFVFQ------Q 108
Cdd:PLN03140 894 QLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRK--TGGYIEGDI----RISGFPKKQeTFARIsGYCEQndihspQ 967
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 109 FNLYAHLTASQNITLALEhVHGWKPLPAQERALALLEKVGMLEKAHHYPA--ELSGGQQQRVAIARALASSPQIILFDEP 186
Cdd:PLN03140 968 VTVRESLIYSAFLRLPKE-VSKEEKMMFVDEVMELVELDNLKDAIVGLPGvtGLSTEQRKRLTIAVELVANPSIIFMDEP 1046
|
170 180 190
....*....|....*....|....*....|..
gi 544825118 187 TSALDPEMIGEVLFVMKALAHSGITMIVVTHE 218
Cdd:PLN03140 1047 TSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQ 1078
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
136-234 |
9.83e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 49.47 E-value: 9.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 136 AQERALALLEKVGML-EKAHHYPAELSGGQQQRVAIARALASSPQIILFDEPTSALDpemIGEVLFVMKALAHSGITMIV 214
Cdd:PLN03073 320 AEARAASILAGLSFTpEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD---LHAVLWLETYLLKWPKTFIV 396
|
90 100
....*....|....*....|
gi 544825118 215 VTHEMQFAREIADRIVFIDG 234
Cdd:PLN03073 397 VSHAREFLNTVVTDILHLHG 416
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
25-221 |
1.66e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 48.79 E-value: 1.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 25 EFRHVDKRYGDHQVLNDINLTITPGEVVAILGPSGSGKSTLIRL-INQLEPLSGgeilvdnkptgrlsgsglrqlRSRVG 103
Cdd:PRK11147 321 EMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLmLGQLQADSG---------------------RIHCG 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 104 F-----VFQQF------------NLyahLTASQNITlalehVHGwkplpaQER-ALALLE------KVGMLE-KAhhypa 158
Cdd:PRK11147 380 TklevaYFDQHraeldpektvmdNL---AEGKQEVM-----VNG------RPRhVLGYLQdflfhpKRAMTPvKA----- 440
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 544825118 159 eLSGGQQQRVAIARALASSPQIILFDEPTSALDPEMIgEVLFVMkaLAHSGITMIVVTHEMQF 221
Cdd:PRK11147 441 -LSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETL-ELLEEL--LDSYQGTVLLVSHDRQF 499
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
39-265 |
2.43e-06 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 48.48 E-value: 2.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 39 LNDINLTITPGEVVAILGPSGSGKSTLIR------LINQL-----EP-----LSGGE-----ILVDNKPTGRLSgsglrq 97
Cdd:COG0178 621 LKNVDVEIPLGVLTCVTGVSGSGKSTLVNdilypaLARKLngakeKPgphdsIEGLEhidkvIDIDQSPIGRTP------ 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 98 lRSR----VGfVFQQF-NLYAHLTASQ-----------NI---------------------------------------T 122
Cdd:COG0178 695 -RSNpatyTG-VFDPIrELFAQTPEAKargykpgrfsfNVkggrceacqgdgvikiemhflpdvyvpcevckgkrynreT 772
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 123 L-------------------ALEHvhgWKPLPAQERALALLEKVGMlekahHY-----PA-ELSGGQQQRVAIARALASS 177
Cdd:COG0178 773 LevkykgkniadvldmtveeALEF---FENIPKIARKLQTLQDVGL-----GYiklgqPAtTLSGGEAQRVKLASELSKR 844
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 178 PQ---IILFDEPTSALDPEMIGEVLFVMKALAHSGITMIVVTHEMQFareI--ADRIvfID--------GGHILETAPPA 244
Cdd:COG0178 845 STgktLYILDEPTTGLHFHDIRKLLEVLHRLVDKGNTVVVIEHNLDV---IktADWI--IDlgpeggdgGGEIVAEGTPE 919
|
330 340
....*....|....*....|.
gi 544825118 245 QFFSQPAHPRAqRFLQKVLDP 265
Cdd:COG0178 920 EVAKVKASYTG-RYLKEYLEA 939
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
160-242 |
4.49e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 47.90 E-value: 4.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 160 LSGGQQQRVAIARALASS---PQIILFDEPTSALDPEMIGEVLFVMKALAHSGITMIVVTHEMQFAReIADrivfidggH 236
Cdd:PRK00635 810 LSGGEIQRLKLAYELLAPskkPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMHVVK-VAD--------Y 880
|
....*.
gi 544825118 237 ILETAP 242
Cdd:PRK00635 881 VLELGP 886
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
141-250 |
1.28e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 46.16 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 141 LALLEKVGM----LEKAhhyPAELSGGQQQRVAIARALASSPQIILF--DEPTSALDPEMIGEVLFVMKALAHSGITMIV 214
Cdd:TIGR00630 469 LGFLIDVGLdylsLSRA---AGTLSGGEAQRIRLATQIGSGLTGVLYvlDEPSIGLHQRDNRRLINTLKRLRDLGNTLIV 545
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 544825118 215 VTHEMQFAREiADRIVFI------DGGHILETAPPAQFFSQP 250
Cdd:TIGR00630 546 VEHDEDTIRA-ADYVIDIgpgageHGGEVVASGTPEEILANP 586
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
39-233 |
7.16e-05 |
|
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: 43.45 E-value: 7.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 39 LNDINLTITPGeVVAILGPSGSGKSTLIRLInqleplsggEILVDNKPTGRLS------GSGLRQLRSRVGFVFQQ---- 108
Cdd:COG3593 14 IKDLSIELSDD-LTVLVGENNSGKSSILEAL---------RLLLGPSSSRKFDeedfylGDDPDLPEIEIELTFGSllsr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 109 -FNLYAHLTASQNITLALEHV----------------HGWKPL---------PAQERALALLEKVG-MLEKAHHYPAELS 161
Cdd:COG3593 84 lLRLLLKEEDKEELEEALEELneelkealkalnellsEYLKELldgldleleLSLDELEDLLKSLSlRIEDGKELPLDRL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 162 G-GQQQRVAIA--RALA-----SSPQIILFDEPTSALDPEMIGEVLFVMKALAHSGITMIVVTHEMQFAREI-ADRIVFI 232
Cdd:COG3593 164 GsGFQRLILLAllSALAelkraPANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTHSPHLLSEVpLENIRRL 243
|
.
gi 544825118 233 D 233
Cdd:COG3593 244 R 244
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
157-217 |
2.49e-04 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 41.61 E-value: 2.49e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 544825118 157 PAELSGGQQQ---RVAIARALASSPQIILFDEPTSALDPEMIGEVLFVMKALAHSGITMIVVTH 217
Cdd:pfam13304 234 AFELSDGTKRllaLLAALLSALPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTH 297
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
39-66 |
7.90e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 40.83 E-value: 7.90e-04
10 20
....*....|....*....|....*...
gi 544825118 39 LNDINLTITPGEVVAILGPSGSGKSTLI 66
Cdd:PRK00349 625 LKNVDVEIPLGKFTCVTGVSGSGKSTLI 652
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
158-204 |
1.18e-03 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 37.21 E-value: 1.18e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 158 AELSGGQQQR---VAIARALAS----------SPQIILFDEPTSALDPEMIGEVLFVMKA 204
Cdd:pfam13558 31 GGLSGGEKQLlayLPLAAALAAqygsaegrppAPRLVFLDEAFAKLDEENIRTALELLRA 90
|
|
| TrwB_TraG_TraD_VirD4 |
cd01127 |
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are ... |
52-129 |
1.22e-03 |
|
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are bacterial conjugation proteins involved in type IV secretion (T4S) systems, versatile bacterial secretion systems mediating transport of protein and/or DNA. They are present in gram-negative and gram-positive bacteria, as well as archaea. They form hexameric rings and belong to the RecA-like NTPases superfamily, which also includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases.
Pssm-ID: 410871 [Multi-domain] Cd Length: 144 Bit Score: 38.35 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 52 VAILGPSGSGKSTLIRLINQLEPLSGGEILV-DNKPTGRLSGS-GLRQLRSRVGFVFQQFNLYAHLTASQNITLALEHVH 129
Cdd:cd01127 2 TLVLGTTGSGKTTSIVIPLLDQAARGGSVIItDPKGELFLVIPdRDDSFAALRALFFNQLFRALTELASLSPGRLPRRVW 81
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
44-66 |
1.44e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 36.04 E-value: 1.44e-03
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
49-80 |
1.99e-03 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 38.53 E-value: 1.99e-03
10 20 30
....*....|....*....|....*....|....*
gi 544825118 49 GEVVAILGPSGSGKSTlirLINQLEP---LSGGEI 80
Cdd:cd01854 85 GKTSVLVGQSGVGKST---LLNALLPelvLATGEI 116
|
|
| CMPK |
cd02020 |
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine ... |
51-80 |
2.80e-03 |
|
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine monophosphate (CMP) to produce cytidine diphosphate (CDP), using ATP as the preferred phosphoryl donor.
Pssm-ID: 238978 [Multi-domain] Cd Length: 147 Bit Score: 37.47 E-value: 2.80e-03
10 20 30
....*....|....*....|....*....|...
gi 544825118 51 VVAILGPSGSGKSTLIRLINQ---LEPLSGGEI 80
Cdd:cd02020 1 IIAIDGPAGSGKSTVAKLLAKklgLPYLDTGGI 33
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
39-65 |
5.72e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 38.07 E-value: 5.72e-03
10 20
....*....|....*....|....*..
gi 544825118 39 LNDINLTITPGEVVAILGPSGSGKSTL 65
Cdd:TIGR00630 12 LKNIDVEIPRDKLVVITGLSGSGKSSL 38
|
|
| Udk |
COG0572 |
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ... |
51-74 |
8.01e-03 |
|
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway/BioSystem: Pyrimidine salvage
Pssm-ID: 440337 [Multi-domain] Cd Length: 206 Bit Score: 36.74 E-value: 8.01e-03
10 20
....*....|....*....|....*
gi 544825118 51 VVAILGPSGSGKSTLI-RLINQLEP 74
Cdd:COG0572 9 IIGIAGPSGSGKTTFArRLAEQLGA 33
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
158-230 |
8.37e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 37.64 E-value: 8.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825118 158 AELSGGQQQRVAIARALASSP----------QIILFDEPTSALDPEMIGEVLFVMKALAHSGITMIVVTHEMQFAREIAD 227
Cdd:TIGR00618 949 ATLSGGETFLASLSLALALADllstsggtvlDSLFIDEGFGSLDEDSLDRAIGILDAIREGSKMIGIISHVPEFRERIPH 1028
|
...
gi 544825118 228 RIV 230
Cdd:TIGR00618 1029 RIL 1031
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
39-65 |
9.09e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 37.31 E-value: 9.09e-03
10 20
....*....|....*....|....*..
gi 544825118 39 LNDINLTITPGEVVAILGPSGSGKSTL 65
Cdd:COG0178 16 LKNIDVDIPRNKLVVITGLSGSGKSSL 42
|
|
| |
