|
Name |
Accession |
Description |
Interval |
E-value |
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-150 |
1.20e-96 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 279.67 E-value: 1.20e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLNRMNDKVSGFRHSGDVLLGGRTIFADRDLMEFRRSVGMLFQRPNPFPMSIMDNV 80
Cdd:PRK14271 42 MGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSIFNYRDVLEFRRRVGMLFQRPNPFPMSIMDNV 121
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 81 VAGVRAHKMAPRKQFKSVAEARLTEVGLWDAVKDRLGDSPFRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:PRK14271 122 LAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPT 191
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
1-150 |
4.25e-88 |
|
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: 256.84 E-value: 4.25e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLNRMNDKVSGFRHSGDVLLGGRTIFADR-DLMEFRRSVGMLFQRPNPFPMSIMDN 79
Cdd:TIGR00972 22 LDIPKNQVTALIGPSGCGKSTLLRSLNRMNDLVPGVRIEGKVLFDGQDIYDKKiDVVELRRRVGMVFQKPNPFPMSIYDN 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2014669168 80 VVAGVRAHKMAPRKQFKSVAEARLTEVGLWDAVKDRLGDSPFRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:TIGR00972 102 IAYGPRLHGIKDKKELDEIVEESLKKAALWDEVKDRLHDSALGLSGGQQQRLCIARALAVEPEVLLLDEPT 172
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-150 |
2.50e-85 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 250.34 E-value: 2.50e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLNRMNDKVSGFRHSGDVLLGGRTIFA-DRDLMEFRRSVGMLFQRPNPFPMSIMDN 79
Cdd:COG1117 32 LDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIPGARVEGEILLDGEDIYDpDVDVVELRRRVGMVFQKPNPFPKSIYDN 111
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2014669168 80 VVAGVRAHKMAPRKQFKSVAEARLTEVGLWDAVKDRLGDSPFRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:COG1117 112 VAYGLRLHGIKSKSELDEIVEESLRKAALWDEVKDRLKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPT 182
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1-150 |
6.03e-77 |
|
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: 227.83 E-value: 6.03e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLNRMNDKVSGFRHSGDVLLGGRTIFA-DRDLMEFRRSVGMLFQRPNPFPMSIMDN 79
Cdd:cd03260 21 LDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGAPDEGEVLLDGKDIYDlDVDVLELRRRVGMVFQKPNPFPGSIYDN 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2014669168 80 VVAGVRAHKMAPRKQFKSVAEARLTEVGLWDAVKDRLGdsPFRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:cd03260 101 VAYGLRLHGIKLKEELDERVEEALRKAALWDEVKDRLH--ALGLSGGQQQRLCLARALANEPEVLLLDEPT 169
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-150 |
8.64e-56 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 175.35 E-value: 8.64e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLNRMNDKVSGFRHSGDVLLGGRTIFADR-DLMEFRRSVGMLFQRPNPFPMSIMDN 79
Cdd:PRK14239 26 LDFYPNEITALIGPSGSGKSTLLRSINRMNDLNPEVTITGSIVYNGHNIYSPRtDTVDLRKEIGMVFQQPNPFPMSIYEN 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2014669168 80 VVAGVRAHKMAPRKQFKSVAEARLTEVGLWDAVKDRLGDSPFRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:PRK14239 106 VVYGLRLKGIKDKQVLDEAVEKSLKGASIWDEVKDRLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPT 176
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1-149 |
2.09e-55 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 174.59 E-value: 2.09e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLNRMNDKVSGFRHSGDVLLGGRTIFA-DRDLMEFRRSVGMLFQRPNPFPMSIMDN 79
Cdd:PRK14243 31 LDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPGFRVEGKVTFHGKNLYApDVDPVEVRRRIGMVFQKPNPFPKSIYDN 110
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 80 VVAGVRAHKMapRKQFKSVAEARLTEVGLWDAVKDRLGDSPFRLSGGQQQLLCLARALAVNPDVLLLDEP 149
Cdd:PRK14243 111 IAYGARINGY--KGDMDELVERSLRQAALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEP 178
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-150 |
3.76e-48 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 155.77 E-value: 3.76e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLNRMNDKVSGFRHSGDVLLGGRTIFA-DRDLMEFRRSVGMLFQRPNPFP-MSIMD 78
Cdd:PRK14267 25 LKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEARVEGEVRLFGRNIYSpDVDPIEVRREVGMVFQYPNPFPhLTIYD 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2014669168 79 NVVAGVRAHKMA-PRKQFKSVAEARLTEVGLWDAVKDRLGDSPFRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:PRK14267 105 NVAIGVKLNGLVkSKKELDERVEWALKKAALWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPT 177
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-150 |
4.87e-48 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 155.46 E-value: 4.87e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLNRMNDKVSGFRHSGDVLLGGRTIFaDRDLMEFRRSVGMLFQRPNPFP-MSIMDN 79
Cdd:PRK14247 24 LEIPDNTITALMGPSGSGKSTLLRVFNRLIELYPEARVSGEVYLDGQDIF-KMDVIELRRRVQMVFQIPNPIPnLSIFEN 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2014669168 80 VVAGVRAHKMAPRKQ--FKSVAEArLTEVGLWDAVKDRLGDSPFRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:PRK14247 103 VALGLKLNRLVKSKKelQERVRWA-LEKAQLWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPT 174
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-149 |
3.92e-45 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 148.26 E-value: 3.92e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLNRMNDKVSGFRHSGDVLLGGRTIFADR-DLMEFRRSVGMLFQRPNPFPMSIMDN 79
Cdd:PRK14258 28 MEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVEGRVEFFNQNIYERRvNLNRLRRQVSMVHPKPNLFPMSVYDN 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 80 VVAGVRAHKMAPRKQFKSVAEARLTEVGLWDAVKDRLGDSPFRLSGGQQQLLCLARALAVNPDVLLLDEP 149
Cdd:PRK14258 108 VAYGVKIVGWRPKLEIDDIVESALKDADLWDEIKHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEP 177
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-150 |
3.15e-42 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 140.13 E-value: 3.15e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLNRMnDKVSgfrhSGDVLLGGRTIFAD-RDLMEFRRSVGMLFQRPNPFP-MSIMD 78
Cdd:COG1126 22 LDVEKGEVVVIIGPSGSGKSTLLRCINLL-EEPD----SGTITVDGEDLTDSkKDINKLRRKVGMVFQQFNLFPhLTVLE 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2014669168 79 NVVAG-VRAHKMaPRKQFKSVAEARLTEVGLwdavKDRLGDSPFRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:COG1126 97 NVTLApIKVKKM-SKAEAEERAMELLERVGL----ADKADAYPAQLSGGQQQRVAIARALAMEPKVMLFDEPT 164
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-150 |
2.82e-41 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 138.26 E-value: 2.82e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLNRMNDKV-SGFRHSGDVLLGGRTIFaDRDLMEFRRSVGMLFQRPNPFP-MSIMD 78
Cdd:PRK14246 31 IKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYdSKIKVDGKVLYFGKDIF-QIDAIKLRKEVGMVFQQPNPFPhLSIYD 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2014669168 79 NVVAGVRAHKMAPRKQFKSVAEARLTEVGLWDAVKDRLGDSPFRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:PRK14246 110 NIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1-150 |
2.54e-38 |
|
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: 129.19 E-value: 2.54e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLNRMnDKVSgfrhSGDVLLGGRTIFAD-RDLMEFRRSVGMLFQRPNPFP-MSIMD 78
Cdd:cd03262 21 LTVKKGEVVVIIGPSGSGKSTLLRCINLL-EEPD----SGTIIIDGLKLTDDkKNINELRQKVGMVFQQFNLFPhLTVLE 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2014669168 79 NVV-AGVRAHKMaPRKQFKSVAEARLTEVGLwdavKDRLGDSPFRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:cd03262 96 NITlAPIKVKGM-SKAEAEERALELLEKVGL----ADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPT 163
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1-150 |
1.33e-36 |
|
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: 123.14 E-value: 1.33e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLnrmndkvSGFRH--SGDVLLGGRTIFaDRDLMEFRRSVGMLFQRPNPFP-MSIM 77
Cdd:pfam00005 6 LTLNPGEILALVGPNGAGKSTLLKLI-------AGLLSptEGTILLDGQDLT-DDERKSLRKEIGYVFQDPQLFPrLTVR 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2014669168 78 DNVVAGVRAHKMApRKQFKSVAEARLTEVGLWDAVKDRLGDSPFRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:pfam00005 78 ENLRLGLLLKGLS-KREKDARAEEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-149 |
3.93e-35 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 124.44 E-value: 3.93e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLnrmndkvSGFRH--SGDVLLGGRTIFadrDLMEFRRSVGMLFQRPNPFP-MSIM 77
Cdd:COG3842 26 LSIEPGEFVALLGPSGCGKTTLLRMI-------AGFETpdSGRILLDGRDVT---GLPPEKRNVGMVFQDYALFPhLTVA 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2014669168 78 DNVVAGVRAHKMAPRKQFKSVAEArLTEVGLwDAVKDRLgdsPFRLSGGQQQLLCLARALAVNPDVLLLDEP 149
Cdd:COG3842 96 ENVAFGLRMRGVPKAEIRARVAEL-LELVGL-EGLADRY---PHQLSGGQQQRVALARALAPEPRVLLLDEP 162
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-150 |
4.43e-35 |
|
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: 126.94 E-value: 4.43e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLNRMNDkvsgfRHSGDVLLGGRTI--FADRDLMEFRRSVGMLFQRP----NPFpM 74
Cdd:COG1123 286 LTLRRGETLGLVGESGSGKSTLARLLLGLLR-----PTSGSILFDGKDLtkLSRRSLRELRRRVQMVFQDPysslNPR-M 359
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2014669168 75 SIMDNVVAGVRAHKMAPRKQFKSVAEARLTEVGLWDAVKDRlgdSPFRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:COG1123 360 TVGDIIAEPLRLHGLLSRAERRERVAELLERVGLPPDLADR---YPHELSGGQRQRVAIARALALEPKLLILDEPT 432
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1-149 |
9.54e-35 |
|
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: 120.32 E-value: 9.54e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLNRMnDKVSgfrhSGDVLLGGRTIFadrDLMEFRRSVGMLFQRPNPFP-MSIMDN 79
Cdd:cd03259 21 LTVEPGEFLALLGPSGCGKTTLLRLIAGL-ERPD----SGEILIDGRDVT---GVPPERRNIGMVFQDYALFPhLTVAEN 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 80 VVAGVRAHKMaPRKQFKSVAEARLTEVGLwdavKDRLGDSPFRLSGGQQQLLCLARALAVNPDVLLLDEP 149
Cdd:cd03259 93 IAFGLKLRGV-PKAEIRARVRELLELVGL----EGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEP 157
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1-150 |
9.56e-35 |
|
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: 120.52 E-value: 9.56e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLNrmndkvsGFRH--SGDVLLGGRTIfADRDLMEFRRSVGMLFQrpNPFPMSIMD 78
Cdd:COG1122 22 LSIEKGEFVAIIGPNGSGKSTLLRLLN-------GLLKptSGEVLVDGKDI-TKKNLRELRRKVGLVFQ--NPDDQLFAP 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2014669168 79 NV---VA-GVRAHKMAPRKQFKSVAEArLTEVGLWDaVKDRlgdSPFRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:COG1122 92 TVeedVAfGPENLGLPREEIRERVEEA-LELVGLEH-LADR---PPHELSGGQKQRVAIAGVLAMEPEVLVLDEPT 162
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1-150 |
1.42e-32 |
|
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: 114.49 E-value: 1.42e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLNRMndkvsGFRHSGDVLLGGRTIfADRDLMEFRRSVGMLFQrpNPFPMSIMDNV 80
Cdd:cd03225 22 LTIKKGEFVLIVGPNGSGKSTLLRLLNGL-----LGPTSGEVLVDGKDL-TKLSLKELRRKVGLVFQ--NPDDQFFGPTV 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2014669168 81 ---VA-GVRAHKMaPRKQFKSVAEARLTEVGLWDaVKDRlgdSPFRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:cd03225 94 eeeVAfGLENLGL-PEEEIEERVEEALELVGLEG-LRDR---SPFTLSGGQKQRVAIAGVLAMDPDILLLDEPT 162
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1-150 |
2.57e-32 |
|
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: 114.12 E-value: 2.57e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLNRMnDKVSgfrhSGDVLLGGRTIFA--DRDLMEFRR-SVGMLFQRPNPFP-MSI 76
Cdd:cd03255 25 LSIEKGEFVAIVGPSGSGKSTLLNILGGL-DRPT----SGEVRVDGTDISKlsEKELAAFRRrHIGFVFQSFNLLPdLTA 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2014669168 77 MDNVVAGVRAHKMaPRKQFKSVAEARLTEVGLwdavKDRLGDSPFRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:cd03255 100 LENVELPLLLAGV-PKKERRERAEELLERVGL----GDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPT 168
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-149 |
4.52e-32 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 114.42 E-value: 4.52e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTlnrmndkVSGFRH--SGDVLLGGRTIfadrdlMEFRRSVGMLFQRPNPFP-MSIM 77
Cdd:COG1116 32 LTVAAGEFVALVGPSGCGKSTLLRL-------IAGLEKptSGEVLVDGKPV------TGPGPDRGVVFQEPALLPwLTVL 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2014669168 78 DNVVAGVRAHKMaPRKQFKSVAEARLTEVGLWDAVKDRlgdsPFRLSGGQQQLLCLARALAVNPDVLLLDEP 149
Cdd:COG1116 99 DNVALGLELRGV-PKAERRERARELLELVGLAGFEDAY----PHQLSGGMRQRVAIARALANDPEVLLMDEP 165
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-152 |
1.20e-31 |
|
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: 113.21 E-value: 1.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLNRMNDkvsgfRHSGDVLLGGRTIfADRDLMEFRRSVGMLFQRPN-PFPMSIMDN 79
Cdd:COG1120 22 LSLPPGEVTALLGPNGSGKSTLLRALAGLLK-----PSSGEVLLDGRDL-ASLSRRELARRIAYVPQEPPaPFGLTVREL 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2014669168 80 VVAGVRAHK---MAPRKQFKSVAEARLTEVGLWDavkdrLGDSPF-RLSGGQQQLLCLARALAVNPDVLLLDEPTRH 152
Cdd:COG1120 96 VALGRYPHLglfGRPSAEDREAVEEALERTGLEH-----LADRPVdELSGGERQRVLIARALAQEPPLLLLDEPTSH 167
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1-149 |
1.32e-31 |
|
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: 112.18 E-value: 1.32e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLnrmndkvSGFRH--SGDVLLGGRTIfadrdlMEFRRSVGMLFQRPNPFP-MSIM 77
Cdd:cd03293 25 LSVEEGEFVALVGPSGCGKSTLLRII-------AGLERptSGEVLVDGEPV------TGPGPDRGYVFQQDALLPwLTVL 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2014669168 78 DNVVAGVRAHKMaPRKQFKSVAEARLTEVGLWDAVKDRlgdsPFRLSGGQQQLLCLARALAVNPDVLLLDEP 149
Cdd:cd03293 92 DNVALGLELQGV-PKAEARERAEELLELVGLSGFENAY----PHQLSGGMRQRVALARALAVDPDVLLLDEP 158
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-149 |
1.33e-31 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 115.24 E-value: 1.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLnrmndkvSGFRH--SGDVLLGGRTIFADRDLMEfrRSVGMLFQRPNPFP-MSIM 77
Cdd:COG1118 23 LEIASGELVALLGPSGSGKTTLLRII-------AGLETpdSGRIVLNGRDLFTNLPPRE--RRVGFVFQHYALFPhMTVA 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2014669168 78 DNVVAGVRaHKMAPRKQFKSVAEARLTEVGLwDAVKDRLgdsPFRLSGGQQQLLCLARALAVNPDVLLLDEP 149
Cdd:COG1118 94 ENIAFGLR-VRPPSKAEIRARVEELLELVQL-EGLADRY---PSQLSGGQRQRVALARALAVEPEVLLLDEP 160
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
10-150 |
2.22e-31 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 111.45 E-value: 2.22e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 10 TLLGPTGSGKTTFLRTLNRMNDkvsgfRHSGDVLLGGRTIfADRDLMEFRRSVGMLFQRPNPFPMSIMDNVVAGVRAHKM 89
Cdd:COG4619 30 AITGPSGSGKSTLLRALADLDP-----PTSGEIYLDGKPL-SAMPPPEWRRQVAYVPQEPALWGGTVRDNLPFPFQLRER 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2014669168 90 APRKQfksVAEARLTEVGLWDAVKDRLGDspfRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:COG4619 104 KFDRE---RALELLERLGLPPDILDKPVE---RLSGGERQRLALIRALLLQPDVLLLDEPT 158
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-150 |
2.43e-31 |
|
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: 111.83 E-value: 2.43e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLNRMNDKVSG--FRHSGDVLLGGRTIFADRdlmefRRSVGMLFQRP----NPFpM 74
Cdd:cd03257 26 FSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGsiIFDGKDLLKLSRRLRKIR-----RKEIQMVFQDPmsslNPR-M 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2014669168 75 SIMDNVVAGVRAHKMAPRKQFKSVAEAR-LTEVGLWDAVKDRLgdsPFRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:cd03257 100 TIGEQIAEPLRIHGKLSKKEARKEAVLLlLVGVGLPEEVLNRY---PHELSGGQRQRVAIARALALNPKLLIADEPT 173
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-150 |
2.58e-31 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 112.11 E-value: 2.58e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLNRMnDKVSGfrhsGDVLLGGRTIFADR-DLMEFRRSVGMLFQRPNPFP-MSIMD 78
Cdd:PRK09493 22 LNIDQGEVVVIIGPSGSGKSTLLRCINKL-EEITS----GDLIVDGLKVNDPKvDERLIRQEAGMVFQQFYLFPhLTALE 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2014669168 79 NVVAGVRAHKMAPRKQFKSVAEARLTEVGLwdavKDRLGDSPFRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:PRK09493 97 NVMFGPLRVRGASKEEAEKQARELLAKVGL----AERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPT 164
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
1-150 |
4.50e-31 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 111.31 E-value: 4.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLnrmndkvSGFRH--SGDVLLGGRTIFADRDlmEFRRSVGMLFQRPNPFP-MSIM 77
Cdd:COG1131 21 LTVEPGEIFGLLGPNGAGKTTTIRML-------LGLLRptSGEVRVLGEDVARDPA--EVRRRIGYVPQEPALYPdLTVR 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2014669168 78 DNVVAGVRAHKMaPRKQFKSVAEARLTEVGLWDAVKDRLGDspfrLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:COG1131 92 ENLRFFARLYGL-PRKEARERIDELLELFGLTDAADRKVGT----LSGGMKQRLGLALALLHDPELLILDEPT 159
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1-150 |
1.04e-30 |
|
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: 108.81 E-value: 1.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLNRMNDKVsgfrhSGDVLLGGRTIFADRDLM-EFRRSVGMLFQRPNPFP-MSIMD 78
Cdd:cd03229 21 LNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPD-----SGSILIDGEDLTDLEDELpPLRRRIGMVFQDFALFPhLTVLE 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2014669168 79 NVVagvrahkmaprkqfksvaearltevglwdavkdrlgdspFRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:cd03229 96 NIA---------------------------------------LGLSGGQQQRVALARALAMDPDVLLLDEPT 128
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
11-150 |
2.30e-29 |
|
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: 107.20 E-value: 2.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 11 LLGPTGSGKTTFLRTLNRMNDKvsgfrHSGDVLLGGRTIfADRDLMEFRRSVGMLFQRP----NPFpMSIMDNVVAGVRA 86
Cdd:COG1124 36 LVGESGSGKSTLLRALAGLERP-----WSGEVTFDGRPV-TRRRRKAFRRRVQMVFQDPyaslHPR-HTVDRILAEPLRI 108
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2014669168 87 HKMAPRKQfkSVAEArLTEVGLWDAVKDRLgdsPFRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:COG1124 109 HGLPDREE--RIAEL-LEQVGLPPSFLDRY---PHQLSGGQRQRVAIARALILEPELLLLDEPT 166
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
11-150 |
2.82e-29 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 106.29 E-value: 2.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 11 LLGPTGSGKTTFLRTLNRMnDKVSgfrhSGDVLLGGRTI--FADRDLMEFRRSVGMLFQ--R--PNpfpMSIMDNVVAGV 84
Cdd:COG2884 33 LTGPSGAGKSTLLKLLYGE-ERPT----SGQVLVNGQDLsrLKRREIPYLRRRIGVVFQdfRllPD---RTVYENVALPL 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2014669168 85 RAHKMAPRKQFKSVAEArLTEVGLWDAVKDRlgdsPFRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:COG2884 105 RVTGKSRKEIRRRVREV-LDLVGLSDKAKAL----PHELSGGEQQRVAIARALVNRPELLLADEPT 165
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-150 |
3.11e-29 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 106.28 E-value: 3.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLNRMnDKVSgfrhSGDVLLGGRTIFA--DRDLMEFRR-SVGMLFQRPNPFP-MSI 76
Cdd:COG1136 29 LSIEAGEFVAIVGPSGSGKSTLLNILGGL-DRPT----SGEVLIDGQDISSlsERELARLRRrHIGFVFQFFNLLPeLTA 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2014669168 77 MDNVVAGVRAHKMAPRKQFKSVAEArLTEVGLwdavKDRLGDSPFRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:COG1136 104 LENVALPLLLAGVSRKERRERAREL-LERVGL----GDRLDHRPSQLSGGQQQRVAIARALVNRPKLILADEPT 172
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1-150 |
8.14e-29 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 105.87 E-value: 8.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLNRMNDKVSGFRHSGDVLLGGRTIFADRDLMEFRRSVGMLFQRPNPFP-MSIMDN 79
Cdd:COG4161 23 LECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDFSQKPSEKAIRLLRQKVGMVFQQYNLWPhLTVMEN 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2014669168 80 VV-AGVRAHKMApRKQFKSVAEARLTEVGLwdavKDRLGDSPFRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:COG4161 103 LIeAPCKVLGLS-KEQAREKAMKLLARLRL----TDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPT 169
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-150 |
1.69e-28 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 105.14 E-value: 1.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLNRMNDKVSGfrhsgDVLLGGRTIFAD--RDLMEFRRSVGMLFQRPNPFP-MSIM 77
Cdd:COG3638 24 LEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSG-----EILVDGQDVTALrgRALRRLRRRIGMIFQQFNLVPrLSVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 78 DNVVAGVRAHKMAPR-------KQFKSVAEARLTEVGLWDAVKDRLGdspfRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:COG3638 99 TNVLAGRLGRTSTWRsllglfpPEDRERALEALERVGLADKAYQRAD----QLSGGQQQRVAIARALVQEPKLILADEPV 174
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1-149 |
1.95e-28 |
|
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: 104.73 E-value: 1.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTlnrmndkVSGFRH--SGDVLLGGRTIfADRDLMEfrRSVGMLFQRPNPFP-MSIM 77
Cdd:cd03296 23 LDIPSGELVALLGPSGSGKTTLLRL-------IAGLERpdSGTILFGGEDA-TDVPVQE--RNVGFVFQHYALFRhMTVF 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2014669168 78 DNVVAGVRahkMAPRKQFKSVAEARLTEVGLWDAVK-DRLGDS-PFRLSGGQQQLLCLARALAVNPDVLLLDEP 149
Cdd:cd03296 93 DNVAFGLR---VKPRSERPPEAEIRAKVHELLKLVQlDWLADRyPAQLSGGQRQRVALARALAVEPKVLLLDEP 163
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-150 |
3.49e-28 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 104.45 E-value: 3.49e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLNRMNDKVSGFRHSGDVLL-GGRTIFADRDLM-EFRRSVGMLFQRPNPFP-MSIM 77
Cdd:PRK11264 24 LEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdTARSLSQQKGLIrQLRQHVGFVFQNFNLFPhRTVL 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2014669168 78 DNVVAGVRAHKMAPRKQFKSVAEARLTEVGLwdAVKDrlgDS-PFRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:PRK11264 104 ENIIEGPVIVKGEPKEEATARARELLAKVGL--AGKE---TSyPRRLSGGQQQRVAIARALAMRPEVILFDEPT 172
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
11-150 |
7.70e-28 |
|
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: 104.75 E-value: 7.70e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 11 LLGPTGSGKTTFLRTLNRMNDKvsGFRHSGDVLLGGRTIFA--DRDLMEFR-RSVGMLFQRP----NPFpMSIMDNVVAG 83
Cdd:COG0444 36 LVGESGSGKSTLARAILGLLPP--PGITSGEILFDGEDLLKlsEKELRKIRgREIQMIFQDPmtslNPV-MTVGDQIAEP 112
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2014669168 84 VRAHKMAPRKQFKSVAEARLTEVGLWDAvKDRLGDSPFRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:COG0444 113 LRIHGGLSKAEARERAIELLERVGLPDP-ERRLDRYPHELSGGMRQRVMIARALALEPKLLIADEPT 178
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
1-150 |
9.26e-28 |
|
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: 103.69 E-value: 9.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLNrmndkvsGFRH--SGDVLLGGRTIFADR--DLMEFRRSVGMLFQRPNP--FPM 74
Cdd:TIGR04521 26 LTIEDGEFVAIIGHTGSGKSTLIQHLN-------GLLKptSGTVTIDGRDITAKKkkKLKDLRKKVGLVFQFPEHqlFEE 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2014669168 75 SIMDNVVAGVRAHKMAPRKQFKSVAEArLTEVGLWDAVKDRlgdSPFRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:TIGR04521 99 TVYKDIAFGPKNLGLSEEEAEERVKEA-LELVGLDEEYLER---SPFELSGGQMRRVAIAGVLAMEPEVLILDEPT 170
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
8-150 |
1.78e-27 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 102.57 E-value: 1.78e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 8 VTTLLGPTGSGKTTFLRTLNRMNDKvsgfrHSGDVLLGGRTI-----------FAD-RDLMEFRRSVGMLFQRPNPFP-M 74
Cdd:COG4598 36 VISIIGSSGSGKSTFLRCINLLETP-----DSGEIRVGGEEIrlkpdrdgelvPADrRQLQRIRTRLGMVFQSFNLWShM 110
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2014669168 75 SIMDNVVAG-VRAHKMaPRKQFKSVAEARLTEVGLWDaVKDRLgdsPFRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:COG4598 111 TVLENVIEApVHVLGR-PKAEAIERAEALLAKVGLAD-KRDAY---PAHLSGGQQQRAAIARALAMEPEVMLFDEPT 182
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
8-150 |
2.12e-27 |
|
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: 101.99 E-value: 2.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 8 VTTLLGPTGSGKTTFLRTLNRMNDKVSGfrhsgDVLLGGRTIFADR--DLMEFRRSVGMLFQRPNPFP-MSIMDNVVAGV 84
Cdd:TIGR02315 30 FVAIIGPSGAGKSTLLRCINRLVEPSSG-----SILLEGTDITKLRgkKLRKLRRRIGMIFQHYNLIErLTVLENVLHGR 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2014669168 85 RAHKMAPRKQF-------KSVAEARLTEVGLWDAVKDRLGdspfRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:TIGR02315 105 LGYKPTWRSLLgrfseedKERALSALERVGLADKAYQRAD----QLSGGQQQRVAIARALAQQPDLILADEPI 173
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1-150 |
5.48e-27 |
|
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: 98.99 E-value: 5.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLNRMNDkvsgfRHSGDVLLGGRTIfADRDLMEFRRSVGMLFQRPNPFPMSIMDNV 80
Cdd:cd03228 23 LTIKPGEKVAIVGPSGSGKSTLLKLLLRLYD-----PTSGEILIDGVDL-RDLDLESLRKNIAYVPQDPFLFSGTIRENI 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 81 vagvrahkmaprkqfksvaearltevglwdavkdrlgdspfrLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:cd03228 97 ------------------------------------------LSGGQRQRIAIARALLRDPPILILDEAT 124
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1-149 |
8.95e-27 |
|
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: 100.45 E-value: 8.95e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLNRMNDKVSGfrhsgDVLLGGRTIfADRDLMEFRRSVGMLFQRPNPFP-MSIMDN 79
Cdd:cd03295 22 LEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSG-----EIFIDGEDI-REQDPVELRRKIGYVIQQIGLFPhMTVEEN 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2014669168 80 VVAgVRAHKMAPRKQFKSVAEARLTEVGLWDA-VKDRLgdsPFRLSGGQQQLLCLARALAVNPDVLLLDEP 149
Cdd:cd03295 96 IAL-VPKLLKWPKEKIRERADELLALVGLDPAeFADRY---PHELSGGQQQRVGVARALAADPPLLLMDEP 162
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-150 |
9.74e-27 |
|
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: 100.05 E-value: 9.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLnrmndkvSGFRH--SGDVLLGGRTIFA--DRDLMEFRRSVGMLFQRPNPF-PMS 75
Cdd:COG1127 26 LDVPRGEILAIIGGSGSGKSVLLKLI-------IGLLRpdSGEILVDGQDITGlsEKELYELRRRIGMLFQGGALFdSLT 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2014669168 76 IMDNVVAGVRAHKMAPRKQFKSVAEARLTEVGLwDAVKDRLgdsPFRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:COG1127 99 VFENVAFPLREHTDLSEAEIRELVLEKLELVGL-PGAADKM---PSELSGGMRKRVALARALALDPEILLYDEPT 169
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-150 |
1.46e-26 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 99.78 E-value: 1.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLNrmndkvsGF--RHSGDVLLGGRTIFADRdlmefrRSVGMLFQRPN---PFPMS 75
Cdd:COG1121 27 LTIPPGEFVAIVGPNGAGKSTLLKAIL-------GLlpPTSGTVRLFGKPPRRAR------RRIGYVPQRAEvdwDFPIT 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2014669168 76 IMDNVVAGVRAHK---MAPRKQFKSVAEARLTEVGLWDAVKDRLGDspfrLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:COG1121 94 VRDVVLMGRYGRRglfRRPSRADREAVDEALERVGLEDLADRPIGE----LSGGQQQRVLLARALAQDPDLLLLDEPF 167
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1-150 |
1.91e-26 |
|
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: 99.50 E-value: 1.91e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLnrmndkvSGFRH--SGDVLLGGRTIFA--DRDLMEFRRSVGMLFQRPNPF-PMS 75
Cdd:cd03261 21 LDVRRGEILAIIGPSGSGKSTLLRLI-------VGLLRpdSGEVLIDGEDISGlsEAELYRLRRRMGMLFQSGALFdSLT 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2014669168 76 IMDNVVAGVRAHKMAPRKQFKSVAEARLTEVGLWDAVKDRlgdsPFRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:cd03261 94 VFENVAFPLREHTRLSEEEIREIVLEKLEAVGLRGAEDLY----PAELSGGMKKRVALARALALDPELLLYDEPT 164
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1-150 |
2.07e-26 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 99.32 E-value: 2.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLNRMNDKVSGFRHSGDVLLGGRTIFADRDLMEFRRSVGMLFQRPNPFP-MSIMDN 79
Cdd:PRK11124 23 LDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSKTPSDKAIRELRRNVGMVFQQYNLWPhLTVQQN 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2014669168 80 VV-AGVRAHKMApRKQFKSVAEARLTEVGLWDAVkDRLgdsPFRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:PRK11124 103 LIeAPCRVLGLS-KDQALARAEKLLERLRLKPYA-DRF---PLHLSGGQQQRVAIARALMMEPQVLLFDEPT 169
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
10-149 |
2.32e-26 |
|
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: 99.23 E-value: 2.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 10 TLLGPTGSGKTTFLRTLnrmndkvSGFRH--SGDVLLGGRTIfadRDLMEFRRSVGMLFQRPNPFP-MSIMDNVVAGVRA 86
Cdd:cd03300 30 TLLGPSGCGKTTLLRLI-------AGFETptSGEILLDGKDI---TNLPPHKRPVNTVFQNYALFPhLTVFENIAFGLRL 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2014669168 87 HKMAPRKQFKSVAEArLTEVGLwDAVKDRlgdSPFRLSGGQQQLLCLARALAVNPDVLLLDEP 149
Cdd:cd03300 100 KKLPKAEIKERVAEA-LDLVQL-EGYANR---KPSQLSGGQQQRVAIARALVNEPKVLLLDEP 157
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1-150 |
5.44e-26 |
|
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: 98.28 E-value: 5.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLnrmndkvSGFRH--SGDVLLGGRTIfadRDLMEFRRS---VGMLFQRPNPFP-M 74
Cdd:cd03219 21 FSVRPGEIHGLIGPNGAGKTTLFNLI-------SGFLRptSGSVLFDGEDI---TGLPPHEIArlgIGRTFQIPRLFPeL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 75 SIMDNVVAGVRAHK---MAPRKQFKSVAEAR------LTEVGLWDaVKDRLGDSpfrLSGGQQQLLCLARALAVNPDVLL 145
Cdd:cd03219 91 TVLENVMVAAQARTgsgLLLARARREEREAReraeelLERVGLAD-LADRPAGE---LSYGQQRRLEIARALATDPKLLL 166
|
....*
gi 2014669168 146 LDEPT 150
Cdd:cd03219 167 LDEPA 171
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-149 |
1.15e-25 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 98.62 E-value: 1.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLNRMNDkvsgfRHSGDVLLGGRTIfADRDLMEFRRSVGMLFQRPNPFP-MSIMDN 79
Cdd:COG1125 23 LTIPAGEFTVLVGPSGCGKTTTLRMINRLIE-----PTSGRILIDGEDI-RDLDPVELRRRIGYVIQQIGLFPhMTVAEN 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2014669168 80 VVA-----GVrahkmaPRKQFKSVAEARLTEVGLW-DAVKDRLgdsPFRLSGGQQQLLCLARALAVNPDVLLLDEP 149
Cdd:COG1125 97 IATvprllGW------DKERIRARVDELLELVGLDpEEYRDRY---PHELSGGQQQRVGVARALAADPPILLMDEP 163
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
1-150 |
2.89e-25 |
|
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: 100.29 E-value: 2.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLnrmndkvSGFRH--SGDVLLGGRTIfADRDLMEFRRSVGMLFQRPNPFPMSIMD 78
Cdd:COG2274 496 LTIKPGERVAIVGRSGSGKSTLLKLL-------LGLYEptSGRILIDGIDL-RQIDPASLRRQIGVVLQDVFLFSGTIRE 567
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2014669168 79 NVVAGvraHKMAPRKQFKSVAEArlteVGLWDAVKD-------RLGDSPFRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:COG2274 568 NITLG---DPDATDEEIIEAARL----AGLHDFIEAlpmgydtVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEAT 639
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1-150 |
8.36e-25 |
|
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: 94.81 E-value: 8.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLnrmndkvSGF--RHSGDVLLGGRTIFADRDLMEFRRSVGMLFQRPNPFP-MSIM 77
Cdd:cd03224 21 LTVPEGEIVALLGRNGAGKTTLLKTI-------MGLlpPRSGSIRFDGRDITGLPPHERARAGIGYVPEGRRIFPeLTVE 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2014669168 78 DNVVAGVRAHKmaprkqfKSVAEARLTEV-GLWDAVKDRLGDSPFRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:cd03224 94 ENLLLGAYARR-------RAKRKARLERVyELFPRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPS 160
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-150 |
1.10e-24 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 96.69 E-value: 1.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLNRMnDKVSgfrhSGDVLLGGRTI--FADRDLMEFRRSVGMLFQRPNPFP-MSIM 77
Cdd:COG1135 26 LTIEKGEIFGIIGYSGAGKSTLIRCINLL-ERPT----SGSVLVDGVDLtaLSERELRAARRKIGMIFQHFNLLSsRTVA 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2014669168 78 DNV-----VAGVRAHKMAPRkqfksVAEArLTEVGLwdavKDRLGDSPFRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:COG1135 101 ENValpleIAGVPKAEIRKR-----VAEL-LELVGL----SDKADAYPSQLSGGQKQRVGIARALANNPKVLLCDEAT 168
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-150 |
1.50e-24 |
|
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: 98.05 E-value: 1.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLNRMNDKvsGFRHSGDVLLGGRTIfADRDLMEFRRSVGMLFQRP--NPFPMSIMD 78
Cdd:COG1123 27 LTIAPGETVALVGESGSGKSTLALALMGLLPH--GGRISGEVLLDGRDL-LELSEALRGRRIGMVFQDPmtQLNPVTVGD 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2014669168 79 NVVAGVRAHKMaPRKQFKSVAEARLTEVGLwdavKDRLGDSPFRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:COG1123 104 QIAEALENLGL-SRAEARARVLELLEAVGL----ERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPT 170
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
11-149 |
2.20e-24 |
|
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: 94.63 E-value: 2.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 11 LLGPTGSGKTTFLRTLNRMNDKVSGfrhsgDVLLGGRTI--FADRDLMEFRR-SVGMLFQRPNPFP-MSIMDNV-----V 81
Cdd:cd03294 55 IMGLSGSGKSTLLRCINRLIEPTSG-----KVLIDGQDIaaMSRKELRELRRkKISMVFQSFALLPhRTVLENVafgleV 129
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2014669168 82 AGVrahkmaPRKQFKSVAEARLTEVGLwdavKDRLGDSPFRLSGGQQQLLCLARALAVNPDVLLLDEP 149
Cdd:cd03294 130 QGV------PRAEREERAAEALELVGL----EGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEA 187
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1-150 |
2.42e-24 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 97.54 E-value: 2.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLNRMNDkVSgfrhSGDVLLGGRTIfADRDLMEFRRSVGMLFQRPNPFPMSIMDNV 80
Cdd:COG1132 361 LTIPPGETVALVGPSGSGKSTLVNLLLRFYD-PT----SGRILIDGVDI-RDLTLESLRRQIGVVPQDTFLFSGTIRENI 434
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2014669168 81 VAGvRAHkmAPRKQFKSVAEArlteVGLWDAVKD-------RLGDSPFRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:COG1132 435 RYG-RPD--ATDEEVEEAAKA----AQAHEFIEAlpdgydtVVGERGVNLSGGQRQRIAIARALLKDPPILILDEAT 504
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-150 |
3.32e-24 |
|
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: 93.95 E-value: 3.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLnrmndkvSGFRH--SGDVLLGGRTIfadRDLMEFRRS---VGMLFQRPNPFP-M 74
Cdd:COG0411 25 LEVERGEIVGLIGPNGAGKTTLFNLI-------TGFYRptSGRILFDGRDI---TGLPPHRIArlgIARTFQNPRLFPeL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 75 SIMDNVVAGVRAHK--------MAPRKQFKSVAEAR------LTEVGLwDAVKDRLGDSpfrLSGGQQQLLCLARALAVN 140
Cdd:COG0411 95 TVLENVLVAAHARLgrgllaalLRLPRARREEREAReraeelLERVGL-ADRADEPAGN---LSYGQQRRLEIARALATE 170
|
170
....*....|
gi 2014669168 141 PDVLLLDEPT 150
Cdd:COG0411 171 PKLLLLDEPA 180
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1-150 |
3.75e-24 |
|
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: 93.40 E-value: 3.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLNRMNDKVSGFRHSGDVLLGGRTIFADRDLmefRRSVGMLFQRPNPFP-MSIMDN 79
Cdd:cd03256 22 LSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQL---RRQIGMIFQQFNLIErLSVLEN 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2014669168 80 VVAGVRAHKMAPR-------KQFKSVAEARLTEVGLWDAVKDRLGdspfRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:cd03256 99 VLSGRLGRRSTWRslfglfpKEEKQRALAALERVGLLDKAYQRAD----QLSGGQQQRVAIARALMQQPKLILADEPV 172
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1-150 |
3.90e-24 |
|
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: 92.98 E-value: 3.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLnrmndkvSGF--RHSGDVLLGGRtifadrDLMEFRRSVGMLFQRPN---PFPMS 75
Cdd:cd03235 20 FEVKPGEFLAIVGPNGAGKSTLLKAI-------LGLlkPTSGSIRVFGK------PLEKERKRIGYVPQRRSidrDFPIS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 76 IMDnVVAGVRAHKM-----APRKQFKSVAEArLTEVGLWDAVKDRLGdspfRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:cd03235 87 VRD-VVLMGLYGHKglfrrLSKADKAKVDEA-LERVGLSELADRQIG----ELSGGQQQRVLLARALVQDPDLLLLDEPF 160
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
1-152 |
4.45e-24 |
|
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: 96.75 E-value: 4.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLnrmndkvSGFRH--SGDVLLGGRTIfADRDLMEFRRSVGMLFQRPNPFPMSIMD 78
Cdd:COG4988 358 LTIPPGERVALVGPSGAGKSTLLNLL-------LGFLPpySGSILINGVDL-SDLDPASWRRQIAWVPQNPYLFAGTIRE 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 79 NVVAGVRAhkmAPRKQFKSVAEArlteVGLWDAVKD-------RLGDSPFRLSGGQQQLLCLARALAVNPDVLLLDEPTR 151
Cdd:COG4988 430 NLRLGRPD---ASDEELEAALEA----AGLDEFVAAlpdgldtPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTA 502
|
.
gi 2014669168 152 H 152
Cdd:COG4988 503 H 503
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-149 |
6.46e-24 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 93.39 E-value: 6.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLnrmndkvSGFRH--SGDVLLGGRTIF---ADRdlmefrrsvGMLFQRPNPFP-M 74
Cdd:COG4525 28 LTIESGEFVVALGASGCGKTTLLNLI-------AGFLApsSGEITLDGVPVTgpgADR---------GVVFQKDALLPwL 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2014669168 75 SIMDNVVAGVRAHKMaPRKQFKSVAEARLTEVGLWDAVKDRlgdsPFRLSGGQQQLLCLARALAVNPDVLLLDEP 149
Cdd:COG4525 92 NVLDNVAFGLRLRGV-PKAERRARAEELLALVGLADFARRR----IWQLSGGMRQRVGIARALAADPRFLLMDEP 161
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-151 |
7.95e-24 |
|
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: 92.61 E-value: 7.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLNRMNDKvsgfrHSGDVLLGGRTIFADRDlmEFRRSVGMLFQRPNPFP-MSIMDN 79
Cdd:COG4555 22 FTAKDGEITGLLGPNGAGKTTLLRMLAGLLKP-----DSGSILIDGEDVRKEPR--EARRQIGVLPDERGLYDrLTVREN 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2014669168 80 VVAGVRAHKMaPRKQFKSVAEARLTEVGLWDAVKDRLGDspfrLSGGQQQLLCLARALAVNPDVLLLDEPTR 151
Cdd:COG4555 95 IRYFAELYGL-FDEELKKRIEELIELLGLEEFLDRRVGE----LSTGMKKKVALARALVHDPKVLLLDEPTN 161
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-150 |
1.04e-23 |
|
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: 92.26 E-value: 1.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLNRMnDKVSgfrhSGDVLLGGRTIF--ADRDLMEFRRSVGMLFQRPNPF-PMSIM 77
Cdd:cd03258 26 LSVPKGEIFGIIGRSGAGKSTLIRCINGL-ERPT----SGSVLVDGTDLTllSGKELRKARRRIGMIFQHFNLLsSRTVF 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2014669168 78 DNV-----VAGVrahkmaPRKQFKSVAEARLTEVGLwdavKDRLGDSPFRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:cd03258 101 ENValpleIAGV------PKAEIEERVLELLELVGL----EDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEAT 168
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
1-152 |
1.12e-23 |
|
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: 95.60 E-value: 1.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLNRMNDkvsgfRHSGDVLLGGRTIfADRDLMEFRRSVGMLFQRPNPFPMSIMDNV 80
Cdd:COG4987 356 LTLPPGERVAIVGPSGSGKSTLLALLLRFLD-----PQSGSITLGGVDL-RDLDEDDLRRRIAVVPQRPHLFDTTLRENL 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 81 -VAgvrahkmAPRKQFKSVAEArLTEVGLWDAVKD-------RLGDSPFRLSGGQQQLLCLARALAVNPDVLLLDEPTRH 152
Cdd:COG4987 430 rLA-------RPDATDEELWAA-LERVGLGDWLAAlpdgldtWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEG 501
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-149 |
2.66e-23 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 93.22 E-value: 2.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTlnrmndkVSGFRHSGdvllGGRTIFADRDL--MEFR-RSVGMLFQRPNPFP-MSI 76
Cdd:PRK10851 23 LDIPSGQMVALLGPSGSGKTTLLRI-------IAGLEHQT----SGHIRFHGTDVsrLHARdRKVGFVFQHYALFRhMTV 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2014669168 77 MDNVVAGVRahkMAPRKQFKSVAEARLTEVGLWDAVK-DRLGDS-PFRLSGGQQQLLCLARALAVNPDVLLLDEP 149
Cdd:PRK10851 92 FDNIAFGLT---VLPRRERPNAAAIKAKVTQLLEMVQlAHLADRyPAQLSGGQKQRVALARALAVEPQILLLDEP 163
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-149 |
4.08e-23 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 92.83 E-value: 4.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLnrmndkvSGFRH--SGDVLLGGRTIFadrDLMEFRRSVGMLFQRPNPFP-MSIM 77
Cdd:COG3839 24 LDIEDGEFLVLLGPSGCGKSTLLRMI-------AGLEDptSGEILIGGRDVT---DLPPKDRNIAMVFQSYALYPhMTVY 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2014669168 78 DNVVAGVRAHKMAPRKQFKSVAEArLTEVGLwDAVKDRLgdsPFRLSGGQQQLLCLARALAVNPDVLLLDEP 149
Cdd:COG3839 94 ENIAFPLKLRKVPKAEIDRRVREA-AELLGL-EDLLDRK---PKQLSGGQRQRVALGRALVREPKVFLLDEP 160
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
11-150 |
5.10e-23 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 92.10 E-value: 5.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 11 LLGPTGSGKTTFLRTLNRMNDKVSGfrhsgDVLLGGRTIFA--DRDLMEFRRSVGMLFQRP----NPfPMSIMDNVVAGV 84
Cdd:COG4608 49 LVGESGCGKSTLGRLLLRLEEPTSG-----EILFDGQDITGlsGRELRPLRRRMQMVFQDPyaslNP-RMTVGDIIAEPL 122
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2014669168 85 RAHKMAPRKQFKSVAEARLTEVGLWDAVKDRLgdsPFRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:COG4608 123 RIHGLASKAERRERVAELLELVGLRPEHADRY---PHEFSGGQRQRIGIARALALNPKLIVCDEPV 185
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1-152 |
5.76e-23 |
|
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: 93.51 E-value: 5.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLnrmndkvSGFR--HSGDVLLGGRTIfADRDLMEFRRSVGMLFQRPNPFPMSIMD 78
Cdd:TIGR02857 343 FTVPPGERVALVGPSGAGKSTLLNLL-------LGFVdpTEGSIAVNGVPL-ADADADSWRDQIAWVPQHPFLFAGTIAE 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 79 NVVAGVRAhkmAPRKQFKSVAEArlteVGLWDAVKDR-------LGDSPFRLSGGQQQLLCLARALAVNPDVLLLDEPTR 151
Cdd:TIGR02857 415 NIRLARPD---ASDAEIREALER----AGLDEFVAALpqgldtpIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTA 487
|
.
gi 2014669168 152 H 152
Cdd:TIGR02857 488 H 488
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1-149 |
6.75e-23 |
|
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: 89.66 E-value: 6.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPArSVTTLLGPTGSGKTTFLRTLNRMnDKVSGfrhsGDVLLGGRTIFADR---DLMEFRRSVGMLFQRPNPFP-MSI 76
Cdd:cd03297 19 FDLNE-EVTGIFGASGAGKSTLLRCIAGL-EKPDG----GTIVLNGTVLFDSRkkiNLPPQQRKIGLVFQQYALFPhLNV 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2014669168 77 MDNVVAGVRAHKMAPRKQFksvAEARLTEVGLwDAVKDRlgdSPFRLSGGQQQLLCLARALAVNPDVLLLDEP 149
Cdd:cd03297 93 RENLAFGLKRKRNREDRIS---VDELLDLLGL-DHLLNR---YPAQLSGGEKQRVALARALAAQPELLLLDEP 158
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
11-149 |
8.00e-23 |
|
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: 91.79 E-value: 8.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 11 LLGPTGSGKTTFLRTLnrmndkvSGFRH--SGDVLLGGRTIfadRDLMEFRRSVGMLFQRPNPFP-MSIMDNVVAGVRAH 87
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLL-------AGFEQpdSGSIMLDGEDV---TNVPPHLRHINMVFQSYALFPhMTVEENVAFGLKMR 70
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2014669168 88 KMaPRKQFKSVAEARLTEVGLWDAVKDRlgdsPFRLSGGQQQLLCLARALAVNPDVLLLDEP 149
Cdd:TIGR01187 71 KV-PRAEIKPRVLEALRLVQLEEFADRK----PHQLSGGQQQRVALARALVFKPKILLLDEP 127
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
11-149 |
1.14e-22 |
|
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: 91.64 E-value: 1.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 11 LLGPTGSGKTTFLRTLNRMNDKvsgfrHSGDVLLGGRTIfadRDLMEFRRSVGMLFQRPNPFP-MSIMDNVVAGVRAHKM 89
Cdd:TIGR03265 35 LLGPSGCGKTTLLRIIAGLERQ-----TAGTIYQGGRDI---TRLPPQKRDYGIVFQSYALFPnLTVADNIAYGLKNRGM 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 90 aPRKQFKSVAEARLTEVGLwDAVKDRLgdsPFRLSGGQQQLLCLARALAVNPDVLLLDEP 149
Cdd:TIGR03265 107 -GRAEVAERVAELLDLVGL-PGSERKY---PGQLSGGQQQRVALARALATSPGLLLLDEP 161
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
1-151 |
2.44e-22 |
|
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: 88.08 E-value: 2.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLNRMNDkvsgfRHSGDVLLGGRtifaDRDLMEFRRSVGMLFQRPNP--FPMSIMD 78
Cdd:cd03226 21 LDLYAGEIIALTGKNGAGKTTLAKILAGLIK-----ESSGSILLNGK----PIKAKERRKSIGYVMQDVDYqlFTDSVRE 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2014669168 79 NVVAGVRAhkmAPRKQFKsvAEARLTEVGLWDAvKDRLgdsPFRLSGGQQQLLCLARALAVNPDVLLLDEPTR 151
Cdd:cd03226 92 ELLLGLKE---LDAGNEQ--AETVLKDLDLYAL-KERH---PLSLSGGQKQRLAIAAALLSGKDLLIFDEPTS 155
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1-150 |
5.59e-22 |
|
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: 87.67 E-value: 5.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLNRMNDKvsgfrHSGDVLLGGRTIfADRDLMEFRRSVGMLFQRPNPFPMSIMDNV 80
Cdd:cd03254 24 FSIKPGETVAIVGPTGAGKTTLINLLMRFYDP-----QKGQILIDGIDI-RDISRKSLRSMIGVVLQDTFLFSGTIMENI 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2014669168 81 VAGvrahkmAPRKQFKSVAEArLTEVGLWDAVKDR-------LGDSPFRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:cd03254 98 RLG------RPNATDEEVIEA-AKEAGAHDFIMKLpngydtvLGENGGNLSQGERQLLAIARAMLRDPKILILDEAT 167
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1-152 |
5.95e-22 |
|
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: 86.34 E-value: 5.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLNRMNdKVSgfrhSGDVLLGGRTIfADRDLMEFRRSVGMLFQrpnpfpmsIMDnv 80
Cdd:cd03214 20 LSIEAGEIVGILGPNGAGKSTLLKTLAGLL-KPS----SGEILLDGKDL-ASLSPKELARKIAYVPQ--------ALE-- 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2014669168 81 vagvrahkmaprkqfksvaearltEVGLWDavkdrLGDSPFR-LSGGQQQLLCLARALAVNPDVLLLDEPTRH 152
Cdd:cd03214 84 ------------------------LLGLAH-----LADRPFNeLSGGERQRVLLARALAQEPPILLLDEPTSH 127
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1-149 |
6.29e-22 |
|
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: 86.93 E-value: 6.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLNRMNDKVSGfrhsgDVLLGGRTIfadRDLMEFRRSVGMLFQRPNPFP-MSIMDN 79
Cdd:cd03301 21 LDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSG-----RIYIGGRDV---TDLPPKDRDIAMVFQNYALYPhMTVYDN 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2014669168 80 VVAGVRAHKMAPRKQFKSVAE-ARLTEVglwDAVKDRLgdsPFRLSGGQQQLLCLARALAVNPDVLLLDEP 149
Cdd:cd03301 93 IAFGLKLRKVPKDEIDERVREvAELLQI---EHLLDRK---PKQLSGGQRQRVALGRAIVREPKVFLMDEP 157
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
10-149 |
7.88e-22 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 89.62 E-value: 7.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 10 TLLGPTGSGKTTFLRTLnrmndkvSGFRH--SGDVLLGGRTIfadRDLMEFRRSVGMLFQRPNPFP-MSIMDNVVAGVRA 86
Cdd:PRK09452 44 TLLGPSGCGKTTVLRLI-------AGFETpdSGRIMLDGQDI---THVPAENRHVNTVFQSYALFPhMTVFENVAFGLRM 113
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2014669168 87 HKMaPRKQFKS-VAEArLTEVGLwDAVKDRlgdSPFRLSGGQQQLLCLARALAVNPDVLLLDEP 149
Cdd:PRK09452 114 QKT-PAAEITPrVMEA-LRMVQL-EEFAQR---KPHQLSGGQQQRVAIARAVVNKPKVLLLDES 171
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1-150 |
8.34e-22 |
|
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: 87.21 E-value: 8.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLNRMNDKVSGfrhsgDVLLGGRTIfADRDLMEFRRSVGMLFQRPNPFPMSIMDNV 80
Cdd:cd03249 24 LTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSG-----EILLDGVDI-RDLNLRWLRSQIGLVSQEPVLFDGTIAENI 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 81 VAGVRAHKMAPRKQFKSVAEARLTEVGLWDAVKDRLGDSPFRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:cd03249 98 RYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEAT 167
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1-152 |
1.21e-21 |
|
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: 84.99 E-value: 1.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLNRMNdkvsgFRHSGDVLLGGRTIfADRDLMEFRRSVGMLFQrpnpfpmsimdnv 80
Cdd:cd00267 20 LTLKAGEIVALVGPNGSGKSTLLRAIAGLL-----KPTSGEILIDGKDI-AKLPLEELRRRIGYVPQ------------- 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2014669168 81 vagvrahkmaprkqfksvaearltevglwdavkdrlgdspfrLSGGQQQLLCLARALAVNPDVLLLDEPTRH 152
Cdd:cd00267 81 ------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSG 110
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
8-150 |
1.84e-21 |
|
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: 85.71 E-value: 1.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 8 VTTLLGPTGSGKTTFLRTLnrmndkvSGFRH--SGDVLLGGRTIFADRDlmEFRRSVGMLFQRPNPFP-MSIMDNVVAGV 84
Cdd:cd03264 27 MYGLLGPNGAGKTTLMRIL-------ATLTPpsSGTIRIDGQDVLKQPQ--KLRRRIGYLPQEFGVYPnFTVREFLDYIA 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2014669168 85 RAHKMAPRKQFKSVAEArLTEVGLWDAVKDRLGDspfrLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:cd03264 98 WLKGIPSKEVKARVDEV-LELVNLGDRAKKKIGS----LSGGMRRRVGIAQALVGDPSILIVDEPT 158
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1-149 |
2.67e-21 |
|
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: 87.85 E-value: 2.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTlnrmndkVSGFRH--SGDVLLGGRTIFaDRDLMEF----RRSVGMLFQRPNPFP- 73
Cdd:COG4148 20 FTLPGRGVTALFGPSGSGKTTLLRA-------IAGLERpdSGRIRLGGEVLQ-DSARGIFlpphRRRIGYVFQEARLFPh 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2014669168 74 MSIMDNVVAGVRAHKMAPRK-QFKSVAEarLTEVGlwdavkDRLGDSPFRLSGGQQQLLCLARALAVNPDVLLLDEP 149
Cdd:COG4148 92 LSVRGNLLYGRKRAPRAERRiSFDEVVE--LLGIG------HLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEP 160
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1-150 |
3.65e-21 |
|
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: 83.99 E-value: 3.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLnrmndkvSGFRH--SGDVLLGGRTIFADRdlMEFRRSVGMLFQRPNPFP-MSIM 77
Cdd:cd03230 21 LTVEKGEIYGLLGPNGAGKTTLIKII-------LGLLKpdSGEIKVLGKDIKKEP--EEVKRRIGYLPEEPSLYEnLTVR 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2014669168 78 DNVvagvrahkmaprkqfksvaearltevglwdavkdrlgdspfRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:cd03230 92 ENL-----------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPT 123
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
10-150 |
4.37e-21 |
|
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: 85.47 E-value: 4.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 10 TLLGPTGSGKTTFLRTlnrmndkVSGFR--HSGDVLLGGRTIfadRDLMEFRRSVGMLFQRPNPFP-MSIMDNVVAGVRa 86
Cdd:cd03299 29 VILGPTGSGKSVLLET-------IAGFIkpDSGKILLNGKDI---TNLPPEKRDISYVPQNYALFPhMTVYKNIAYGLK- 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2014669168 87 HKMAPRKQFksvaEARLTEVGLWDAVKDRLGDSPFRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:cd03299 98 KRKVDKKEI----ERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPF 157
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1-149 |
5.23e-21 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 87.08 E-value: 5.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTlnrmndkVSGFRH--SGDVLLGGRTIfADRDLMEfrRSVGMLFQRPNPFP-MSIM 77
Cdd:PRK11432 27 LTIKQGTMVTLLGPSGCGKTTVLRL-------VAGLEKptEGQIFIDGEDV-THRSIQQ--RDICMVFQSYALFPhMSLG 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2014669168 78 DNVVAGVRAHKMAPRKQFKSVAEArLTEVGLwDAVKDRLGDspfRLSGGQQQLLCLARALAVNPDVLLLDEP 149
Cdd:PRK11432 97 ENVGYGLKMLGVPKEERKQRVKEA-LELVDL-AGFEDRYVD---QISGGQQQRVALARALILKPKVLLFDEP 163
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
11-150 |
5.25e-21 |
|
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: 87.82 E-value: 5.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 11 LLGPTGSGKTTFLRTLNRMNdkvsgfRHSGDVLLGGRTIFA--DRDLMEFRRSVGMLFQrpNPF----P-MSIMDNVVAG 83
Cdd:COG4172 317 LVGESGSGKSTLGLALLRLI------PSEGEIRFDGQDLDGlsRRALRPLRRRMQVVFQ--DPFgslsPrMTVGQIIAEG 388
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2014669168 84 VRAHKMAP-RKQFKSVAEARLTEVGLWDAVKDRLgdsPFRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:COG4172 389 LRVHGPGLsAAERRARVAEALEEVGLDPAARHRY---PHEFSGGQRQRIAIARALILEPKLLVLDEPT 453
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
8-149 |
1.12e-20 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 83.69 E-value: 1.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 8 VTTLLGPTGSGKTTFLRTLNRMNDkvSGFRHSGDVLLGGRTIfadRDLMEFRRSVGMLFQRPNPFP-MSIMDNVVAGVRA 86
Cdd:COG4136 29 ILTLMGPSGSGKSTLLAAIAGTLS--PAFSASGEVLLNGRRL---TALPAEQRRIGILFQDDLLFPhLSVGENLAFALPP 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2014669168 87 HkmAPRKQFKSVAEARLTEVGLwDAVKDRlgdSPFRLSGGQQQLLCLARALAVNPDVLLLDEP 149
Cdd:COG4136 104 T--IGRAQRRARVEQALEEAGL-AGFADR---DPATLSGGQRARVALLRALLAEPRALLLDEP 160
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1-150 |
1.41e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 84.79 E-value: 1.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLNRMNdkvsgFRHSGDVLLGGRTIFAdRDLMEFRRSVGMLFQRPNP--FPMSIMD 78
Cdd:PRK13647 26 LSIPEGSKTALLGPNGAGKSTLLLHLNGIY-----LPQRGRVKVMGREVNA-ENEKWVRSKVGLVFQDPDDqvFSSTVWD 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2014669168 79 NVVAGVRAHKMAPrKQFKSVAEARLTEVGLWDaVKDRlgdSPFRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:PRK13647 100 DVAFGPVNMGLDK-DEVERRVEEALKAVRMWD-FRDK---PPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPM 166
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
3-150 |
1.54e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 85.07 E-value: 1.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 3 FPARSVTTLLGPTGSGKTTFLRTLNRMNDKVSGfrhsgDVLLGGRTIFA---DRDLMEFRRSVGMLFQRPNP--FPMSIM 77
Cdd:PRK13634 30 IPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSG-----TVTIGERVITAgkkNKKLKPLRKKVGIVFQFPEHqlFEETVE 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2014669168 78 DNVVAGVRAHKMaPRKQFKSVAEARLTEVGLWDAVKDRlgdSPFRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:PRK13634 105 KDICFGPMNFGV-SEEDAKQKAREMIELVGLPEELLAR---SPFELSGGQMRRVAIAGVLAMEPEVLVLDEPT 173
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-150 |
1.56e-20 |
|
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: 83.30 E-value: 1.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLnrmndkvSGFRH--SGDVLLGGRTIFADRDlmEFRRSVGMLFQRPNPFP-MSIM 77
Cdd:COG4133 23 FTLAAGEALALTGPNGSGKTTLLRIL-------AGLLPpsAGEVLWNGEPIRDARE--DYRRRLAYLGHADGLKPeLTVR 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2014669168 78 DNVVAGVRAHKMAPRKQfkSVAEArLTEVGLwdavkDRLGDSPFR-LSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:COG4133 94 ENLRFWAALYGLRADRE--AIDEA-LEAVGL-----AGLADLPVRqLSAGQKRRVALARLLLSPAPLWLLDEPF 159
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-149 |
2.24e-20 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 83.27 E-value: 2.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLrtlnrmnDKVSGFR--HSGDVLLGGRTIfadRDLMEFRRSVGMLFQRPNPFP-MSIM 77
Cdd:COG3840 20 LTIAAGERVAILGPSGAGKSTLL-------NLIAGFLppDSGRILWNGQDL---TALPPAERPVSMLFQENNLFPhLTVA 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2014669168 78 DNVVAGVRAHKMAPRKQFKSVAEArLTEVGLwDAVKDRLgdsPFRLSGGQQQLLCLARALAVNPDVLLLDEP 149
Cdd:COG3840 90 QNIGLGLRPGLKLTAEQRAQVEQA-LERVGL-AGLLDRL---PGQLSGGQRQRVALARCLVRKRPILLLDEP 156
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-150 |
3.07e-20 |
|
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: 83.11 E-value: 3.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLnrmndkvSGF--RHSGDVLLGGRTIFADR--DLMefRRSVGMLFQRPNPFP-MS 75
Cdd:COG0410 24 LEVEEGEIVALLGRNGAGKTTLLKAI-------SGLlpPRSGSIRFDGEDITGLPphRIA--RLGIGYVPEGRRIFPsLT 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2014669168 76 IMDNVVAGVRAHKMAPRkqfksvAEARLTEV-GLWDAVKDRLGDSPFRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:COG0410 95 VEENLLLGAYARRDRAE------VRADLERVyELFPRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPS 164
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1-150 |
1.08e-19 |
|
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: 81.51 E-value: 1.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLNRMNDkVSgfrhSGDVLLGGRTIfADRDLMEFRRSVGMLFQRPNPFPMSIMDNV 80
Cdd:cd03251 23 LDIPAGETVALVGPSGSGKSTLVNLIPRFYD-VD----SGRILIDGHDV-RDYTLASLRRQIGLVSQDVFLFNDTVAENI 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2014669168 81 VAGVRAhkmAPRKQFKSVAE-ARLTEV--GLWDAVKDRLGDSPFRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:cd03251 97 AYGRPG---ATREEVEEAARaANAHEFimELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEAT 166
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1-150 |
1.51e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 82.47 E-value: 1.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLNRMNDKVSGFRHSGDVLLGGRTifADRDLMEFRRSVGMLFQRPNP--FPMSIMD 78
Cdd:PRK13643 27 LEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTS--KQKEIKPVRKKVGVVFQFPESqlFEETVLK 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2014669168 79 NVVAGVRAHKMApRKQFKSVAEARLTEVGLwdaVKDRLGDSPFRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:PRK13643 105 DVAFGPQNFGIP-KEKAEKIAAEKLEMVGL---ADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPT 172
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
11-150 |
3.08e-19 |
|
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: 82.81 E-value: 3.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 11 LLGPTGSGKT-TFLRTLNRMNDKVSgfRHSGDVLLGGRTIFA--DRDLMEFR-RSVGMLFQRP----NPFpMSIMDNVVA 82
Cdd:COG4172 41 LVGESGSGKSvTALSILRLLPDPAA--HPSGSILFDGQDLLGlsERELRRIRgNRIAMIFQEPmtslNPL-HTIGKQIAE 117
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2014669168 83 GVRAHKMAPRKQFKSVAEARLTEVGLWDAvKDRLGDSPFRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:COG4172 118 VLRLHRGLSGAAARARALELLERVGIPDP-ERRLDAYPHQLSGGQRQRVMIAMALANEPDLLIADEPT 184
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
11-150 |
3.33e-19 |
|
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: 80.17 E-value: 3.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 11 LLGPTGSGKTTFLRTLNRMnDKVSgfrhSGDVLLGGRTIFA-DRD-LMEFR-RSVGMLFQR----PNpfpMSIMDNVvag 83
Cdd:COG4181 43 IVGASGSGKSTLLGLLAGL-DRPT----SGTVRLAGQDLFAlDEDaRARLRaRHVGFVFQSfqllPT---LTALENV--- 111
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2014669168 84 vrahkMAP-----RKQFKSVAEARLTEVGLwdavKDRLGDSPFRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:COG4181 112 -----MLPlelagRRDARARARALLERVGL----GHRLDHYPAQLSGGEQQRVALARAFATEPAILFADEPT 174
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
7-150 |
3.88e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 80.94 E-value: 3.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 7 SVTTLLGPTGSGKTTFLRTLNRMNDKVSGfrhsgDVLLGGRTIFAD---RDLMEFRRSVGMLFQRPNP--FPMSIMDNVV 81
Cdd:PRK13649 34 SYTAFIGHTGSGKSTIMQLLNGLHVPTQG-----SVRVDDTLITSTsknKDIKQIRKKVGLVFQFPESqlFEETVLKDVA 108
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2014669168 82 AGVRAHKMAPrKQFKSVAEARLTEVGLWDAVKDRlgdSPFRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:PRK13649 109 FGPQNFGVSQ-EEAEALAREKLALVGISESLFEK---NPFELSGGQMRRVAIAGILAMEPKILVLDEPT 173
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-150 |
9.04e-19 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 80.62 E-value: 9.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLNRMNdKVSgfrhSGDVLLGGR--TIFADRDLMEFRRSVGMLFQRPN-------- 70
Cdd:PRK11153 26 LHIPAGEIFGVIGASGAGKSTLIRCINLLE-RPT----SGRVLVDGQdlTALSEKELRKARRQIGMIFQHFNllssrtvf 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 71 ---PFPMSImdnvvAGVrahkmaPRKQFKSVAEARLTEVGLWDAvKDRLgdsPFRLSGGQQQLLCLARALAVNPDVLLLD 147
Cdd:PRK11153 101 dnvALPLEL-----AGT------PKAEIKARVTELLELVGLSDK-ADRY---PAQLSGGQKQRVAIARALASNPKVLLCD 165
|
...
gi 2014669168 148 EPT 150
Cdd:PRK11153 166 EAT 168
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
11-149 |
1.46e-18 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 80.65 E-value: 1.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 11 LLGPTGSGKTTFLRTLnrmndkvSGFRH--SGDVLLGGRTIfadRDLMEFRRSVGMLFQRPNPFP-MSIMDNVVAGVRAH 87
Cdd:PRK11607 50 LLGASGCGKSTLLRML-------AGFEQptAGQIMLDGVDL---SHVPPYQRPINMMFQSYALFPhMTVEQNIAFGLKQD 119
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2014669168 88 KMaPRKQFKSVAEARLTEVGLWDAVKDRlgdsPFRLSGGQQQLLCLARALAVNPDVLLLDEP 149
Cdd:PRK11607 120 KL-PKAEIASRVNEMLGLVHMQEFAKRK----PHQLSGGQRQRVALARSLAKRPKLLLLDEP 176
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
5-150 |
1.48e-18 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 79.24 E-value: 1.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 5 ARSVTTLLGPTGSGKTTFLRTLNRMNDKVSGFRHSGDVLL-------GGRTIFADRDLMEFRRSVGMLFQRPNPFP-MSI 76
Cdd:PRK10619 30 AGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlvrdkdGQLKVADKNQLRLLRTRLTMVFQHFNLWShMTV 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2014669168 77 MDNVV-AGVRAHKMApRKQFKSVAEARLTEVGLWDAVKDRLgdsPFRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:PRK10619 110 LENVMeAPIQVLGLS-KQEARERAVKYLAKVGIDERAQGKY---PVHLSGGQQQRVSIARALAMEPEVLLFDEPT 180
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
4-152 |
1.52e-18 |
|
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: 78.22 E-value: 1.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 4 PARSVTTLLGPTGSGKTTFLRTLNRMNDKVSGfrhsgDVLLGGRTI--FADRDLMEFRRSVGMLFQRPNPFP-MSIMDNV 80
Cdd:cd03292 25 SAGEFVFLVGPSGAGKSTLLKLIYKEELPTSG-----TIRVNGQDVsdLRGRAIPYLRRKIGVVFQDFRLLPdRNVYENV 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2014669168 81 VAGVRAHKMAPRKQFKSVAEArLTEVGLwdavKDRLGDSPFRLSGGQQQLLCLARALAVNPDVLLLDEPTRH 152
Cdd:cd03292 100 AFALEVTGVPPREIRKRVPAA-LELVGL----SHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGN 166
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-150 |
2.28e-18 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 78.66 E-value: 2.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLnrmndkvSGFR--HSGDVLLGGRTIfADRDLMEFRRSVGMLFQRPN-PFPMSIM 77
Cdd:PRK13548 23 LTLRPGEVVAILGPNGAGKSTLLRAL-------SGELspDSGEVRLNGRPL-ADWSPAELARRRAVLPQHSSlSFPFTVE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 78 DnVVAGVRAHKMAPRKQFKSVAEARLTEVGLWDavkdrLGDSPFR-LSGGQQQLLCLARALA------VNPDVLLLDEPT 150
Cdd:PRK13548 95 E-VVAMGRAPHGLSRAEDDALVAAALAQVDLAH-----LAGRDYPqLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPT 168
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1-150 |
2.50e-18 |
|
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: 77.93 E-value: 2.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTT---FLRTLNRMNdkvsgfrhSGDVLLGGRTIFADRDlmEFRRSVGMLFQRPNPFP-MSI 76
Cdd:cd03263 23 LNVYKGEIFGLLGHNGAGKTTtlkMLTGELRPT--------SGTAYINGYSIRTDRK--AARQSLGYCPQFDALFDeLTV 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2014669168 77 MDNVV--AGVRAHkmaPRKQFKSVAEARLTEVGLWDAVKDRLGDspfrLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:cd03263 93 REHLRfyARLKGL---PKSEIKEEVELLLRVLGLTDKANKRART----LSGGMKRKLSLAIALIGGPSVLLLDEPT 161
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
11-150 |
5.89e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 77.75 E-value: 5.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 11 LLGPTGSGKTTFLRTLNRMNdkvsgFRHSGDVLLGGRTIfADRDLMEFRRSVGMLFQRP-NPF-PMSIMDNVVAGVRAHK 88
Cdd:PRK13635 38 IVGHNGSGKSTLAKLLNGLL-----LPEAGTITVGGMVL-SEETVWDVRRQVGMVFQNPdNQFvGATVQDDVAFGLENIG 111
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2014669168 89 MaPRKQFKSVAEARLTEVGLwdavKDRLGDSPFRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:PRK13635 112 V-PREEMVERVDQALRQVGM----EDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEAT 168
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
11-150 |
5.95e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 77.90 E-value: 5.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 11 LLGPTGSGKTTFLRTLNRMNDKVSGFRHSGDVLLGGRTifADRDLMEFRRSVGMLFQRPNP--FPMSIMDNVVAGVRAHK 88
Cdd:PRK13646 38 IVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKT--KDKYIRPVRKRIGMVFQFPESqlFEDTVEREIIFGPKNFK 115
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2014669168 89 MaPRKQFKSVAEARLTEVGLwdaVKDRLGDSPFRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:PRK13646 116 M-NLDEVKNYAHRLLMDLGF---SRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPT 173
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
1-152 |
6.60e-18 |
|
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: 79.33 E-value: 6.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLNRMNDKvsgfrHSGDVLLGGRTIfADRDLMEFRRSVGMLFQRPNPFPMSIMDNV 80
Cdd:TIGR02868 356 LDLPPGERVAILGPSGSGKSTLLATLAGLLDP-----LQGEVTLDGVPV-SSLDQDEVRRRVSVCAQDAHLFDTTVRENL 429
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2014669168 81 VAGvrAHKMAPRKQFKSVAEARLTEV--GLWDAVKDRLGDSPFRLSGGQQQLLCLARALAVNPDVLLLDEPTRH 152
Cdd:TIGR02868 430 RLA--RPDATDEELWAALERVGLADWlrALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEH 501
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-149 |
7.59e-18 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 77.50 E-value: 7.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLNRMNDKvsgfrHSGDVLLGGRTI--FADRDLMEFRRSVGMLFQRPNPFP-MSIM 77
Cdd:PRK11831 28 LTVPRGKITAIMGPSGIGKTTLLRLIGGQIAP-----DHGEILFDGENIpaMSRSRLYTVRKRMSMLFQSGALFTdMNVF 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2014669168 78 DNVVAGVRAHKMAPRKQFKSVAEARLTEVGLWDAVKDRlgdsPFRLSGGQQQLLCLARALAVNPDVLLLDEP 149
Cdd:PRK11831 103 DNVAYPLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLM----PSELSGGMARRAALARAIALEPDLIMFDEP 170
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
1-149 |
1.05e-17 |
|
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: 77.84 E-value: 1.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTlnrmndkVSGFR--HSGDVLLGGRTIFADR---DLMEFRRSVGMLFQRPNPFP-M 74
Cdd:TIGR02142 18 FTLPGQGVTAIFGRSGSGKTTLIRL-------IAGLTrpDEGEIVLNGRTLFDSRkgiFLPPEKRRIGYVFQEARLFPhL 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2014669168 75 SIMDNVVAGVRAHKMAPRKqfksVAEARLTEVGLWDAVKDRLgdsPFRLSGGQQQLLCLARALAVNPDVLLLDEP 149
Cdd:TIGR02142 91 SVRGNLRYGMKRARPSERR----ISFERVIELLGIGHLLGRL---PGRLSGGEKQRVAIGRALLSSPRLLLMDEP 158
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
1-150 |
1.98e-17 |
|
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: 77.86 E-value: 1.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLnrmndkVSGFR-HSGDVLLGGRTIfADRDLMEFRRSVGMLFQRPNPFPMSIMDN 79
Cdd:TIGR01193 495 LTIKMNSKTTIVGMSGSGKSTLAKLL------VGFFQaRSGEILLNGFSL-KDIDRHTLRQFINYLPQEPYIFSGSILEN 567
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2014669168 80 VVAGVRAHKMAPR-KQFKSVAEARLTEVGLWDAVKDRLGDSPFRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:TIGR01193 568 LLLGAKENVSQDEiWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDEST 639
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
11-150 |
2.98e-17 |
|
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: 75.51 E-value: 2.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 11 LLGPTGSGKTTFLRTLNRMNDKVSGfrhsGDVLLGGRTiFADRDLMEFRRSVGML---FQRPNPFPMSIMDNVVAGVRA- 86
Cdd:COG1119 34 ILGPNGAGKSTLLSLITGDLPPTYG----NDVRLFGER-RGGEDVWELRKRIGLVspaLQLRFPRDETVLDVVLSGFFDs 108
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2014669168 87 ---HKMAPRKQfKSVAEARLTEVGLWDavkdrLGDSPFR-LSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:COG1119 109 iglYREPTDEQ-RERARELLELLGLAH-----LADRPFGtLSQGEQRRVLIARALVKDPELLILDEPT 170
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
1-150 |
3.40e-17 |
|
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: 74.56 E-value: 3.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLnrmndkvSGFRH--SGDVLLGGRTIFadrDLMEFRRSVGMLFQRPNPFP-MSIM 77
Cdd:cd03268 21 LHVKKGEIYGFLGPNGAGKTTTMKII-------LGLIKpdSGEITFDGKSYQ---KNIEALRRIGALIEAPGFYPnLTAR 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2014669168 78 DNVVAGVRAHkMAPRKQFKSVaearLTEVGLWDAVKDRLGDspfrLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:cd03268 91 ENLRLLARLL-GIRKKRIDEV----LDVVGLKDSAKKKVKG----FSLGMKQRLGIALALLGNPDLLILDEPT 154
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-150 |
5.19e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 75.27 E-value: 5.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLNRMNDKVSGfrhsgDVLLGGRTI-FADRDLMEFRRSVGMLFQRPNP--FPMSIM 77
Cdd:PRK13636 27 INIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSG-----RILFDGKPIdYSRKGLMKLRESVGMVFQDPDNqlFSASVY 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2014669168 78 DNVVAGVRAHKMaPRKQFKSVAEARLTEVGLwdavkDRLGDSPFR-LSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:PRK13636 102 QDVSFGAVNLKL-PEDEVRKRVDNALKRTGI-----EHLKDKPTHcLSFGQKKRVAIAGVLVMEPKVLVLDEPT 169
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
10-150 |
5.40e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 75.47 E-value: 5.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 10 TLLGPTGSGKTTFLRTLNRMNDKvsgfrHSGDVLLGGRTIFADR-DLMEFRRSVGMLFQRP--NPFPMSIMDNVVAGVRA 86
Cdd:PRK13637 37 GLIGHTGSGKSTLIQHLNGLLKP-----TSGKIIIDGVDITDKKvKLSDIRKKVGLVFQYPeyQLFEETIEKDIAFGPIN 111
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2014669168 87 HKMAPRKQFKSVAEArLTEVGL-WDAVKDRlgdSPFRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:PRK13637 112 LGLSEEEIENRVKRA-MNIVGLdYEDYKDK---SPFELSGGQKRRVAIAGVVAMEPKILILDEPT 172
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
1-150 |
1.03e-16 |
|
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: 73.71 E-value: 1.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLnrmndkvSGF--RHSGDVLLGGRTIFADRDLMEFRRSVGMLFQRPNPFP-MSIM 77
Cdd:TIGR03410 21 LEVPKGEVTCVLGRNGVGKTTLLKTL-------MGLlpVKSGSIRLDGEDITKLPPHERARAGIAYVPQGREIFPrLTVE 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2014669168 78 DNVVAGVRAHKMAPRKQFKSVAEarLTEVgLWDAVKDRLGDspfrLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:TIGR03410 94 ENLLTGLAALPRRSRKIPDEIYE--LFPV-LKEMLGRRGGD----LSGGQQQQLAIARALVTRPKLLLLDEPT 159
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1-152 |
1.82e-16 |
|
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: 71.86 E-value: 1.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLnrmndkvSGFRH--SGDVLLGGRTIFaDRDLMEFRRSVGMLFQRPNPFPMSIMD 78
Cdd:cd03246 23 FSIEPGESLAIIGPSGSGKSTLARLI-------LGLLRptSGRVRLDGADIS-QWDPNELGDHVGYLPQDDELFSGSIAE 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2014669168 79 NVvagvrahkmaprkqfksvaearltevglwdavkdrlgdspfrLSGGQQQLLCLARALAVNPDVLLLDEPTRH 152
Cdd:cd03246 95 NI------------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSH 126
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
4-150 |
1.85e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 73.63 E-value: 1.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 4 PARSVTTLLGPTGSGKTTFLRTLNRMnDKVSgfrhSGDVLLGGRTIfADRDLMEFRRSVGMLFQRP-NPFPMSIMDNVVA 82
Cdd:PRK13648 33 PKGQWTSIVGHNGSGKSTIAKLMIGI-EKVK----SGEIFYNNQAI-TDDNFEKLRKHIGIVFQNPdNQFVGSIVKYDVA 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2014669168 83 -GVRAHkMAPRKQFKSVAEARLTEVGLWDavkdRLGDSPFRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:PRK13648 107 fGLENH-AVPYDEMHRRVSEALKQVDMLE----RADYEPNALSGGQKQRVAIAGVLALNPSVIILDEAT 170
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
11-150 |
2.14e-16 |
|
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: 72.62 E-value: 2.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 11 LLGPTGSGKTTFLRTLnrmndkvSGFR--HSGDVLLGG---RTIfadrDLMEFRRSVGMLFQRPNPFPMSIMDNVVAGVR 85
Cdd:cd03245 35 IIGRVGSGKSTLLKLL-------AGLYkpTSGSVLLDGtdiRQL----DPADLRRNIGYVPQDVTLFYGTLRDNITLGAP 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2014669168 86 AHKmaprkqfksvaEARLTEV----GLWDAVKD-------RLGDSPFRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:cd03245 104 LAD-----------DERILRAaelaGVTDFVNKhpngldlQIGERGRGLSGGQRQAVALARALLNDPPILLLDEPT 168
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
10-150 |
2.87e-16 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 72.44 E-value: 2.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 10 TLLGPTGSGKTTFLRTLNrMNDKVSgfrhSGDVLLGGRTI----FADRdlMEFRRS-VGMLFQRPNPFP-MSIMDNVVAG 83
Cdd:NF038007 35 SIMGPSGSGKSTLLNIIG-MFDSLD----SGSLTLAGKEVtnlsYSQK--IILRRElIGYIFQSFNLIPhLSIFDNVALP 107
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2014669168 84 VRAHKMAPRKQFKSVAEArLTEVGLwdavKDRLGDSPFRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:NF038007 108 LKYRGVAKKERIERVNQV-LNLFGI----DNRRNHKPMQLSGGQQQRVAIARAMVSNPALLLADEPT 169
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
10-150 |
4.48e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 72.84 E-value: 4.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 10 TLLGPTGSGKTTFLRTLNRMNDKvsgfrHSGDVLLGGRTIFADrDLMEFRRSVGMLFQRP-NPFPMSIMDNVVAGVRAHK 88
Cdd:PRK13650 37 SIIGHNGSGKSTTVRLIDGLLEA-----ESGQIIIDGDLLTEE-NVWDIRHKIGMVFQNPdNQFVGATVEDDVAFGLENK 110
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2014669168 89 MAPRKQFKSVAEARLTEVGLWDaVKDRlgdSPFRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:PRK13650 111 GIPHEEMKERVNEALELVGMQD-FKER---EPARLSGGQKQRVAIAGAVAMRPKIIILDEAT 168
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
4-150 |
4.54e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 72.91 E-value: 4.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 4 PARSVTTLLGPTGSGKTTFLRTLNRM-----NDK----VSGfrhsgdVLLGGRTIFadrdlmEFRRSVGMLFQRP-NPF- 72
Cdd:PRK13640 31 PRGSWTALIGHNGSGKSTISKLINGLllpddNPNskitVDG------ITLTAKTVW------DIREKVGIVFQNPdNQFv 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2014669168 73 PMSIMDNVVAGVRaHKMAPRKQFKSVAEARLTEVGLWDAVKDRlgdsPFRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:PRK13640 99 GATVGDDVAFGLE-NRAVPRPEMIKIVRDVLADVGMLDYIDSE----PANLSGGQKQRVAIAGILAVEPKIIILDEST 171
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
4-150 |
6.63e-16 |
|
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: 71.49 E-value: 6.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 4 PARSVTTLLGPTGSGKTTFLRTLNRMNDkVSgfrhSGDVLLGGRTIfADRDLMEFRRSVGMLFQRPNPFPMSIMDNVVAG 83
Cdd:cd03253 25 PAGKKVAIVGPSGSGKSTILRLLFRFYD-VS----SGSILIDGQDI-REVTLDSLRRAIGVVPQDTVLFNDTIGYNIRYG 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 84 -VRAhkmAPRKQFKSVAEARLTE--VGLWDAVKDRLGDSPFRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:cd03253 99 rPDA---TDEEVIEAAKAAQIHDkiMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLDEAT 165
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-150 |
6.88e-16 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 71.97 E-value: 6.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLNRMNDKVsgfrhSGDVLLGGRTI--FADRDLMefrRSVGMLFQR-PNPFPMSIM 77
Cdd:PRK11231 23 LSLPTGKITALIGPNGCGKSTLLKCFARLLTPQ-----SGTVFLGDKPIsmLSSRQLA---RRLALLPQHhLTPEGITVR 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2014669168 78 DNVVAGVRAH-----KMAPRKQfKSVAEA-RLTEVglwDAVKDRLGDSpfrLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:PRK11231 95 ELVAYGRSPWlslwgRLSAEDN-ARVNQAmEQTRI---NHLADRRLTD---LSGGQRQRAFLAMVLAQDTPVVLLDEPT 166
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1-150 |
7.92e-16 |
|
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: 71.15 E-value: 7.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLNRMNDkvSGFRHSGDVLLGGRtifaDRDLMEFRRSVGMLFQrpnpfpmsiMDNV 80
Cdd:cd03234 28 LHVESGQVMAILGSSGSGKTTLLDAISGRVE--GGGTTSGQILFNGQ----PRKPDQFQKCVAYVRQ---------DDIL 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2014669168 81 VAG--VR------AHKMAPRKQFKSVAEARLTEVGLWDAVKDRLGDSPFR-LSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:cd03234 93 LPGltVRetltytAILRLPRKSSDAIRKKRVEDVLLRDLALTRIGGNLVKgISGGERRRVSIAVQLLWDPKVLILDEPT 171
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
8-150 |
1.02e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 71.65 E-value: 1.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 8 VTTLLGPTGSGKTTFLRTLNRMNDKVSGfrhsgDVLLGGRTI-FADRDLMEFRRSVGMLFQRPNP--FPMSIMDNVVAGV 84
Cdd:PRK13639 30 MVALLGPNGAGKSTLFLHFNGILKPTSG-----EVLIKGEPIkYDKKSLLEVRKTVGIVFQNPDDqlFAPTVEEDVAFGP 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2014669168 85 RAHKMAPRKQFKSVAEArLTEVGLWDAVKDrlgdSPFRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:PRK13639 105 LNLGLSKEEVEKRVKEA-LKAVGMEGFENK----PPHHLSGGQKKRVAIAGILAMKPEIIVLDEPT 165
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
1-150 |
1.03e-15 |
|
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: 72.83 E-value: 1.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLNRmndkvsgFRH--SGDVLLGGRTIfADRDLMEFRRSVGMLFQRPNPFPMSIMD 78
Cdd:TIGR02203 353 LVIEPGETVALVGRSGSGKSTLVNLIPR-------FYEpdSGQILLDGHDL-ADYTLASLRRQVALVSQDVVLFNDTIAN 424
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2014669168 79 NVVAGVRAHkmAPRKQFKSVAE-ARLTEV--GLWDAVKDRLGDSPFRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:TIGR02203 425 NIAYGRTEQ--ADRAEIERALAaAYAQDFvdKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEAT 497
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
11-150 |
1.26e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 71.66 E-value: 1.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 11 LLGPTGSGKTTFLRTLN-----------------RMNDKVSGFRHSGDVLLGGRTIFAD-RDLMEFRRSVGMLFQ--RPN 70
Cdd:PRK13651 38 IIGQTGSGKTTFIEHLNalllpdtgtiewifkdeKNKKKTKEKEKVLEKLVIQKTRFKKiKKIKEIRRRVGVVFQfaEYQ 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 71 PFPMSIMDNVVAGVRAHKMaPRKQFKSVAEARLTEVGLWDAVKDRlgdSPFRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:PRK13651 118 LFEQTIEKDIIFGPVSMGV-SKEEAKKRAAKYIELVGLDESYLQR---SPFELSGGQKRRVALAGILAMEPDFLVFDEPT 193
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
8-150 |
1.34e-15 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 72.36 E-value: 1.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 8 VTTLLGPTGSGKTTFLRTLnrmndkvSGF--RHSGDVLLGGRTI-FAD-RDLMefRRSVGMLFQRPNPFP-MSIMDNVVA 82
Cdd:COG1129 32 VHALLGENGAGKSTLMKIL-------SGVyqPDSGEILLDGEPVrFRSpRDAQ--AAGIAIIHQELNLVPnLSVAENIFL 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 83 G--VRAHKMAPRKQFKSVAEARLTEVGLWDAVKDRLGDspfrLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:COG1129 103 GrePRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGD----LSVAQQQLVEIARALSRDARVLILDEPT 168
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1-149 |
1.43e-15 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 71.25 E-value: 1.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLnrmndkvSGFRH-SGDVLLGGRTifadrDLMEFRRSVGMLFQRPNPFP-MSIMD 78
Cdd:PRK11247 33 LHIPAGQFVAVVGRSGCGKSTLLRLL-------AGLETpSAGELLAGTA-----PLAEAREDTRLMFQDARLLPwKKVID 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2014669168 79 NVVAGVRAHkmaprkqFKSVAEARLTEVGLwdavKDRLGDSPFRLSGGQQQLLCLARALAVNPDVLLLDEP 149
Cdd:PRK11247 101 NVGLGLKGQ-------WRDAALQALAAVGL----ADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEP 160
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
11-152 |
1.89e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 72.02 E-value: 1.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 11 LLGPTGSGKTTFLRTLnrmndkvsgfrhSGDVLLGGRTIFADRDLmefrrSVGMLFQRPNPFP-MSIMDNVVAGVR---- 85
Cdd:COG0488 29 LVGRNGAGKSTLLKIL------------AGELEPDSGEVSIPKGL-----RIGYLPQEPPLDDdLTVLDTVLDGDAelra 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 86 --------AHKMA-PRKQFKSVAE--ARLTEVGLWDA------------VKDRLGDSPFR-LSGGQQQLLCLARALAVNP 141
Cdd:COG0488 92 leaeleelEAKLAePDEDLERLAElqEEFEALGGWEAearaeeilsglgFPEEDLDRPVSeLSGGWRRRVALARALLSEP 171
|
170
....*....|.
gi 2014669168 142 DVLLLDEPTRH 152
Cdd:COG0488 172 DLLLLDEPTNH 182
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
8-148 |
2.02e-15 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 71.99 E-value: 2.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 8 VTTLLGPTGSGKTTFLRTLNRMNDKVSGfrhsgDVLLGGRTI--FADRDLMEFRRS-VGMLFQRPNPFP-MSIMDNVVAG 83
Cdd:PRK10070 56 IFVIMGLSGSGKSTMVRLLNRLIEPTRG-----QVLIDGVDIakISDAELREVRRKkIAMVFQSFALMPhMTVLDNTAFG 130
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2014669168 84 VRAHKMAPRKQFKSVAEArLTEVGLwdavKDRLGDSPFRLSGGQQQLLCLARALAVNPDVLLLDE 148
Cdd:PRK10070 131 MELAGINAEERREKALDA-LRQVGL----ENYAHSYPDELSGGMRQRVGLARALAINPDILLMDE 190
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
12-149 |
2.14e-15 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 70.50 E-value: 2.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 12 LGPTGSGKTTFLrtlnrmnDKVSGFR--HSGDVLLGGRTIF---ADRdlmefrrsvGMLFQRPNPFP-MSIMDNVVAGVR 85
Cdd:PRK11248 33 LGPSGCGKTTLL-------NLIAGFVpyQHGSITLDGKPVEgpgAER---------GVVFQNEGLLPwRNVQDNVAFGLQ 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2014669168 86 AHKMaPRKQFKSVAEARLTEVGLWDAVKDRlgdsPFRLSGGQQQLLCLARALAVNPDVLLLDEP 149
Cdd:PRK11248 97 LAGV-EKMQRLEIAHQMLKKVGLEGAEKRY----IWQLSGGQRQRVGIARALAANPQLLLLDEP 155
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
8-150 |
2.23e-15 |
|
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: 70.19 E-value: 2.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 8 VTTLLGPTGSGKTTFLRTLNRMNDKvsgfrHSGDVLLGGRTIfADRDLMEFRRSVGMLFQRPNPFPMSIMDNVVAGVRAH 87
Cdd:cd03248 42 VTALVGPSGSGKSTVVALLENFYQP-----QGGQVLLDGKPI-SQYEHKYLHSKVSLVGQEPVLFARSLQDNIAYGLQSC 115
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2014669168 88 KMAPRKQFKSVAEARLTEVGLWDAVKDRLGDSPFRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:cd03248 116 SFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEAT 178
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1-150 |
2.31e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 71.80 E-value: 2.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDF--PARSVTTLLGPTGSGKTTFLRTLnrmndkvSGF-RHSGDVLLGGrTIFADRDLMEFRRSVGMLFQRPNPFPMSIM 77
Cdd:PRK11174 369 LNFtlPAGQRIALVGPSGAGKTSLLNAL-------LGFlPYQGSLKING-IELRELDPESWRKHLSWVGQNPQLPHGTLR 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 78 DNVVAGvraHKMAPRKQFKSVAE-ARLTE------VGLWDAVKDRLGdspfRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:PRK11174 441 DNVLLG---NPDASDEQLQQALEnAWVSEflpllpQGLDTPIGDQAA----GLSVGQAQRLALARALLQPCQLLLLDEPT 513
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
7-149 |
2.63e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 70.63 E-value: 2.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 7 SVTTLLGPTGSGKTTFLRTLNRMNdKVSgfrhSGDVLLGGRTIFAD---RDLMEFRRSVGMLFQRPNP--FPMSIMDNVV 81
Cdd:PRK13641 34 SFVALVGHTGSGKSTLMQHFNALL-KPS----SGTITIAGYHITPEtgnKNLKKLRKKVSLVFQFPEAqlFENTVLKDVE 108
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2014669168 82 AGVRAHKmAPRKQFKSVAEARLTEVGLWDAVKDRlgdSPFRLSGGQQQLLCLARALAVNPDVLLLDEP 149
Cdd:PRK13641 109 FGPKNFG-FSEDEAKEKALKWLKKVGLSEDLISK---SPFELSGGQMRRVAIAGVMAYEPEILCLDEP 172
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-150 |
2.68e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 70.40 E-value: 2.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLnrmndkvSGF--RHSGDVLLGGRTIFADrDLMEFRRSVGMLFQRP-NPF-PMSI 76
Cdd:PRK13632 30 FEINEGEYVAILGHNGSGKSTISKIL-------TGLlkPQSGEIKIDGITISKE-NLKEIRKKIGIIFQNPdNQFiGATV 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2014669168 77 MDNVVAGVRaHKMAPRKQFKSVAEARLTEVGLwdavKDRLGDSPFRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:PRK13632 102 EDDIAFGLE-NKKVPPKKMKDIIDDLAKKVGM----EDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDEST 170
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
11-149 |
2.68e-15 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 70.00 E-value: 2.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 11 LLGPTGSGKTTFLRTlnrmndkVSGF--RHSGDVLLGGRTIfadRDLMEFRRS---VGMLFQRPNPF-PMSIMDNVVAGV 84
Cdd:TIGR04406 32 LLGPNGAGKTTSFYM-------IVGLvrPDAGKILIDGQDI---THLPMHERArlgIGYLPQEASIFrKLTVEENIMAVL 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2014669168 85 RAHKMAPRKQFKSVAEARLTEVGLwdavkDRLGDSP-FRLSGGQQQLLCLARALAVNPDVLLLDEP 149
Cdd:TIGR04406 102 EIRKDLDRAEREERLEALLEEFQI-----SHLRDNKaMSLSGGERRRVEIARALATNPKFILLDEP 162
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1-149 |
3.13e-15 |
|
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: 69.44 E-value: 3.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLrtlnrmnDKVSGFR--HSGDVLLGGrtifADRDLME-FRRSVGMLFQRPNPFP-MSI 76
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLL-------NLIAGFEtpQSGRVLING----VDVTAAPpADRPVSMLFQENNLFAhLTV 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2014669168 77 MDNVVAGvRAHKMAPRKQFKSVAEARLTEVGLWDAVKDRlgdsPFRLSGGQQQLLCLARALAVNPDVLLLDEP 149
Cdd:cd03298 88 EQNVGLG-LSPGLKLTAEDRQAIEVALARVGLAGLEKRL----PGELSGGERQRVALARVLVRDKPVLLLDEP 155
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
2-150 |
6.39e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 69.88 E-value: 6.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 2 DFPARSVTTLLGPTGSGKTTFLRTLNRMNDKVSGFRHSGDVLLGGRTIFAD----------RDLMEFRRSVGMLFQRP-- 69
Cdd:PRK13631 48 TFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHElitnpyskkiKNFKELRRRVSMVFQFPey 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 70 NPFPMSIMDNVVAGVRAHKMaPRKQFKSVAEARLTEVGLWDAVKDRlgdSPFRLSGGQQQLLCLARALAVNPDVLLLDEP 149
Cdd:PRK13631 128 QLFKDTIEKDIMFGPVALGV-KKSEAKKLAKFYLNKMGLDDSYLER---SPFGLSGGQKRRVAIAGILAIQPEILIFDEP 203
|
.
gi 2014669168 150 T 150
Cdd:PRK13631 204 T 204
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
13-150 |
6.72e-15 |
|
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: 68.67 E-value: 6.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 13 GPTGSGKTTFLRTLNRMNDKVSGfrhsgDVLLGGRTIfADRDLMEFRRSVGMLFQRPNPFPMSIMDNvvagvrahkMAPR 92
Cdd:cd03244 37 GRTGSGKSSLLLALFRLVELSSG-----SILIDGVDI-SKIGLHDLRSRISIIPQDPVLFSGTIRSN---------LDPF 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2014669168 93 KQF--KSVAEArLTEVGLWDAVKDRLGDSPFR-------LSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:cd03244 102 GEYsdEELWQA-LERVGLKEFVESLPGGLDTVveeggenLSVGQRQLLCLARALLRKSKILVLDEAT 167
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
11-149 |
1.55e-14 |
|
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: 67.95 E-value: 1.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 11 LLGPTGSGKTTFLRTlnrmndkVSGFRH--SGDVLLGGRTIfadRDLMEFRRS---VGMLFQRPNPF-PMSIMDNVVAGV 84
Cdd:cd03218 31 LLGPNGAGKTTTFYM-------IVGLVKpdSGKILLDGQDI---TKLPMHKRArlgIGYLPQEASIFrKLTVEENILAVL 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2014669168 85 RAHKMaPRKQFKSVAEARLTEVGLwDAVKDRLGDSpfrLSGGQQQLLCLARALAVNPDVLLLDEP 149
Cdd:cd03218 101 EIRGL-SKKEREEKLEELLEEFHI-THLRKSKASS---LSGGERRRVEIARALATNPKFLLLDEP 160
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
11-152 |
3.16e-14 |
|
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: 68.62 E-value: 3.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 11 LLGPTGSGKTTFLRTLnrmndkVSGFR-HSGDVLLGGRTIFA-DRDlmEFRRSVGMLFQRPNPFPMSIMDNVV--AGVRA 86
Cdd:COG4618 363 VIGPSGSGKSTLARLL------VGVWPpTAGSVRLDGADLSQwDRE--ELGRHIGYLPQDVELFDGTIAENIArfGDADP 434
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2014669168 87 HKMaprkqfksVAEARLTEV-----GLWDAVKDRLGDSPFRLSGGQQQLLCLARALAVNPDVLLLDEPTRH 152
Cdd:COG4618 435 EKV--------VAAAKLAGVhemilRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSN 497
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-149 |
3.43e-14 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 67.35 E-value: 3.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLNRM--NDKVSGFRhsgdVLLGGRTIFAD----RDLMEFRRSVGMLFQRPNPFP- 73
Cdd:PRK09984 25 LNIHHGEMVALLGPSGSGKSTLLRHLSGLitGDKSAGSH----IELLGRTVQREgrlaRDIRKSRANTGYIFQQFNLVNr 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 74 MSIMDNVVAGVRAHKMAPRKQF-------KSVAEARLTEVGLWDAVKDRLGDspfrLSGGQQQLLCLARALAVNPDVLLL 146
Cdd:PRK09984 101 LSVLENVLIGALGSTPFWRTCFswftreqKQRALQALTRVGMVHFAHQRVST----LSGGQQQRVAIARALMQQAKVILA 176
|
...
gi 2014669168 147 DEP 149
Cdd:PRK09984 177 DEP 179
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1-150 |
3.53e-14 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 68.59 E-value: 3.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLnrMndkvsGFR--HSGDVLLGGRTI--FADRDLmefRRSVGMLFQRPNPFPMSI 76
Cdd:PRK10790 362 LSVPSRGFVALVGHTGSGKSTLASLL--M-----GYYplTEGEIRLDGRPLssLSHSVL---RQGVAMVQQDPVVLADTF 431
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2014669168 77 MDNVVAGvraHKMAPRKQFKSVAEARLTEV--GLWDAVKDRLGDSPFRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:PRK10790 432 LANVTLG---RDISEEQVWQALETVQLAELarSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEAT 504
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
7-152 |
3.57e-14 |
|
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: 66.42 E-value: 3.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 7 SVTTLLGPTGSGKTTFLRTLnrmNDKVSGFRHSGDVLLGGRtifaDRDLMEFRRSVGMLFQrpnpfpmsimDNVVAGvra 86
Cdd:cd03213 36 ELTAIMGPSGAGKSTLLNAL---AGRRTGLGVSGEVLINGR----PLDKRSFRKIIGYVPQ----------DDILHP--- 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2014669168 87 hkmaprkqFKSVAEArltevgLWDAVKDRlgdspfRLSGGQQQLLCLARALAVNPDVLLLDEPTRH 152
Cdd:cd03213 96 --------TLTVRET------LMFAAKLR------GLSGGERKRVSIALELVSNPSLLFLDEPTSG 141
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
16-151 |
5.04e-14 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 67.74 E-value: 5.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 16 GSGKTTFLRTLnrmndkvsgF----RHSGDVLLGGRTI-FAD-RDLM--------EFRRSVGmLFQrpnpfPMSIMDNVV 81
Cdd:COG1129 288 GAGRTELARAL---------FgadpADSGEIRLDGKPVrIRSpRDAIragiayvpEDRKGEG-LVL-----DLSIRENIT 352
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2014669168 82 AGVRAhKMAPRKQFKSVAEARLTEvglwdAVKDRLG---DSPFR----LSGGQQQLLCLARALAVNPDVLLLDEPTR 151
Cdd:COG1129 353 LASLD-RLSRGGLLDRRRERALAE-----EYIKRLRiktPSPEQpvgnLSGGNQQKVVLAKWLATDPKVLILDEPTR 423
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1-150 |
5.35e-14 |
|
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: 66.24 E-value: 5.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLNRMNDKVSGFRH-SG-DVLlggrtifadRDLMEFRRSVGMLFQRPNPFP-MSIM 77
Cdd:cd03265 21 FRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATvAGhDVV---------REPREVRRRIGIVFQDLSVDDeLTGW 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2014669168 78 DNVVAGVRAHKMaPRKQFKSVAEARLTEVGLWDAvKDRLGDSpfrLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:cd03265 92 ENLYIHARLYGV-PGAERRERIDELLDFVGLLEA-ADRLVKT---YSGGMRRRLEIARSLVHRPEVLFLDEPT 159
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
13-149 |
5.62e-14 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 67.75 E-value: 5.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 13 GPTGSGKTTFLRTLNRMNDKVSGfrhsgDVLLGGRTIfadRDLMEFRRSVGMLFQRPNPFP-MSIMDNVVAGVRAHKMAP 91
Cdd:PRK11000 36 GPSGCGKSTLLRMIAGLEDITSG-----DLFIGEKRM---NDVPPAERGVGMVFQSYALYPhLSVAENMSFGLKLAGAKK 107
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2014669168 92 RKQFKSVAEArlTEVGLWDAVKDRlgdSPFRLSGGQQQLLCLARALAVNPDVLLLDEP 149
Cdd:PRK11000 108 EEINQRVNQV--AEVLQLAHLLDR---KPKALSGGQRQRVAIGRTLVAEPSVFLLDEP 160
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1-150 |
6.32e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 67.54 E-value: 6.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLNRMNDKvsgfrHSGDVLLGGRTI--FADRDLmefRRSVGMLFQRPNPFPMSIMD 78
Cdd:PRK11160 361 LQIKAGEKVALLGRTGCGKSTLLQLLTRAWDP-----QQGEILLNGQPIadYSEAAL---RQAISVVSQRVHLFSATLRD 432
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2014669168 79 NVVAgvrAHKMAPRKQFKSVaearLTEVGLWDAVKDR------LGDSPFRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:PRK11160 433 NLLL---AAPNASDEALIEV----LQQVGLEKLLEDDkglnawLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPT 503
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
8-150 |
1.04e-13 |
|
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: 65.97 E-value: 1.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 8 VTTLLGPTGSGKTTFLRTLNRMNdkvsgFRHSGDVLLGGRTIfADRDLMEFRRSVGMLFQRPNPFPMSIMDNVVAGVRAH 87
Cdd:cd03252 30 VVGIVGRSGSGKSTLTKLIQRFY-----VPENGRVLVDGHDL-ALADPAWLRRQVGVVLQENVLFNRSIRDNIALADPGM 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2014669168 88 KMAPRKQFKSVAEARLTEVGLWDAVKDRLGDSPFRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:cd03252 104 SMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEAT 166
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
11-148 |
1.76e-13 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 65.48 E-value: 1.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 11 LLGPTGSGKTTFLRTLNRMNDKvsgfrHSGDVLLGGRTI--FADRDLMEFRRSVGMLFQRP----NPF---------PMS 75
Cdd:PRK10419 43 LLGRSGCGKSTLARLLVGLESP-----SQGNVSWRGEPLakLNRAQRKAFRRDIQMVFQDSisavNPRktvreiirePLR 117
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2014669168 76 IMDNVVAGVRAHKmaprkqfksvAEARLTEVGLWDAVKDRLgdsPFRLSGGQQQLLCLARALAVNPDVLLLDE 148
Cdd:PRK10419 118 HLLSLDKAERLAR----------ASEMLRAVDLDDSVLDKR---PPQLSGGQLQRVCLARALAVEPKLLILDE 177
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
1-150 |
2.38e-13 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 64.18 E-value: 2.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLNRMNDKVSGFRHSGDvllggrtifadrdlmefRRSVGMLFQR---PNPFPMSIM 77
Cdd:NF040873 13 LTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-----------------GARVAYVPQRsevPDSLPLTVR 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2014669168 78 DNVVAGVRAHKMA---PRKQFKSVAEARLTEVGLWDAVKDRLGDspfrLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:NF040873 76 DLVAMGRWARRGLwrrLTRDDRAAVDDALERVGLADLAGRQLGE----LSGGQRQRALLAQGLAQEADLLLLDEPT 147
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
11-150 |
3.30e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 65.50 E-value: 3.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 11 LLGPTGSGKTTFLRTLNRMndkvsgFRHSGDVLLGGRTI--FADRDLMEFRRSVGMLFQRP----NPfPMSIMDNVVAGV 84
Cdd:PRK15134 317 LVGESGSGKSTTGLALLRL------INSQGEIWFDGQPLhnLNRRQLLPVRHRIQVVFQDPnsslNP-RLNVLQIIEEGL 389
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2014669168 85 RAHK--MAPRKQFKSVAEArLTEVGLWDAVKDRLgdsPFRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:PRK15134 390 RVHQptLSAAQREQQVIAV-MEEVGLDPETRHRY---PAEFSGGQRQRIAIARALILKPSLIILDEPT 453
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
11-149 |
3.34e-13 |
|
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: 64.11 E-value: 3.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 11 LLGPTGSGKTTFLrtlnrmnDKVSGFRH--SGDVLLGGRTIFAdrdLMEFRRSVGMLFQRPNPFP-MSIMDNVVAGVR-A 86
Cdd:TIGR01277 29 IMGPSGAGKSTLL-------NLIAGFIEpaSGSIKVNDQSHTG---LAPYQRPVSMLFQENNLFAhLTVRQNIGLGLHpG 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2014669168 87 HKMAPRKQFKSVAEARltEVGLWDAVkDRLgdsPFRLSGGQQQLLCLARALAVNPDVLLLDEP 149
Cdd:TIGR01277 99 LKLNAEQQEKVVDAAQ--QVGIADYL-DRL---PEQLSGGQRQRVALARCLVRPNPILLLDEP 155
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
10-150 |
3.37e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 65.11 E-value: 3.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 10 TLLGPTGSGKTTFLRTLNRMNDKVSGFrhsgdVLLGGRTIFADrDLMEFRRSVGMLFQRP-NPFPMSIMDNVVAGVRAHK 88
Cdd:PRK13642 37 SIIGQNGSGKSTTARLIDGLFEEFEGK-----VKIDGELLTAE-NVWNLRRKIGMVFQNPdNQFVGATVEDDVAFGMENQ 110
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2014669168 89 MAPRKQFKSVAEARLTEVGLWDaVKDRlgdSPFRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:PRK13642 111 GIPREEMIKRVDEALLAVNMLD-FKTR---EPARLSGGQKQRVAVAGIIALRPEIIILDEST 168
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1-150 |
3.83e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 65.03 E-value: 3.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLNRMNdkvsgFRHSGDVLLGGRTIFAD----RDLMEFRRSVGMLFQRP--NPFPM 74
Cdd:PRK13645 32 LTFKKNKVTCVIGTTGSGKSTMIQLTNGLI-----ISETGQTIVGDYAIPANlkkiKEVKRLRKEIGLVFQFPeyQLFQE 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2014669168 75 SIMDNVVAGVRAHKMAPRKQFKSVAEArlteVGLWDAVKDRLGDSPFRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:PRK13645 107 TIEKDIAFGPVNLGENKQEAYKKVPEL----LKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPT 178
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
11-150 |
5.41e-13 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 64.98 E-value: 5.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 11 LLGPTGSGKTTFLRTLNRMNDKVSGFrhsgdVLLGGRTIfADRDLMEFRRSVGMLFQRPNPFPMSIMDNVVAG------V 84
Cdd:PRK13657 366 IVGPTGAGKSTLINLLQRVFDPQSGR-----ILIDGTDI-RTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGrpdatdE 439
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2014669168 85 RAHKMAPRKQFKSVAEARLtevglwDAVKDRLGDSPFRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:PRK13657 440 EMRAAAERAQAHDFIERKP------DGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEAT 499
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
11-149 |
5.67e-13 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 63.89 E-value: 5.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 11 LLGPTGSGKTT-FlrtlnRMndkVSGFRH--SGDVLLGGRTIfadRDLMEFRRS---VGMLFQRPNPF-PMSIMDNVVAG 83
Cdd:COG1137 34 LLGPNGAGKTTtF-----YM---IVGLVKpdSGRIFLDGEDI---THLPMHKRArlgIGYLPQEASIFrKLTVEDNILAV 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2014669168 84 VRAHKMaPRKQFKSVAEARLTEVGLwDAVKDRLGDSpfrLSGGQQQLLCLARALAVNPDVLLLDEP 149
Cdd:COG1137 103 LELRKL-SKKEREERLEELLEEFGI-THLRKSKAYS---LSGGERRRVEIARALATNPKFILLDEP 163
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
11-150 |
5.94e-13 |
|
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: 64.89 E-value: 5.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 11 LLGPTGSGKTTFLRTLnrmndkvSGFRH--SGDVLLGG---RTIfadrDLMEFRRSVGMLFQRPNPFPMSIMDNVVAGVR 85
Cdd:TIGR03375 496 IIGRIGSGKSTLLKLL-------LGLYQptEGSVLLDGvdiRQI----DPADLRRNIGYVPQDPRLFYGTLRDNIALGAP 564
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2014669168 86 AhkmaprkqfksVAEARLTEV----GLWDAVK------DRL----GDSpfrLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:TIGR03375 565 Y-----------ADDEEILRAaelaGVTEFVRrhpdglDMQigerGRS---LSGGQRQAVALARALLRDPPILLLDEPT 629
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
8-151 |
6.47e-13 |
|
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: 63.54 E-value: 6.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 8 VTTLLGPTGSGKTTFLRTLNRMNDKVSGFrhsgdVLLGGrtIFADRDLMEFRRSVGMLFQRPNPFP-MSIMDNVVAGVRA 86
Cdd:cd03266 33 VTGLLGPNGAGKTTTLRMLAGLLEPDAGF-----ATVDG--FDVVKEPAEARRRLGFVSDSTGLYDrLTARENLEYFAGL 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2014669168 87 HKMAPRKqfksvAEARLTEVGlwdavkDRLGDSPFR------LSGGQQQLLCLARALAVNPDVLLLDEPTR 151
Cdd:cd03266 106 YGLKGDE-----LTARLEELA------DRLGMEELLdrrvggFSTGMRQKVAIARALVHDPPVLLLDEPTT 165
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-150 |
7.16e-13 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 64.75 E-value: 7.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLNRMnDKVSgfrhSGDVLLGGRTIFA-DRD-LMEFRRS-VGMLFQRPNPFP-MSI 76
Cdd:PRK10535 29 LDIYAGEMVAIVGASGSGKSTLMNILGCL-DKPT----SGTYRVAGQDVATlDADaLAQLRREhFGFIFQRYHLLShLTA 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2014669168 77 MDNV-VAGVRAHkmAPRKQFKSVAEARLTEVGLwdavKDRLGDSPFRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:PRK10535 104 AQNVeVPAVYAG--LERKQRLLRAQELLQRLGL----EDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPT 172
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
10-149 |
7.94e-13 |
|
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: 63.25 E-value: 7.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 10 TLLGPTGSGKTTFLrtlnrmnDKVSGFRH--SGDVLLGGRTIFA-DRDLMefrrsvgMLFQRPNPFP-MSIMDNVVAGV- 84
Cdd:TIGR01184 15 SLIGHSGCGKSTLL-------NLISGLAQptSGGVILEGKQITEpGPDRM-------VVFQNYSLLPwLTVRENIALAVd 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2014669168 85 RAHKMAPRKQFKSVAEARLTEVGLWDAVKDRlgdsPFRLSGGQQQLLCLARALAVNPDVLLLDEP 149
Cdd:TIGR01184 81 RVLPDLSKSERRAIVEEHIALVGLTEAADKR----PGQLSGGMKQRVAIARALSIRPKVLLLDEP 141
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
11-148 |
9.14e-13 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 63.67 E-value: 9.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 11 LLGPTGSGKTTFLRTLNRMNDKVSGfrhsgDVLLGGRTIFA-DRDLME-FRRSVGMLFQ-RPNPFpmsimdNVVAGVRAH 87
Cdd:TIGR02769 42 LLGRSGCGKSTLARLLLGLEKPAQG-----TVSFRGQDLYQlDRKQRRaFRRDVQLVFQdSPSAV------NPRMTVRQI 110
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2014669168 88 KMAPRKQFKSVAEAR--------LTEVGLWDAVKDRLgdsPFRLSGGQQQLLCLARALAVNPDVLLLDE 148
Cdd:TIGR02769 111 IGEPLRHLTSLDESEqkariaelLDMVGLRSEDADKL---PRQLSGGQLQRINIARALAVKPKLIVLDE 176
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1-149 |
9.59e-13 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 64.13 E-value: 9.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLrtlnrmnDKVSGFRH--SGDVLLGGRTIFaDRDLMEF----RRSVGMLFQRPNPFP- 73
Cdd:PRK11144 19 LTLPAQGITAIFGRSGAGKTSLI-------NAISGLTRpqKGRIVLNGRVLF-DAEKGIClppeKRRIGYVFQDARLFPh 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2014669168 74 MSIMDNVVAGVrAHKMAPrkQFKSVaearlteVGLW--DAVKDRLgdsPFRLSGGQQQLLCLARALAVNPDVLLLDEP 149
Cdd:PRK11144 91 YKVRGNLRYGM-AKSMVA--QFDKI-------VALLgiEPLLDRY---PGSLSGGEKQRVAIGRALLTAPELLLMDEP 155
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
11-149 |
2.19e-12 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 62.29 E-value: 2.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 11 LLGPTGSGKTTFLRTlnrmndkVSGFR--HSGDVLLGG----RTIFAdrdlmefRRSVGMLFQRPNPFP-MSIMDNVVAG 83
Cdd:PRK10771 30 ILGPSGAGKSTLLNL-------IAGFLtpASGSLTLNGqdhtTTPPS-------RRPVSMLFQENNLFShLTVAQNIGLG 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2014669168 84 vrahkMAP--------RKQFKSVAEarltEVGLWDAVkDRLgdsPFRLSGGQQQLLCLARALAVNPDVLLLDEP 149
Cdd:PRK10771 96 -----LNPglklnaaqREKLHAIAR----QMGIEDLL-ARL---PGQLSGGQRQRVALARCLVREQPILLLDEP 156
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
7-150 |
2.67e-12 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 63.20 E-value: 2.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 7 SVTTLLGPTGSGKTTFLRTLNRMNDKVSGfrhsgDVLLGGRTIfADRDLMEFRRSVGMLFQRPNPFPMSIMDNVVAGVRA 86
Cdd:TIGR00958 508 EVVALVGPSGSGKSTVAALLQNLYQPTGG-----QVLLDGVPL-VQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTD 581
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2014669168 87 HKMAPRKQFKSVAEARLTEVGLWDAVKDRLGDSPFRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:TIGR00958 582 TPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEAT 645
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
11-150 |
3.04e-12 |
|
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: 60.79 E-value: 3.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 11 LLGPTGSGKTTFLRTLNRMNDKvsgfrHSGDVLLGGRTIFADRDLMefRRSVGMLFQRPNPFPMSIMDNVVAgvrahkma 90
Cdd:cd03247 33 LLGRSGSGKSTLLQLLTGDLKP-----QQGEITLDGVPVSDLEKAL--SSLISVLNQRPYLFDTTLRNNLGR-------- 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 91 prkqfksvaearltevglwdavkdrlgdspfRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:cd03247 98 -------------------------------RFSGGERQRLALARILLQDAPIVLLDEPT 126
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
11-150 |
3.36e-12 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 62.76 E-value: 3.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 11 LLGPTGSGKTTFLRTLNRMNDKvsGFRHSGDVLLGGRTIfadrDLMEFRRSVGMLFQRPNPFPMSIMD---NVVAGVRAH 87
Cdd:TIGR00955 56 VMGSSGAGKTTLMNALAFRSPK--GVKGSGSVLLNGMPI----DAKEMRAISAYVQQDDLFIPTLTVRehlMFQAHLRMP 129
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2014669168 88 KMAPRKQFKSVAEARLTEVGLWDAVKDRLGDsPFR---LSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:TIGR00955 130 RRVTKKEKRERVDEVLQALGLRKCANTRIGV-PGRvkgLSGGERKRLAFASELLTDPPLLFCDEPT 194
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1-150 |
3.67e-12 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 62.11 E-value: 3.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLNRMNDKVsgfrhSGDVLLGGRTIfADRDLMEFRRSVGMLFQR-PNPFPMSIMDN 79
Cdd:PRK10575 32 LTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPS-----EGEILLDAQPL-ESWSSKAFARKVAYLPQQlPAAEGMTVREL 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2014669168 80 VVAG-------VRAHKMAPRKQfksVAEArLTEVGLwDAVKDRLGDSpfrLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:PRK10575 106 VAIGrypwhgaLGRFGAADREK---VEEA-ISLVGL-KPLAHRLVDS---LSGGERQRAWIAMLVAQDSRCLLLDEPT 175
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
11-150 |
4.20e-12 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 61.43 E-value: 4.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 11 LLGPTGSGKTTFLRTLNRMNDKvsgfrHSGDVLLGGRTI--FADRDLMEFRRSVGMLFQRPNPF-PMSIMDNV-----VA 82
Cdd:PRK10908 33 LTGHSGAGKSTLLKLICGIERP-----SAGKIWFSGHDItrLKNREVPFLRRQIGMIFQDHHLLmDRTVYDNVaipliIA 107
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2014669168 83 GVRAHKMAPRkqfksvAEARLTEVGLWDAVKDrlgdSPFRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:PRK10908 108 GASGDDIRRR------VSAALDKVGLLDKAKN----FPIQLSGGEQQRVGIARAVVNKPAVLLADEPT 165
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1-149 |
7.12e-12 |
|
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: 60.18 E-value: 7.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRT-LNRMNdkvsgfRHSGDVLLGGRTIFADrdlmefrrsvgmlfQRPNPFPMSIMDN 79
Cdd:cd03250 26 LEVPKGELVAIVGPVGSGKSSLLSAlLGELE------KLSGSVSVPGSIAYVS--------------QEPWIQNGTIREN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 80 VVAG-----------VRAhkMAPRKQFKSVAEARLTEVGlwdavkDRlGDSpfrLSGGQQQLLCLARALAVNPDVLLLDE 148
Cdd:cd03250 86 ILFGkpfdeeryekvIKA--CALEPDLEILPDGDLTEIG------EK-GIN---LSGGQKQRISLARAVYSDADIYLLDD 153
|
.
gi 2014669168 149 P 149
Cdd:cd03250 154 P 154
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1-150 |
8.06e-12 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 61.16 E-value: 8.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLNRMNDKVsgfrhSGDVLLGGRTI--FADRdlmEFRRSVGMLFQRP-NPFPMSIM 77
Cdd:PRK10253 28 VEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPA-----HGHVWLDGEHIqhYASK---EVARRIGLLAQNAtTPGDITVQ 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2014669168 78 DNVVAGVRAHKmaP-----RKQFKSVAEARLTEVGlwdaVKDRLGDSPFRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:PRK10253 100 ELVARGRYPHQ--PlftrwRKEDEEAVTKAMQATG----ITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPT 171
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
10-148 |
8.09e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 61.80 E-value: 8.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 10 TLLGPTGSGKTTFLRTLNRMNDKvsgfrHSGDVLLGGRTI--FADRDLMEFRRSVGMLFQRP----NPfPMSIMDNVVAG 83
Cdd:PRK10261 354 SLVGESGSGKSTTGRALLRLVES-----QGGEIIFNGQRIdtLSPGKLQALRRDIQFIFQDPyaslDP-RQTVGDSIMEP 427
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2014669168 84 VRAHKMAPRKQFKSVAEARLTEVGLWDAVKDRLgdsPFRLSGGQQQLLCLARALAVNPDVLLLDE 148
Cdd:PRK10261 428 LRVHGLLPGKAAAARVAWLLERVGLLPEHAWRY---PHEFSGGQRQRICIARALALNPKVIIADE 489
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
8-149 |
1.24e-11 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 60.29 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 8 VTTLLGPTGSGKTTFLRTlnrmndkVSGFRHSGdvllGGRTIFADRDL------MEFRRSVGMLFQRPNPFP-MSIMDNV 80
Cdd:PRK10895 31 IVGLLGPNGAGKTTTFYM-------VVGIVPRD----AGNIIIDDEDIsllplhARARRGIGYLPQEASIFRrLSVYDNL 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2014669168 81 VAGVRAHKMAPRKQFKSVAEARLTEVGLwDAVKDRLGDSpfrLSGGQQQLLCLARALAVNPDVLLLDEP 149
Cdd:PRK10895 100 MAVLQIRDDLSAEQREDRANELMEEFHI-EHLRDSMGQS---LSGGERRRVEIARALAANPKFILLDEP 164
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
4-150 |
1.40e-11 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 59.79 E-value: 1.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 4 PARSVTtLLGPTGSGKTTFLRTLNRMNDKvsgfrHSGDVLLGGRTIFA--DRDLMEFR-RSVGMLFQRPNPFP-MSIMDN 79
Cdd:PRK10584 35 RGETIA-LIGESGSGKSTLLAILAGLDDG-----SSGEVSLVGQPLHQmdEEARAKLRaKHVGFVFQSFMLIPtLNALEN 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2014669168 80 VV--AGVRAHKmapRKQFKSVAEARLTEVGLwdavKDRLGDSPFRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:PRK10584 109 VElpALLRGES---SRQSRNGAKALLEQLGL----GKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPT 174
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
11-150 |
1.68e-11 |
|
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: 59.76 E-value: 1.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 11 LLGPTGSGKTTFLRTLNRMNDKVSG---FRHSGDVL----LGGRTIFADRdlmefRRSVGMLFQRPNPFP-MSIMDnVVA 82
Cdd:COG4778 42 LTGPSGAGKSTLLKCIYGNYLPDSGsilVRHDGGWVdlaqASPREILALR-----RRTIGYVSQFLRVIPrVSALD-VVA 115
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2014669168 83 GVRAHKMAPRKQFKSVAEARLTEVG----LWDAvkdrlgdSPFRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:COG4778 116 EPLLERGVDREEARARARELLARLNlperLWDL-------PPATFSGGEQQRVNIARGFIADPPLLLLDEPT 180
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
5-150 |
1.71e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 60.81 E-value: 1.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 5 ARSVTTLLGPTGSGKTTFLRTLNRMND------------------------------------------KVSG------- 35
Cdd:PTZ00265 1193 SKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltKEGGsgedstv 1272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 36 FRHSGDVLLGGRTIfADRDLMEFRRSVGMLFQRPNPFPMSIMDNVVAG---------VRAHKMAPRKQF-KSVAEARLTE 105
Cdd:PTZ00265 1273 FKNSGKILLDGVDI-CDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGkedatredvKRACKFAAIDEFiESLPNKYDTN 1351
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2014669168 106 VGLWdavkdrlGDSpfrLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:PTZ00265 1352 VGPY-------GKS---LSGGQKQRIAIARALLREPKILLLDEAT 1386
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
11-150 |
1.72e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 60.10 E-value: 1.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 11 LLGPTGSGKTTFLRTLNRMNdkvsgFRHSGDVLLGGRTIFADRDLMEFRRSVGMLFQRP-NPFPMSIMDNVVA-GVRAHK 88
Cdd:PRK13633 41 ILGRNGSGKSTIAKHMNALL-----IPSEGKVYVDGLDTSDEENLWDIRNKAGMVFQNPdNQIVATIVEEDVAfGPENLG 115
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2014669168 89 MAPRKQFKSVAEArLTEVGLWDAVKDrlgdSPFRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:PRK13633 116 IPPEEIRERVDES-LKKVGMYEYRRH----APHLLSGGQKQRVAIAGILAMRPECIIFDEPT 172
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
10-150 |
1.83e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 60.10 E-value: 1.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 10 TLLGPTGSGKTTFLRTLnrmndkvsgfrhSGDVLL-GGRTIFADRD---LMEFRRS--VGMLFQrpNPF----P-MSIMD 78
Cdd:COG1101 36 TVIGSNGAGKSTLLNAI------------AGSLPPdSGSILIDGKDvtkLPEYKRAkyIGRVFQ--DPMmgtaPsMTIEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 79 N-VVAGVRAHKM--------APRKQFKsvaeARLTEVGLwdAVKDRLGDSPFRLSGGQQQLLCLARALAVNPDVLLLDEP 149
Cdd:COG1101 102 NlALAYRRGKRRglrrgltkKRRELFR----ELLATLGL--GLENRLDTKVGLLSGGQRQALSLLMATLTKPKLLLLDEH 175
|
.
gi 2014669168 150 T 150
Cdd:COG1101 176 T 176
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-150 |
2.32e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 59.64 E-value: 2.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLrtlnrMNdkVSGF--RHSGDVLLGGRTI-FADRDLMEFRRSVGMLFQRPNP--FPMS 75
Cdd:PRK13638 22 LDFSLSPVTGLVGANGCGKSTLF-----MN--LSGLlrPQKGAVLWQGKPLdYSKRGLLALRQQVATVFQDPEQqiFYTD 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2014669168 76 IMDNVVAGVRAHKMAPRKQFKSVAEArLTEVglwDAvkDRLGDSPFR-LSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:PRK13638 95 IDSDIAFSLRNLGVPEAEITRRVDEA-LTLV---DA--QHFRHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPT 164
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
11-150 |
2.50e-11 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 60.24 E-value: 2.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 11 LLGPTGSGKTTFLRTlnrMNDKVSgfRHSGDVLLGGRTIfADRDLMEFRRSVGMLfqrPNPFPMSIMDNVVAGVRAHKMA 90
Cdd:PRK09536 34 LVGPNGAGKTTLLRA---INGTLT--PTAGTVLVAGDDV-EALSARAASRRVASV---PQDTSLSFEFDVRQVVEMGRTP 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2014669168 91 PRKQFKSVAEA--RLTEVGLWDAVKDRLGDSPF-RLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:PRK09536 105 HRSRFDTWTETdrAAVERAMERTGVAQFADRPVtSLSGGERQRVLLARALAQATPVLLLDEPT 167
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
4-150 |
2.70e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 59.82 E-value: 2.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 4 PARSVTTLLGPTGSGKTTFLRTLNRMNDKVSGfrhsgDVLLGGRTIfADRDLMEFRRSVGMLFQRPNP--FPMSIMDNVV 81
Cdd:PRK13652 28 PRNSRIAVIGPNGAGKSTLFRHFNGILKPTSG-----SVLIRGEPI-TKENIREVRKFVGLVFQNPDDqiFSPTVEQDIA 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2014669168 82 AGVRAHKMAPRKQFKSVAEArLTEVGLWDaVKDRLgdsPFRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:PRK13652 102 FGPINLGLDEETVAHRVSSA-LHMLGLEE-LRDRV---PHHLSGGEKKRVAIAGVIAMEPQVLVLDEPT 165
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-149 |
3.32e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 59.35 E-value: 3.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 4 PARSVTTLLGPTGSGKTTFLRTLNRMNDKvsgfrHSGDVLLGGRTI-FADRD----LMEFRRsvgmLFQRpnpfpMSIMD 78
Cdd:COG4152 25 PKGEIFGLLGPNGAGKTTTIRIILGILAP-----DSGEVLWDGEPLdPEDRRrigyLPEERG----LYPK-----MKVGE 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2014669168 79 NVVAGVRAHKMaPRKQFKSVAEARLTEVGLWDAVKDRLGDspfrLSGGQQQLLCLARALAVNPDVLLLDEP 149
Cdd:COG4152 91 QLVYLARLKGL-SKAEAKRRADEWLERLGLGDRANKKVEE----LSKGNQQKVQLIAALLHDPELLILDEP 156
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
11-152 |
4.50e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 59.58 E-value: 4.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 11 LLGPTGSGKTTFLRTLnrmndkvsgfrhSGDVLLG-GRTIFAdRDLMefrrsVGMLFQRPnpfPM----SIMDNVVAGVR 85
Cdd:PRK11147 34 LVGRNGAGKSTLMKIL------------NGEVLLDdGRIIYE-QDLI-----VARLQQDP---PRnvegTVYDFVAEGIE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 86 ------------AHKMAPRKQFKSVAE-ARLTEV----GLW---DAVKDRL------GDSPF-RLSGGQQQLLCLARALA 138
Cdd:PRK11147 93 eqaeylkryhdiSHLVETDPSEKNLNElAKLQEQldhhNLWqleNRINEVLaqlgldPDAALsSLSGGWLRKAALGRALV 172
|
170
....*....|....
gi 2014669168 139 VNPDVLLLDEPTRH 152
Cdd:PRK11147 173 SNPDVLLLDEPTNH 186
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
16-151 |
5.56e-11 |
|
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: 57.44 E-value: 5.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 16 GSGKTTFLRTLnrmndkvSGFRH--SGDVLLGGR--TIFADRDLM--------EFRRSVGmLFQrpnpfPMSIMDNVVAg 83
Cdd:cd03215 36 GNGQTELAEAL-------FGLRPpaSGEITLDGKpvTRRSPRDAIragiayvpEDRKREG-LVL-----DLSVAENIAL- 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2014669168 84 vrahkmaprkqfksvaearltevglwdavkdrlgdsPFRLSGGQQQLLCLARALAVNPDVLLLDEPTR 151
Cdd:cd03215 102 ------------------------------------SSLLSGGNQQKVVLARWLARDPRVLILDEPTR 133
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1-150 |
9.54e-11 |
|
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: 56.67 E-value: 9.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLnrmndkvSGFRH--SGDVLLGGRTIfadrdlmefrrsvgmlfqrpnpfpmsimd 78
Cdd:cd03216 21 LSVRRGEVHALLGENGAGKSTLMKIL-------SGLYKpdSGEILVDGKEV----------------------------- 64
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2014669168 79 nvvagvrahkmaprkQFKSVAEARltevglwdavkdRLGDSP-FRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:cd03216 65 ---------------SFASPRDAR------------RAGIAMvYQLSVGERQMVEIARALARNARLLILDEPT 110
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
5-150 |
9.70e-11 |
|
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: 57.42 E-value: 9.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 5 ARSVTTLLGPTGSGKTTFLRTLNRMNDKVSGfrhsgDVLLGGRTIfADRDLMEFRRSVGMLFQRPNPFPMSIMDNVVagv 84
Cdd:cd03369 33 AGEKIGIVGRTGAGKSTLILALFRFLEAEEG-----KIEIDGIDI-STIPLEDLRSSLTIIPQDPTLFSGTIRSNLD--- 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2014669168 85 RAHKMAPRKQFKSVaeaRLTEVGLwdavkdrlgdspfRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:cd03369 104 PFDEYSDEEIYGAL---RVSEGGL-------------NLSQGQRQLLCLARALLKRPRVLVLDEAT 153
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
11-150 |
1.38e-10 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 57.13 E-value: 1.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 11 LLGPTGSGKTTFLRTLNRMNDKVSGfrhsgDVLLGGRTI--FADRDLMEFR-RSVGMLFQRPNPFP-MSIMDNVVAGVRA 86
Cdd:PRK11629 40 IVGSSGSGKSTLLHLLGGLDTPTSG-----DVIFNGQPMskLSSAAKAELRnQKLGFIYQFHHLLPdFTALENVAMPLLI 114
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2014669168 87 HKMAPrKQFKSVAEARLTEVGLWDAVKDRlgdsPFRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:PRK11629 115 GKKKP-AEINSRALEMLAAVGLEHRANHR----PSELSGGERQRVAIARALVNNPRLVLADEPT 173
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
13-149 |
1.63e-10 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 57.79 E-value: 1.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 13 GPTGSGKTTFLRTLNRMNDKVSGfrhsgDVLLGGR--TIFADRDLMEFRRSVGMLFQRP----NPfPMSIMDNVVAGVRA 86
Cdd:PRK15079 54 GESGCGKSTFARAIIGLVKATDG-----EVAWLGKdlLGMKDDEWRAVRSDIQMIFQDPlaslNP-RMTIGEIIAEPLRT 127
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2014669168 87 H--KMaPRKQFKSVAEARLTEVGLWDAVKDRLgdsPFRLSGGQQQLLCLARALAVNPDVLLLDEP 149
Cdd:PRK15079 128 YhpKL-SRQEVKDRVKAMMLKVGLLPNLINRY---PHEFSGGQCQRIGIARALILEPKLIICDEP 188
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
11-150 |
2.71e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 57.20 E-value: 2.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 11 LLGPTGSGKTTFLrtlNRMNDKVSGFRHSGDVLLGGRTIfaDRDLMefrRSVGMLFQRPNPFP-MSIMDNVV--AGVRAH 87
Cdd:PLN03211 99 VLGPSGSGKSTLL---NALAGRIQGNNFTGTILANNRKP--TKQIL---KRTGFVTQDDILYPhLTVRETLVfcSLLRLP 170
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2014669168 88 KMAPRKQFKSVAEARLTEVGLWDAVKDRLGDSPFR-LSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:PLN03211 171 KSLTKQEKILVAESVISELGLTKCENTIIGNSFIRgISGGERKRVSIAHEMLINPSLLILDEPT 234
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
4-149 |
8.01e-10 |
|
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: 55.82 E-value: 8.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 4 PARSVTTLLGPTGSGKTTFLRTLNRMNDKVSGfrhsgDVLLGGRTIFA-DRDlmEFRRSVGMLFQRPNPFPMSIMDNVVa 82
Cdd:TIGR01842 342 QAGEALAIIGPSGSGKSTLARLIVGIWPPTSG-----SVRLDGADLKQwDRE--TFGKHIGYLPQDVELFPGTVAENIA- 413
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2014669168 83 gvRAHKMA-PRKqfkSVAEARLTEV-----GLWDAVKDRLGDSPFRLSGGQQQLLCLARALAVNPDVLLLDEP 149
Cdd:TIGR01842 414 --RFGENAdPEK---IIEAAKLAGVhelilRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEP 481
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
123-152 |
8.25e-10 |
|
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: 53.61 E-value: 8.25e-10
10 20 30
....*....|....*....|....*....|
gi 2014669168 123 LSGGQQQLLCLARALAVNPDVLLLDEPTRH 152
Cdd:cd03221 71 LSGGEKMRLALAKLLLENPNLLLLDEPTNH 100
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
11-149 |
1.05e-09 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 55.23 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 11 LLGPTGSGKTTFLRtlnrMndkVSGFRH--SGDVLLGGRTIF----ADRDlmefrrsVGMLFQRPNPFP-MSIMDNVVAG 83
Cdd:PRK11650 35 LVGPSGCGKSTLLR----M---VAGLERitSGEIWIGGRVVNelepADRD-------IAMVFQNYALYPhMSVRENMAYG 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2014669168 84 VRAHKMAPRKQFKSVAE-ARLTEVGlwdAVKDRlgdSPFRLSGGQQQLLCLARALAVNPDVLLLDEP 149
Cdd:PRK11650 101 LKIRGMPKAEIEERVAEaARILELE---PLLDR---KPRELSGGQRQRVAMGRAIVREPAVFLFDEP 161
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-150 |
1.32e-09 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 55.12 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTL--LGPTGSGK--TTF-LRTLNRMNDKVSGfrhsgDVLLGGRTI--FADRDLMEFR-RSVGMLFQRP--- 69
Cdd:PRK09473 35 LNFSLRAGETLgiVGESGSGKsqTAFaLMGLLAANGRIGG-----SATFNGREIlnLPEKELNKLRaEQISMIFQDPmts 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 70 -NPFpMSIMDNVVAGVRAHK-MaprkqfkSVAEARLTEVGLWDAVK-----DRLGDSPFRLSGGQQQLLCLARALAVNPD 142
Cdd:PRK09473 110 lNPY-MRVGEQLMEVLMLHKgM-------SKAEAFEESVRMLDAVKmpearKRMKMYPHEFSGGMRQRVMIAMALLCRPK 181
|
....*...
gi 2014669168 143 VLLLDEPT 150
Cdd:PRK09473 182 LLIADEPT 189
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
11-152 |
1.86e-09 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 54.92 E-value: 1.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 11 LLGPTGSGKTTFLRTLNRMndkvsgFRHSGDVLLGGRTiFADRDLMEFRRSVGMLfqrpnpfPMSIMdnVVAGVRAHKMA 90
Cdd:TIGR01271 1250 LLGRTGSGKSTLLSALLRL------LSTEGEIQIDGVS-WNSVTLQTWRKAFGVI-------PQKVF--IFSGTFRKNLD 1313
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 91 PRKQFKSVAEARLT-EVGLWDAVK---DRLG----DSPFRLSGGQQQLLCLARALAVNPDVLLLDEPTRH 152
Cdd:TIGR01271 1314 PYEQWSDEEIWKVAeEVGLKSVIEqfpDKLDfvlvDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAH 1383
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
11-150 |
2.29e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 54.22 E-value: 2.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 11 LLGPTGSGKTTFLRTLNrmndkvsGFR--HSGDVLLGGRTIFADRDLMEFRRSVGMLFQRPNP--FPMSIMDNVVAGVRA 86
Cdd:PRK13644 33 IIGKNGSGKSTLALHLN-------GLLrpQKGKVLVSGIDTGDFSKLQGIRKLVGIVFQNPETqfVGRTVEEDLAFGPEN 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2014669168 87 HKMAPRKQFKSVAEArLTEVGLwDAVKDRlgdSPFRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:PRK13644 106 LCLPPIEIRKRVDRA-LAEIGL-EKYRHR---SPKTLSGGQGQCVALAGILTMEPECLIFDEVT 164
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
13-150 |
2.40e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 54.20 E-value: 2.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 13 GPTGSGKTTFLRTLNRMNDKVSG--FRHSGDVLLGGRTIFADRdlmefRRSVGMLFQRP----NPF---------PMSIM 77
Cdd:PRK11308 48 GESGCGKSTLARLLTMIETPTGGelYYQGQDLLKADPEAQKLL-----RQKIQIVFQNPygslNPRkkvgqileePLLIN 122
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2014669168 78 DNVVAGVRAHKmaprkqfksvAEARLTEVGLWDAVKDRLgdsPFRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:PRK11308 123 TSLSAAERREK----------ALAMMAKVGLRPEHYDRY---PHMFSGGQRQRIAIARALMLDPDVVVADEPV 182
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
1-150 |
2.49e-09 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 54.64 E-value: 2.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLNRMNDKvsgfrHSGDVLLGGRTIfADRDLMEFRRSVGMLFQRPNPFPMSIMDNV 80
Cdd:PRK11176 364 FKIPAGKTVALVGRSGSGKSTIANLLTRFYDI-----DEGEILLDGHDL-RDYTLASLRNQVALVSQNVHLFNDTIANNI 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 81 VAG----------VRAHKMAPRKQFKSVAEARLTEVglwdavkdrLGDSPFRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:PRK11176 438 AYArteqysreqiEEAARMAYAMDFINKMDNGLDTV---------IGENGVLLSGGQRQRIAIARALLRDSPILILDEAT 508
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-150 |
3.63e-09 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 53.88 E-value: 3.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLnrmndkvSGFRH--SGDVLLGGRTI-FAD-RDLMefRRSVGMLFQRPNPFP-MS 75
Cdd:COG3845 26 LTVRPGEIHALLGENGAGKSTLMKIL-------YGLYQpdSGEILIDGKPVrIRSpRDAI--ALGIGMVHQHFMLVPnLT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 76 IMDNVVAGvrahkMAPRKQF---KSVAEARLTEV----GL---WDA-VKDrlgdspfrLSGGQQQLLCLARALAVNPDVL 144
Cdd:COG3845 97 VAENIVLG-----LEPTKGGrldRKAARARIRELseryGLdvdPDAkVED--------LSVGEQQRVEILKALYRGARIL 163
|
....*.
gi 2014669168 145 LLDEPT 150
Cdd:COG3845 164 ILDEPT 169
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
11-150 |
3.95e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 54.09 E-value: 3.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 11 LLGPTGSGKTTFLRTLNRMNDKVSGFRHSGDVLLGGRT-------IFADRDLMEFRRS-VGMLFQRP----NP-FPmsIM 77
Cdd:PRK10261 47 IVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSrqvielsEQSAAQMRHVRGAdMAMIFQEPmtslNPvFT--VG 124
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2014669168 78 DNVVAGVRAHKMAPRKQFKSVAEARLTEVGLWDAvKDRLGDSPFRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:PRK10261 125 EQIAESIRLHQGASREEAMVEAKRMLDQVRIPEA-QTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPT 196
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
11-150 |
4.33e-09 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 53.66 E-value: 4.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 11 LLGPTGSGKTTFLRTLNRMNDKVSGFRHSGDVLLGGRTIFAdrdlmefRRSVGMLFQRPNPFP-MSIMDNVVAGVRAHKM 89
Cdd:PRK13537 38 LLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA-------RQRVGVVPQFDNLDPdFTVRENLLVFGRYFGL 110
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2014669168 90 aprkqfkSVAEARLTEVGLWDAVK-DRLGDSPFR-LSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:PRK13537 111 -------SAAAARALVPPLLEFAKlENKADAKVGeLSGGMKRRLTLARALVNDPDVLVLDEPT 166
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1-150 |
4.60e-09 |
|
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: 52.67 E-value: 4.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLNRMNDKvsgfrHSGDVLLGGRTI-FADRDLMefrrsvGMLFQRPNPFP-MSIMD 78
Cdd:cd03269 21 FSVEKGEIFGLLGPNGAGKTTTIRMILGIILP-----DSGEVLFDGKPLdIAARNRI------GYLPEERGLYPkMKVID 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2014669168 79 NVVAGVRAHKMaPRKQFKSVAEARLTEVGLWDAVKDRLGDspfrLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:cd03269 90 QLVYLAQLKGL-KKEEARRRIDEWLERLELSEYANKRVEE----LSKGNQQKVQFIAAVIHDPELLILDEPF 156
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
11-148 |
6.36e-09 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 53.18 E-value: 6.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 11 LLGPTGSGKTTFLRTLNRMNDkVSgfrhSGDVLLGGRTIfADRDLMEFRRSVGMLFQRPNPFPMSIMDNVVAGvraHKMA 90
Cdd:PRK10789 346 ICGPTGSGKSTLLSLIQRHFD-VS----EGDIRFHDIPL-TKLQLDSWRSRLAVVSQTPFLFSDTVANNIALG---RPDA 416
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2014669168 91 PRKQFKSVAeaRLTEVG-----LWDAVKDRLGDSPFRLSGGQQQLLCLARALAVNPDVLLLDE 148
Cdd:PRK10789 417 TQQEIEHVA--RLASVHddilrLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDD 477
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
4-149 |
7.25e-09 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 52.33 E-value: 7.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 4 PARSVTTLLGPTGSGKTTFL-RTLNRMNdKVSGFRHSGDVLLGGRTiFADRDLMEfRRSVGMLFQRPNPFPMSIMDNVVA 82
Cdd:cd03290 25 PTGQLTMIVGQVGCGKSSLLlAILGEMQ-TLEGKVHWSNKNESEPS-FEATRSRN-RYSVAYAAQKPWLLNATVEENITF 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2014669168 83 GVRAHKmaprKQFKSVAEARLTEVGLwDAV----KDRLGDSPFRLSGGQQQLLCLARALAVNPDVLLLDEP 149
Cdd:cd03290 102 GSPFNK----QRYKAVTDACSLQPDI-DLLpfgdQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDP 167
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
13-150 |
8.73e-09 |
|
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: 51.98 E-value: 8.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 13 GPTGSGKTTFLRTLnrmndkvSGFRH--SGDVLLGGRTIFADRDlmEFRRSVGMLFQRPNPFP-MSIMDNVVAGVRAHKM 89
Cdd:TIGR01189 33 GPNGIGKTTLLRIL-------AGLLRpdSGEVRWNGTPLAEQRD--EPHENILYLGHLPGLKPeLSALENLHFWAAIHGG 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2014669168 90 APRKqfksvAEARLTEVGLWDavkdrLGDSPFR-LSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:TIGR01189 104 AQRT-----IEDALAAVGLTG-----FEDLPAAqLSAGQQRRLALARLWLSRRPLWILDEPT 155
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
13-150 |
9.61e-09 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 52.89 E-value: 9.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 13 GPTGSGKTTFLRTLnrmndkvSGFRHSGDvllgGRTIFADRDlmefrrsvGMLF--QRPNpFPMSIMDNVVAGVRAHKMA 90
Cdd:COG4178 396 GPSGSGKSTLLRAI-------AGLWPYGS----GRIARPAGA--------RVLFlpQRPY-LPLGTLREALLYPATAEAF 455
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2014669168 91 PRKQFKSVaearLTEVGLwDAVKDRLGDS---PFRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:COG4178 456 SDAELREA----LEAVGL-GHLAERLDEEadwDQVLSLGEQQRLAFARLLLHKPDWLFLDEAT 513
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
8-150 |
1.03e-08 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 52.19 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 8 VTTLLGPTGSGKTTFLRTLnrmndkVSGFRHSGdvllgGRTIFADRDLMEF------RRSVGMLFQRPNPFP-MSIMDNV 80
Cdd:PRK11614 33 IVTLIGANGAGKTTLLGTL------CGDPRATS-----GRIVFDGKDITDWqtakimREAVAIVPEGRRVFSrMTVEENL 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2014669168 81 VAGvraHKMAPRKQFKSvaeaRLTEV-GLWDAVKDRLGDSPFRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:PRK11614 102 AMG---GFFAERDQFQE----RIKWVyELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPS 165
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
11-150 |
1.04e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 52.86 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 11 LLGPTGSGKTTFLRTLNRMNDkVSGfrhsGDVLLGGRTIFAdRDLMEFRRSVGMLFQRPNPFPMSIMDNVVAGVRAhkma 90
Cdd:PTZ00243 1341 IVGRTGSGKSTLLLTFMRMVE-VCG----GEIRVNGREIGA-YGLRELRRQFSMIPQDPVLFDGTVRQNVDPFLEA---- 1410
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 91 prkqfkSVAE--ARLTEVGLWDAV-------KDRLGDSPFRLSGGQQQLLCLARA-LAVNPDVLLLDEPT 150
Cdd:PTZ00243 1411 ------SSAEvwAALELVGLRERVasesegiDSRVLEGGSNYSVGQRQLMCMARAlLKKGSGFILMDEAT 1474
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
11-150 |
1.37e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 52.72 E-value: 1.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 11 LLGPTGSGKTTFLRTLNRMNDKVSGfrhsgDVLLGGRTIFADRDLMEFRRSVGMLFQRPNPFPMSIMDNVVAGVRAHK-- 88
Cdd:PTZ00265 416 FVGESGCGKSTILKLIERLYDPTEG-----DIIINDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSLYSLKdl 490
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 89 --------------------------------------------MAPRKQFKSVAEARLTEV-----------GLWDAVK 113
Cdd:PTZ00265 491 ealsnyynedgndsqenknkrnscrakcagdlndmsnttdsnelIEMRKNYQTIKDSEVVDVskkvlihdfvsALPDKYE 570
|
170 180 190
....*....|....*....|....*....|....*..
gi 2014669168 114 DRLGDSPFRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:PTZ00265 571 TLVGSNASKLSGGQKQRISIARAIIRNPKILILDEAT 607
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
11-152 |
1.50e-08 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 51.78 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 11 LLGPTGSGKTTFLRTLNRMndkvsgFRHSGDVLLGGRTiFADRDLMEFRRSVGMLFQRPNPFPMSIMDNvvagvrahkMA 90
Cdd:cd03289 35 LLGRTGSGKSTLLSAFLRL------LNTEGDIQIDGVS-WNSVPLQKWRKAFGVIPQKVFIFSGTFRKN---------LD 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2014669168 91 PRKQFKS-----VAEarltEVGLWDAVKD-------RLGDSPFRLSGGQQQLLCLARALAVNPDVLLLDEPTRH 152
Cdd:cd03289 99 PYGKWSDeeiwkVAE----EVGLKSVIEQfpgqldfVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAH 168
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1-152 |
1.79e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 51.11 E-value: 1.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLnrmndkvsgfrhsgdvllggrtifadRDLMEFRRSVGMLFQRPNPFP--MSIMD 78
Cdd:COG2401 51 LEIEPGEIVLIVGASGSGKSTLLRLL--------------------------AGALKGTPVAGCVDVPDNQFGreASLID 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2014669168 79 NVvagvrahkmaPRKQFKSVAEARLTEVGLWDAVKDRlgdSPFR-LSGGQQQLLCLARALAVNPDVLLLDEPTRH 152
Cdd:COG2401 105 AI----------GRKGDFKDAVELLNAVGLSDAVLWL---RRFKeLSTGQKFRFRLALLLAERPKLLVIDEFCSH 166
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
13-150 |
1.84e-08 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 51.25 E-value: 1.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 13 GPTGSGKTTFLRTLNRMNDKVSGfrhsgdvllggRTIFADRDLM-----EFRRSVGMLFQRPNPFPMSIMDNVVA--GVR 85
Cdd:PRK10247 40 GPSGCGKSTLLKIVASLISPTSG-----------TLLFEGEDIStlkpeIYRQQVSYCAQTPTLFGDTVYDNLIFpwQIR 108
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2014669168 86 AHKMAPRKQFKSVAEARLTEVGLWDAVKDrlgdspfrLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:PRK10247 109 NQQPDPAIFLDDLERFALPDTILTKNIAE--------LSGGEKQRISLIRNLQFMPKVLLLDEIT 165
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
11-152 |
2.22e-08 |
|
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: 51.86 E-value: 2.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 11 LLGPTGSGKTTFLRTLNRMnDKvsgfRHSGDVLLG-GRTifadrdlmefrrsVGMLFQRPNPFP-MSIMDNVVAGVRAHK 88
Cdd:TIGR03719 36 VLGLNGAGKSTLLRIMAGV-DK----DFNGEARPQpGIK-------------VGYLPQEPQLDPtKTVRENVEEGVAEIK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 89 MA-------------PRKQFKSVAE--ARLTE----VGLW----------DAVKDRLGDSPF-RLSGGQQQLLCLARALA 138
Cdd:TIGR03719 98 DAldrfneisakyaePDADFDKLAAeqAELQEiidaADAWdldsqleiamDALRCPPWDADVtKLSGGERRRVALCRLLL 177
|
170
....*....|....
gi 2014669168 139 VNPDVLLLDEPTRH 152
Cdd:TIGR03719 178 SKPDMLLLDEPTNH 191
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
11-150 |
2.87e-08 |
|
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: 50.79 E-value: 2.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 11 LLGPTGSGKTTFLRTLnrmndkvSGFRH--SGDVLLGGRTIFADRDlmEFRRSVGMLFQRPNP--FPMSIMDNVVAGVRA 86
Cdd:cd03267 52 FIGPNGAGKTTTLKIL-------SGLLQptSGEVRVAGLVPWKRRK--KFLRRIGVVFGQKTQlwWDLPVIDSFYLLAAI 122
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2014669168 87 HKMAPRKQFKSVAE-ARLTEVGlwdavkdRLGDSPFR-LSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:cd03267 123 YDLPPARFKKRLDElSELLDLE-------ELLDTPVRqLSLGQRMRAEIAAALLHEPEILFLDEPT 181
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-150 |
4.00e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 51.07 E-value: 4.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLnrmndkvSGFRH--SGDVLLGGRTI-FAD-RDLMEfrRSVGMLFQRPNPFP-MS 75
Cdd:PRK11288 25 FDCRAGQVHALMGENGAGKSTLLKIL-------SGNYQpdAGSILIDGQEMrFAStTAALA--AGVAIIYQELHLVPeMT 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2014669168 76 IMDNVVAGVRAHK--MAPRKQFKSVAEARLTEVGLwdavkDRLGDSPFR-LSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:PRK11288 96 VAENLYLGQLPHKggIVNRRLLNYEAREQLEHLGV-----DIDPDTPLKyLSIGQRQMVEIAKALARNARVIAFDEPT 168
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
119-151 |
4.49e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 50.70 E-value: 4.49e-08
10 20 30
....*....|....*....|....*....|....*..
gi 2014669168 119 SPF----RLSGGQQQLLCLARALAVNPDVLLLDEPTR 151
Cdd:PRK13549 398 SPElaiaRLSGGNQQKAVLAKCLLLNPKILILDEPTR 434
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1-150 |
5.06e-08 |
|
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: 50.78 E-value: 5.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLNRMNDKVSGfrhsgDVLLGGRTIFADRDLMefRRSVGMLFQRPNPFP-MSIMDN 79
Cdd:TIGR01257 951 ITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSG-----TVLVGGKDIETNLDAV--RQSLGMCPQHNILFHhLTVAEH 1023
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2014669168 80 VVAGVRAhKMAPRKQFKSVAEARLTEVGLWDAVKDRLGDspfrLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:TIGR01257 1024 ILFYAQL-KGRSWEEAQLEMEAMLEDTGLHHKRNEEAQD----LSGGMQRKLSVAIAFVGDAKVVVLDEPT 1089
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
106-149 |
5.14e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 50.78 E-value: 5.14e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2014669168 106 VGLWDAVKDR-----------------LGDSPFR-LSGGQQQLLCLARALAVNPDVLLLDEP 149
Cdd:PRK10938 367 IGIYQAVSDRqqklaqqwldilgidkrTADAPFHsLSWGQQRLALIVRALVKHPTLLILDEP 428
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
8-150 |
6.91e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 50.13 E-value: 6.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 8 VTTLLGPTGSGKTtflrtlnrmndkVSGFRHSGDVLLGGRTI-----FADRDLM-----EFRRSVG----MLFQRP---- 69
Cdd:PRK11022 35 VVGIVGESGSGKS------------VSSLAIMGLIDYPGRVMaekleFNGQDLQrisekERRNLVGaevaMIFQDPmtsl 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 70 NP---FPMSIMDnvvaGVRAHKMAPRKQFKSVAEARLTEVGLWDAvKDRLGDSPFRLSGGQQQLLCLARALAVNPDVLLL 146
Cdd:PRK11022 103 NPcytVGFQIME----AIKVHQGGNKKTRRQRAIDLLNQVGIPDP-ASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIA 177
|
....
gi 2014669168 147 DEPT 150
Cdd:PRK11022 178 DEPT 181
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
11-150 |
1.56e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 49.32 E-value: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 11 LLGPTGSGKTTFLRTLNRMNDKVSGFRHSGDVLLGGRTIF--ADRDLMEFR-RSVGMLFQRP----NPFpMSIMDNVVAG 83
Cdd:PRK15134 40 LVGESGSGKSVTALSILRLLPSPPVVYPSGDIRFHGESLLhaSEQTLRGVRgNKIAMIFQEPmvslNPL-HTLEKQLYEV 118
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2014669168 84 VRAHKMAPRKQFKSVAEARLTEVGLWDAVKdRLGDSPFRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:PRK15134 119 LSLHRGMRREAARGEILNCLDRVGIRQAAK-RLTDYPHQLSGGERQRVMIAMALLTRPELLIADEPT 184
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-149 |
1.82e-07 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 48.54 E-value: 1.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLNRMNDKvsgfrHSGDVLLGGRTIfADRDLMEFRRSVGMLFQRpNPFPMSIMdnv 80
Cdd:COG4604 22 LTIPKGGITALIGPNGAGKSTLLSMISRLLPP-----DSGEVLVDGLDV-ATTPSRELAKRLAILRQE-NHINSRLT--- 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2014669168 81 vagVRA---------HKMAPRKQ-FKSVAEArLTEVGLwDAVKDRLGDSpfrLSGGQQQLLCLARALAVNPDVLLLDEP 149
Cdd:COG4604 92 ---VRElvafgrfpySKGRLTAEdREIIDEA-IAYLDL-EDLADRYLDE---LSGGQRQRAFIAMVLAQDTDYVLLDEP 162
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
11-152 |
2.37e-07 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 48.52 E-value: 2.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 11 LLGPTGSGKTTFLRTL-NRMNDkvsgfrHSGDVLLGGRTIFA--DRDLMEFRrsvgmlfqrPNpfpMSIMDNVVAG---- 83
Cdd:COG0488 346 LIGPNGAGKSTLLKLLaGELEP------DSGTVKLGETVKIGyfDQHQEELD---------PD---KTVLDELRDGapgg 407
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2014669168 84 ----VRAH--KM--APRKQFKSVAearltevglwdavkdrlgdspfRLSGGQQQLLCLARALAVNPDVLLLDEPTRH 152
Cdd:COG0488 408 teqeVRGYlgRFlfSGDDAFKPVG----------------------VLSGGEKARLALAKLLLSPPNVLLLDEPTNH 462
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
11-150 |
3.29e-07 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 48.29 E-value: 3.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 11 LLGPTGSGKTTFLRTLNRMNDKVSGFRHSGDVLLGGRTIFAdrdlmefRRSVGMLFQRPNPFP-MSIMDNVVAGVRAHKM 89
Cdd:PRK13536 72 LLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLA-------RARIGVVPQFDNLDLeFTVRENLLVFGRYFGM 144
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2014669168 90 APRkQFKSVAEARLTEVGLWDAVKDRLGDspfrLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:PRK13536 145 STR-EIEAVIPSLLEFARLESKADARVSD----LSGGMKRRLTLARALINDPQLLILDEPT 200
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
119-151 |
3.30e-07 |
|
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: 48.28 E-value: 3.30e-07
10 20 30
....*....|....*....|....*....|....*..
gi 2014669168 119 SPF----RLSGGQQQLLCLARALAVNPDVLLLDEPTR 151
Cdd:TIGR02633 396 SPFlpigRLSGGNQQKAVLAKMLLTNPRVLILDEPTR 432
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1-150 |
3.39e-07 |
|
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: 48.28 E-value: 3.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDF--PARSVTTLLGPTGSGKTTFLRTLNRMNDkVSgfrhSGDVLLGGRTIfadRDLME--FRRSVGMLFQRPNPFPMSI 76
Cdd:COG5265 377 VSFevPAGKTVAIVGPSGAGKSTLARLLFRFYD-VT----SGRILIDGQDI---RDVTQasLRAAIGIVPQDTVLFNDTI 448
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2014669168 77 MDNVVAGvRAHkmAPRKQFKSVAE-ARLTE--VGLWDAVKDRLGDSPFRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:COG5265 449 AYNIAYG-RPD--ASEEEVEAAARaAQIHDfiESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEAT 522
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
122-151 |
3.58e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 48.25 E-value: 3.58e-07
10 20 30
....*....|....*....|....*....|
gi 2014669168 122 RLSGGQQQLLCLARALAVNPDVLLLDEPTR 151
Cdd:NF040905 404 NLSGGNQQKVVLSKWLFTDPDVLILDEPTR 433
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
11-150 |
3.61e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 48.43 E-value: 3.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 11 LLGPTGSGKTTFLRTLNRMNDkvsgfrhsgdvLLGGRTIFADRDLMEF-----RRSVGMLFQRPNPFPMSIMDNVvagvr 85
Cdd:PLN03232 1267 VVGRTGAGKSSMLNALFRIVE-----------LEKGRIMIDDCDVAKFgltdlRRVLSIIPQSPVLFSGTVRFNI----- 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 86 ahkmaprKQFKSVAEArltevGLWDA-----VKDRLGDSPFRL-----------SGGQQQLLCLARALAVNPDVLLLDEP 149
Cdd:PLN03232 1331 -------DPFSEHNDA-----DLWEAlerahIKDVIDRNPFGLdaevseggenfSVGQRQLLSLARALLRRSKILVLDEA 1398
|
.
gi 2014669168 150 T 150
Cdd:PLN03232 1399 T 1399
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
4-149 |
5.77e-07 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 47.18 E-value: 5.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 4 PARSVTTLLGPTGSGKTTFLRTLnrmndkvSGFRH--SGDV-LLGGRTIFADRdlmefRRSVGMLFQRPN---PFPMSIM 77
Cdd:PRK15056 31 PGGSIAALVGVNGSGKSTLFKAL-------MGFVRlaSGKIsILGQPTRQALQ-----KNLVAYVPQSEEvdwSFPVLVE 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2014669168 78 DNVVAGVRAHK---MAPRKQFKSVAEARLTEVGLWDAVKDRLGDspfrLSGGQQQLLCLARALAVNPDVLLLDEP 149
Cdd:PRK15056 99 DVVMMGRYGHMgwlRRAKKRDRQIVTAALARVDMVEFRHRQIGE----LSGGQKKRVFLARAIAQQGQVILLDEP 169
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
8-152 |
6.40e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 47.50 E-value: 6.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 8 VTTLLGPTGSGKTTFLRTLnrmndkvsgfrhSGDVL--LGGRTIFADRD--LMEFRRSVgmLFqrpNPFpmsimDNVVAG 83
Cdd:PRK13409 101 VTGILGPNGIGKTTAVKIL------------SGELIpnLGDYEEEPSWDevLKRFRGTE--LQ---NYF-----KKLYNG 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 84 -VR-AHK-----MAPrKQFK-SVAE--ARLTEVGLWDAVKDRLG-----DSPFR-LSGGQQQLLCLARALAVNPDVLLLD 147
Cdd:PRK13409 159 eIKvVHKpqyvdLIP-KVFKgKVREllKKVDERGKLDEVVERLGlenilDRDISeLSGGELQRVAIAAALLRDADFYFFD 237
|
....*
gi 2014669168 148 EPTRH 152
Cdd:PRK13409 238 EPTSY 242
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
9-150 |
6.86e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 46.79 E-value: 6.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 9 TTLLGPTGSGKTTFLRTLnrmndkvSGFRH--SGDVLLGGRtifaDRDLMEFRRSVGMLFQRP--NPFpMSIMDNVV--A 82
Cdd:PRK13539 31 LVLTGPNGSGKTTLLRLI-------AGLLPpaAGTIKLDGG----DIDDPDVAEACHYLGHRNamKPA-LTVAENLEfwA 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2014669168 83 GVRAhkmaprkQFKSVAEARLTEVGLwdavkDRLGDSPFR-LSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:PRK13539 99 AFLG-------GEELDIAAALEAVGL-----APLAHLPFGyLSAGQKRRVALARLLVSNRPIWILDEPT 155
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
123-151 |
7.09e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 47.31 E-value: 7.09e-07
10 20
....*....|....*....|....*....
gi 2014669168 123 LSGGQQQLLCLARALAVNPDVLLLDEPTR 151
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEPTR 424
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
7-150 |
8.65e-07 |
|
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: 46.47 E-value: 8.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 7 SVTTLLGPTGSGKTTFLRTL-NRmndKVSGFRhSGDVLLGGRTIfadrdLMEFRRSVGMLFQRPNPFPMSimdnvvagvr 85
Cdd:cd03232 34 TLTALMGESGAGKTTLLDVLaGR---KTAGVI-TGEILINGRPL-----DKNFQRSTGYVEQQDVHSPNL---------- 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2014669168 86 ahkmaprkqfkSVAEARLTEVGLWDavkdrlgdspfrLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:cd03232 95 -----------TVREALRFSALLRG------------LSVEQRKRLTIGVELAAKPSILFLDEPT 136
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
11-152 |
8.89e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 47.04 E-value: 8.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 11 LLGPTGSGKTTFLRTLNRMnDKVSgfrhSGDVLLG-GRTifadrdlmefrrsVGMLFQRP--NPfPMSIMDNVVAGVrAH 87
Cdd:PRK11819 38 VLGLNGAGKSTLLRIMAGV-DKEF----EGEARPApGIK-------------VGYLPQEPqlDP-EKTVRENVEEGV-AE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 88 KMAPRKQFKSVAE----------------ARLTEV----GLW----------DAVkdRL--GDSPF-RLSGGQQQLLCLA 134
Cdd:PRK11819 98 VKAALDRFNEIYAayaepdadfdalaaeqGELQEIidaaDAWdldsqleiamDAL--RCppWDAKVtKLSGGERRRVALC 175
|
170
....*....|....*...
gi 2014669168 135 RALAVNPDVLLLDEPTRH 152
Cdd:PRK11819 176 RLLLEKPDMLLLDEPTNH 193
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
11-150 |
9.57e-07 |
|
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: 46.33 E-value: 9.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 11 LLGPTGSGKTTFLRTLNRMNDKVsgfrhSGDVLLGGRTIFADRDlmEFRRSVGMLFQRPN-PFPMSIMDNVvagvraHKM 89
Cdd:cd03231 31 VTGPNGSGKTTLLRILAGLSPPL-----AGRVLLNGGPLDFQRD--SIARGLLYLGHAPGiKTTLSVLENL------RFW 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2014669168 90 APRKQFKSVAEArLTEVGLwdavkDRLGDSPF-RLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:cd03231 98 HADHSDEQVEEA-LARVGL-----NGFEDRPVaQLSAGQQRRVALARLLLSGRPLWILDEPT 153
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
11-151 |
1.11e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 46.97 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 11 LLGPTGSGKTTFLRTLnrmndkvSGFR--HSGDVLLGGRTIFADRD----------LMEFRRSVGMLFQRPnpfpmsIMD 78
Cdd:PRK15439 294 LAGVVGAGRTELAETL-------YGLRpaRGGRIMLNGKEINALSTaqrlarglvyLPEDRQSSGLYLDAP------LAW 360
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2014669168 79 NVVAgVRAHKM---APRKQFKSVAEARLTEVGlwdaVKDRLGDSPFR-LSGGQQQLLCLARALAVNPDVLLLDEPTR 151
Cdd:PRK15439 361 NVCA-LTHNRRgfwIKPARENAVLERYRRALN----IKFNHAEQAARtLSGGNQQKVLIAKCLEASPQLLIVDEPTR 432
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
13-152 |
1.27e-06 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 46.39 E-value: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 13 GPTGSGKTTFLRT-LNRMNDKVSGFRHSGDVLLGGRTIFadrdLMefrrsvgmlfqrpnpfPMSIMDNVVAGVRAHKMap 91
Cdd:cd03291 70 GSTGSGKTSLLMLiLGELEPSEGKIKHSGRISFSSQFSW----IM----------------PGTIKENIIFGVSYDEY-- 127
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2014669168 92 rkQFKSVAEA-RLTEVGLWDAVKDR--LGDSPFRLSGGQQQLLCLARALAVNPDVLLLDEPTRH 152
Cdd:cd03291 128 --RYKSVVKAcQLEEDITKFPEKDNtvLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGY 189
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
13-152 |
1.35e-06 |
|
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: 46.83 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 13 GPTGSGKTTFLRT-LNRMNDKVSGFRHSGdvllggRTIFADrdlmefrrsvgmlfQRPNPFPMSIMDNVVAGVRAHKMap 91
Cdd:TIGR01271 459 GSTGSGKSSLLMMiMGELEPSEGKIKHSG------RISFSP--------------QTSWIMPGTIKDNIIFGLSYDEY-- 516
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2014669168 92 rkQFKSVAEA-RLTEVGLWDAVKDR--LGDSPFRLSGGQQQLLCLARALAVNPDVLLLDEPTRH 152
Cdd:TIGR01271 517 --RYTSVIKAcQLEEDIALFPEKDKtvLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTH 578
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1-149 |
1.55e-06 |
|
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: 45.60 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTL-NRMNDKVSGfrhsGDVLLGGRTIFA----DRdlmeFRRSVGMLFQRPNPFPms 75
Cdd:cd03217 21 LTIKKGEVHALMGPNGSGKSTLAKTImGHPKYEVTE----GEILFKGEDITDlppeER----ARLGIFLAFQYPPEIP-- 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2014669168 76 imdnvvaGVRahkmaprkqfksvaearltevglwdaVKDRLGDSPFRLSGGQQQLLCLARALAVNPDVLLLDEP 149
Cdd:cd03217 91 -------GVK--------------------------NADFLRYVNEGFSGGEKKRNEILQLLLLEPDLAILDEP 131
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
1-149 |
1.56e-06 |
|
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: 46.48 E-value: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDF--PARSVTTLLGPTGSGKTTFLRTLNRMNDKVSGFRHsgdvllggrtifadrdlmeFRRSVGMLFQRPNPFPMSIMD 78
Cdd:TIGR00957 657 ITFsiPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVH-------------------MKGSVAYVPQQAWIQNDSLRE 717
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2014669168 79 NVVAGvraHKMAPrKQFKSVAEA--RLTEVGLWDAvKDR--LGDSPFRLSGGQQQLLCLARALAVNPDVLLLDEP 149
Cdd:TIGR00957 718 NILFG---KALNE-KYYQQVLEAcaLLPDLEILPS-GDRteIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDP 787
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
11-150 |
2.10e-06 |
|
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: 46.16 E-value: 2.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 11 LLGPTGSGKTTFLRTLNRmNDKVSgfrhSGDVLLGGRTIFADrdLMEFRRSVGMLFQrpnpfpMSIMDNVVAGvRAH--- 87
Cdd:TIGR01257 1970 LLGVNGAGKTTTFKMLTG-DTTVT----SGDATVAGKSILTN--ISDVHQNMGYCPQ------FDAIDDLLTG-REHlyl 2035
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2014669168 88 ----KMAPRKQFKSVAEARLTEVGLwDAVKDRLGDSpfrLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:TIGR01257 2036 yarlRGVPAEEIEKVANWSIQSLGL-SLYADRLAGT---YSGGNKRKLSTAIALIGCPPLVLLDEPT 2098
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-149 |
2.21e-06 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 45.75 E-value: 2.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLnrmndkvSGFRH--SGDVLLGGRTIFADRDLMEFRRSVGMLFQRPNPF-PMSIM 77
Cdd:PRK11300 26 LEVREQEIVSLIGPNGAGKTTVFNCL-------TGFYKptGGTILLRGQHIEGLPGHQIARMGVVRTFQHVRLFrEMTVI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 78 DN------------VVAGVRAHKMAPRKQFKSVAEAR--LTEVGLWDAVKDRLGDspfrLSGGQQQLLCLARALAVNPDV 143
Cdd:PRK11300 99 ENllvaqhqqlktgLFSGLLKTPAFRRAESEALDRAAtwLERVGLLEHANRQAGN----LAYGQQRRLEIARCMVTQPEI 174
|
....*.
gi 2014669168 144 LLLDEP 149
Cdd:PRK11300 175 LMLDEP 180
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
8-150 |
4.81e-06 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 44.82 E-value: 4.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 8 VTTLLGPTGSGKTTFLRTLN---RMNDKVSGFRHSGDVLLGGRTIfADRDLMEFRRSVGMLFQRPNP-FPMSIMDNVVAG 83
Cdd:PRK13547 29 VTALLGRNGAGKSTLLKALAgdlTGGGAPRGARVTGDVTLNGEPL-AAIDAPRLARLRAVLPQAAQPaFAFSAREIVLLG 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2014669168 84 VRAHkmAPRKQFKSVAEARLTEVGLWDAVKDRL-GDSPFRLSGGQQQLLCLARALA---------VNPDVLLLDEPT 150
Cdd:PRK13547 108 RYPH--ARRAGALTHRDGEIAWQALALAGATALvGRDVTTLSGGELARVQFARVLAqlwpphdaaQPPRYLLLDEPT 182
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
111-151 |
6.86e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 44.52 E-value: 6.86e-06
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2014669168 111 AVKDRLGDSPFR-LSGGQQQLLCLARALAVNPDVLLLDEPTR 151
Cdd:PRK11288 384 NIKTPSREQLIMnLSGGNQQKAILGRWLSEDMKVILLDEPTR 425
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
8-150 |
7.02e-06 |
|
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: 44.39 E-value: 7.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 8 VTTLLGPTGSGKTTFLRTLnrmndkvsgfrhSGDVL--LGGRTIFADRD--LMEFRRS-VGMLFQRpnpfpmsimdnVVA 82
Cdd:COG1245 101 VTGILGPNGIGKSTALKIL------------SGELKpnLGDYDEEPSWDevLKRFRGTeLQDYFKK-----------LAN 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 83 G-VR-AHK-----MAPrKQFK-SVAE--ARLTEVGLWDAVKDRLGDSPFR------LSGGQQQLLCLARALAVNPDVLLL 146
Cdd:COG1245 158 GeIKvAHKpqyvdLIP-KVFKgTVREllEKVDERGKLDELAEKLGLENILdrdiseLSGGELQRVAIAAALLRDADFYFF 236
|
....
gi 2014669168 147 DEPT 150
Cdd:COG1245 237 DEPS 240
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
11-150 |
7.88e-06 |
|
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: 43.30 E-value: 7.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 11 LLGPTGSGKTTFLRTLNrmndkvsGFRHSGdvllGGRTIF-ADRDLMefrrsvgMLFQRPnpfpmsimdnvvagvrahKM 89
Cdd:cd03223 32 ITGPSGTGKSSLFRALA-------GLWPWG----SGRIGMpEGEDLL-------FLPQRP------------------YL 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2014669168 90 APrkqfksvaeARLTEVGL--WDAVkdrlgdspfrLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:cd03223 76 PL---------GTLREQLIypWDDV----------LSGGEQQRLAFARLLLHKPKFVFLDEAT 119
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
1-149 |
9.70e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 44.20 E-value: 9.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLNrmndkvsgfrhsgdvllgGRTIFADRDLMEFRRSVGMLFQRPNPFPMSIMDNV 80
Cdd:PLN03232 638 LEIPVGSLVAIVGGTGEGKTSLISAML------------------GELSHAETSSVVIRGSVAYVPQVSWIFNATVRENI 699
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2014669168 81 VAGvraHKMAPRKQFKSV-AEARLTEVGLWdAVKDR--LGDSPFRLSGGQQQLLCLARALAVNPDVLLLDEP 149
Cdd:PLN03232 700 LFG---SDFESERYWRAIdVTALQHDLDLL-PGRDLteIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDP 767
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-150 |
1.60e-05 |
|
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: 43.64 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLNRMNDKVSGfrhSGDVLLGGRTI-FADRDLMEFRRS---VGMLFQRPNPFP-MS 75
Cdd:TIGR03269 305 LEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSG---EVNVRVGDEWVdMTKPGPDGRGRAkryIGILHQEYDLYPhRT 381
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2014669168 76 IMDNVVAGVRAH---KMAPRKQFKSVAEARLTEvglwDAVKDRLGDSPFRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:TIGR03269 382 VLDNLTEAIGLElpdELARMKAVITLKMVGFDE----EKAEEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPT 455
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
11-150 |
1.60e-05 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 43.15 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 11 LLGPTGSGKTTFLRTLnrmndkvSGFRH--SGDVLLGGRTIFADRdlMEFRRSVGMLF-QRPNPFP-MSIMDN-----VV 81
Cdd:COG4586 53 FIGPNGAGKSTTIKML-------TGILVptSGEVRVLGYVPFKRR--KEFARRIGVVFgQRSQLWWdLPAIDSfrllkAI 123
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2014669168 82 AGVrahkmaPRKQFKsvaeARLTE-VGLWDaVKDRLgDSPFR-LSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:COG4586 124 YRI------PDAEYK----KRLDElVELLD-LGELL-DTPVRqLSLGQRMRCELAAALLHRPKILFLDEPT 182
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
124-152 |
1.66e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 43.31 E-value: 1.66e-05
10 20
....*....|....*....|....*....
gi 2014669168 124 SGGQQQLLCLARALAVNPDVLLLDEPTRH 152
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNH 374
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
11-150 |
1.89e-05 |
|
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: 43.40 E-value: 1.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 11 LLGPTGSGKTTFLRTLNRMNDKVSGfrhsgDVLLGGRTIfADRDLMEFRRSVGMLFQRPNPFPMSIMDNVVAGVR----- 85
Cdd:TIGR00957 1317 IVGRTGAGKSSLTLGLFRINESAEG-----EIIIDGLNI-AKIGLHDLRFKITIIPQDPVLFSGSLRMNLDPFSQysdee 1390
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2014669168 86 ---AHKMAPRKQFKSVAEARLTEvglwdavkdRLGDSPFRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:TIGR00957 1391 vwwALELAHLKTFVSALPDKLDH---------ECAEGGENLSVGQRQLVCLARALLRKTKILVLDEAT 1449
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
1-149 |
1.92e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 43.23 E-value: 1.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLnrmndkvsgfrhsgdvlLGGRTIFADRDLMEfrRSVGMLFQRPNPFPMSIMDNV 80
Cdd:PTZ00243 681 VSVPRGKLTVVLGATGSGKSTLLQSL-----------------LSQFEISEGRVWAE--RSIAYVPQQAWIMNATVRGNI 741
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2014669168 81 V-----AGVRAHKMAPRKQFksvaEARLTEVGlwDAVKDRLGDSPFRLSGGQQQLLCLARALAVNPDVLLLDEP 149
Cdd:PTZ00243 742 LffdeeDAARLADAVRVSQL----EADLAQLG--GGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDP 809
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
13-149 |
2.76e-05 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 42.10 E-value: 2.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 13 GPTGSGKTTFLRTLnrmndkvSGFRH--SGDVLLGGRTIFADRDlmEFRRSVGMLFQRPNPFP-MSIMDNVVAGVRAHKM 89
Cdd:PRK13538 34 GPNGAGKTSLLRIL-------AGLARpdAGEVLWQGEPIRRQRD--EYHQDLLYLGHQPGIKTeLTALENLRFYQRLHGP 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2014669168 90 APRKQfksVAEArLTEVGLwdavkDRLGDSPFR-LSGGQQQLLCLARALAVNPDVLLLDEP 149
Cdd:PRK13538 105 GDDEA---LWEA-LAQVGL-----AGFEDVPVRqLSAGQQRRVALARLWLTRAPLWILDEP 156
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
16-151 |
2.80e-05 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 42.71 E-value: 2.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 16 GSGKTTFLRTLnrmndkvSGFRH--SGDVLLGGRTIfADRDLMEFRRSvGMLF-----QR----PNpfpMSIMDNVVAGv 84
Cdd:COG3845 294 GNGQSELAEAL-------AGLRPpaSGSIRLDGEDI-TGLSPRERRRL-GVAYipedrLGrglvPD---MSVAENLILG- 360
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2014669168 85 rAHKMAP--------RKQFKSVAEARLTEvglWDaVKDRLGDSPFR-LSGGQQQLLCLARALAVNPDVLLLDEPTR 151
Cdd:COG3845 361 -RYRRPPfsrggfldRKAIRAFAEELIEE---FD-VRTPGPDTPARsLSGGNQQKVILARELSRDPKLLIAAQPTR 431
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
11-150 |
2.83e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 42.61 E-value: 2.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 11 LLGPTGSGKTTFLRTLnrmndkvSG-FRH---SGDVLLGGRTIFAD--RDlMEfRRSVGMLFQR----PNpfpMSIMDNV 80
Cdd:PRK13549 36 LCGENGAGKSTLMKVL-------SGvYPHgtyEGEIIFEGEELQASniRD-TE-RAGIAIIHQElalvKE---LSVLENI 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2014669168 81 VAG---VRAHKMAPRKQFkSVAEARLTEVGLWDAVKDRLGDspfrLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:PRK13549 104 FLGneiTPGGIMDYDAMY-LRAQKLLAQLKLDINPATPVGN----LGLGQQQLVEIAKALNKQARLLILDEPT 171
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
11-150 |
2.86e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 42.80 E-value: 2.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 11 LLGPTGSGKTTFLRTLNRMNDKvsgfrHSGDVLLGGRTIfADRDLMEFRRSVGMLFQRPNPFPMSIMDNVvAGVRAHKMA 90
Cdd:PLN03130 1270 IVGRTGAGKSSMLNALFRIVEL-----ERGRILIDGCDI-SKFGLMDLRKVLGIIPQAPVLFSGTVRFNL-DPFNEHNDA 1342
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2014669168 91 prKQFKSVAEARLTEV------GLwDAVKDRLGDSpfrLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:PLN03130 1343 --DLWESLERAHLKDVirrnslGL-DAEVSEAGEN---FSVGQRQLLSLARALLRRSKILVLDEAT 1402
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
3-150 |
3.75e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 42.30 E-value: 3.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 3 FPARsVTTLLGPTGSGKTTFLRTLNRMNDKVSGFRHsgdvLLGGRTIFAD-RDLMEfrRSVGMLFQRPNPFP-MSIMDNV 80
Cdd:PRK10762 28 YPGR-VMALVGENGAGKSTMMKVLTGIYTRDAGSIL----YLGKEVTFNGpKSSQE--AGIGIIHQELNLIPqLTIAENI 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2014669168 81 VAG---VRAHKMAPRKQFKSVAEARLTEVGLWDAVKDRLGDspfrLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:PRK10762 101 FLGrefVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGE----LSIGEQQMVEIAKVLSFESKVIIMDEPT 169
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-148 |
6.20e-05 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 41.31 E-value: 6.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTL--LGPTGSGKTTFLRTLNRMNDKVSGfrhsgDVLLGGRTI-FADRDLMEFRrsVGMLFQRP----NP-- 71
Cdd:PRK15112 32 LSFTLREGQTLaiIGENGSGKSTLAKMLAGMIEPTSG-----ELLIDDHPLhFGDYSYRSQR--IRMIFQDPstslNPrq 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 72 -------FPMSIMDnvvagvrahKMAPRKQFKSVAEArLTEVGLwdaVKDRLGDSPFRLSGGQQQLLCLARALAVNPDVL 144
Cdd:PRK15112 105 risqildFPLRLNT---------DLEPEQREKQIIET-LRQVGL---LPDHASYYPHMLAPGQKQRLGLARALILRPKVI 171
|
....
gi 2014669168 145 LLDE 148
Cdd:PRK15112 172 IADE 175
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
58-150 |
6.47e-05 |
|
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: 41.71 E-value: 6.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 58 FRRSVGMLFQRPnpFPM----SIMDNVVagvRAHKMAPRKQFKSVAEArlteVGLWDAVK--DRLGDSPFRLSGGQQQLL 131
Cdd:TIGR03269 107 IRKRIAIMLQRT--FALygddTVLDNVL---EALEEIGYEGKEAVGRA----VDLIEMVQlsHRITHIARDLSGGEKQRV 177
|
90
....*....|....*....
gi 2014669168 132 CLARALAVNPDVLLLDEPT 150
Cdd:TIGR03269 178 VLARQLAKEPFLFLADEPT 196
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
8-150 |
6.68e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 41.63 E-value: 6.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 8 VTTLLGPTGSGKTTFLRTL-NRMNdkvSGFRHSGDVLLGGRTIFAdrdlmEFRRSVGMLFQRPNPFPMSIMDNVV---AG 83
Cdd:TIGR00956 791 LTALMGASGAGKTTLLNVLaERVT---TGVITGGDRLVNGRPLDS-----SFQRSIGYVQQQDLHLPTSTVRESLrfsAY 862
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2014669168 84 VRAHKMAPRKQFKSVAEA--RLTEV-GLWDAVkdrLGDSPFRLSGGQQQLLCLARALAVNPDVLL-LDEPT 150
Cdd:TIGR00956 863 LRQPKSVSKSEKMEYVEEviKLLEMeSYADAV---VGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPT 930
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
11-150 |
7.08e-05 |
|
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: 41.73 E-value: 7.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 11 LLGPTGSGKTTFLRTLNRMNDKVSgfrHSGDVLLGGRTIFADRDLMEFRRSVGMLFQRPNPFP-MSIMDNVVAGVRAHKM 89
Cdd:TIGR02633 32 LCGENGAGKSTLMKILSGVYPHGT---WDGEIYWSGSPLKASNIRDTERAGIVIIHQELTLVPeLSVAENIFLGNEITLP 108
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2014669168 90 APRKQFKSV---AEARLTEVGLwDAVKDRLGDSpfRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:TIGR02633 109 GGRMAYNAMylrAKNLLRELQL-DADNVTRPVG--DYGGGQQQLVEIAKALNKQARLLILDEPS 169
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
13-150 |
7.66e-05 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 41.05 E-value: 7.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 13 GPTGSGKTTFLRTLNRMNDKVSGfrhsgDVLLGGRTIfADRDLMEFRRSVGMLFQRPNPFPMSIMDNVVAgvrAHKMAPR 92
Cdd:cd03288 54 GRTGSGKSSLSLAFFRMVDIFDG-----KIVIDGIDI-SKLPLHTLRSRLSIILQDPILFSGSIRFNLDP---ECKCTDD 124
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2014669168 93 KQFKSVAEARLTEV-----GLWDAVKDRLGDSpfrLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:cd03288 125 RLWEALEIAQLKNMvkslpGGLDAVVTEGGEN---FSVGQRQLFCLARAFVRKSSILIMDEAT 184
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-150 |
8.12e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 41.31 E-value: 8.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTLnrmndkvSGFRH--SGDVLLGGRTIFADRDLMEFRRSVGMLFQRPNPF-PMSIM 77
Cdd:PRK09700 26 LTVYPGEIHALLGENGAGKSTLMKVL-------SGIHEptKGTITINNINYNKLDHKLAAQLGIGIIYQELSVIdELTVL 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2014669168 78 DNVVAG------VRAHKMAPRKQFKSVAEARLTEVGLWDAVKDRLGDspfrLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:PRK09700 99 ENLYIGrhltkkVCGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVAN----LSISHKQMLEIAKTLMLDAKVIIMDEPT 173
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
123-151 |
1.10e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 40.87 E-value: 1.10e-04
10 20
....*....|....*....|....*....
gi 2014669168 123 LSGGQQQLLCLARALAVNPDVLLLDEPTR 151
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTR 420
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
11-148 |
1.44e-04 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 40.45 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 11 LLGPTGSGKTTFLRTLNRMnDKVSgfrhSGDVLLGGRTIFadrdLMEFrrSVGMlfqrpNPFpMSIMDNVVAGVRAHKMa 90
Cdd:COG1134 57 IIGRNGAGKSTLLKLIAGI-LEPT----SGRVEVNGRVSA----LLEL--GAGF-----HPE-LTGRENIYLNGRLLGL- 118
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2014669168 91 PRKQfksvAEARLTEV----GLWDAVkdrlgDSPFR-LSGGQQQLLCLARALAVNPDVLLLDE 148
Cdd:COG1134 119 SRKE----IDEKFDEIvefaELGDFI-----DQPVKtYSSGMRARLAFAVATAVDPDILLVDE 172
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
8-152 |
1.69e-04 |
|
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: 39.90 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 8 VTTLLGPTGSGKTTFLRTLnrmndKVSGFrhsGDVLLGGRTIFADRDL-----------MEFRRSVG--MLFQRPnpfpM 74
Cdd:cd03240 24 LTLIVGQNGAGKTTIIEAL-----KYALT---GELPPNSKGGAHDPKLiregevraqvkLAFENANGkkYTITRS----L 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 75 SIMDNVVagvrahkMAPRKQFKSVAEarltevglwdavkdrlgDSPFRLSGGQQQLLCLARALA------VNPDVLLLDE 148
Cdd:cd03240 92 AILENVI-------FCHQGESNWPLL-----------------DMRGRCSGGEKVLASLIIRLAlaetfgSNCGILALDE 147
|
....
gi 2014669168 149 PTRH 152
Cdd:cd03240 148 PTTN 151
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
11-150 |
1.71e-04 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 40.30 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 11 LLGPTGSGKTTFlrtLNRMndkvSG-FRHSGDVLLGGRTIfADRDLMEFRRSVGMLFQRPNP-FPMSIMdnvvagvraHK 88
Cdd:PRK03695 27 LVGPNGAGKSTL---LARM----AGlLPGSGSIQFAGQPL-EAWSAAELARHRAYLSQQQTPpFAMPVF---------QY 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2014669168 89 MA---PRKQFKSVAEARLTEVGLWDAVKDRLGDSPFRLSGGQQQLLCLARAL-----AVNPD--VLLLDEPT 150
Cdd:PRK03695 90 LTlhqPDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVlqvwpDINPAgqLLLLDEPM 161
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
11-151 |
2.16e-04 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 39.89 E-value: 2.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 11 LLGPTGSGKTTFLRT-LNRMND--KVSGFR-HSGDVLLGGRTIFADRDLMefRRSVGMLFQRPNPF--PMS-----IMDN 79
Cdd:COG4170 38 LVGESGSGKSLIAKAiCGITKDnwHVTADRfRWNGIDLLKLSPRERRKII--GREIAMIFQEPSSCldPSAkigdqLIEA 115
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2014669168 80 VVAG-VRAHKMAPRKQFKSVAEARLTEVGLWDAvKDRLGDSPFRLSGGQQQLLCLARALAVNPDVLLLDEPTR 151
Cdd:COG4170 116 IPSWtFKGKWWQRFKWRKKRAIELLHRVGIKDH-KDIMNSYPHELTEGECQKVMIAMAIANQPRLLIADEPTN 187
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
133-152 |
2.90e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 39.88 E-value: 2.90e-04
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
114-150 |
3.60e-04 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 39.14 E-value: 3.60e-04
10 20 30
....*....|....*....|....*....|....*..
gi 2014669168 114 DRLGDSPFRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:PRK11701 143 ARIDDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPT 179
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
123-151 |
5.84e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 39.00 E-value: 5.84e-04
10 20
....*....|....*....|....*....
gi 2014669168 123 LSGGQQQLLCLARALAVNPDVLLLDEPTR 151
Cdd:PRK09700 410 LSGGNQQKVLISKWLCCCPEVIIFDEPTR 438
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1-150 |
6.91e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 38.57 E-value: 6.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLrTLnrmndkVSGFR--HSGDV-LLGGRtiFADRDlmeFRRSVG-----MlfqrP--- 69
Cdd:NF033858 22 LDIPAGCMVGLIGPDGVGKSSLL-SL------IAGARkiQQGRVeVLGGD--MADAR---HRRAVCpriayM----Pqgl 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 70 --NPFP-MSIMDNV--VAGVRAHKMAPRkqfksvaEARLTEvgLWDAVkdrlGDSPFR------LSGGQQQLLCLARALA 138
Cdd:NF033858 86 gkNLYPtLSVFENLdfFGRLFGQDAAER-------RRRIDE--LLRAT----GLAPFAdrpagkLSGGMKQKLGLCCALI 152
|
170
....*....|..
gi 2014669168 139 VNPDVLLLDEPT 150
Cdd:NF033858 153 HDPDLLILDEPT 164
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
122-151 |
7.01e-04 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 38.56 E-value: 7.01e-04
10 20 30
....*....|....*....|....*....|
gi 2014669168 122 RLSGGQQQLLCLARALAVNPDVLLLDEPTR 151
Cdd:PRK09544 120 KLSGGETQRVLLARALLNRPQLLVLDEPTQ 149
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
7-150 |
1.02e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 38.17 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 7 SVTTLLGPTGSGKTTFLRTLNRMNDKvsgfrHSGDVLLGGRTIFADRDLMEFRRSVGMLFQRPNPF-PMSIMDNVVAGVR 85
Cdd:PRK10982 25 SIHALMGENGAGKSTLLKCLFGIYQK-----DSGSILFQGKEIDFKSSKEALENGISMVHQELNLVlQRSVMDNMWLGRY 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2014669168 86 AHK--MAPRKQFKSVAEARLTEVGLWDAVKDRLGDspfrLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:PRK10982 100 PTKgmFVDQDKMYRDTKAIFDELDIDIDPRAKVAT----LSVSQMQMIEIAKAFSYNAKIVIMDEPT 162
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
11-150 |
1.74e-03 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 37.47 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 11 LLGPTGSGKTTFLRTLNRMNDkvSGFRHSGDvllggRTIFADRDLM-----EFRRSVG----MLFQRP----NPfPMSIM 77
Cdd:PRK15093 38 LVGESGSGKSLIAKAICGVTK--DNWRVTAD-----RMRFDDIDLLrlsprERRKLVGhnvsMIFQEPqsclDP-SERVG 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2014669168 78 DNVVAGVRA--HKMAPRKQF---KSVAEARLTEVGLWDAvKDRLGDSPFRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:PRK15093 110 RQLMQNIPGwtYKGRWWQRFgwrKRRAIELLHRVGIKDH-KDAMRSFPYELTEGECQKVMIAIALANQPRLLIADEPT 186
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
8-150 |
1.84e-03 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 36.99 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 8 VTTLLGPTGSGKT-TFLRTLNRMNDKVSgfRHSGDVLLGGRTIFADrdlmEFR-RSVGMLFQRP----NPFpMSIMDNVV 81
Cdd:PRK10418 31 VLALVGGSGSGKSlTCAAALGILPAGVR--QTAGRVLLDGKPVAPC----ALRgRKIATIMQNPrsafNPL-HTMHTHAR 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 82 AGVRAHKMAPRKQfksVAEARLTEVGLWDAvkDRLGDS-PFRLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:PRK10418 104 ETCLALGKPADDA---TLTAALEAVGLENA--ARVLKLyPFEMSGGMLQRMMIALALLCEAPFIIADEPT 168
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
114-152 |
2.09e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 37.46 E-value: 2.09e-03
10 20 30
....*....|....*....|....*....|....*....
gi 2014669168 114 DRLGDSPFRLSGGQQQLLCLARALAVNPDVLLLDEPTRH 152
Cdd:PRK10636 422 DKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNH 460
|
|
| KaiC-like |
cd01124 |
Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most studied in cyanobacteria. ... |
3-22 |
2.26e-03 |
|
Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most studied in cyanobacteria. KaiC, an autokinase, autophosphatase, and ATPase, is part of the core oscillator, composed of three proteins: KaiA, KaiB, and KaiC. The circadian oscillation is regulated via KaiC phosphorylation.
Pssm-ID: 410869 [Multi-domain] Cd Length: 222 Bit Score: 36.86 E-value: 2.26e-03
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1-148 |
2.57e-03 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 36.69 E-value: 2.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLRTL-NRMNDKVSgfrhsgdvllGGRTIFADRDLMEFR------RSVGMLFQRP---- 69
Cdd:PRK09580 22 LEVRPGEVHAIMGPNGSGKSTLSATLaGREDYEVT----------GGTVEFKGKDLLELSpedragEGIFMAFQYPveip 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 70 ---NPFPMSIMDNVVAGVRAHKMAPRKQFKSVAEARLTEVGLWDAVKDRLGDSPFrlSGGQQQLLCLARALAVNPDVLLL 146
Cdd:PRK09580 92 gvsNQFFLQTALNAVRSYRGQEPLDRFDFQDLMEEKIALLKMPEDLLTRSVNVGF--SGGEKKRNDILQMAVLEPELCIL 169
|
..
gi 2014669168 147 DE 148
Cdd:PRK09580 170 DE 171
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
124-152 |
2.62e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 37.07 E-value: 2.62e-03
10 20
....*....|....*....|....*....
gi 2014669168 124 SGGQQQLLCLARALAVNPDVLLLDEPTRH 152
Cdd:PRK10636 151 SGGWRMRLNLAQALICRSDLLLLDEPTNH 179
|
|
| ClpX |
COG1219 |
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ... |
11-29 |
4.11e-03 |
|
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440832 [Multi-domain] Cd Length: 409 Bit Score: 36.18 E-value: 4.11e-03
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
6-152 |
4.89e-03 |
|
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: 35.43 E-value: 4.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 6 RSVTTLLGPTGSGKTTFLRTLNRMNDKvsgfrhsgdvllggrtifadrdlmefrrsvgmlfqrpnpfpmsimdnvvagvr 85
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGP----------------------------------------------------- 28
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2014669168 86 ahkmaPRKQFKSVAEARLTEVGLWDAVKDRLGDSPFRLSGGQQQLLCLARALAVNPDVLLLDEPTRH 152
Cdd:smart00382 29 -----PGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSL 90
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
1-149 |
5.16e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 36.25 E-value: 5.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2014669168 1 LDFPARSVTTLLGPTGSGKTTFLrtlnrmndkvsgfrhsgDVLLGGRTIFADRDLMeFRRSVGMLFQRPNPFPMSIMDNV 80
Cdd:PLN03130 638 LDVPVGSLVAIVGSTGEGKTSLI-----------------SAMLGELPPRSDASVV-IRGTVAYVPQVSWIFNATVRDNI 699
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2014669168 81 VAGV--------RA-HKMAPRKQFKSVAEARLTEVGlwdavkdrlgDSPFRLSGGQQQLLCLARALAVNPDVLLLDEP 149
Cdd:PLN03130 700 LFGSpfdperyeRAiDVTALQHDLDLLPGGDLTEIG----------ERGVNISGGQKQRVSMARAVYSNSDVYIFDDP 767
|
|
| RAD55 |
COG0467 |
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms]; |
3-22 |
5.58e-03 |
|
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
Pssm-ID: 440235 [Multi-domain] Cd Length: 221 Bit Score: 35.66 E-value: 5.58e-03
|
| clpX |
PRK05342 |
ATP-dependent Clp protease ATP-binding subunit ClpX; |
11-29 |
5.78e-03 |
|
ATP-dependent Clp protease ATP-binding subunit ClpX;
Pssm-ID: 235422 [Multi-domain] Cd Length: 412 Bit Score: 35.90 E-value: 5.78e-03
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
123-150 |
6.06e-03 |
|
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: 36.07 E-value: 6.06e-03
10 20
....*....|....*....|....*...
gi 2014669168 123 LSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:TIGR03719 444 LSGGERNRVHLAKTLKSGGNVLLLDEPT 471
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
99-150 |
6.91e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 35.54 E-value: 6.91e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2014669168 99 AEARLTEVGLWDAVKDRLGDspfrLSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:NF040905 120 ARELLAKVGLDESPDTLVTD----IGVGKQQLVEIAKALSKDVKLLILDEPT 167
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
108-152 |
8.45e-03 |
|
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: 35.53 E-value: 8.45e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2014669168 108 LWDAVKDRLGDSPFR-------------------LSGGQQQLLCLARALAVNPDVLLLDEPTRH 152
Cdd:COG1245 422 LRSANTDDFGSSYYKteiikplgleklldknvkdLSGGELQRVAIAACLSRDADLYLLDEPSAH 485
|
|
| PulE |
COG2804 |
Type II secretory pathway ATPase GspE/PulE or T4P pilus assembly pathway ATPase PilB [Cell ... |
8-34 |
8.81e-03 |
|
Type II secretory pathway ATPase GspE/PulE or T4P pilus assembly pathway ATPase PilB [Cell motility, Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 442055 [Multi-domain] Cd Length: 561 Bit Score: 35.55 E-value: 8.81e-03
10 20 30
....*....|....*....|....*....|.
gi 2014669168 8 VTtllGPTGSGKTT----FLRTLNRMNDKVS 34
Cdd:COG2804 318 VT---GPTGSGKTTtlyaALNELNTPERNII 345
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
123-150 |
9.09e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 35.48 E-value: 9.09e-03
10 20
....*....|....*....|....*...
gi 2014669168 123 LSGGQQQLLCLARALAVNPDVLLLDEPT 150
Cdd:PRK11819 446 LSGGERNRLHLAKTLKQGGNVLLLDEPT 473
|
|
| |
