|
Name |
Accession |
Description |
Interval |
E-value |
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
16-212 |
5.81e-64 |
|
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: 198.33 E-value: 5.81e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 16 GKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNWKQAKAyIQKDIIYLHQQP--YLFDA 93
Cdd:COG1122 13 GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRE-LRRKVGLVFQNPddQLFAP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 94 SVTDNIAYGLYRSGERKSNVHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQ 173
Cdd:COG1122 92 TVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRR 171
|
170 180 190
....*....|....*....|....*....|....*....
gi 504819384 174 QTAKLLQRLKDEGVTIMISSHEAHTVEHIADHHIHIEHG 212
Cdd:COG1122 172 ELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDG 210
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
25-212 |
6.40e-57 |
|
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: 179.97 E-value: 6.40e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 25 LDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNWKQAKAYIQKdIIYLHQQP--YLFDASVTDNIAYG 102
Cdd:cd03225 22 LTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRK-VGLVFQNPddQFFGPTVEEEVAFG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 103 LYRSGERKSNVHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQQTAKLLQRL 182
Cdd:cd03225 101 LENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKL 180
|
170 180 190
....*....|....*....|....*....|
gi 504819384 183 KDEGVTIMISSHEAHTVEHIADHHIHIEHG 212
Cdd:cd03225 181 KAEGKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-212 |
9.75e-54 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 172.97 E-value: 9.75e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 1 MSTLVSYKNLAITLSGKLVL-NIkHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNWKQAK-AYI- 77
Cdd:COG1121 3 MMPAIELENLTVSYGGRPVLeDV-SLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRRiGYVp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 78 QKDIIYLHqqpylFDASVTDNIAYGLYRS----GERKSNVHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARIL 153
Cdd:COG1121 82 QRAEVDWD-----FPITVRDVVLMGRYGRrglfRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQ 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 504819384 154 SPRLLLLDEPTASMDSTAKQQTAKLLQRLKDEGVTIMISSHEAHTVEHIADHHIHIEHG 212
Cdd:COG1121 157 DPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRG 215
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
6-213 |
3.35e-52 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 167.69 E-value: 3.35e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 6 SYKNLAITLSGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNWKQAKAYIQKdIIYLH 85
Cdd:COG4619 2 ELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQ-VAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 86 QQPYLFDASVTDNIAYGlYRSGERKSNvHKKVTQALDWADLSH-LAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPT 164
Cdd:COG4619 81 QEPALWGGTVRDNLPFP-FQLRERKFD-RERALELLERLGLPPdILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 504819384 165 ASMDSTAKQQTAKLLQRL-KDEGVTIMISSHEAHTVEHIADHHIHIEHGN 213
Cdd:COG4619 159 SALDPENTRRVEELLREYlAEEGRAVLWVSHDPEQIERVADRVLTLEAGR 208
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
8-212 |
3.16e-49 |
|
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: 161.18 E-value: 3.16e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 8 KNLAITLSGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLnwKQAKAYIQKDIIYLHQQ 87
Cdd:COG4555 5 ENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDV--RKEPREARRQIGVLPDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 88 PYLFDA-SVTDNIAY--GLYrsGERKSNVHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPT 164
Cdd:COG4555 83 RGLYDRlTVRENIRYfaELY--GLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPT 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 504819384 165 ASMDSTAKQQTAKLLQRLKDEGVTIMISSHEAHTVEHIADHHIHIEHG 212
Cdd:COG4555 161 NGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKG 208
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
25-212 |
6.80e-49 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 160.23 E-value: 6.80e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 25 LDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLnWKQAKAyIQKDIIYLHQQPYLFDA-SVTDNIAY-- 101
Cdd:COG1131 21 LTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDV-ARDPAE-VRRRIGYVPQEPALYPDlTVRENLRFfa 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 102 GLYrsGERKSNVHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQQTAKLLQR 181
Cdd:COG1131 99 RLY--GLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRE 176
|
170 180 190
....*....|....*....|....*....|.
gi 504819384 182 LKDEGVTIMISSHEAHTVEHIADHHIHIEHG 212
Cdd:COG1131 177 LAAEGKTVLLSTHYLEEAERLCDRVAIIDKG 207
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
8-212 |
3.84e-47 |
|
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: 155.00 E-value: 3.84e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 8 KNLAITLSGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGltlnwkQAKAYIQKDIIYLHQQ 87
Cdd:cd03235 3 EDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFG------KPLEKERKRIGYVPQR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 88 PYL---FDASVTDNIAYGLYRS---GERKSNVHK-KVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLL 160
Cdd:cd03235 77 RSIdrdFPISVRDVVLMGLYGHkglFRRLSKADKaKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 504819384 161 DEPTASMDSTAKQQTAKLLQRLKDEGVTIMISSHEAHTVEHIADHHIHIEHG 212
Cdd:cd03235 157 DEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLNRT 208
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-212 |
7.86e-47 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 154.82 E-value: 7.86e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 1 MSTLVSYKNLAITL-SGKL---VLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQG---LTLNWKQA 73
Cdd:COG1136 1 MSPLLELRNLTKSYgTGEGevtALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGqdiSSLSEREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 74 KAYIQKDIIYLHQQPYLFDA-SVTDNIAYGLYRSGERKSNVHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARI 152
Cdd:COG1136 81 ARLRRRHIGFVFQFFNLLPElTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504819384 153 LSPRLLLLDEPTASMDSTAKQQTAKLLQRL-KDEGVTIMISSHEAHTVEHiADHHIHIEHG 212
Cdd:COG1136 161 NRPKLILADEPTGNLDSKTGEEVLELLRELnRELGTTIVMVTHDPELAAR-ADRVIRLRDG 220
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
8-211 |
2.16e-45 |
|
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: 150.32 E-value: 2.16e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 8 KNLAITLSGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLnwKQAKAYIQKDIIYLHQQ 87
Cdd:COG4133 6 ENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPI--RDAREDYRRRLAYLGHA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 88 PYLFDA-SVTDNIA-----YGLYRSGERksnvhkkVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLD 161
Cdd:COG4133 84 DGLKPElTVRENLRfwaalYGLRADREA-------IDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 504819384 162 EPTASMDSTAKQQTAKLLQRLKDEGVTIMISSHeaHTVEHIADHHIHIEH 211
Cdd:COG4133 157 EPFTALDAAGVALLAELIAAHLARGGAVLLTTH--QPLELAAARVLDLGD 204
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
25-212 |
1.14e-44 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 149.05 E-value: 1.14e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 25 LDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGL---TLNWKQAkAYIQKDIIYLHQ-QPYLFDASVTDNIA 100
Cdd:COG2884 23 LEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQdlsRLKRREI-PYLRRRIGVVFQdFRLLPDRTVYENVA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 101 YGLYRSGERKSNVHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQQTAKLLQ 180
Cdd:COG2884 102 LPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLE 181
|
170 180 190
....*....|....*....|....*....|..
gi 504819384 181 RLKDEGVTIMISSHEAHTVEHIADHHIHIEHG 212
Cdd:COG2884 182 EINRRGTTVLIATHDLELVDRMPKRVLELEDG 213
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
19-213 |
7.67e-44 |
|
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: 146.87 E-value: 7.67e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 19 VLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQG---LTLNWKQAKAYIQKDIIYLHQQPYLF-DAS 94
Cdd:cd03255 19 ALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGtdiSKLSEKELAAFRRRHIGFVFQSFNLLpDLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 95 VTDNIAYGLYRSGERKSNVHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQQ 174
Cdd:cd03255 99 ALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLDSETGKE 178
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 504819384 175 TAKLLQRL-KDEGVTIMISSHEaHTVEHIADHHIHIEHGN 213
Cdd:cd03255 179 VMELLRELnKEAGTTIVVVTHD-PELAEYADRIIELRDGK 217
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
19-196 |
2.02e-42 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 142.18 E-value: 2.02e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 19 VLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNW-KQAKAYIQKDIIYLHQQP--YLFDASV 95
Cdd:TIGR01166 7 VLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDYsRKGLLERRQRVGLVFQDPddQLFAADV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 96 TDNIAYGLYRSGERKSNVHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQQT 175
Cdd:TIGR01166 87 DQDVAFGPLNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPAGREQM 166
|
170 180
....*....|....*....|.
gi 504819384 176 AKLLQRLKDEGVTIMISSHEA 196
Cdd:TIGR01166 167 LAILRRLRAEGMTVVISTHDV 187
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
8-215 |
2.35e-42 |
|
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: 142.66 E-value: 2.35e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 8 KNLAITLSGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLnwkQAKAYIQKDIIYLHQQ 87
Cdd:cd03259 4 KGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV---TGVPPERRNIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 88 PYLFD-ASVTDNIAYGLYRSGERKSNVHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTAS 166
Cdd:cd03259 81 YALFPhLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 504819384 167 MDSTAKQQTAKLLQRL-KDEGVTIMISSH---EAHTvehIADHHIHIEHGNAL 215
Cdd:cd03259 161 LDAKLREELREELKELqRELGITTIYVTHdqeEALA---LADRIAVMNEGRIV 210
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-205 |
2.69e-41 |
|
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: 140.89 E-value: 2.69e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 1 MSTLVSYKNLAITLSGKLVL-NIkHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQG---LTLNWKQAKAy 76
Cdd:COG1127 2 SEPMIEVRNLTKSFGDRVVLdGV-SLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGqdiTGLSEKELYE- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 77 IQKDIIYLHQQPYLFDA-SVTDNIAYGLYRSGE-RKSNVHKKVTQALDWADLSHLAHR-PAkQLSGGEKQRVALTRARIL 153
Cdd:COG1127 80 LRRRIGMLFQGGALFDSlTVFENVAFPLREHTDlSEAEIRELVLEKLELVGLPGAADKmPS-ELSGGMRKRVALARALAL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 504819384 154 SPRLLLLDEPTASMDSTAKQQTAKLLQRLKDE-GVTIMISSHEAHTVEHIADH 205
Cdd:COG1127 159 DPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADR 211
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
5-205 |
3.38e-41 |
|
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: 140.33 E-value: 3.38e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 5 VSYKNLAITLSGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQG---LTLNWKQAKAyIQKDI 81
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGediSGLSEAELYR-LRRRM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 82 IYLHQQPYLFDA-SVTDNIAYGLYRSGER-KSNVHKKVTQALDWADLSHLAH-RPAkQLSGGEKQRVALTRARILSPRLL 158
Cdd:cd03261 80 GMLFQSGALFDSlTVFENVAFPLREHTRLsEEEIREIVLEKLEAVGLRGAEDlYPA-ELSGGMKKRVALARALALDPELL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 504819384 159 LLDEPTASMDSTAKQQTAKLLQRLKDE-GVTIMISSHEAHTVEHIADH 205
Cdd:cd03261 159 LYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADR 206
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
8-195 |
4.04e-41 |
|
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: 140.95 E-value: 4.04e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 8 KNLAITLSGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTL-NWKQAKayIQKDIIYLHQ 86
Cdd:COG1120 5 ENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLaSLSRRE--LARRIAYVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 87 QPYL-FDASVTDNIAYGLY----RSGERKSNVHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLD 161
Cdd:COG1120 83 EPPApFGLTVRELVALGRYphlgLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLLD 162
|
170 180 190
....*....|....*....|....*....|....*
gi 504819384 162 EPTASMDSTAKQQTAKLLQRL-KDEGVTIMISSHE 195
Cdd:COG1120 163 EPTSHLDLAHQLEVLELLRRLaRERGRTVVMVLHD 197
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
25-205 |
8.17e-41 |
|
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: 145.82 E-value: 8.17e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 25 LDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQG---LTLNWKQAKAYiQKDIIYLHQQPYL-FDA--SVTDN 98
Cdd:COG1123 286 LTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGkdlTKLSRRSLREL-RRRVQMVFQDPYSsLNPrmTVGDI 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 99 IAYGLYRSGE-RKSNVHKKVTQALDWADLS-HLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQQTA 176
Cdd:COG1123 365 IAEPLRLHGLlSRAERRERVAELLERVGLPpDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQIL 444
|
170 180 190
....*....|....*....|....*....|
gi 504819384 177 KLLQRLKDE-GVTIMISSHEAHTVEHIADH 205
Cdd:COG1123 445 NLLRDLQRElGLTYLFISHDLAVVRYIADR 474
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
25-212 |
1.33e-40 |
|
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: 142.17 E-value: 1.33e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 25 LDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNWKQAKAYI---QKDIIYLHQQPYLF-DASVTDNIA 100
Cdd:TIGR02142 18 FTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLppeKRRIGYVFQEARLFpHLSVRGNLR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 101 YGLYRS-GERKSNVHKKVTQALDwadLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQQTAKLL 179
Cdd:TIGR02142 98 YGMKRArPSERRISFERVIELLG---IGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYL 174
|
170 180 190
....*....|....*....|....*....|....
gi 504819384 180 QRLKDE-GVTIMISSHEAHTVEHIADHHIHIEHG 212
Cdd:TIGR02142 175 ERLHAEfGIPILYVSHSLQEVLRLADRVVVLEDG 208
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
10-212 |
2.97e-40 |
|
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: 141.39 E-value: 2.97e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 10 LAITLS-GKLVLNIKhLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTlnWKQAKAYI-----QKDIIY 83
Cdd:COG4148 5 VDFRLRrGGFTLDVD-FTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEV--LQDSARGIflpphRRRIGY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 84 LHQQPYLFD-ASVTDNIAYGLYRSGERKSNVHkkVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDE 162
Cdd:COG4148 82 VFQEARLFPhLSVRGNLLYGRKRAPRAERRIS--FDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 504819384 163 PTASMDSTAKQQTAKLLQRLKDE-GVTIMISSHEAHTVEHIADHHIHIEHG 212
Cdd:COG4148 160 PLAALDLARKAEILPYLERLRDElDIPILYVSHSLDEVARLADHVVLLEQG 210
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
24-212 |
3.12e-40 |
|
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: 137.71 E-value: 3.12e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 24 HLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNWKQAKAY--IQKDIIYLHQQPYLFDA-SVTDNIA 100
Cdd:cd03258 25 SLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELrkARRRIGMIFQHFNLLSSrTVFENVA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 101 YGLYRSGERKSNVHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQQTAKLLQ 180
Cdd:cd03258 105 LPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLR 184
|
170 180 190
....*....|....*....|....*....|...
gi 504819384 181 RLKDE-GVTIMISSHEAHTVEHIADHHIHIEHG 212
Cdd:cd03258 185 DINRElGLTIVLITHEMEVVKRICDRVAVMEKG 217
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
15-212 |
4.35e-40 |
|
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: 135.59 E-value: 4.35e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 15 SGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNwKQAKAYIQKDIIYLHQQPYLFDAS 94
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLR-DLDLESLRKNIAYVPQDPFLFSGT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 95 VTDNIayglyrsgerksnvhkkvtqaldwadlshlahrpakqLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQQ 174
Cdd:cd03228 92 IRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEAL 134
|
170 180 190
....*....|....*....|....*....|....*...
gi 504819384 175 TAKLLQRLKDEGVTIMIsSHEAHTVEHiADHHIHIEHG 212
Cdd:cd03228 135 ILEALRALAKGKTVIVI-AHRLSTIRD-ADRIIVLDDG 170
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
24-204 |
5.52e-40 |
|
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: 136.93 E-value: 5.52e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 24 HLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLK-----PDSASINYQGLTLNwkqakaYIQKDIIYLH-------QQPYLF 91
Cdd:cd03260 20 SLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIY------DLDVDVLELRrrvgmvfQKPNPF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 92 DASVTDNIAYGLYRSGER-KSNVHKKVTQALDWADLSHLAHRP--AKQLSGGEKQRVALTRARILSPRLLLLDEPTASMD 168
Cdd:cd03260 94 PGSIYDNVAYGLRLHGIKlKEELDERVEEALRKAALWDEVKDRlhALGLSGGQQQRLCLARALANEPEVLLLDEPTSALD 173
|
170 180 190
....*....|....*....|....*....|....*.
gi 504819384 169 STAKQQTAKLLQRLKDEgVTIMISSHEAHTVEHIAD 204
Cdd:cd03260 174 PISTAKIEELIAELKKE-YTIVIVTHNMQQAARVAD 208
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
8-212 |
3.06e-39 |
|
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: 133.29 E-value: 3.06e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 8 KNLAITLSGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNWKQAKayIQKDIIYLHQQ 87
Cdd:cd03230 4 RNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEE--VKRRIGYLPEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 88 PYLFDA-SVTDNIayglyrsgerksnvhkkvtqaldwadlshlahrpakQLSGGEKQRVALTRARILSPRLLLLDEPTAS 166
Cdd:cd03230 82 PSLYENlTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTSG 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 504819384 167 MDSTAKQQTAKLLQRLKDEGVTIMISSHEAHTVEHIADHHIHIEHG 212
Cdd:cd03230 126 LDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNG 171
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
25-212 |
7.36e-39 |
|
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: 141.05 E-value: 7.36e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 25 LDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNWKQAKAyIQKDIIYLHQQPYLFDASVTDNIAygLY 104
Cdd:COG4988 358 LTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPAS-WRRQIAWVPQNPYLFAGTIRENLR--LG 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 105 R---SGERksnvhkkVTQALDWADLSHLAHR-P----------AKQLSGGEKQRVALTRArILSPR-LLLLDEPTASMDS 169
Cdd:COG4988 435 RpdaSDEE-------LEAALEAAGLDEFVAAlPdgldtplgegGRGLSGGQAQRLALARA-LLRDApLLLLDEPTAHLDA 506
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 504819384 170 TAKQQTAKLLQRLKdEGVTIMISSHEAHTVEHiADHHIHIEHG 212
Cdd:COG4988 507 ETEAEILQALRRLA-KGRTVILITHRLALLAQ-ADRILVLDDG 547
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
25-205 |
9.58e-39 |
|
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: 134.10 E-value: 9.58e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 25 LDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNWKQAKAYIQKDIIYLHQQPYLF-DASVTDNI---- 99
Cdd:cd03219 21 FSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIGRTFQIPRLFpELTVLENVmvaa 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 100 ------AYGLYRSGERKSNVHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQ 173
Cdd:cd03219 101 qartgsGLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETE 180
|
170 180 190
....*....|....*....|....*....|..
gi 504819384 174 QTAKLLQRLKDEGVTIMISSHEAHTVEHIADH 205
Cdd:cd03219 181 ELAELIRELRERGITVLLVEHDMDVVMSLADR 212
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
25-212 |
1.87e-38 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 132.76 E-value: 1.87e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 25 LDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQG---LTLNWKQAKAYIQK-DIIYlhqQPY--LFDASVTDN 98
Cdd:TIGR02673 23 LHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGedvNRLRGRQLPLLRRRiGVVF---QDFrlLPDRTVYEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 99 IAYGLYRSGERKSNVHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQQTAKL 178
Cdd:TIGR02673 100 VALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLADEPTGNLDPDLSERILDL 179
|
170 180 190
....*....|....*....|....*....|....
gi 504819384 179 LQRLKDEGVTIMISSHEAHTVEHIADHHIHIEHG 212
Cdd:TIGR02673 180 LKRLNKRGTTVIVATHDLSLVDRVAHRVIILDDG 213
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-196 |
7.42e-38 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 134.84 E-value: 7.42e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 1 MSTLVSYKNLAITLSGKLVLNIKHLDIPAHQ-CTLLtGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNWKQAKayiQK 79
Cdd:COG3842 2 AMPALELENVSKRYGDVTALDDVSLSIEPGEfVALL-GPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPE---KR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 80 DIIYLHQQ----PYLfdaSVTDNIAYGLYRSGERKSNVHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSP 155
Cdd:COG3842 78 NVGMVFQDyalfPHL---TVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEP 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 504819384 156 RLLLLDEPTASMDSTAKQQTAKLLQRL-KDEGVTIMISSH---EA 196
Cdd:COG3842 155 RVLLLDEPLSALDAKLREEMREELRRLqRELGITFIYVTHdqeEA 199
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
25-196 |
1.33e-37 |
|
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: 130.67 E-value: 1.33e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 25 LDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGltlnwkQAKAYIQKDIIYLHQQPYLFD-ASVTDNIAYGL 103
Cdd:cd03293 25 LSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDG------EPVTGPGPDRGYVFQQDALLPwLTVLDNVALGL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 104 YRSGERKSNVHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDStakqQTAKLLQRL- 182
Cdd:cd03293 99 ELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDA----LTREQLQEEl 174
|
170 180
....*....|....*....|.
gi 504819384 183 ----KDEGVTIMISSH---EA 196
Cdd:cd03293 175 ldiwRETGKTVLLVTHdidEA 195
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
15-194 |
1.48e-37 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 131.33 E-value: 1.48e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 15 SGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQG---LTLNWKQAKAyIQKDIIYLHQQPYLF 91
Cdd:COG3638 14 GGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGqdvTALRGRALRR-LRRRIGMIFQQFNLV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 92 D-ASVTDNI-----AY--------GLYRSGERKsnvhkKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSPRL 157
Cdd:COG3638 93 PrLSVLTNVlagrlGRtstwrsllGLFPPEDRE-----RALEALERVGLADKAYQRADQLSGGQQQRVAIARALVQEPKL 167
|
170 180 190
....*....|....*....|....*....|....*...
gi 504819384 158 LLLDEPTASMDSTAKQQTAKLLQRL-KDEGVTIMISSH 194
Cdd:COG3638 168 ILADEPVASLDPKTARQVMDLLRRIaREDGITVVVNLH 205
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
25-196 |
2.11e-37 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 131.37 E-value: 2.11e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 25 LDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNWKQAkayiqkDIIYLHQQPYLFD-ASVTDNIAYGL 103
Cdd:COG1116 32 LTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP------DRGVVFQEPALLPwLTVLDNVALGL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 104 YRSGERKSNVHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDStakqQTAKLLQRL- 182
Cdd:COG1116 106 ELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLLMDEPFGALDA----LTRERLQDEl 181
|
170 180
....*....|....*....|.
gi 504819384 183 ----KDEGVTIMISSH---EA 196
Cdd:COG1116 182 lrlwQETGKTVLFVTHdvdEA 202
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
6-212 |
4.02e-37 |
|
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: 127.36 E-value: 4.02e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 6 SYKNLAITLSGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNWKQAKAYiQKDIIYLH 85
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEEL-RRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 86 QqpylfdasvtdniayglyrsgerksnvhkkvtqaldwadlshlahrpakqLSGGEKQRVALTRARILSPRLLLLDEPTA 165
Cdd:cd00267 80 Q--------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTS 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 504819384 166 SMDSTAKQQTAKLLQRLKDEGVTIMISSHEAHTVEHIADHHIHIEHG 212
Cdd:cd00267 110 GLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
8-189 |
4.13e-37 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 130.62 E-value: 4.13e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 8 KNLAITLSGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLN----WKQAK--AYiqkdi 81
Cdd:COG4559 5 ENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAawspWELARrrAV----- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 82 iyLHQQPYL-FDASVTDNIAYGLYRSGERKSNVHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALtrARIL------- 153
Cdd:COG4559 80 --LPQHSSLaFPFTVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQL--ARVLaqlwepv 155
|
170 180 190
....*....|....*....|....*....|....*...
gi 504819384 154 --SPRLLLLDEPTASMDSTAKQQTAKLLQRLKDEGVTI 189
Cdd:COG4559 156 dgGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGV 193
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
24-212 |
6.13e-37 |
|
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: 129.92 E-value: 6.13e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 24 HLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNWKQAKAYiQKDIIYLHQQPYL-FDA--SVTDNIA 100
Cdd:COG1124 25 SLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAF-RRRVQMVFQDPYAsLHPrhTVDRILA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 101 YGLYRSGERksNVHKKVTQALDWADL-SHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQQTAKLL 179
Cdd:COG1124 104 EPLRIHGLP--DREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILEPELLLLDEPTSALDVSVQAEILNLL 181
|
170 180 190
....*....|....*....|....*....|....
gi 504819384 180 QRLKDE-GVTIMISSHEAHTVEHIADHHIHIEHG 212
Cdd:COG1124 182 KDLREErGLTYLFVSHDLAVVAHLCDRVAVMQNG 215
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
32-203 |
8.77e-37 |
|
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: 128.99 E-value: 8.77e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 32 CTLLtGQNGSGKTTLLKIMSGLLKPDSASINYQGLTL-NWKQAKayiqKDIIYLHQQPYLF-DASVTDNIAYGLYRSGER 109
Cdd:cd03299 28 FVIL-GPTGSGKSVLLETIAGFIKPDSGKILLNGKDItNLPPEK----RDISYVPQNYALFpHMTVYKNIAYGLKKRKVD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 110 KSNVHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQQTAKLLQRLKDE-GVT 188
Cdd:cd03299 103 KKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEfGVT 182
|
170
....*....|....*
gi 504819384 189 IMissHEAHTVEHIA 203
Cdd:cd03299 183 VL---HVTHDFEEAW 194
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
15-212 |
1.04e-36 |
|
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: 136.12 E-value: 1.04e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 15 SGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNwKQAKAYIQKDIIYLHQQPYLFDAS 94
Cdd:COG2274 486 DSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLR-QIDPASLRRQIGVVLQDVFLFSGT 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 95 VTDNIAYGLYRSGErksnvhKKVTQALDWADLSH-LAHRP----------AKQLSGGEKQRVALTRARILSPRLLLLDEP 163
Cdd:COG2274 565 IRENITLGDPDATD------EEIIEAARLAGLHDfIEALPmgydtvvgegGSNLSGGQRQRLAIARALLRNPRILILDEA 638
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 504819384 164 TASMDSTAKQQTAKLLQRLKdEGVTIMISSHEAHTVEHiADHHIHIEHG 212
Cdd:COG2274 639 TSALDAETEAIILENLRRLL-KGRTVIIIAHRLSTIRL-ADRIIVLDKG 685
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
20-165 |
1.22e-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: 126.22 E-value: 1.22e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 20 LNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNWKQAKAYiQKDIIYLHQQPYLF-DASVTDN 98
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSL-RKEIGYVFQDPQLFpRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504819384 99 IAYGLYRSGERKSNVHKKVTQALDWADLSHLAHRPA----KQLSGGEKQRVALTRARILSPRLLLLDEPTA 165
Cdd:pfam00005 80 LRLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVgerpGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
4-205 |
2.07e-36 |
|
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: 128.01 E-value: 2.07e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 4 LVSYKNLAITLSG-----KLVLNIkHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQG--LTLNWKQAKAY 76
Cdd:cd03257 1 LLEVKNLSVSFPTgggsvKALDDV-SFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGkdLLKLSRRLRKI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 77 IQKDIIYLHQQPYL-FDASVT--DNIAYGLYRSGERKSNVHKKVTQALDWADL---SHLAHRPAKQLSGGEKQRVALTRA 150
Cdd:cd03257 80 RRKEIQMVFQDPMSsLNPRMTigEQIAEPLRIHGKLSKKEARKEAVLLLLVGVglpEEVLNRYPHELSGGQRQRVAIARA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 504819384 151 RILSPRLLLLDEPTASMDSTAKQQTAKLLQRLKDE-GVTIMISSHEAHTVEHIADH 205
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADR 215
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
8-213 |
2.25e-36 |
|
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: 126.40 E-value: 2.25e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 8 KNLAITLSGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNWKQAKAYIQKdiiylhqq 87
Cdd:cd03214 3 ENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARK-------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 88 pylfdasvtdnIAYglyrsgerksnvhkkVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASM 167
Cdd:cd03214 75 -----------IAY---------------VPQALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHL 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 504819384 168 DSTAKQQTAKLLQRLKDE-GVTIMISSHEAHTVEHIADHHIHIEHGN 213
Cdd:cd03214 129 DIAHQIELLELLRRLARErGKTVVMVLHDLNLAARYADRVILLKDGR 175
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-212 |
2.54e-36 |
|
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: 133.49 E-value: 2.54e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 1 MSTLVSYKNLAITLSGKLVLNIKH--LDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPD---SASINYQGLTLnWKQAKA 75
Cdd:COG1123 1 MTPLLEVRDLSVRYPGGDVPAVDGvsLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDL-LELSEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 76 YIQKDIIYLHQQPY--LFDASVTDNIAYGLYRSGERKSNVHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARIL 153
Cdd:COG1123 80 LRGRRIGMVFQDPMtqLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 154 SPRLLLLDEPTASMDSTAKQQTAKLLQRLKDE-GVTIMISSHEAHTVEHIADHHIHIEHG 212
Cdd:COG1123 160 DPDLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEIADRVVVMDDG 219
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
20-212 |
5.56e-36 |
|
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: 126.26 E-value: 5.56e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 20 LNIKhLDIPAhQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNWKQAKAYI---QKDIIYLHQQPYLF-DASV 95
Cdd:cd03297 15 LKID-FDLNE-EVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINLppqQRKIGLVFQQYALFpHLNV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 96 TDNIAYGLYRSGERKSNVhkKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQQT 175
Cdd:cd03297 93 RENLAFGLKRKRNREDRI--SVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQL 170
|
170 180 190
....*....|....*....|....*....|....*...
gi 504819384 176 AKLLQRLKDE-GVTIMISSHEAHTVEHIADHHIHIEHG 212
Cdd:cd03297 171 LPELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDG 208
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-205 |
1.11e-35 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 129.04 E-value: 1.11e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 1 MSTlVSYKNLAITLSGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNWKQAKayiQKD 80
Cdd:COG3839 1 MAS-LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPK---DRN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 81 IIYLHQQPYLFDA-SVTDNIAYGLYRSGERKSNVHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLL 159
Cdd:COG3839 77 IAMVFQSYALYPHmTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 504819384 160 LDEPTASMDSTAKQQT----AKLLQRLkdeGVTIMISSH---EAHTvehIADH 205
Cdd:COG3839 157 LDEPLSNLDAKLRVEMraeiKRLHRRL---GTTTIYVTHdqvEAMT---LADR 203
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
17-212 |
1.82e-35 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 128.34 E-value: 1.82e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 17 KLVLNIkHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASInyqglTLNWKQAKAYI---QKDIIYLHQQPYLF-D 92
Cdd:COG1118 16 TLLDDV-SLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRI-----VLNGRDLFTNLpprERRVGFVFQHYALFpH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 93 ASVTDNIAYGLYRSGERKSNVHKKVTQALDWADLSHLAHR-PAkQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTA 171
Cdd:COG1118 90 MTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRyPS-QLSGGQRQRVALARALAVEPEVLLLDEPFGALDAKV 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 504819384 172 KQQTAKLLQRLKDE-GVTIMISSH---EAHTVehiADHHIHIEHG 212
Cdd:COG1118 169 RKELRRWLRRLHDElGGTTVFVTHdqeEALEL---ADRVVVMNQG 210
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
8-194 |
2.70e-35 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 124.26 E-value: 2.70e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 8 KNLAITLSGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQG---LTLNWKQAKAYIQKDIIYL 84
Cdd:TIGR03608 2 KNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGqetPPLNSKKASKFRREKLGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 85 HQQPYLFDA-SVTDNIAYGLYRSGERKSNVHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEP 163
Cdd:TIGR03608 82 FQNFALIENeTVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADEP 161
|
170 180 190
....*....|....*....|....*....|.
gi 504819384 164 TASMDSTAKQQTAKLLQRLKDEGVTIMISSH 194
Cdd:TIGR03608 162 TGSLDPKNRDEVLDLLLELNDEGKTIIIVTH 192
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
25-212 |
4.72e-35 |
|
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: 124.08 E-value: 4.72e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 25 LDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNWKQAKAYIQKDIIYLHQQPYLF-DASVTDNIAYGL 103
Cdd:cd03224 21 LTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIGYVPEGRRIFpELTVEENLLLGA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 104 YRSGERKsnvhkkVTQALDWA-----DLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQQTAKL 178
Cdd:cd03224 101 YARRRAK------RKARLERVyelfpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEA 174
|
170 180 190
....*....|....*....|....*....|....
gi 504819384 179 LQRLKDEGVTIMISSHEAHTVEHIADHHIHIEHG 212
Cdd:cd03224 175 IRELRDEGVTILLVEQNARFALEIADRAYVLERG 208
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
19-215 |
4.92e-35 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 125.50 E-value: 4.92e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 19 VLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNW-KQAKAYIQKDIIYLHQQP--YLFDASV 95
Cdd:PRK13638 16 VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYsKRGLLALRQQVATVFQDPeqQIFYTDI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 96 TDNIAYGLYRSGERKSNVHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQQT 175
Cdd:PRK13638 96 DSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQM 175
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 504819384 176 AKLLQRLKDEGVTIMISSHEAHTVEHIADHHIHIEHGNAL 215
Cdd:PRK13638 176 IAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQIL 215
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
8-186 |
1.02e-34 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 124.50 E-value: 1.02e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 8 KNLAITLSGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLN----WKQAK--AYiqkdi 81
Cdd:PRK13548 6 RNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLAdwspAELARrrAV----- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 82 iyLHQQPYL-FDASVTDNIAYGLYRSGERKSNVHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALtrARIL------- 153
Cdd:PRK13548 81 --LPQHSSLsFPFTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQL--ARVLaqlwepd 156
|
170 180 190
....*....|....*....|....*....|....
gi 504819384 154 -SPRLLLLDEPTASMDSTAKQQTAKLLQRLKDEG 186
Cdd:PRK13548 157 gPPRWLLLDEPTSALDLAHQHHVLRLARQLAHER 190
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
25-212 |
1.21e-34 |
|
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: 122.90 E-value: 1.21e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 25 LDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLN--WKQAKAYIQKDI-IYLHQQPYLFDASVTDNIAY 101
Cdd:cd03292 22 ISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSdlRGRAIPYLRRKIgVVFQDFRLLPDRNVYENVAF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 102 GLYRSGERKSNVHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQQTAKLLQR 181
Cdd:cd03292 102 ALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKK 181
|
170 180 190
....*....|....*....|....*....|.
gi 504819384 182 LKDEGVTIMISSHEAHTVEHIADHHIHIEHG 212
Cdd:cd03292 182 INKAGTTVVVATHAKELVDTTRHRVIALERG 212
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
16-212 |
2.16e-34 |
|
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: 121.98 E-value: 2.16e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 16 GKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNWKQAkayiQKDIIYLHQQP--YLFDA 93
Cdd:cd03226 12 GTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKER----RKSIGYVMQDVdyQLFTD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 94 SVTDNIAYGLyrsgERKSNVHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQ 173
Cdd:cd03226 88 SVREELLLGL----KELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNME 163
|
170 180 190
....*....|....*....|....*....|....*....
gi 504819384 174 QTAKLLQRLKDEGVTIMISSHEAHTVEHIADHHIHIEHG 212
Cdd:cd03226 164 RVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANG 202
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
19-213 |
2.23e-34 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 125.97 E-value: 2.23e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 19 VLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNWKQAKayiQKDIIYLHQQPYLF-DASVTD 97
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHAR---DRKVGFVFQHYALFrHMTVFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 98 NIAYGLY----RSGERKSNVHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQ 173
Cdd:PRK10851 94 NIAFGLTvlprRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRK 173
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 504819384 174 QTAKLLQRLKDE-GVTIMISSHEAHTVEHIADHHIHIEHGN 213
Cdd:PRK10851 174 ELRRWLRQLHEElKFTSVFVTHDQEEAMEVADRVVVMSQGN 214
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
5-217 |
5.66e-34 |
|
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: 121.17 E-value: 5.66e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 5 VSYKNLAITLSGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASI-----NYQGLTLNWKQAKAYIQK 79
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEItfdgkSYQKNIEALRRIGALIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 80 DIIYlhqqPYLfdaSVTDNIAYGLYRSGERKSNVHkkvtQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLL 159
Cdd:cd03268 81 PGFY----PNL---TARENLRLLARLLGIRKKRID----EVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 504819384 160 LDEPTASMDSTAKQQTAKLLQRLKDEGVTIMISSHEAHTVEHIADHHIHIEHGNALIR 217
Cdd:cd03268 150 LDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEE 207
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
8-212 |
5.67e-34 |
|
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: 119.98 E-value: 5.67e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 8 KNLAITLSGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNWKQAKAYIQK-DIIYLHQ 86
Cdd:cd03229 4 KNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLRrRIGMVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 87 QPYLF-DASVTDNIAYGLyrsgerksnvhkkvtqaldwadlshlahrpakqlSGGEKQRVALTRARILSPRLLLLDEPTA 165
Cdd:cd03229 84 DFALFpHLTVLENIALGL----------------------------------SGGQQQRVALARALAMDPDVLLLDEPTS 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 504819384 166 SMDSTAKQQTAKLLQRLKDE-GVTIMISSHEAHTVEHIADHHIHIEHG 212
Cdd:cd03229 130 ALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
5-199 |
7.04e-34 |
|
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: 121.58 E-value: 7.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 5 VSYKNLAITLSGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGltlnwkqakayiqKDIIYL 84
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDG-------------KDITNL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 85 --HQQPY--------LF-DASVTDNIAYGLYRSGERKSNVHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARIL 153
Cdd:cd03300 68 ppHKRPVntvfqnyaLFpHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVN 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 504819384 154 SPRLLLLDEPTASMDSTAKQQTAKLLQRLKDE-GVTIMISSH---EAHTV 199
Cdd:cd03300 148 EPKVLLLDEPLGALDLKLRKDMQLELKRLQKElGITFVFVTHdqeEALTM 197
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
25-213 |
1.33e-33 |
|
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: 120.91 E-value: 1.33e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 25 LDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNWKQAKayiQKDIIYLHQQPYLF-DASVTDNIAYGL 103
Cdd:cd03296 23 LDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ---ERNVGFVFQHYALFrHMTVFDNVAFGL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 104 --YRSGER--KSNVHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQQTAKLL 179
Cdd:cd03296 100 rvKPRSERppEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWL 179
|
170 180 190
....*....|....*....|....*....|....*
gi 504819384 180 QRLKDE-GVTIMISSHEAHTVEHIADHHIHIEHGN 213
Cdd:cd03296 180 RRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGR 214
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
9-205 |
1.35e-33 |
|
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: 120.73 E-value: 1.35e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 9 NLAITLSGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNWKQAKAYIQKDIIYLHQQP 88
Cdd:cd03218 5 NLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLGIGYLPQEA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 89 YLF-DASVTDNIAYGLYRSGERKSNVHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASM 167
Cdd:cd03218 85 SIFrKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGV 164
|
170 180 190
....*....|....*....|....*....|....*...
gi 504819384 168 DSTAKQQTAKLLQRLKDEGVTIMISSHEAHTVEHIADH 205
Cdd:cd03218 165 DPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDR 202
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
24-205 |
4.30e-33 |
|
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: 120.14 E-value: 4.30e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 24 HLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGltlnwkqakayiqKDIIYL--H-----------QQPYL 90
Cdd:COG0411 24 SLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDG-------------RDITGLppHriarlgiartfQNPRL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 91 F-DASVTDNIAYGL-----------------YRSGERKsnVHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARI 152
Cdd:COG0411 91 FpELTVLENVLVAAharlgrgllaallrlprARREERE--ARERAEELLERVGLADRADEPAGNLSYGQQRRLEIARALA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 504819384 153 LSPRLLLLDEPTASMDSTAKQQTAKLLQRLKDE-GVTIMISSHEAHTVEHIADH 205
Cdd:COG0411 169 TEPKLLLLDEPAAGLNPEETEELAELIRRLRDErGITILLIEHDMDLVMGLADR 222
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
16-217 |
5.37e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 118.03 E-value: 5.37e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 16 GKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNW-KQAKAYIQKDIIYLHQQP--YLFD 92
Cdd:PRK13636 18 GTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYsRKGLMKLRESVGMVFQDPdnQLFS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 93 ASVTDNIAYGLYRSGERKSNVHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAK 172
Cdd:PRK13636 98 ASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGV 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 504819384 173 QQTAKLLQRLKDE-GVTIMISSHEAHTVEHIADHHIHIEHGNALIR 217
Cdd:PRK13636 178 SEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQ 223
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
15-212 |
7.69e-32 |
|
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: 121.80 E-value: 7.69e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 15 SGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASInyqglTLNWKQAKAYIQKD----IIYLHQQPYL 90
Cdd:COG4987 346 AGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSI-----TLGGVDLRDLDEDDlrrrIAVVPQRPHL 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 91 FDASVTDNIAYGLYRSGERKsnvhkkVTQALDWADLSHLAHRP-----------AKQLSGGEKQRVALTRArILSPR-LL 158
Cdd:COG4987 421 FDTTLRENLRLARPDATDEE------LWAALERVGLGDWLAALpdgldtwlgegGRRLSGGERRRLALARA-LLRDApIL 493
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 504819384 159 LLDEPTASMDS-TAKQQTAKLLQRLKDEGVtIMIsSHEAHTVEHiADHHIHIEHG 212
Cdd:COG4987 494 LLDEPTEGLDAaTEQALLADLLEALAGRTV-LLI-THRLAGLER-MDRILVLEDG 545
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
37-194 |
1.16e-31 |
|
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: 115.38 E-value: 1.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 37 GQNGSGKTTLLKIMSGLLKPDSASINYQGLTLnWKQAKAYIQKDIIYLHQQPYLFDASVTDNIAYG-LYRSGERksnvhk 115
Cdd:cd03245 37 GRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDI-RQLDPADLRRNIGYVPQDVTLFYGTLRDNITLGaPLADDER------ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 116 kVTQALDWADLSHLAHRPAK-----------QLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKqqtAKLLQRLKD 184
Cdd:cd03245 110 -ILRAAELAGVTDFVNKHPNgldlqigergrGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSE---ERLKERLRQ 185
|
170
....*....|..
gi 504819384 185 --EGVTIMISSH 194
Cdd:cd03245 186 llGDKTLIIITH 197
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
5-204 |
1.48e-31 |
|
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: 115.04 E-value: 1.48e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 5 VSYKNLAITLSGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNWKQAKayiQKDIIYL 84
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK---DRDIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 85 HQQPYLF-DASVTDNIAYGLYRSGERKSNVHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEP 163
Cdd:cd03301 78 FQNYALYpHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEP 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 504819384 164 TASMDS----TAKQQTAKLLQRLkdeGVTIMISSH---EAHTvehIAD 204
Cdd:cd03301 158 LSNLDAklrvQMRAELKRLQQRL---GTTTIYVTHdqvEAMT---MAD 199
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
25-209 |
1.09e-30 |
|
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: 112.98 E-value: 1.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 25 LDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDS--ASINYQGLTLNWKQAKAYI----QKDIIYlhqqPYLfdaSVTDN 98
Cdd:cd03263 23 LNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSgtAYINGYSIRTDRKAARQSLgycpQFDALF----DEL---TVREH 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 99 IA-YGLYRsGERKSNVHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQQTAK 177
Cdd:cd03263 96 LRfYARLK-GLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWD 174
|
170 180 190
....*....|....*....|....*....|..
gi 504819384 178 LLQRLKdEGVTIMISSHEAHTVEHIADhHIHI 209
Cdd:cd03263 175 LILEVR-KGRSIILTTHSMDEAEALCD-RIAI 204
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
25-199 |
1.64e-30 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 111.56 E-value: 1.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 25 LDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGltlnwkqakayiQKDIIYLHQQ---PYLFDASVTDNIAY 101
Cdd:NF040873 13 LTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG------------GARVAYVPQRsevPDSLPLTVRDLVAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 102 GLY--RSGERKSNV--HKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQQTAK 177
Cdd:NF040873 81 GRWarRGLWRRLTRddRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIA 160
|
170 180
....*....|....*....|..
gi 504819384 178 LLQRLKDEGVTIMISSHEAHTV 199
Cdd:NF040873 161 LLAEEHARGATVVVVTHDLELV 182
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
17-212 |
1.69e-30 |
|
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: 112.46 E-value: 1.69e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 17 KLVLNIKHLD--IPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNwkQAKAYIQKDIIYLHQQPYLFD-A 93
Cdd:cd03266 16 KTVQAVDGVSftVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVV--KEPAEARRRLGFVSDSTGLYDrL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 94 SVTDNIAY--GLYrsGERKSNVHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTA 171
Cdd:cd03266 94 TARENLEYfaGLY--GLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 504819384 172 KQQTAKLLQRLKDEGVTIMISSHEAHTVEHIADHHIHIEHG 212
Cdd:cd03266 172 TRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRG 212
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
4-220 |
1.76e-30 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 112.88 E-value: 1.76e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 4 LVSYKNLAITLSGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNWKQAKAY-IQKDII 82
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERlIRQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 83 YLHQQPYLF-DASVTDNIAYGLYR-SGERKSNVHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLL 160
Cdd:PRK09493 81 MVFQQFYLFpHLTALENVMFGPLRvRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLF 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504819384 161 DEPTASMDSTAKQQTAKLLQRLKDEGVTIMISSHEAHTVEHIADHHIHIEHG--------NALI-RPPN 220
Cdd:PRK09493 161 DEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGriaedgdpQVLIkNPPS 229
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
8-213 |
8.03e-30 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 110.26 E-value: 8.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 8 KNLAITLSGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDsasINYQG-LTLNWKQ--AKAYIQKDIIYL 84
Cdd:COG4136 5 ENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPA---FSASGeVLLNGRRltALPAEQRRIGIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 85 HQQPYLFD-ASVTDNIAYGLyRSGERKSNVHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEP 163
Cdd:COG4136 82 FQDDLLFPhLSVGENLAFAL-PPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 504819384 164 TASMDSTAKQQTAKL-LQRLKDEGV-TIMISsheaHTVEHIADHHIHIEHGN 213
Cdd:COG4136 161 FSKLDAALRAQFREFvFEQIRQRGIpALLVT----HDEEDAPAAGRVLDLGN 208
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
5-212 |
8.61e-30 |
|
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: 110.31 E-value: 8.61e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 5 VSYKNLAITLSGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNWKQAKAY-IQKDIIY 83
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINeLRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 84 LHQQPYLF-DASVTDNIAYGL-YRSGERKSNVHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLD 161
Cdd:cd03262 81 VFQQFNLFpHLTVLENITLAPiKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 504819384 162 EPTASMDSTAKQQTAKLLQRLKDEGVTIMISSHEAHTVEHIADHHIHIEHG 212
Cdd:cd03262 161 EPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDG 211
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
25-212 |
1.11e-29 |
|
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: 110.46 E-value: 1.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 25 LDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNWKQAKAYIQKDIIYLHQQPYLF-DASVTDNIAYGL 103
Cdd:COG0410 24 LEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLGIGYVPEGRRIFpSLTVEENLLLGA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 104 YRSGERKsnvhkKVTQALDWA-----DLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTA----SMdstaKQQ 174
Cdd:COG0410 104 YARRDRA-----EVRADLERVyelfpRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLglapLI----VEE 174
|
170 180 190
....*....|....*....|....*....|....*...
gi 504819384 175 TAKLLQRLKDEGVTIMISSHEAHTVEHIADHHIHIEHG 212
Cdd:COG0410 175 IFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERG 212
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
37-212 |
1.28e-29 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 112.86 E-value: 1.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 37 GQNGSGKTTLLKIMSGLLKPDSASINYQGL---TLNWKQAKAyIQKDIIYLHQQPYLFDA-SVTDNIAYGLYRSGERKSN 112
Cdd:COG1135 38 GYSGAGKSTLIRCINLLERPTSGSVLVDGVdltALSERELRA-ARRKIGMIFQHFNLLSSrTVAENVALPLEIAGVPKAE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 113 VHKKVTQALDWADLSHLAHR-PAkQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQQTAKLLQRLKDE-GVTIM 190
Cdd:COG1135 117 IRKRVAELLELVGLSDKADAyPS-QLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRElGLTIV 195
|
170 180
....*....|....*....|..
gi 504819384 191 ISSHEAHTVEHIADHHIHIEHG 212
Cdd:COG1135 196 LITHEMDVVRRICDRVAVLENG 217
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
25-212 |
1.92e-29 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 110.08 E-value: 1.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 25 LDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNWKQAK-AYIQKDIIYLHQQPYLF-DASVTDNIAYG 102
Cdd:COG1126 22 LDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDiNKLRRKVGMVFQQFNLFpHLTVLENVTLA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 103 LYRS-GERKSNVHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQQTAKLLQR 181
Cdd:COG1126 102 PIKVkKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRD 181
|
170 180 190
....*....|....*....|....*....|.
gi 504819384 182 LKDEGVTIMISSHEAHTVEHIADHHIHIEHG 212
Cdd:COG1126 182 LAKEGMTMVVVTHEMGFAREVADRVVFMDGG 212
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
8-216 |
2.16e-29 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 109.41 E-value: 2.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 8 KNLAITLSGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNWKQAKayiqkDIIYLHQQ 87
Cdd:TIGR03740 4 KNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWTRKDLH-----KIGSLIES 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 88 PYLF-DASVTDNIAYGLYRSGERKSnvhkKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTAS 166
Cdd:TIGR03740 79 PPLYeNLTARENLKVHTTLLGLPDS----RIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEPTNG 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 504819384 167 MDSTAKQQTAKLLQRLKDEGVTIMISSHEAHTVEHIADhHIHIEHGNALI 216
Cdd:TIGR03740 155 LDPIGIQELRELIRSFPEQGITVILSSHILSEVQQLAD-HIGIISEGVLG 203
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
25-209 |
4.87e-29 |
|
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: 113.92 E-value: 4.87e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 25 LDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLnWKQAKAYIQKDIIYLHQQPYLFDASVTDNIAygLY 104
Cdd:TIGR02857 343 FTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPL-ADADADSWRDQIAWVPQHPFLFAGTIAENIR--LA 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 105 RSGERKSNVHKKVTQALDW---ADLSHLAHRP----AKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQQTAK 177
Cdd:TIGR02857 420 RPDASDAEIREALERAGLDefvAALPQGLDTPigegGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLE 499
|
170 180 190
....*....|....*....|....*....|..
gi 504819384 178 LLQRLKdEGVTIMISSHEAHTVEhIADHHIHI 209
Cdd:TIGR02857 500 ALRALA-QGRTVLLVTHRLALAA-LADRIVVL 529
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
8-213 |
6.49e-29 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 109.00 E-value: 6.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 8 KNLAITLSGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSasinyqGLTLNWKQAKAYIQKDIIYLHQQ 87
Cdd:PRK11247 16 NAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSA------GELLAGTAPLAEAREDTRLMFQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 88 PYLFD-ASVTDNIAYGLyrsgerKSNVHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTAS 166
Cdd:PRK11247 90 ARLLPwKKVIDNVGLGL------KGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 504819384 167 MDSTAKQQTAKLLQRL-KDEGVTIMISSHEAHTVEHIADHHIHIEHGN 213
Cdd:PRK11247 164 LDALTRIEMQDLIESLwQQHGFTVLLVTHDVSEAVAMADRVLLIEEGK 211
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
8-212 |
1.13e-28 |
|
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: 108.04 E-value: 1.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 8 KNLAITL-SGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNWKQAKAY--IQKDIIYL 84
Cdd:cd03256 4 ENLSKTYpNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALrqLRRQIGMI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 85 HQQPYLFD-ASVTDNIAYG------LYRSGERKSNVHKKVT--QALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSP 155
Cdd:cd03256 84 FQQFNLIErLSVLENVLSGrlgrrsTWRSLFGLFPKEEKQRalAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 504819384 156 RLLLLDEPTASMDSTAKQQTAKLLQRL-KDEGVTIMISSHEAHTVEHIADHHIHIEHG 212
Cdd:cd03256 164 KLILADEPVASLDPASSRQVMDLLKRInREEGITVIVSLHQVDLAREYADRIVGLKDG 221
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
19-214 |
1.57e-28 |
|
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: 105.76 E-value: 1.57e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 19 VLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNwKQAKAYIQKDIIYLHQQPYLFDASVTDN 98
Cdd:cd03246 17 VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADIS-QWDPNELGDHVGYLPQDDELFSGSIAEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 99 IayglyrsgerksnvhkkvtqaldwadlshlahrpakqLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQQTAKL 178
Cdd:cd03246 96 I-------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQA 138
|
170 180 190
....*....|....*....|....*....|....*.
gi 504819384 179 LQRLKDEGVTIMISSHEAHTVEhIADHHIHIEHGNA 214
Cdd:cd03246 139 IAALKAAGATRIVIAHRPETLA-SADRILVLEDGRV 173
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
5-212 |
1.61e-28 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 112.59 E-value: 1.61e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 5 VSYKNLAITL-SGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLlkpdsasinyqgltlnWKQAKAYIQ----K 79
Cdd:COG4178 363 LALEDLTLRTpDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGL----------------WPYGSGRIArpagA 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 80 DIIYLHQQPYLFDASVTDNIAYGlyRSGERKSNvhKKVTQALDWADLSHLAHRP------AKQLSGGEKQRVALTRARIL 153
Cdd:COG4178 427 RVLFLPQRPYLPLGTLREALLYP--ATAEAFSD--AELREALEAVGLGHLAERLdeeadwDQVLSLGEQQRLAFARLLLH 502
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504819384 154 SPRLLLLDEPTASMDSTAKqqtAKLLQRLKDE--GVTImIS-SHEAhTVEHIADHHIHIEHG 212
Cdd:COG4178 503 KPDWLFLDEATSALDEENE---AALYQLLREElpGTTV-ISvGHRS-TLAAFHDRVLELTGD 559
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
8-213 |
2.31e-28 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 107.79 E-value: 2.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 8 KNLAITLSGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNWKQAKAYIQKdIIYLHQQ 87
Cdd:PRK11231 6 ENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARR-LALLPQH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 88 PYLFDA-SVTDNIAYGlyRS------GERKSNVHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALtrARILS--PRLL 158
Cdd:PRK11231 85 HLTPEGiTVRELVAYG--RSpwlslwGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFL--AMVLAqdTPVV 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 504819384 159 LLDEPTASMDSTAKQQTAKLLQRLKDEGVTIMISSHEAHTVEHIADHHIHIEHGN 213
Cdd:PRK11231 161 LLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGH 215
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
35-204 |
4.18e-28 |
|
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: 105.74 E-value: 4.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 35 LTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLnwKQAKAYIQKDIIYLHQQPYLFDA-SVTDNIAYGLYRSGERKSNV 113
Cdd:cd03264 30 LLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDV--LKQPQKLRRRIGYLPQEFGVYPNfTVREFLDYIAWLKGIPSKEV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 114 HKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQQTAKLLQRLKdEGVTIMISS 193
Cdd:cd03264 108 KARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELG-EDRIVILST 186
|
170
....*....|.
gi 504819384 194 HEAHTVEHIAD 204
Cdd:cd03264 187 HIVEDVESLCN 197
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-212 |
4.83e-28 |
|
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: 105.98 E-value: 4.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 1 MSTLVSYKNLAIT-----LSGKL--VLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINY--QGLTLNWK 71
Cdd:COG4778 1 MTTLLEVENLSKTftlhlQGGKRlpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWVDLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 72 QAKAYiqkDIIYLHQQP--YlfdasVT------------DNIAYGLYRSGERKSNVHKKVTQALDWADL-SHLAHRPAKQ 136
Cdd:COG4778 81 QASPR---EILALRRRTigY-----VSqflrviprvsalDVVAEPLLERGVDREEARARARELLARLNLpERLWDLPPAT 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504819384 137 LSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQQTAKLLQRLKDEGVTIMISSHEAHTVEHIADHHIHIEHG 212
Cdd:COG4778 153 FSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
25-194 |
6.09e-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 upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 106.75 E-value: 6.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 25 LDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGL-TLN----WKqakayIQKDIIYLHQQPylfD-----AS 94
Cdd:TIGR04520 23 LSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLdTLDeenlWE-----IRKKVGMVFQNP---DnqfvgAT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 95 VTDNIAYGLYRSGERKSNVHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALtrARIL--SPRLLLLDEPTASMDSTAK 172
Cdd:TIGR04520 95 VEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAI--AGVLamRPDIIILDEATSMLDPKGR 172
|
170 180
....*....|....*....|...
gi 504819384 173 QQTAKLLQRL-KDEGVTIMISSH 194
Cdd:TIGR04520 173 KEVLETIRKLnKEEGITVISITH 195
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
35-204 |
8.70e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 106.70 E-value: 8.70e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 35 LTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNW-KQAKAYIQKDIIYLHQQP--YLFDASVTDNIAYGLYRSGERKS 111
Cdd:PRK13639 33 LLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYdKKSLLEVRKTVGIVFQNPddQLFAPTVEEDVAFGPLNLGLSKE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 112 NVHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALtrARILS--PRLLLLDEPTASMDSTAKQQTAKLLQRLKDEGVTI 189
Cdd:PRK13639 113 EVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAI--AGILAmkPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITI 190
|
170
....*....|....*
gi 504819384 190 MISSHEAHTVEHIAD 204
Cdd:PRK13639 191 IISTHDVDLVPVYAD 205
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
35-219 |
9.40e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 106.67 E-value: 9.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 35 LTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNWKQAK-AYIQKDIIYLHQQP--YLFDASVTDNIAYGLYRSGERKS 111
Cdd:PRK13637 38 LIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKlSDIRKKVGLVFQYPeyQLFEETIEKDIAFGPINLGLSEE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 112 NVHKKVTQALDWADLSH--LAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQQTAKLLQRLKDE-GVT 188
Cdd:PRK13637 118 EIENRVKRAMNIVGLDYedYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEyNMT 197
|
170 180 190
....*....|....*....|....*....|..
gi 504819384 189 IMISSHEAHTVEHIADHHIHIEHGN-ALIRPP 219
Cdd:PRK13637 198 IILVSHSMEDVAKLADRIIVMNKGKcELQGTP 229
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
8-194 |
9.54e-28 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 104.96 E-value: 9.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 8 KNLAITLSGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGltlnwkqaKAYIQKDII----Y 83
Cdd:PRK13539 6 EDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDG--------GDIDDPDVAeachY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 84 L-HQ---QPYLfdaSVTDNIAY--GLYRSGERksnvhkKVTQALDWADLSHLAHRPAKQLSGGEKQRVALtrARIL-SPR 156
Cdd:PRK13539 78 LgHRnamKPAL---TVAENLEFwaAFLGGEEL------DIAAALEAVGLAPLAHLPFGYLSAGQKRRVAL--ARLLvSNR 146
|
170 180 190
....*....|....*....|....*....|....*....
gi 504819384 157 LL-LLDEPTASMDSTAKQQTAKLLQRLKDEGVTIMISSH 194
Cdd:PRK13539 147 PIwILDEPTAALDAAAVALFAELIRAHLAQGGIVIAATH 185
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
25-204 |
9.68e-28 |
|
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: 103.28 E-value: 9.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 25 LDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASInyqgltlnwkqakayiqkdiiYLHQQPYLFdASVTDNIAYGLY 104
Cdd:cd03216 21 LSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEI---------------------LVDGKEVSF-ASPRDARRAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 105 RsgerksnVHkkvtqaldwadlshlahrpakQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQQTAKLLQRLKD 184
Cdd:cd03216 79 M-------VY---------------------QLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRA 130
|
170 180
....*....|....*....|
gi 504819384 185 EGVTIMISSHEAHTVEHIAD 204
Cdd:cd03216 131 QGVAVIFISHRLDEVFEIAD 150
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
5-221 |
1.18e-27 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 107.88 E-value: 1.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 5 VSYKNLAITLSGKLVLNIKHLDIP-AHQCTLLtGQNGSGKTTLLKIMSGLLKPDSASINYQG--LTLNWKQakayiQKDI 81
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKqGTMVTLL-GPSGCGKTTVLRLVAGLEKPTEGQIFIDGedVTHRSIQ-----QRDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 82 IYLHQQPYLF-DASVTDNIAYGLYRSGERKSNVHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLL 160
Cdd:PRK11432 81 CMVFQSYALFpHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504819384 161 DEPTASMDS----TAKQQTAKLLQRLkdeGVTIMISSH---EAHTVehiADHHIHIEHGN--------ALIRPPNS 221
Cdd:PRK11432 161 DEPLSNLDAnlrrSMREKIRELQQQF---NITSLYVTHdqsEAFAV---SDTVIVMNKGKimqigspqELYRQPAS 230
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
25-212 |
1.27e-27 |
|
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: 105.11 E-value: 1.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 25 LDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLtLNWKQAKAYIQKDIIYLHQQPYL-FDASVTDNIA--- 100
Cdd:cd03267 42 FTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGL-VPWKRRKKFLRRIGVVFGQKTQLwWDLPVIDSFYlla 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 101 --YGLyRSGERKSNVhKKVTQALDwadLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQQTAKL 178
Cdd:cd03267 121 aiYDL-PPARFKKRL-DELSELLD---LEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNF 195
|
170 180 190
....*....|....*....|....*....|....*
gi 504819384 179 LQRL-KDEGVTIMISSHEAHTVEHIADHHIHIEHG 212
Cdd:cd03267 196 LKEYnRERGTTVLLTSHYMKDIEALARRVLVIDKG 230
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
8-216 |
1.71e-27 |
|
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: 105.05 E-value: 1.71e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 8 KNLAITLSGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNWKQAKAYIQKDIIYLHQQ 87
Cdd:TIGR04406 5 ENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARLGIGYLPQE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 88 PYLF-DASVTDNIAYGLYRSGERKSNVHKKVTQAL-DWADLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTA 165
Cdd:TIGR04406 85 ASIFrKLTVEENIMAVLEIRKDLDRAEREERLEALlEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDEPFA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 504819384 166 SMDSTAKQQTAKLLQRLKDEGVTIMISSHEAHTVEHIADHHIHIEHGNALI 216
Cdd:TIGR04406 165 GVDPIAVGDIKKIIKHLKERGIGVLITDHNVRETLDICDRAYIISDGKVLA 215
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
25-205 |
6.30e-27 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 107.41 E-value: 6.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 25 LDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNWKQAKAYIQKDIIYLHQQPYLF-DASVTDNIAYGL 103
Cdd:COG1129 25 LELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAGIAIIHQELNLVpNLSVAENIFLGR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 104 Y--RSG---ERKsnVHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQQTAKL 178
Cdd:COG1129 105 EprRGGlidWRA--MRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRI 182
|
170 180
....*....|....*....|....*..
gi 504819384 179 LQRLKDEGVTIMISSHEAHTVEHIADH 205
Cdd:COG1129 183 IRRLKAQGVAIIYISHRLDEVFEIADR 209
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
25-216 |
6.89e-27 |
|
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: 102.74 E-value: 6.89e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 25 LDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGltlnwKQAKAYIQKDIIYLHQQPYLF-DASVTDNIAYGL 103
Cdd:cd03269 21 FSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG-----KPLDIAARNRIGYLPEERGLYpKMKVIDQLVYLA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 104 YRSGERKSNVHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQQTAKLLQRLK 183
Cdd:cd03269 96 QLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELA 175
|
170 180 190
....*....|....*....|....*....|...
gi 504819384 184 DEGVTIMISSHEAHTVEHIADHHIHIEHGNALI 216
Cdd:cd03269 176 RAGKTVILSTHQMELVEELCDRVLLLNKGRAVL 208
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
25-196 |
7.05e-27 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 103.79 E-value: 7.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 25 LDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASInyqglTLNWKQAKA-------YIQKDIIYlhqqPYLfdaSVTD 97
Cdd:COG4525 28 LTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEI-----TLDGVPVTGpgadrgvVFQKDALL----PWL---NVLD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 98 NIAYGLYRSGERKSNVHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQQTAK 177
Cdd:COG4525 96 NVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQE 175
|
170 180
....*....|....*....|...
gi 504819384 178 LLQRL-KDEGVTIMISSH---EA 196
Cdd:COG4525 176 LLLDVwQRTGKGVFLITHsveEA 198
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
5-195 |
1.70e-26 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 105.31 E-value: 1.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 5 VSYKNLAITLSGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNWKQAKAyIQKDIIYL 84
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARA-ASRRVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 85 HQQPYL-FDASVTDNIAYG----LYRSGERKSNVHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLL 159
Cdd:PRK09536 83 PQDTSLsFEFDVRQVVEMGrtphRSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLL 162
|
170 180 190
....*....|....*....|....*....|....*.
gi 504819384 160 LDEPTASMDSTAKQQTAKLLQRLKDEGVTIMISSHE 195
Cdd:PRK09536 163 LDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHD 198
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
34-205 |
1.81e-26 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 106.26 E-value: 1.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 34 LLtGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNWKQAKAYIQKDIIYLHQQPYLFDA-SVTDNIAYGLYRSGERKSN 112
Cdd:COG3845 36 LL-GENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAIALGIGMVHQHFMLVPNlTVAENIVLGLEPTKGGRLD 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 113 vHKKVTQALdwADLS---HLA---HRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMdsTAkQQTAKL---LQRLK 183
Cdd:COG3845 115 -RKAARARI--RELSeryGLDvdpDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVL--TP-QEADELfeiLRRLA 188
|
170 180
....*....|....*....|..
gi 504819384 184 DEGVTIMISSHEAHTVEHIADH 205
Cdd:COG3845 189 AEGKSIIFITHKLREVMAIADR 210
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
10-224 |
2.47e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 102.43 E-value: 2.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 10 LAITLSGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNWKQAKAYI-----QKDIIYL 84
Cdd:PRK14246 16 LYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIFQIdaiklRKEVGMV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 85 HQQPYLF-DASVTDNIAYGLYRSG-ERKSNVHKKVTQALD----WADLSHLAHRPAKQLSGGEKQRVALTRARILSPRLL 158
Cdd:PRK14246 96 FQQPNPFpHLSIYDNIAYPLKSHGiKEKREIKKIVEECLRkvglWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504819384 159 LLDEPTASMDSTAKQQTAKLLQRLKDEgVTIMISSHEAHTVEHIADHHIHIEHGNaLIRPPNSNNV 224
Cdd:PRK14246 176 LMDEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGE-LVEWGSSNEI 239
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
25-212 |
3.82e-26 |
|
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: 101.36 E-value: 3.82e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 25 LDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQG--LT-LNwKQAKAYIQKDIIYLHQQPYLFDASVT--DNI 99
Cdd:COG4181 33 LEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGqdLFaLD-EDARARLRARHVGFVFQSFQLLPTLTalENV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 100 AYGLYRSGERksNVHKKVTQALDWADLSH-LAHRPAkQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQQTAKL 178
Cdd:COG4181 112 MLPLELAGRR--DARARARALLERVGLGHrLDHYPA-QLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDL 188
|
170 180 190
....*....|....*....|....*....|....*...
gi 504819384 179 LQRLKDE-GVTIMISSHEahtvEHIA---DHHIHIEHG 212
Cdd:COG4181 189 LFELNRErGTTLVLVTHD----PALAarcDRVLRLRAG 222
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
25-215 |
3.91e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 102.12 E-value: 3.91e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 25 LDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNWKQAKaYIQKDIIYLHQQP--YLFDASVTDNIAYG 102
Cdd:PRK13647 26 LSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEK-WVRSKVGLVFQDPddQVFSSTVWDDVAFG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 103 LYRSGERKSNVHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQQTAKLLQRL 182
Cdd:PRK13647 105 PVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRL 184
|
170 180 190
....*....|....*....|....*....|...
gi 504819384 183 KDEGVTIMISSHEAHTVEHIADHHIHIEHGNAL 215
Cdd:PRK13647 185 HNQGKTVIVATHDVDLAAEWADQVIVLKEGRVL 217
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
31-212 |
5.44e-26 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 100.62 E-value: 5.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 31 QCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNWKQAKaYIQKDIIYLHQQPYLFDASVTDNIAYGLyrsgerK 110
Cdd:cd03248 41 EVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHK-YLHSKVSLVGQEPVLFARSLQDNIAYGL------Q 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 111 SNVHKKVTQALDWAD----LSHLAHRP-------AKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQQTAKLL 179
Cdd:cd03248 114 SCSFECVKEAAQKAHahsfISELASGYdtevgekGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQAL 193
|
170 180 190
....*....|....*....|....*....|...
gi 504819384 180 QRlKDEGVTIMISSHEAHTVEHiADHHIHIEHG 212
Cdd:cd03248 194 YD-WPERRTVLVIAHRLSTVER-ADQILVLDGG 224
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-204 |
5.74e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 101.65 E-value: 5.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 1 MSTLV---SYKNLAITLSGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDS-----ASINYQGLTLNWKQ 72
Cdd:PRK14258 1 MSKLIpaiKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIYERR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 73 AKA-YIQKDIIYLHQQPYLFDASVTDNIAYGLYRSGER-KSNVHKKVTQALD----WADLSHLAHRPAKQLSGGEKQRVA 146
Cdd:PRK14258 81 VNLnRLRRQVSMVHPKPNLFPMSVYDNVAYGVKIVGWRpKLEIDDIVESALKdadlWDEIKHKIHKSALDLSGGQQQRLC 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 147 LTRARILSPRLLLLDEPTASMDSTAKQQTAKLLQ--RLKDEgVTIMISSHEAHTVEHIAD 204
Cdd:PRK14258 161 IARALAVKPKVLLMDEPCFGLDPIASMKVESLIQslRLRSE-LTMVIVSHNLHQVSRLSD 219
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
16-212 |
5.93e-26 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 105.25 E-value: 5.93e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 16 GKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASI-----NYQGLTLNWkqakayIQKDIIYLHQQPYL 90
Cdd:COG1132 352 DRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRIlidgvDIRDLTLES------LRRQIGVVPQDTFL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 91 FDASVTDNIAYGlyrsgeRKSNVHKKVTQALDWADLSHLAHR-PAK----------QLSGGEKQRVALTRARILSPRLLL 159
Cdd:COG1132 426 FSGTIRENIRYG------RPDATDEEVEEAAKAAQAHEFIEAlPDGydtvvgergvNLSGGQRQRIAIARALLKDPPILI 499
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 504819384 160 LDEPTASMDStakqQTAKLLQR-LKD--EGVTIMISSHEAHTVEHiADHHIHIEHG 212
Cdd:COG1132 500 LDEATSALDT----ETEALIQEaLERlmKGRTTIVIAHRLSTIRN-ADRILVLDDG 550
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
15-194 |
6.46e-26 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 105.22 E-value: 6.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 15 SGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTL-NWkqAKAYIQKDIIYLHQQPYLFDA 93
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLsQW--DREELGRHIGYLPQDVELFDG 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 94 SVTDNIAyglyRSGERKSNvhkKVTQALDWADLSHLAHRPAK-----------QLSGGEKQRVALTRARILSPRLLLLDE 162
Cdd:COG4618 421 TIAENIA----RFGDADPE---KVVAAAKLAGVHEMILRLPDgydtrigeggaRLSGGQRQRIGLARALYGDPRLVVLDE 493
|
170 180 190
....*....|....*....|....*....|..
gi 504819384 163 PTASMDSTAKQQTAKLLQRLKDEGVTIMISSH 194
Cdd:COG4618 494 PNSNLDDEGEAALAAAIRALKARGATVVVITH 525
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
18-212 |
7.45e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 101.37 E-value: 7.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 18 LVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNwKQAKAYIQKDIIYLHQQP--YLFDASV 95
Cdd:PRK13648 23 FTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAIT-DDNFEKLRKHIGIVFQNPdnQFVGSIV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 96 TDNIAYGLYRSGERKSNVHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQQT 175
Cdd:PRK13648 102 KYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNL 181
|
170 180 190
....*....|....*....|....*....|....*...
gi 504819384 176 AKLLQRLKDE-GVTIMISSHEAHTVEHiADHHIHIEHG 212
Cdd:PRK13648 182 LDLVRKVKSEhNITIISITHDLSEAME-ADHVIVMNKG 218
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
25-215 |
8.96e-26 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 100.21 E-value: 8.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 25 LDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNwKQAKAyiQKDIIYLHQQPYLFDA-SVTDNIAYGL 103
Cdd:COG3840 20 LTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLT-ALPPA--ERPVSMLFQENNLFPHlTVAQNIGLGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 104 yRSGERKSNV-HKKVTQALDWADLSHLAHR-PAkQLSGGEKQRVALTRArILSPR-LLLLDEPTASMDSTAKQQTAKLLQ 180
Cdd:COG3840 97 -RPGLKLTAEqRAQVEQALERVGLAGLLDRlPG-QLSGGQRQRVALARC-LVRKRpILLLDEPFSALDPALRQEMLDLVD 173
|
170 180 190
....*....|....*....|....*....|....*.
gi 504819384 181 RLKDE-GVTIMISSHEAHTVEHIADHHIHIEHGNAL 215
Cdd:COG3840 174 ELCRErGLTVLMVTHDPEDAARIADRVLLVADGRIA 209
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-194 |
1.10e-25 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 100.10 E-value: 1.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 1 MSTLVSyKNLAITLSGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASInyqglTLN---------WK 71
Cdd:COG1137 1 MMTLEA-ENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRI-----FLDgedithlpmHK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 72 QAkayiQKDIIYLHQQPYLF-DASVTDNIAYGLYRSGERKSNVHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRA 150
Cdd:COG1137 75 RA----RLGIGYLPQEASIFrKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 504819384 151 RILSPRLLLLDEPTASMDSTAKQQTAKLLQRLKDEGVTIMISSH 194
Cdd:COG1137 151 LATNPKFILLDEPFAGVDPIAVADIQKIIRHLKERGIGVLITDH 194
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-181 |
1.16e-25 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 102.72 E-value: 1.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 2 STLVSYKNLAITLSGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNWKQAKayiQKDI 81
Cdd:PRK09452 12 SPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE---NRHV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 82 IYLHQQPYLF-DASVTDNIAYGLYRSGERKSNVHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLL 160
Cdd:PRK09452 89 NTVFQSYALFpHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLL 168
|
170 180
....*....|....*....|....
gi 504819384 161 DEPTASMDSTAKQQTA---KLLQR 181
Cdd:PRK09452 169 DESLSALDYKLRKQMQnelKALQR 192
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-204 |
1.20e-25 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 100.62 E-value: 1.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 1 MSTLVSYKNLAITLSGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMS--GLLKPD---SASINYQGLTLNWKQAKA 75
Cdd:PRK14239 2 TEPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDLNPEvtiTGSIVYNGHNIYSPRTDT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 76 Y-IQKDIIYLHQQPYLFDASVTDNIAYGLYRSGERKSN-----VHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTR 149
Cdd:PRK14239 82 VdLRKEIGMVFQQPNPFPMSIYENVVYGLRLKGIKDKQvldeaVEKSLKGASIWDEVKDRLHDSALGLSGGQQQRVCIAR 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 504819384 150 ARILSPRLLLLDEPTASMDSTAKQQTAKLLQRLKDEgVTIMISSHEAHTVEHIAD 204
Cdd:PRK14239 162 VLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSMQQASRISD 215
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
35-212 |
1.99e-25 |
|
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: 98.98 E-value: 1.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 35 LTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNWKQAKayIQKDIIYLHQQPYLFDA-SVTDNIA-----YGlYRSGE 108
Cdd:cd03265 31 LLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPRE--VRRRIGIVFQDLSVDDElTGWENLYiharlYG-VPGAE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 109 RKsnvhKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQQTAKLLQRLKDE-GV 187
Cdd:cd03265 108 RR----ERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEfGM 183
|
170 180
....*....|....*....|....*
gi 504819384 188 TIMISSHEAHTVEHIADHHIHIEHG 212
Cdd:cd03265 184 TILLTTHYMEEAEQLCDRVAIIDHG 208
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
34-195 |
2.08e-25 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 99.18 E-value: 2.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 34 LLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNWKQAK--AYIQKDIIYLHQQPYLF-DASVTDNIAYGLYRSGERK 110
Cdd:PRK10908 32 FLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNRevPFLRRQIGMIFQDHHLLmDRTVYDNVAIPLIIAGASG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 111 SNVHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQQTAKLLQRLKDEGVTIM 190
Cdd:PRK10908 112 DDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVL 191
|
....*
gi 504819384 191 ISSHE 195
Cdd:PRK10908 192 MATHD 196
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
2-212 |
2.56e-25 |
|
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: 99.39 E-value: 2.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 2 STLVSYKNLAITLSGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKP-DSASINYQGLTLN----WKqakay 76
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPtYGNDVRLFGERRGgedvWE----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 77 IQKDIIY----LHQQpYLFDASVTDNIAYGLYRSGERKSNV----HKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALT 148
Cdd:COG1119 76 LRKRIGLvspaLQLR-FPRDETVLDVVLSGFFDSIGLYREPtdeqRERARELLELLGLAHLADRPFGTLSQGEQRRVLIA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504819384 149 RARILSPRLLLLDEPTASMDSTAKQQTAKLLQRLKDEGVT--IMISsheaHTVEHIAD---HHIHIEHG 212
Cdd:COG1119 155 RALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPtlVLVT----HHVEEIPPgitHVLLLKDG 219
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
37-192 |
3.15e-25 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 100.09 E-value: 3.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 37 GQNGSGKTTLLKIMSGLLKPDSASINYQGLTLN----WKqakayIQKDIIYLHQQP--YLFDASVTDNIAYGLYRSGERK 110
Cdd:PRK13635 40 GHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSeetvWD-----VRRQVGMVFQNPdnQFVGATVQDDVAFGLENIGVPR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 111 SNVHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQQTAKLLQRLKDEGVTIM 190
Cdd:PRK13635 115 EEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITV 194
|
..
gi 504819384 191 IS 192
Cdd:PRK13635 195 LS 196
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
19-195 |
3.85e-25 |
|
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: 102.82 E-value: 3.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 19 VLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLnWKQAKAYIQKDIIYLHQQPYLFDASVTDN 98
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPV-SSLDQDEVRRRVSVCAQDAHLFDTTVREN 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 99 IAYGlyrsgeRKSNVHKKVTQALDWADL-SHLAHRP----------AKQLSGGEKQRVALTRARILSPRLLLLDEPTASM 167
Cdd:TIGR02868 429 LRLA------RPDATDEELWAALERVGLaDWLRALPdgldtvlgegGARLSGGERQRLALARALLADAPILLLDEPTEHL 502
|
170 180
....*....|....*....|....*....
gi 504819384 168 DS-TAKQQTAKLLQRLkDEGVTIMISSHE 195
Cdd:TIGR02868 503 DAeTADELLEDLLAAL-SGRTVVLITHHL 530
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
5-215 |
4.39e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 99.49 E-value: 4.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 5 VSYKNLAITL--SGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSAS---INYQGLTLNWKQAKAYIQK 79
Cdd:PRK13640 6 VEFKHVSFTYpdSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 80 -DIIYLHQQPYLFDASVTDNIAYGLYRSGERKSNVHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSPRLL 158
Cdd:PRK13640 86 vGIVFQNPDNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKII 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 504819384 159 LLDEPTASMDSTAKQQTAKLLQRL-KDEGVTIMISSHEAHTVEHiADHHIHIEHGNAL 215
Cdd:PRK13640 166 ILDESTSMLDPAGKEQILKLIRKLkKKNNLTVISITHDIDEANM-ADQVLVLDDGKLL 222
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
8-212 |
4.62e-25 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 102.45 E-value: 4.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 8 KNLAITLSGKLVL-NIkHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGltlNWKqakayiqkdIIYLHQ 86
Cdd:COG0488 2 ENLSKSFGGRPLLdDV-SLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK---GLR---------IGYLPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 87 QPYLFD-ASVTDNIAYGLYR--------------------SGERKSNVHKKVTQALDWAD-------LSHL------AHR 132
Cdd:COG0488 69 EPPLDDdLTVLDTVLDGDAElraleaeleeleaklaepdeDLERLAELQEEFEALGGWEAearaeeiLSGLgfpeedLDR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 133 PAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAkqqTAKLLQRLKDEGVTIMISSHEAHTVEHIADHHIHIEHG 212
Cdd:COG0488 149 PVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES---IEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRG 225
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
25-212 |
7.51e-25 |
|
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: 98.00 E-value: 7.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 25 LDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQG-----LTLNWkqakayIQKDIIYLHQQPYLFDASVTDNI 99
Cdd:cd03249 24 LTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGvdirdLNLRW------LRSQIGLVSQEPVLFDGTIAENI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 100 AYGLYRSGE-------RKSNVHKKVTQALDWADlSHLAHRpAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAK 172
Cdd:cd03249 98 RYGKPDATDeeveeaaKKANIHDFIMSLPDGYD-TLVGER-GSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAESE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 504819384 173 QQTAKLLQRLKdEGVTIMISSHEAHTVEHiADHHIHIEHG 212
Cdd:cd03249 176 KLVQEALDRAM-KGRTTIVIAHRLSTIRN-ADLIAVLQNG 213
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
16-195 |
8.54e-25 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 98.23 E-value: 8.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 16 GKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNWKQAkayiQKDIIYLHQQ--PYLfda 93
Cdd:PRK11248 13 GKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGA----ERGVVFQNEGllPWR--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 94 SVTDNIAYGLYRSGERKSNVHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQ 173
Cdd:PRK11248 86 NVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTRE 165
|
170 180
....*....|....*....|...
gi 504819384 174 QTAKLLQRL-KDEGVTIMISSHE 195
Cdd:PRK11248 166 QMQTLLLKLwQETGKQVLLITHD 188
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
2-213 |
9.45e-25 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 97.48 E-value: 9.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 2 STLVSYKNLAITLSGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNWKQAKAYIQKdI 81
Cdd:PRK10247 5 SPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQ-V 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 82 IYLHQQPYLFDASVTDNIAYGLYRSGERKSnvHKKVTQALDWADL-SHLAHRPAKQLSGGEKQRVALTRARILSPRLLLL 160
Cdd:PRK10247 84 SYCAQTPTLFGDTVYDNLIFPWQIRNQQPD--PAIFLDDLERFALpDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 504819384 161 DEPTASMDSTAKQQTAKLLQRL-KDEGVTIMISSHEAHTVEHiADHHIHIE-HGN 213
Cdd:PRK10247 162 DEITSALDESNKHNVNEIIHRYvREQNIAVLWVTHDKDEINH-ADKVITLQpHAG 215
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
5-211 |
1.10e-24 |
|
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: 95.68 E-value: 1.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 5 VSYKNLAITL-SGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLlkpdsasinyqgltlnWKQAKAYIQK---- 79
Cdd:cd03223 1 IELENLSLATpDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGL----------------WPWGSGRIGMpege 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 80 DIIYLHQQPYLFDASVTDNIAYglyrsgerksnvhkkvtqalDWADlshlahrpakQLSGGEKQRVALTRARILSPRLLL 159
Cdd:cd03223 65 DLLFLPQRPYLPLGTLREQLIY--------------------PWDD----------VLSGGEQQRLAFARLLLHKPKFVF 114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 504819384 160 LDEPTASMDstaKQQTAKLLQRLKDEGVTIMISSHEaHTVEHIADHHIHIEH 211
Cdd:cd03223 115 LDEATSALD---EESEDRLYQLLKELGITVISVGHR-PSLWKFHDRVLDLDG 162
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
8-212 |
1.19e-24 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 94.82 E-value: 1.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 8 KNLAITLSGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINyqgltlnwkqakayiqkdiiylhqq 87
Cdd:cd03221 4 ENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVT------------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 88 pylfdasvtdniayglyrsgerksnVHKKVTqaldwadLSHLAhrpakQLSGGEKQRVALTRARILSPRLLLLDEPTASM 167
Cdd:cd03221 59 -------------------------WGSTVK-------IGYFE-----QLSGGEKMRLALAKLLLENPNLLLLDEPTNHL 101
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 504819384 168 DSTAKQQtakLLQRLKDEGVTIMISSHEAHTVEHIADHHIHIEHG 212
Cdd:cd03221 102 DLESIEA---LEEALKEYPGTVILVSHDRYFLDQVATKIIELEDG 143
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
8-200 |
1.38e-24 |
|
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: 96.27 E-value: 1.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 8 KNLAITLSGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNwKQAKAYiQKDIIYLHQQ 87
Cdd:TIGR01189 4 RNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLA-EQRDEP-HENILYLGHL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 88 PYLFDA-SVTDNIAYGLYRSGERKSNVHkkvtQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTAS 166
Cdd:TIGR01189 82 PGLKPElSALENLHFWAAIHGGAQRTIE----DALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTA 157
|
170 180 190
....*....|....*....|....*....|....*
gi 504819384 167 MDSTAKQQTAKLL-QRLKDEGVTIMISSHEAHTVE 200
Cdd:TIGR01189 158 LDKAGVALLAGLLrAHLARGGIVLLTTHQDLGLVE 192
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
19-212 |
1.45e-24 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 97.39 E-value: 1.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 19 VLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNWKQ-----AKAYIQKDIIYLHQQ----PY 89
Cdd:COG4161 17 ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDFSQkpsekAIRLLRQKVGMVFQQynlwPH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 90 LfdaSVTDN-IAYGLYRSGERKSNVHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMD 168
Cdd:COG4161 97 L---TVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALD 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 504819384 169 STAKQQTAKLLQRLKDEGVTIMISSHEAHTVEHIADHHIHIEHG 212
Cdd:COG4161 174 PEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKG 217
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
16-212 |
1.90e-24 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 99.18 E-value: 1.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 16 GKLVLNIKhLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNWKQAKAYI---QKDIIYLHQQPYLF- 91
Cdd:PRK11144 11 GDLCLTVN-LTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGICLppeKRRIGYVFQDARLFp 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 92 DASVTDNIAYGLyrsgERKSNVH-KKVTQALDwadLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDST 170
Cdd:PRK11144 90 HYKVRGNLRYGM----AKSMVAQfDKIVALLG---IEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLP 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 504819384 171 AKQQTAKLLQRLKDEgVTIMI--SSHEAHTVEHIADHHIHIEHG 212
Cdd:PRK11144 163 RKRELLPYLERLARE-INIPIlyVSHSLDEILRLADRVVVLEQG 205
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
25-205 |
1.99e-24 |
|
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: 98.59 E-value: 1.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 25 LDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKP---DSASINYQG---LTLNWKQAKAYIQKDIIYLHQQPYlfdAS---- 94
Cdd:COG0444 26 FDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGedlLKLSEKELRKIRGREIQMIFQDPM---TSlnpv 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 95 --VTDNIAYGL-YRSGERKSNVHKKVTQALDWADLSHLAHRPAK---QLSGGEKQRVALTRARILSPRLLLLDEPTASMD 168
Cdd:COG0444 103 mtVGDQIAEPLrIHGGLSKAEARERAIELLERVGLPDPERRLDRyphELSGGMRQRVMIARALALEPKLLIADEPTTALD 182
|
170 180 190
....*....|....*....|....*....|....*...
gi 504819384 169 STAKQQTAKLLQRLKDE-GVTIMISSHEAHTVEHIADH 205
Cdd:COG0444 183 VTIQAQILNLLKDLQRElGLAILFITHDLGVVAEIADR 220
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
37-194 |
2.54e-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: 97.33 E-value: 2.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 37 GQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNWKQAKAYIQ---KDIIYLHQQPYLF-DASVTDNIAYGLYRSGERKSN 112
Cdd:cd03294 57 GLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElrrKKISMVFQSFALLpHRTVLENVAFGLEVQGVPRAE 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 113 VHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQQTAKLLQRLKDE-GVTIMI 191
Cdd:cd03294 137 REERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAElQKTIVF 216
|
...
gi 504819384 192 SSH 194
Cdd:cd03294 217 ITH 219
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
8-182 |
3.05e-24 |
|
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: 95.64 E-value: 3.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 8 KNLAITLSGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNwkQAKAYIQKDIIYLHQQ 87
Cdd:cd03231 4 DELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLD--FQRDSIARGLLYLGHA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 88 PYLFDA-SVTDNIAYglyrsgERKSNVHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTAS 166
Cdd:cd03231 82 PGIKTTlSVLENLRF------WHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTA 155
|
170
....*....|....*.
gi 504819384 167 MDstaKQQTAKLLQRL 182
Cdd:cd03231 156 LD---KAGVARFAEAM 168
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
2-213 |
3.20e-24 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 97.17 E-value: 3.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 2 STLVSYKNLAITLSGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNWKQAKAYIQKdI 81
Cdd:PRK10575 9 DTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARK-V 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 82 IYLHQQ-PYLFDASVTDNIAYGLY----RSGERKSNVHKKVTQALDWADLSHLAHRPAKQLSGGEKQR--VALTRARilS 154
Cdd:PRK10575 88 AYLPQQlPAAEGMTVRELVAIGRYpwhgALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRawIAMLVAQ--D 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 155 PRLLLLDEPTASMDSTAKQQTAKLLQRLKDE-GVTIMISSHEAHTVEHIADHHIHIEHGN 213
Cdd:PRK10575 166 SRCLLLDEPTSALDIAHQVDVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGE 225
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
24-212 |
4.08e-24 |
|
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: 95.25 E-value: 4.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 24 HLD--IPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNWKQAKAyiqKDIIYLHQQPYLF-DASVTDNIA 100
Cdd:cd03298 16 HFDltFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD---RPVSMLFQENNLFaHLTVEQNVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 101 YGLYRSGERKSNVHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQQTAKLLQ 180
Cdd:cd03298 93 LGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVL 172
|
170 180 190
....*....|....*....|....*....|...
gi 504819384 181 RLKDE-GVTIMISSHEAHTVEHIADHHIHIEHG 212
Cdd:cd03298 173 DLHAEtKMTVLMVTHQPEDAKRLAQRVVFLDNG 205
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
15-212 |
6.89e-24 |
|
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: 95.37 E-value: 6.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 15 SGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNwKQAKAYIQKDIIYLHQQPYLFDAS 94
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIR-DISRKSLRSMIGVVLQDTFLFSGT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 95 VTDNIAYGLYRSGERKSNVHKKVTQALDWAD------LSHLAHRpAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMD 168
Cdd:cd03254 93 IMENIRLGRPNATDEEVIEAAKEAGAHDFIMklpngyDTVLGEN-GGNLSQGERQLLAIARAMLRDPKILILDEATSNID 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 504819384 169 STAKQQTAKLLQRLKDEGVTIMIsSHEAHTVEHiADHHIHIEHG 212
Cdd:cd03254 172 TETEKLIQEALEKLMKGRTSIII-AHRLSTIKN-ADKILVLDDG 213
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
8-212 |
1.09e-23 |
|
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: 95.06 E-value: 1.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 8 KNLAITL-SGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNWKQAKAY--IQKDIIYL 84
Cdd:TIGR02315 5 ENLSKVYpNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLrkLRRRIGMI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 85 HQQPYLFD-ASVTDNIAYGlyRSGeRKSNVH-----------KKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARI 152
Cdd:TIGR02315 85 FQHYNLIErLTVLENVLHG--RLG-YKPTWRsllgrfseedkERALSALERVGLADKAYQRADQLSGGQQQRVAIARALA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504819384 153 LSPRLLLLDEPTASMDSTAKQQTAKLLQRL-KDEGVTIMISSHEAHTVEHIADHHIHIEHG 212
Cdd:TIGR02315 162 QQPDLILADEPIASLDPKTSKQVMDYLKRInKEDGITVIINLHQVDLAKKYADRIVGLKAG 222
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
5-212 |
1.22e-23 |
|
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: 94.60 E-value: 1.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 5 VSYKNLAITLSGKLVLNIKH--LDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNWKQAKAYiQKDII 82
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDisLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASL-RRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 83 YLHQQPYLFDASVTDNIAYGLYRSGE-------RKSNVHKKVTQALDWADlSHLAHRPAKqLSGGEKQRVALTRARILSP 155
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYGRPGATReeveeaaRAANAHEFIMELPEGYD-TVIGERGVK-LSGGQRQRIAIARALLKDP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 504819384 156 RLLLLDEPTASMDSTAKQQTAKLLQRLKdEGVTIMISSHEAHTVEHiADHHIHIEHG 212
Cdd:cd03251 158 PILILDEATSALDTESERLVQAALERLM-KNRTTFVIAHRLSTIEN-ADRIVVLEDG 212
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
33-212 |
1.45e-23 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 98.64 E-value: 1.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 33 TLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNWKQAKaYIQKDIIYLHQQPYLFDASVTDNIAYGL-------YR 105
Cdd:TIGR00958 510 VALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHH-YLHRQVALVGQEPVLFSGSVRENIAYGLtdtpdeeIM 588
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 106 SGERKSNVHKKVTQALDWADLSHLAHrpAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQqtakLLQRLKD- 184
Cdd:TIGR00958 589 AAAKAANAHDFIMEFPNGYDTEVGEK--GSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQ----LLQESRSr 662
|
170 180
....*....|....*....|....*...
gi 504819384 185 EGVTIMISSHEAHTVEHiADHHIHIEHG 212
Cdd:TIGR00958 663 ASRTVLLIAHRLSTVER-ADQILVLKKG 689
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
8-212 |
1.73e-23 |
|
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: 97.95 E-value: 1.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 8 KNLAITLSGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGL--LKPDSASINYQ--------------------- 64
Cdd:TIGR03269 4 KNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYHvalcekcgyverpskvgepcp 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 65 --GLTLN------WKQAKAY---IQKDIIYLHQQPYLF--DASVTDNIAYGLYRSGERKSnvhKKVTQALDWADLSHLAH 131
Cdd:TIGR03269 84 vcGGTLEpeevdfWNLSDKLrrrIRKRIAIMLQRTFALygDDTVLDNVLEALEEIGYEGK---EAVGRAVDLIEMVQLSH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 132 RP---AKQLSGGEKQRVALTRARILSPRLLLLDEPTASMD-STAKQQTAKLLQRLKDEGVTIMISSHEAHTVEHIADHHI 207
Cdd:TIGR03269 161 RIthiARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDpQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAI 240
|
....*
gi 504819384 208 HIEHG 212
Cdd:TIGR03269 241 WLENG 245
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-194 |
2.04e-23 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 94.72 E-value: 2.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 1 MSTLVSYKNLAITLSGKLVL-NIkHLDIPAHQCTLLTGQNGSGKTTLLKIMSGL--LKPD---SASINYQGLTLNWKQAK 74
Cdd:COG1117 8 LEPKIEVRNLNVYYGDKQALkDI-NLDIPENKVTALIGPSGCGKSTLLRCLNRMndLIPGarvEGEILLDGEDIYDPDVD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 75 AY-IQKDIIYLHQQPYLFDASVTDNIAYGLYRSGER-KSNVHKKVTQALD----WADLSHLAHRPAKQLSGGEKQRVALT 148
Cdd:COG1117 87 VVeLRRRVGMVFQKPNPFPKSIYDNVAYGLRLHGIKsKSELDEIVEESLRkaalWDEVKDRLKKSALGLSGGQQQRLCIA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 504819384 149 RARILSPRLLLLDEPTASMDSTAkqqTAK---LLQRLKDEgVTIMISSH 194
Cdd:COG1117 167 RALAVEPEVLLMDEPTSALDPIS---TAKieeLILELKKD-YTIVIVTH 211
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
24-212 |
2.07e-23 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 94.31 E-value: 2.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 24 HLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNWKQAKAyiQKDIIYLHQQ-----------PYLfd 92
Cdd:PRK11124 22 TLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSKTPS--DKAIRELRRNvgmvfqqynlwPHL-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 93 aSVTDNIAYGLYR-SGERKSNVHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTA 171
Cdd:PRK11124 98 -TVQQNLIEAPCRvLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEI 176
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 504819384 172 KQQTAKLLQRLKDEGVTIMISSHEAHTVEHIADHHIHIEHG 212
Cdd:PRK11124 177 TAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENG 217
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-205 |
2.13e-23 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 97.81 E-value: 2.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 1 MSTLVSYKNLAITLSGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTL-NWKQAKAyiQK 79
Cdd:PRK15439 8 APPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCaRLTPAKA--HQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 80 DIIYL-HQQPYLF-DASVTDNIAYGLYRSGERKsnvhKKVTQALdwADL-SHLA-HRPAKQLSGGEKQRVALTRARILSP 155
Cdd:PRK15439 86 LGIYLvPQEPLLFpNLSVKENILFGLPKRQASM----QKMKQLL--AALgCQLDlDSSAGSLEVADRQIVEILRGLMRDS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 504819384 156 RLLLLDEPTASMDSTAKQQTAKLLQRLKDEGVTIMISSHEAHTVEHIADH 205
Cdd:PRK15439 160 RILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADR 209
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
25-216 |
2.37e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 95.18 E-value: 2.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 25 LDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGltlnwkqakayiqkdiiylhqQPylFDASVTDNIAY--- 101
Cdd:COG4152 22 FTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDG---------------------EP--LDPEDRRRIGYlpe 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 102 --GLYRS--------------GERKSNVHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTA 165
Cdd:COG4152 79 erGLYPKmkvgeqlvylarlkGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFS 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 504819384 166 SMDSTAKQQTAKLLQRLKDEGVTIMISSHEAHTVEHIADHHIHIEHGNALI 216
Cdd:COG4152 159 GLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVL 209
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
5-228 |
3.14e-23 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 94.56 E-value: 3.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 5 VSYKNlaitlsGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNwkqaKAYIQKDIIYL 84
Cdd:PRK15056 14 VTWRN------GHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR----QALQKNLVAYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 85 HQQP---YLFDASVTDNIAYGLYRS----GERKSNVHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSPRL 157
Cdd:PRK15056 84 PQSEevdWSFPVLVEDVVMMGRYGHmgwlRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQV 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504819384 158 LLLDEPTASMDSTAKQQTAKLLQRLKDEGVTIMISSHEAHTVEHIADHHIHIEhGNALIRPPNSNNVTMIN 228
Cdd:PRK15056 164 ILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMVK-GTVLASGPTETTFTAEN 233
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
33-205 |
4.12e-23 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 93.75 E-value: 4.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 33 TLLTGQNGSGKTTLLKIMSGLLkPDSASINYQGLTLN-WKQAKAYIQKdiIYLHQQ-PYLFDASVTDNIAYGLYRSGERK 110
Cdd:COG4138 25 IHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSdWSAAELARHR--AYLSQQqSPPFAMPVFQYLALHQPAGASSE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 111 SNVH--KKVTQALDWADLshlAHRPAKQLSGGEKQRVALTRArIL--------SPRLLLLDEPTASMDSTakQQTA--KL 178
Cdd:COG4138 102 AVEQllAQLAEALGLEDK---LSRPLTQLSGGEWQRVRLAAV-LLqvwptinpEGQLLLLDEPMNSLDVA--QQAAldRL 175
|
170 180
....*....|....*....|....*...
gi 504819384 179 LQRLKDEGVTIMISSHE-AHTVEHiADH 205
Cdd:COG4138 176 LRELCQQGITVVMSSHDlNHTLRH-ADR 202
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
4-205 |
4.74e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 94.10 E-value: 4.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 4 LVSYKNLAITLSG-KLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNWKQAKAyIQKDII 82
Cdd:PRK13652 3 LIETRDLCYSYSGsKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIRE-VRKFVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 83 YLHQQP--YLFDASVTDNIAYGLYRSGERKSNVHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLL 160
Cdd:PRK13652 82 LVFQNPddQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 504819384 161 DEPTASMDSTAKQQTAKLLQRLKDE-GVTIMISSHEAHTVEHIADH 205
Cdd:PRK13652 162 DEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADY 207
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
17-192 |
8.48e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 93.13 E-value: 8.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 17 KLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNwKQAKAYIQKDIIYLHQQP--YLFDAS 94
Cdd:PRK13632 22 NNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITIS-KENLKEIRKKIGIIFQNPdnQFIGAT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 95 VTDNIAYGLYRSGERKSNVHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQQ 174
Cdd:PRK13632 101 VEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKRE 180
|
170
....*....|....*...
gi 504819384 175 TAKLLQRLKDEGVTIMIS 192
Cdd:PRK13632 181 IKKIMVDLRKTRKKTLIS 198
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
4-212 |
2.02e-22 |
|
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: 95.17 E-value: 2.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 4 LVSYKNLAITLSG--KLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQG-----LTLnwkqakAY 76
Cdd:TIGR02203 330 DVEFRNVTFRYPGrdRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGhdladYTL------AS 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 77 IQKDIIYLHQQPYLFDASVTDNIAYGlyrsgERKSNVHKKVTQALDWADLSHLA-------HRP----AKQLSGGEKQRV 145
Cdd:TIGR02203 404 LRRQVALVSQDVVLFNDTIANNIAYG-----RTEQADRAEIERALAAAYAQDFVdklplglDTPigenGVLLSGGQRQRL 478
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504819384 146 ALTRARILSPRLLLLDEPTASMDSTAKQQTAKLLQRLKDEGVTIMIsSHEAHTVEHiADHHIHIEHG 212
Cdd:TIGR02203 479 AIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVI-AHRLSTIEK-ADRIVVMDDG 543
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
9-215 |
2.72e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 92.38 E-value: 2.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 9 NLAITLSGKLVLNIKHLD-----IPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSAS--INYQGLTLNWKQAKAY--IQK 79
Cdd:PRK13645 11 NVSYTYAKKTPFEFKALNntsltFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQtiVGDYAIPANLKKIKEVkrLRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 80 DIIYLHQQP--YLFDASVTDNIAYGLYRSGERKSNVHKKVTQALDWADLSH-LAHRPAKQLSGGEKQRVALTRARILSPR 156
Cdd:PRK13645 91 EIGLVFQFPeyQLFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEdYVKRSPFELSGGQKRRVALAGIIAMDGN 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 157 LLLLDEPTASMDSTAKQQTAKLLQRL-KDEGVTIMISSHEAHTVEHIADHHIHIEHGNAL 215
Cdd:PRK13645 171 TLVLDEPTGGLDPKGEEDFINLFERLnKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVI 230
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
25-212 |
3.26e-22 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 92.94 E-value: 3.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 25 LDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASI--NYQGLT-LNWKQAKAYiQKDIIYLHQQPYLFDA-SVTDNIA 100
Cdd:PRK11153 26 LHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVlvDGQDLTaLSEKELRKA-RRQIGMIFQHFNLLSSrTVFDNVA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 101 YGLYRSGERKSNVHKKVTQALDWADLSHLAHR-PAkQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQQTAKLL 179
Cdd:PRK11153 105 LPLELAGTPKAEIKARVTELLELVGLSDKADRyPA-QLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELL 183
|
170 180 190
....*....|....*....|....*....|....
gi 504819384 180 QRLKDE-GVTIMISSHEAHTVEHIADHHIHIEHG 212
Cdd:PRK11153 184 KDINRElGLTIVLITHEMDVVKRICDRVAVIDAG 217
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
16-212 |
3.49e-22 |
|
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: 90.75 E-value: 3.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 16 GKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQG-----LTLNwkqakaYIQKDIIYLHQQPYL 90
Cdd:cd03253 13 GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGqdireVTLD------SLRRAIGVVPQDTVL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 91 FDASVTDNIAYGLYRSGE-------RKSNVHKKVTQALDWADlSHLAHRPAKqLSGGEKQRVALTRARILSPRLLLLDEP 163
Cdd:cd03253 87 FNDTIGYNIRYGRPDATDeevieaaKAAQIHDKIMRFPDGYD-TIVGERGLK-LSGGEKQRVAIARAILKNPPILLLDEA 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 504819384 164 TASMDSTAKQQTAKLLQRLKDEGVTIMIsSHEAHTVEHiADHHIHIEHG 212
Cdd:cd03253 165 TSALDTHTEREIQAALRDVSKGRTTIVI-AHRLSTIVN-ADKIIVLKDG 211
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
25-215 |
3.98e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 91.72 E-value: 3.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 25 LDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGL----TLNWKQAKAYIQK-DIIYLHQQPYLFDASVTDNI 99
Cdd:PRK13643 27 LEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIvvssTSKQKEIKPVRKKvGVVFQFPESQLFEETVLKDV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 100 AYGLYRSGERKSNVHKKVTQALDWADLS-HLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQQTAKL 178
Cdd:PRK13643 107 AFGPQNFGIPKEKAEKIAAEKLEMVGLAdEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQL 186
|
170 180 190
....*....|....*....|....*....|....*..
gi 504819384 179 LQRLKDEGVTIMISSHEAHTVEHIADHHIHIEHGNAL 215
Cdd:PRK13643 187 FESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHII 223
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-190 |
4.37e-22 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 92.98 E-value: 4.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 1 MSTLVSYKNLAITLSGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNwkQAKAYiQKD 80
Cdd:PRK11607 16 LTPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLS--HVPPY-QRP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 81 IIYLHQQPYLF-DASVTDNIAYGLYRSGERKSNVHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLL 159
Cdd:PRK11607 93 INMMFQSYALFpHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLL 172
|
170 180 190
....*....|....*....|....*....|.
gi 504819384 160 LDEPTASMDStakqqtaKLLQRLKDEGVTIM 190
Cdd:PRK11607 173 LDEPMGALDK-------KLRDRMQLEVVDIL 196
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-205 |
4.77e-22 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 91.36 E-value: 4.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 1 MSTLVSYKNLAITLSGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTL-NWKQAKAY-IQ 78
Cdd:PRK11831 4 VANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpAMSRSRLYtVR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 79 KDIIYLHQQPYLF-DASVTDNIAYGLyRSGER--KSNVHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSP 155
Cdd:PRK11831 84 KRMSMLFQSGALFtDMNVFDNVAYPL-REHTQlpAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEP 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 504819384 156 RLLLLDEPTASMDSTakqqTAKLLQRLKDE-----GVTIMISSHEAHTVEHIADH 205
Cdd:PRK11831 163 DLIMFDEPFVGQDPI----TMGVLVKLISElnsalGVTCVVVSHDVPEVLSIADH 213
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-207 |
5.79e-22 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 90.56 E-value: 5.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 1 MSTLVSYKNLAITLSGKLVLNIKHLDI-PAHQCTLLtGQNGSGKTTLLKIMSGLLKPDSASINYQGltlnwkqakayiQK 79
Cdd:PRK09544 1 MTSLVSLENVSVSFGQRRVLSDVSLELkPGKILTLL-GPNGAGKSTLVRVVLGLVAPDEGVIKRNG------------KL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 80 DIIYLHQQPYLfDASVTDNIA-YGLYRSGERKSNVhkkvTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSPRLL 158
Cdd:PRK09544 68 RIGYVPQKLYL-DTTLPLTVNrFLRLRPGTKKEDI----LPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLL 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 504819384 159 LLDEPTASMDSTAKQQTAKLLQRLKDE-GVTIMISSHEAHTVEHIAD------HHI 207
Cdd:PRK09544 143 VLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDevlclnHHI 198
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-213 |
6.97e-22 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 90.58 E-value: 6.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 1 MSTLVsYKNLAITLSGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNWKQAKAYIQKD 80
Cdd:PRK11264 1 MSAIE-VKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLSQQKGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 81 IIYLHQQ-PYLFDA-------SVTDNIAYG-LYRSGERKSNVHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRAR 151
Cdd:PRK11264 80 IRQLRQHvGFVFQNfnlfphrTVLENIIEGpVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504819384 152 ILSPRLLLLDEPTASMDSTAKQQTAKLLQRLKDEGVTIMISSHEAHTVEHIADHHIHIEHGN 213
Cdd:PRK11264 160 AMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGR 221
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
8-204 |
9.53e-22 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 92.99 E-value: 9.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 8 KNLAI-TLSGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKpdsasinYQG-LTLNWKQ----AKAYIQKDI 81
Cdd:PRK11174 353 EDLEIlSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLP-------YQGsLKINGIElrelDPESWRKHL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 82 IYLHQQPYLFDASVTDNIAYGLYRSGErksnvhKKVTQALDWADLSH--------LAHRPAKQ---LSGGEKQRVALTRA 150
Cdd:PRK11174 426 SWVGQNPQLPHGTLRDNVLLGNPDASD------EQLQQALENAWVSEflpllpqgLDTPIGDQaagLSVGQAQRLALARA 499
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 504819384 151 RILSPRLLLLDEPTASMDSTAKQQTAKLLQRLKDEGVTIMISsheaHTVEHIAD 204
Cdd:PRK11174 500 LLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVT----HQLEDLAQ 549
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-212 |
1.51e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 90.63 E-value: 1.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 1 MST-LVSYKNLAITLSGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNWKQAKAYIQK 79
Cdd:PRK13537 3 MSVaPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 80 DII--YLHQQPylfDASVTDNI-AYGLYrSGERKSNVHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSPR 156
Cdd:PRK13537 83 GVVpqFDNLDP---DFTVRENLlVFGRY-FGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 504819384 157 LLLLDEPTASMDSTAKQQTAKLLQRLKDEGVTIMISSHEAHTVEHIADHHIHIEHG 212
Cdd:PRK13537 159 VLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEG 214
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
15-212 |
1.80e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 92.05 E-value: 1.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 15 SGKLVLNIKHLD---------------IPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYqGLTLNWkqakAYIQK 79
Cdd:COG0488 311 LGKKVLELEGLSksygdktllddlslrIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVKI----GYFDQ 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 80 DIIYLHQqpylfDASVTDNIAYGlyRSGERKSNVHkkvtqaldwadlSHL---------AHRPAKQLSGGEKQRVALtrA 150
Cdd:COG0488 386 HQEELDP-----DKTVLDELRDG--APGGTEQEVR------------GYLgrflfsgddAFKPVGVLSGGEKARLAL--A 444
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504819384 151 RIL--SPRLLLLDEPTASMDSTAKQQtakLLQRLKD-EGvTIMISSHEAHTVEHIADHHIHIEHG 212
Cdd:COG0488 445 KLLlsPPNVLLLDEPTNHLDIETLEA---LEEALDDfPG-TVLLVSHDRYFLDRVATRILEFEDG 505
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-204 |
2.21e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 89.46 E-value: 2.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 2 STLVSYKNLAITLSGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKI---MSGLLKPDSA--SINYQGLTLNWKQAKAY 76
Cdd:PRK14243 8 ETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrLNDLIPGFRVegKVTFHGKNLYAPDVDPV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 77 -IQKDIIYLHQQPYLFDASVTDNIAYGL----YRsGERKSNVHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRAR 151
Cdd:PRK14243 88 eVRRRIGMVFQKPNPFPKSIYDNIAYGAringYK-GDMDELVERSLRQAALWDEVKDKLKQSGLSLSGGQQQRLCIARAI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 504819384 152 ILSPRLLLLDEPTASMDSTAKQQTAKLLQRLKdEGVTIMISSHEAHTVEHIAD 204
Cdd:PRK14243 167 AVQPEVILMDEPCSALDPISTLRIEELMHELK-EQYTIIIVTHNMQQAARVSD 218
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
35-214 |
2.42e-21 |
|
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: 88.68 E-value: 2.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 35 LTGQNGSGKTTLLKIMSGLLKPDSASINYQGltlnwKQAKAYIQKDIIYLHQQPYLFDASVTDNIAYGLYR--SGERKSN 112
Cdd:TIGR01184 16 LIGHSGCGKSTLLNLISGLAQPTSGGVILEG-----KQITEPGPDRMVVFQNYSLLPWLTVRENIALAVDRvlPDLSKSE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 113 VHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQQ-TAKLLQRLKDEGVTIMI 191
Cdd:TIGR01184 91 RRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNlQEELMQIWEEHRVTVLM 170
|
170 180
....*....|....*....|...
gi 504819384 192 SSHEAHTVEHIADHHIHIEHGNA 214
Cdd:TIGR01184 171 VTHDVDEALLLSDRVVMLTNGPA 193
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
37-195 |
2.57e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 89.41 E-value: 2.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 37 GQNGSGKTTLLKIMSGLLKPDSASINYQGLTLN----WKqakayIQKDIIYLHQQP--YLFDASVTDNIAYGLYRSGERK 110
Cdd:PRK13650 40 GHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTeenvWD-----IRHKIGMVFQNPdnQFVGATVEDDVAFGLENKGIPH 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 111 SNVHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQQTAKLLQRLKDE-GVTI 189
Cdd:PRK13650 115 EEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTV 194
|
....*.
gi 504819384 190 MISSHE 195
Cdd:PRK13650 195 ISITHD 200
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
25-205 |
3.10e-21 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 90.18 E-value: 3.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 25 LDIPAHqCTL-LTGQNGSGKTTLLKIMSGLLKPDSASINYQG---LTLNWKQAKAY---IQkdIIYlhQQPYlfdAS--- 94
Cdd:COG4608 39 FDIRRG-ETLgLVGESGCGKSTLGRLLLRLEEPTSGEILFDGqdiTGLSGRELRPLrrrMQ--MVF--QDPY---ASlnp 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 95 ---VTDNIA-----YGLYRSGERKsnvhKKVTQALDWADL--SHlAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPT 164
Cdd:COG4608 111 rmtVGDIIAeplriHGLASKAERR----ERVAELLELVGLrpEH-ADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPV 185
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 504819384 165 ASMDSTAKQQTAKLLQRLKDE-GVTIMISSHEAHTVEHIADH 205
Cdd:COG4608 186 SALDVSIQAQVLNLLEDLQDElGLTYLFISHDLSVVRHISDR 227
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-194 |
3.35e-21 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 88.41 E-value: 3.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 1 MSTLVSyKNLAITLSGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNWKQAKAYIQKD 80
Cdd:PRK10895 1 MATLTA-KNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 81 IIYLHQQPYLFDA-SVTDNIAYGL-YRSGERKSNVHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSPRLL 158
Cdd:PRK10895 80 IGYLPQEASIFRRlSVYDNLMAVLqIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFI 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 504819384 159 LLDEPTASMDSTAKQQTAKLLQRLKDEGVTIMISSH 194
Cdd:PRK10895 160 LLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDH 195
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
17-205 |
3.56e-21 |
|
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: 88.51 E-value: 3.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 17 KLVLNIKhLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNwKQAKAYIQKDIIYLHQQPYLF-DASV 95
Cdd:cd03295 15 KAVNNLN-LEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIR-EQDPVELRRKIGYVIQQIGLFpHMTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 96 TDNIAYGLYRSGERKSNVHKKVTQALDWADL--SHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQ 173
Cdd:cd03295 93 EENIALVPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALDPITRD 172
|
170 180 190
....*....|....*....|....*....|...
gi 504819384 174 QTAKLLQRLKDE-GVTIMISSHEAHTVEHIADH 205
Cdd:cd03295 173 QLQEEFKRLQQElGKTIVFVTHDIDEAFRLADR 205
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-215 |
4.03e-21 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 88.51 E-value: 4.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 1 MSTLVSYKNLAITLSGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNWKQAKAYIQKD 80
Cdd:PRK11300 2 SQPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 81 IIYLHQQPYLF-DASVTDN------------IAYGL-----YRSGERKsnvhkKVTQALDWAD---LSHLAHRPAKQLSG 139
Cdd:PRK11300 82 VVRTFQHVRLFrEMTVIENllvaqhqqlktgLFSGLlktpaFRRAESE-----ALDRAATWLErvgLLEHANRQAGNLAY 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504819384 140 GEKQRVALTRARILSPRLLLLDEPTASMDSTAKQQTAKLLQRLKDE-GVTIMISSHEAHTVEHIADHHIHIEHGNAL 215
Cdd:PRK11300 157 GQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGTPL 233
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
35-197 |
6.84e-21 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 87.56 E-value: 6.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 35 LTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNW--KQAKAYIQ-KDIIYLHQQPYLF-DASVTDNIAYGLYRSGERK 110
Cdd:PRK11629 40 IVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKlsSAAKAELRnQKLGFIYQFHHLLpDFTALENVAMPLLIGKKKP 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 111 SNVHKKVTQALDWADLSHLA-HRPAkQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQQTAKLLQRL-KDEGVT 188
Cdd:PRK11629 120 AEINSRALEMLAAVGLEHRAnHRPS-ELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELnRLQGTA 198
|
....*....
gi 504819384 189 IMISSHEAH 197
Cdd:PRK11629 199 FLVVTHDLQ 207
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
15-212 |
1.04e-20 |
|
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: 85.44 E-value: 1.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 15 SGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASInyqglTLNWKQAKAY---IQKDIIYLHQQPYLF 91
Cdd:cd03247 13 QEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEI-----TLDGVPVSDLekaLSSLISVLNQRPYLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 92 DASVTDNIAyglyrsgerksnvhkkvtqaldwadlshlahrpaKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTA 171
Cdd:cd03247 88 DTTLRNNLG----------------------------------RRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPIT 133
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 504819384 172 KQQTAKLL-QRLKDEgvTIMISSHEAHTVEHiADHHIHIEHG 212
Cdd:cd03247 134 ERQLLSLIfEVLKDK--TLIWITHHLTGIEH-MDKILFLENG 172
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
15-212 |
1.36e-20 |
|
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: 85.98 E-value: 1.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 15 SGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGltlnwkqakayiqkDIIYLHQQPYLFDAS 94
Cdd:cd03250 16 ETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG--------------SIAYVSQEPWIQNGT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 95 VTDNIAYGLYRSGERksnvHKKVTQA--LDwADLSHLAHRPAKQ-------LSGGEKQRVALTRARILSPRLLLLDEPTA 165
Cdd:cd03250 82 IRENILFGKPFDEER----YEKVIKAcaLE-PDLEILPDGDLTEigekginLSGGQKQRISLARAVYSDADIYLLDDPLS 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 504819384 166 SMDS-TAKQQTAKLLQRLKDEGVTIMISSHEAHTVEHiADHHIHIEHG 212
Cdd:cd03250 157 AVDAhVGRHIFENCILGLLLNNKTRILVTHQLQLLPH-ADQIVVLDNG 203
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-195 |
1.39e-20 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 87.38 E-value: 1.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 1 MSTLVSYKNLAITLSGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNWKQAKAYIQKD 80
Cdd:PRK09984 1 MQTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAGSHIELLGRTVQREGRLARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 81 II-------YLHQQPYLFDA-SVTDNIAYG------LYRSGERKSNVHKK--VTQALDWADLSHLAHRPAKQLSGGEKQR 144
Cdd:PRK09984 81 IRksrantgYIFQQFNLVNRlSVLENVLIGalgstpFWRTCFSWFTREQKqrALQALTRVGMVHFAHQRVSTLSGGQQQR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 504819384 145 VALTRARILSPRLLLLDEPTASMDSTAKQQTAKLLQRL-KDEGVTIMISSHE 195
Cdd:PRK09984 161 VAIARALMQQAKVILADEPIASLDPESARIVMDTLRDInQNDGITVVVTLHQ 212
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
6-212 |
1.56e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 88.35 E-value: 1.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 6 SYKNLAITLSG-------KLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLnwkQAKAYIQ 78
Cdd:PRK13536 36 SMSTVAIDLAGvsksygdKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPV---PARARLA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 79 KDIIYLHQQpylFDA-----SVTDN-IAYGLYrSGERKSNVHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARI 152
Cdd:PRK13536 113 RARIGVVPQ---FDNldlefTVRENlLVFGRY-FGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALI 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 153 LSPRLLLLDEPTASMDSTAKQQTAKLLQRLKDEGVTIMISSHEAHTVEHIADHHIHIEHG 212
Cdd:PRK13536 189 NDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAG 248
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
24-209 |
7.64e-20 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 83.70 E-value: 7.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 24 HLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNwKQAKAYIQkDIIYLHQQPYLFDA-SVTDNIAYG 102
Cdd:PRK13538 21 SFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIR-RQRDEYHQ-DLLYLGHQPGIKTElTALENLRFY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 103 LYRSGERKSNVhkkVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTA-KQQTAKLLQR 181
Cdd:PRK13538 99 QRLHGPGDDEA---LWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGvARLEALLAQH 175
|
170 180
....*....|....*....|....*...
gi 504819384 182 LKDEGVTIMiSSHeaHTVEHIADHHIHI 209
Cdd:PRK13538 176 AEQGGMVIL-TTH--QDLPVASDKVRKL 200
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
35-212 |
8.74e-20 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 83.25 E-value: 8.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 35 LTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNWKQAKAYIQKDIIYL----HQQPYLFDASVTDNIAyglyrsgerk 110
Cdd:cd03215 31 IAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIAYVpedrKREGLVLDLSVAENIA---------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 111 snvhkkvtqaldwadLSHLahrpakqLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQQTAKLLQRLKDEGVTIM 190
Cdd:cd03215 101 ---------------LSSL-------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVL 158
|
170 180
....*....|....*....|..
gi 504819384 191 ISSHEAHTVEHIADHHIHIEHG 212
Cdd:cd03215 159 LISSELDELLGLCDRILVMYEG 180
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
35-217 |
9.70e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 85.27 E-value: 9.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 35 LTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNW----KQAKAyIQKDIIYLHQQP--YLFDASVTDNIAYGLYRSGE 108
Cdd:PRK13641 38 LVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPetgnKNLKK-LRKKVSLVFQFPeaQLFENTVLKDVEFGPKNFGF 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 109 RKSNVHKKVTQALDWADLSH-LAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQQTAKLLQRLKDEGV 187
Cdd:PRK13641 117 SEDEAKEKALKWLKKVGLSEdLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGH 196
|
170 180 190
....*....|....*....|....*....|
gi 504819384 188 TIMISSHEAHTVEHIADHHIHIEHGNaLIR 217
Cdd:PRK13641 197 TVILVTHNMDDVAEYADDVLVLEHGK-LIK 225
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-194 |
1.06e-19 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 86.89 E-value: 1.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 1 MSTLVSYKNLAITLSGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNWKQAKAYIQKD 80
Cdd:PRK11288 1 SSPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 81 IIYLHQQPYLF-DASVTDNIAYGlyRSGERKSNVHKKVTQALDWADLSHLA-----HRPAKQLSGGEKQRVALTRARILS 154
Cdd:PRK11288 81 VAIIYQELHLVpEMTVAENLYLG--QLPHKGGIVNRRLLNYEAREQLEHLGvdidpDTPLKYLSIGQRQMVEIAKALARN 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 504819384 155 PRLLLLDEPTASMDSTAKQQTAKLLQRLKDEGVTIMISSH 194
Cdd:PRK11288 159 ARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSH 198
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
8-195 |
1.18e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 85.52 E-value: 1.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 8 KNLAITLSGKLVLNIKHLD-----IPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYqgLTLNWKQAKA------Y 76
Cdd:PRK13651 6 KNIVKIFNKKLPTELKALDnvsveINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEW--IFKDEKNKKKtkekekV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 77 IQKDIIylhQQPY------------------------LFDASVTDNIAYGLYRSGERKSNVHKKVTQALDWADL--SHLA 130
Cdd:PRK13651 84 LEKLVI---QKTRfkkikkikeirrrvgvvfqfaeyqLFEQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLdeSYLQ 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504819384 131 HRPAkQLSGGEKQRVALtrARILS--PRLLLLDEPTASMDSTAKQQTAKLLQRLKDEGVTIMISSHE 195
Cdd:PRK13651 161 RSPF-ELSGGQKRRVAL--AGILAmePDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHD 224
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
8-205 |
1.22e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 84.58 E-value: 1.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 8 KNLAITLSGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGL--LKPD---SASINYQGLTLnWKQAKAYIQKDII 82
Cdd:PRK14247 7 RDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLieLYPEarvSGEVYLDGQDI-FKMDVIELRRRVQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 83 YLHQQPY-LFDASVTDNIAYG--LYRSGERKSNVHKKVTQALD----WADLSHLAHRPAKQLSGGEKQRVALTRARILSP 155
Cdd:PRK14247 86 MVFQIPNpIPNLSIFENVALGlkLNRLVKSKKELQERVRWALEkaqlWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 504819384 156 RLLLLDEPTASMDSTAKQQTAKLLQRLKDEgVTIMISSHEAHTVEHIADH 205
Cdd:PRK14247 166 EVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDY 214
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
25-205 |
1.29e-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: 86.66 E-value: 1.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 25 LDIPAHQcTL-LTGQNGSGKTTLLKIMSGLLkPDSASINYQG---LTLNWKQAKAY---IQkdIIYlhQQPYlfdAS--- 94
Cdd:COG4172 307 LTLRRGE-TLgLVGESGSGKSTLGLALLRLI-PSEGEIRFDGqdlDGLSRRALRPLrrrMQ--VVF--QDPF---GSlsp 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 95 ---VTDNIAYGL--YRSGERKSNVHKKVTQALDWADLSH-LAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMD 168
Cdd:COG4172 378 rmtVGQIIAEGLrvHGPGLSAAERRARVAEALEEVGLDPaARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALD 457
|
170 180 190
....*....|....*....|....*....|....*...
gi 504819384 169 STAKQQTAKLLQRLKDE-GVTIMISSHEAHTVEHIADH 205
Cdd:COG4172 458 VSVQAQILDLLRDLQREhGLAYLFISHDLAVVRALAHR 495
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
19-212 |
1.30e-19 |
|
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: 84.47 E-value: 1.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 19 VLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGL---TLNWKQAKAYiQKDIIYLHQQ-PYLFDA- 93
Cdd:TIGR02769 26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQdlyQLDRKQRRAF-RRDVQLVFQDsPSAVNPr 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 94 -SVTDNIAYGLyRSGER--KSNVHKKVTQALDWADL--SHLAHRPAkQLSGGEKQRVALTRARILSPRLLLLDEPTASMD 168
Cdd:TIGR02769 105 mTVRQIIGEPL-RHLTSldESEQKARIAELLDMVGLrsEDADKLPR-QLSGGQLQRINIARALAVKPKLIVLDEAVSNLD 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 504819384 169 STAKQQTAKLLQRLKDE-GVTIMISSHEAHTVEHIADHHIHIEHG 212
Cdd:TIGR02769 183 MVLQAVILELLRKLQQAfGTAYLFITHDLRLVQSFCQRVAVMDKG 227
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
24-212 |
1.38e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 85.07 E-value: 1.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 24 HLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTL----NWKQAKAYIQK-DIIYLHQQPYLFDASVTDN 98
Cdd:PRK13634 27 NVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkKNKKLKPLRKKvGIVFQFPEHQLFEETVEKD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 99 IAYGLYRSGERKSNVHKKVTQALDWADLSH-LAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQQTAK 177
Cdd:PRK13634 107 ICFGPMNFGVSEEDAKQKAREMIELVGLPEeLLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMME 186
|
170 180 190
....*....|....*....|....*....|....*.
gi 504819384 178 LLQRL-KDEGVTIMISSHEAHTVEHIADHHIHIEHG 212
Cdd:PRK13634 187 MFYKLhKEKGLTTVLVTHSMEDAARYADQIVVMHKG 222
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
37-212 |
1.50e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 85.14 E-value: 1.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 37 GQNGSGKTTLLKIMSGLLKPDSASINYQGLTlNWKQAKAY---I-----QK----------DIIYLHQQPYlfdaSVTDN 98
Cdd:COG4586 55 GPNGAGKSTTIKMLTGILVPTSGEVRVLGYV-PFKRRKEFarrIgvvfgQRsqlwwdlpaiDSFRLLKAIY----RIPDA 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 99 iayglyrsgERKSNVhKKVTQALDwadLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQQTAKL 178
Cdd:COG4586 130 ---------EYKKRL-DELVELLD---LGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREF 196
|
170 180 190
....*....|....*....|....*....|....*
gi 504819384 179 LQRL-KDEGVTIMISSHEAHTVEHIADHHIHIEHG 212
Cdd:COG4586 197 LKEYnRERGTTILLTSHDMDDIEALCDRVIVIDHG 231
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-204 |
1.72e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 84.38 E-value: 1.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 9 NLAITLSGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSgLLKPDSASINYQGLTL-------NWKQAKAYiQKDI 81
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLN-RMNDKVSGYRYSGDVLlggrsifNYRDVLEF-RRRV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 82 IYLHQQPYLFDASVTDNI-----AYGLYRSGERKSNVHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSPR 156
Cdd:PRK14271 104 GMLFQRPNPFPMSIMDNVlagvrAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPE 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 504819384 157 LLLLDEPTASMDSTAKQQTAKLLQRLKDEgVTIMISSHEAHTVEHIAD 204
Cdd:PRK14271 184 VLLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISD 230
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
35-213 |
2.19e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 84.45 E-value: 2.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 35 LTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNWKQAKAY---IQKDIIYLHQQP--YLFDASVTDNIAYGLYRSGER 109
Cdd:PRK13646 38 IVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYirpVRKRIGMVFQFPesQLFEDTVEREIIFGPKNFKMN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 110 KSNVHKKVTQAL-DWADLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQQTAKLLQRLK-DEGV 187
Cdd:PRK13646 118 LDEVKNYAHRLLmDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtDENK 197
|
170 180
....*....|....*....|....*.
gi 504819384 188 TIMISSHEAHTVEHIADHHIHIEHGN 213
Cdd:PRK13646 198 TIILVSHDMNEVARYADEVIVMKEGS 223
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
35-204 |
2.42e-19 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 83.44 E-value: 2.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 35 LTGQNGSGKTTLLKIMSGLLkPDSASINYQGLTL-NWKQAKAYIQKDiiYL-HQQPYLFDASVTDNIAygLYR-SGERKS 111
Cdd:PRK03695 27 LVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLeAWSAAELARHRA--YLsQQQTPPFAMPVFQYLT--LHQpDKTRTE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 112 NVHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRA-----RILSP--RLLLLDEPTASMDSTakQQTA--KLLQRL 182
Cdd:PRK03695 102 AVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVvlqvwPDINPagQLLLLDEPMNSLDVA--QQAAldRLLSEL 179
|
170 180
....*....|....*....|...
gi 504819384 183 KDEGVTIMISSHEA-HTVEHiAD 204
Cdd:PRK03695 180 CQQGIAVVMSSHDLnHTLRH-AD 201
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
25-213 |
3.54e-19 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 82.58 E-value: 3.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 25 LDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQG-----LTLNwkqakAYIQKDiiylhqqpylfdASVTDNI 99
Cdd:cd03220 43 FEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGrvsslLGLG-----GGFNPE------------LTGRENI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 100 AYGLYRSGERKSNVHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQQTAKLL 179
Cdd:cd03220 106 YLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRL 185
|
170 180 190
....*....|....*....|....*....|....
gi 504819384 180 QRLKDEGVTIMISSHEAHTVEHIADHHIHIEHGN 213
Cdd:cd03220 186 RELLKQGKTVILVSHDPSSIKRLCDRALVLEKGK 219
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
17-194 |
3.78e-19 |
|
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: 82.70 E-value: 3.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 17 KLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLkpDSASINYQGLTLNWKQAKAYIQKDII-YLHQQPYLFDA-S 94
Cdd:cd03234 20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRV--EGGGTTSGQILFNGQPRKPDQFQKCVaYVRQDDILLPGlT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 95 VTDNIAY-GLYRSGERKSNVHKKVTqaldWAD--LSHLAHRPA-----KQLSGGEKQRVALTRARILSPRLLLLDEPTAS 166
Cdd:cd03234 98 VRETLTYtAILRLPRKSSDAIRKKR----VEDvlLRDLALTRIggnlvKGISGGERRRVSIAVQLLWDPKVLILDEPTSG 173
|
170 180
....*....|....*....|....*...
gi 504819384 167 MDSTAKQQTAKLLQRLKDEGVTIMISSH 194
Cdd:cd03234 174 LDSFTALNLVSTLSQLARRNRIVILTIH 201
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
25-213 |
3.94e-19 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 84.70 E-value: 3.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 25 LDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNWKQ-AKAYI----QKDIIYlhqqPYLfdaSVTDNI 99
Cdd:PRK11000 24 LDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPpAERGVgmvfQSYALY----PHL---SVAENM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 100 AYGLYRSGERKSNVHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQQT---- 175
Cdd:PRK11000 97 SFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMriei 176
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 504819384 176 AKLLQRLkdeGVTIMISSH---EAHTvehIADHHIHIEHGN 213
Cdd:PRK11000 177 SRLHKRL---GRTMIYVTHdqvEAMT---LADKIVVLDAGR 211
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
16-212 |
4.54e-19 |
|
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: 82.53 E-value: 4.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 16 GKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNwKQAKAYIQKDIIYLHQQPYLFDASV 95
Cdd:cd03252 14 GPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLA-LADPAWLRRQVGVVLQENVLFNRSI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 96 TDNIAyglyrSGERKSNVHkKVTQALDWADlshlAHRPAKQ---------------LSGGEKQRVALTRARILSPRLLLL 160
Cdd:cd03252 93 RDNIA-----LADPGMSME-RVIEAAKLAG----AHDFISElpegydtivgeqgagLSGGQRQRIAIARALIHNPRILIF 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 504819384 161 DEPTASMDSTAKQQTAKLLQRLKDeGVTIMISSHEAHTVEHiADHHIHIEHG 212
Cdd:cd03252 163 DEATSALDYESEHAIMRNMHDICA-GRTVIIIAHRLSTVKN-ADRIIVMEKG 212
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
9-195 |
8.60e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 81.15 E-value: 8.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 9 NLAITLSGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLnwKQAKAYIQKDIIYLHQQ- 87
Cdd:PRK13540 6 ELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI--KKDLCTYQKQLCFVGHRs 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 88 ---PYLfdaSVTDNIAYGLYrsgerKSNVHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPT 164
Cdd:PRK13540 84 ginPYL---TLRENCLYDIH-----FSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPL 155
|
170 180 190
....*....|....*....|....*....|.
gi 504819384 165 ASMDSTAKQQTAKLLQRLKDEGVTIMISSHE 195
Cdd:PRK13540 156 VALDELSLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
15-217 |
9.57e-19 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 84.38 E-value: 9.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 15 SGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNwKQAKAYIQKDIIYLHQQPYLFDAS 94
Cdd:PRK10790 352 DDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLS-SLSHSVLRQGVAMVQQDPVVLADT 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 95 VTDNIAYGLYRSGErksnvhkKVTQALDWADLSHLAH--------RPAKQ---LSGGEKQRVALTRARILSPRLLLLDEP 163
Cdd:PRK10790 431 FLANVTLGRDISEE-------QVWQALETVQLAELARslpdglytPLGEQgnnLSVGQKQLLALARVLVQTPQILILDEA 503
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 504819384 164 TASMDSTAKQQTAKLLQRLKDEGVTIMIssheAHTVEHI--ADHHIHIEHGNALIR 217
Cdd:PRK10790 504 TANIDSGTEQAIQQALAAVREHTTLVVI----AHRLSTIveADTILVLHRGQAVEQ 555
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
16-212 |
9.75e-19 |
|
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: 84.41 E-value: 9.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 16 GKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNwKQAKAYIQKDIIYLHQQPYLFDASV 95
Cdd:TIGR01193 486 GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLK-DIDRHTLRQFINYLPQEPYIFSGSI 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 96 TDNIAYGlyrsgERKSNVHKKVTQALDWADL------------SHLAHRpAKQLSGGEKQRVALTRARILSPRLLLLDEP 163
Cdd:TIGR01193 565 LENLLLG-----AKENVSQDEIWAACEIAEIkddienmplgyqTELSEE-GSSISGGQKQRIALARALLTDSKVLILDES 638
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 504819384 164 TASMDSTAKQQTAKLLQRLKDEgvTIMISSHEAhTVEHIADHHIHIEHG 212
Cdd:TIGR01193 639 TSNLDTITEKKIVNNLLNLQDK--TIIFVAHRL-SVAKQSDKIIVLDHG 684
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
20-204 |
1.04e-18 |
|
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: 84.08 E-value: 1.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 20 LNIKHLDIPAhqctlLTGQNGSGKTTLLKIMSGLLKPDSASINYQ------GLT----LNWKQAKAYIQkdiiYLHQQPY 89
Cdd:TIGR03269 305 LEVKEGEIFG-----IVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvgdewvDMTkpgpDGRGRAKRYIG----ILHQEYD 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 90 LF-DASVTDNI--AYGLYRSGE--RKSNVHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPT 164
Cdd:TIGR03269 376 LYpHRTVLDNLteAIGLELPDElaRMKAVITLKMVGFDEEKAEEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPT 455
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 504819384 165 ASMDSTAKQQTAKLLQRLKDE-GVTIMISSHEAHTVEHIAD 204
Cdd:TIGR03269 456 GTMDPITKVDVTHSILKAREEmEQTFIIVSHDMDFVLDVCD 496
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
35-195 |
1.28e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 82.06 E-value: 1.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 35 LTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNWKQAKAyIQKDIIYLHQQP--YLFDASVTDNIAYGLYRSGERKSN 112
Cdd:PRK13642 38 IIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWN-LRRKIGMVFQNPdnQFVGATVEDDVAFGMENQGIPREE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 113 VHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQQTAKLLQRLKDE-GVTIMI 191
Cdd:PRK13642 117 MIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKyQLTVLS 196
|
....
gi 504819384 192 SSHE 195
Cdd:PRK13642 197 ITHD 200
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-216 |
1.35e-18 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 81.46 E-value: 1.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 1 MSTLVSYKNLAITLSGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTL-NWKQAKAyIQK 79
Cdd:PRK11614 2 EKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDItDWQTAKI-MRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 80 DIIYLHQQPYLFD-ASVTDNIAYGLYRSgeRKSNVHKKVTQALD-WADLSHLAHRPAKQLSGGEKQRVALTRARILSPRL 157
Cdd:PRK11614 81 AVAIVPEGRRVFSrMTVEENLAMGGFFA--ERDQFQERIKWVYElFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 504819384 158 LLLDEPTASMDSTAKQQTAKLLQRLKDEGVTIMISSHEAHTVEHIADHHIHIEHGNALI 216
Cdd:PRK11614 159 LLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVL 217
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
5-194 |
2.87e-18 |
|
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: 79.52 E-value: 2.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 5 VSYKNLAITL------SGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKP--DSASINYQGLTL---NWKQA 73
Cdd:cd03213 4 LSFRNLTVTVksspskSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRPLdkrSFRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 74 KAYI-QKDIIYlhqqPYLfdasvtdniayglyrsgerksnvhkKVTQALDWAdlSHLahrpaKQLSGGEKQRVALTRARI 152
Cdd:cd03213 84 IGYVpQDDILH----PTL-------------------------TVRETLMFA--AKL-----RGLSGGERKRVSIALELV 127
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 504819384 153 LSPRLLLLDEPTASMDSTAKQQTAKLLQRLKDEGVTIMISSH 194
Cdd:cd03213 128 SNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIH 169
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
35-212 |
3.82e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 80.80 E-value: 3.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 35 LTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNWKQAKAYIQKDIIYLHQQP--YLFDASVTDNIAYGLYRSGERKSN 112
Cdd:PRK13644 33 IIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKLVGIVFQNPetQFVGRTVEEDLAFGPENLCLPPIE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 113 VHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQQTAKLLQRLKDEGVTIMIS 192
Cdd:PRK13644 113 IRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYI 192
|
170 180
....*....|....*....|
gi 504819384 193 SHEAHTVeHIADHHIHIEHG 212
Cdd:PRK13644 193 THNLEEL-HDADRIIVMDRG 211
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
5-204 |
5.43e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 80.56 E-value: 5.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 5 VSYKNLAIT-LSGKLVLNIkHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKP-------DSASINYQGLTLNWKQakay 76
Cdd:PRK13649 8 VSYTYQAGTpFEGRALFDV-NLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPtqgsvrvDDTLITSTSKNKDIKQ---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 77 IQKDIIYLHQQP--YLFDASVTDNIAYGLYRSGERKSNVHKKVTQALDWADLSH-LAHRPAKQLSGGEKQRVALTRARIL 153
Cdd:PRK13649 83 IRKKVGLVFQFPesQLFEETVLKDVAFGPQNFGVSQEEAEALAREKLALVGISEsLFEKNPFELSGGQMRRVAIAGILAM 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 504819384 154 SPRLLLLDEPTASMDSTAKQQTAKLLQRLKDEGVTIMISSHEAHTVEHIAD 204
Cdd:PRK13649 163 EPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYAD 213
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
37-212 |
6.80e-18 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 79.36 E-value: 6.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 37 GQNGSGKTTLLKIMSGLLKPDSASINYQGlTLNWkqakayiqkdiiylhqqpyLF--------DASVTDNI-----AYGL 103
Cdd:COG1134 59 GRNGAGKSTLLKLIAGILEPTSGRVEVNG-RVSA-------------------LLelgagfhpELTGRENIylngrLLGL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 104 yrsgeRKSNVHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQQTAKLLQRLK 183
Cdd:COG1134 119 -----SRKEIDEKFDEIVEFAELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELR 193
|
170 180
....*....|....*....|....*....
gi 504819384 184 DEGVTIMISSHEAHTVEHIADHHIHIEHG 212
Cdd:COG1134 194 ESGRTVIFVSHSMGAVRRLCDRAIWLEKG 222
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-204 |
1.01e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 81.37 E-value: 1.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 1 MSTLVSYKNLAITLSGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNWKQAKAYIQKD 80
Cdd:PRK09700 2 ATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 81 IIYLHQQPYLFDA-SVTDNIAYGlyRSGERK---------SNVHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRA 150
Cdd:PRK09700 82 IGIIYQELSVIDElTVLENLYIG--RHLTKKvcgvniidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKT 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 504819384 151 RILSPRLLLLDEPTASMDSTAKQQTAKLLQRLKDEGVTIMISSHEAHTVEHIAD 204
Cdd:PRK09700 160 LMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICD 213
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
37-204 |
2.40e-17 |
|
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: 80.21 E-value: 2.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 37 GQNGSGKTTLLKIMSGLLKPDSASINYQgLTLNWK-QakaYIQKDIIYLHQQpYLFDASvTDNIAYGLYRSgerksnvhk 115
Cdd:COG1245 373 GPNGIGKTTFAKILAGVLKPDEGEVDED-LKISYKpQ---YISPDYDGTVEE-FLRSAN-TDDFGSSYYKT--------- 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 116 KVTQALdwaDLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQQTAKLLQRLKDE-GVTIMISSH 194
Cdd:COG1245 438 EIIKPL---GLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENrGKTAMVVDH 514
|
170
....*....|
gi 504819384 195 EAHTVEHIAD 204
Cdd:COG1245 515 DIYLIDYISD 524
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-205 |
3.37e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 77.96 E-value: 3.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 1 MSTLVSYKNLAITLSGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSAS-----INYQGLTLNWKQAKA 75
Cdd:PRK14267 1 MKFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEArvegeVRLFGRNIYSPDVDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 76 Y-IQKDIIYLHQQPYLF-DASVTDNIAYGLYRSG--ERKSNVHKKVTQALD----WADLSHLAHRPAKQLSGGEKQRVAL 147
Cdd:PRK14267 81 IeVRREVGMVFQYPNPFpHLTIYDNVAIGVKLNGlvKSKKELDERVEWALKkaalWDEVKDRLNDYPSNLSGGQRQRLVI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 504819384 148 TRARILSPRLLLLDEPTASMDSTAKQQTAKLLQRLKDEgVTIMISSHEAHTVEHIADH 205
Cdd:PRK14267 161 ARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDY 217
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
35-204 |
3.77e-17 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 79.68 E-value: 3.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 35 LTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNWKQAKAYIQKDIIYL----HQQPYLFDASVTDNIAYGLYRSGERK 110
Cdd:COG1129 283 IAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDAIRAGIAYVpedrKGEGLVLDLSIRENITLASLDRLSRG 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 111 SNVHKK--VTQALDWADLSHL----AHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQQTAKLLQRLKD 184
Cdd:COG1129 363 GLLDRRreRALAEEYIKRLRIktpsPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAA 442
|
170 180
....*....|....*....|.
gi 504819384 185 EGVTI-MISShEAHTVEHIAD 204
Cdd:COG1129 443 EGKAViVISS-ELPELLGLSD 462
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
37-215 |
6.47e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 77.97 E-value: 6.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 37 GQNGSGKTTLLKIMSGLLKPDSASI-------------NYQGLTLNWKQAKAY--IQKDIIYLHQQP--YLFDASVTDNI 99
Cdd:PRK13631 59 GNSGSGKSTLVTHFNGLIKSKYGTIqvgdiyigdkknnHELITNPYSKKIKNFkeLRRRVSMVFQFPeyQLFKDTIEKDI 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 100 AYGLYRSGERKSNVHKKVTQALDWADL--SHLAHRPAkQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQQTAK 177
Cdd:PRK13631 139 MFGPVALGVKKSEAKKLAKFYLNKMGLddSYLERSPF-GLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQ 217
|
170 180 190
....*....|....*....|....*....|....*...
gi 504819384 178 LLQRLKDEGVTIMISSHEAHTVEHIADHHIHIEHGNAL 215
Cdd:PRK13631 218 LILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKIL 255
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
17-212 |
6.48e-17 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 77.42 E-value: 6.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 17 KLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGL---TLNWKQAKAYiQKDIIYLHQQ-PYLFD 92
Cdd:PRK10419 25 QTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEplaKLNRAQRKAF-RRDIQMVFQDsISAVN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 93 A--SVTDNIAYGL-YRSGERKSNVHKKVTQALDWADL--SHLAHRPAkQLSGGEKQRVALTRARILSPRLLLLDEPTASM 167
Cdd:PRK10419 104 PrkTVREIIREPLrHLLSLDKAERLARASEMLRAVDLddSVLDKRPP-QLSGGQLQRVCLARALAVEPKLLILDEAVSNL 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 504819384 168 DSTAKQQTAKLLQRLKDE-GVTIMISSHEAHTVEHIADHHIHIEHG 212
Cdd:PRK10419 183 DLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNG 228
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-194 |
7.10e-17 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 78.89 E-value: 7.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 1 MSTLVSYKNLAITLSGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNWKQAKAYIQKD 80
Cdd:PRK10762 1 MQALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 81 IIYLHQQPYLFDA-SVTDNIAYGlyrsgerksnvHKKVTQ--ALDW------AD-------LSHLAHRPAKQLSGGEKQR 144
Cdd:PRK10762 81 IGIIHQELNLIPQlTIAENIFLG-----------REFVNRfgRIDWkkmyaeADkllarlnLRFSSDKLVGELSIGEQQM 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 504819384 145 VALTRARILSPRLLLLDEPTASMDSTAKQQTAKLLQRLKDEGVTIMISSH 194
Cdd:PRK10762 150 VEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISH 199
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
16-207 |
1.11e-16 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 76.29 E-value: 1.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 16 GKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNWKqaKAYIQKDiiylhqqpylFDASV 95
Cdd:cd03237 11 GEFTLEVEGGSISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYK--PQYIKAD----------YEGTV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 96 TD---NIAYGLYRSGERKSNVHK--KVTQALDwadlshlahRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDST 170
Cdd:cd03237 79 RDllsSITKDFYTHPYFKTEIAKplQIEQILD---------REVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVE 149
|
170 180 190
....*....|....*....|....*....|....*...
gi 504819384 171 AKQQTAKLLQRLKDEG-VTIMISSHEAHTVEHIADHHI 207
Cdd:cd03237 150 QRLMASKVIRRFAENNeKTAFVVEHDIIMIDYLADRLI 187
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
14-204 |
1.13e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 78.17 E-value: 1.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 14 LSGKLVLNIKhLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNWKQAKAYIQKDIIYL---HQQPYL 90
Cdd:PRK15439 274 LTGEGFRNIS-LEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGLVYLpedRQSSGL 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 91 F-DASVTDNIA------YGLYRSGERKSNVHKKVTQALDwADLSHlAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEP 163
Cdd:PRK15439 353 YlDAPLAWNVCalthnrRGFWIKPARENAVLERYRRALN-IKFNH-AEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEP 430
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 504819384 164 TASMDSTAKQQTAKLLQRLKDEGVTIMISSHEAHTVEHIAD 204
Cdd:PRK15439 431 TRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMAD 471
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
3-204 |
1.34e-16 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 78.31 E-value: 1.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 3 TLVSYKNLAITLsGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQgLTLNWK-QakaYIQKDI 81
Cdd:PRK13409 339 TLVEYPDLTKKL-GDFSLEVEGGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-LKISYKpQ---YIKPDY 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 82 iylHQQPYLFDASVTDNIAYGLYRSgerksnvhkKVTQALdwaDLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLD 161
Cdd:PRK13409 414 ---DGTVEDLLRSITDDLGSSYYKS---------EIIKPL---QLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLD 478
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 504819384 162 EPTASMDSTAKQQTAKLLQRLKDE-GVTIMISSHEAHTVEHIAD 204
Cdd:PRK13409 479 EPSAHLDVEQRLAVAKAIRRIAEErEATALVVDHDIYMIDYISD 522
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
31-195 |
1.89e-16 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 75.20 E-value: 1.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 31 QCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTL---NWKQAKAYIQKDIIYLHQQPYLFDA-SVTDNIAYGLYRS 106
Cdd:PRK10584 37 ETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLhqmDEEARAKLRAKHVGFVFQSFMLIPTlNALENVELPALLR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 107 GERKSNVHKKVTQALDWADLS-HLAHRPAkQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQQTAKLLQRL-KD 184
Cdd:PRK10584 117 GESSRQSRNGAKALLEQLGLGkRLDHLPA-QLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLnRE 195
|
170
....*....|.
gi 504819384 185 EGVTIMISSHE 195
Cdd:PRK10584 196 HGTTLILVTHD 206
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
17-194 |
2.08e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 76.28 E-value: 2.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 17 KLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGL-TLN----WKqakayIQKDIIYLHQQP--Y 89
Cdd:PRK13633 23 KLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLdTSDeenlWD-----IRNKAGMVFQNPdnQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 90 LFDASVTDNIAYGLYRSGERKSNVHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDS 169
Cdd:PRK13633 98 IVATIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDP 177
|
170 180
....*....|....*....|....*.
gi 504819384 170 TAKQQTAKLLQRL-KDEGVTIMISSH 194
Cdd:PRK13633 178 SGRREVVNTIKELnKKYGITIILITH 203
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
37-215 |
2.93e-16 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 76.28 E-value: 2.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 37 GQNGSGKTTLLKIMSGLLKPDSASINYQG---LTLNWKQAKAyIQKDIIYLHQQPYlfdAS------VTDNIAYGL--YR 105
Cdd:PRK15079 54 GESGCGKSTFARAIIGLVKATDGEVAWLGkdlLGMKDDEWRA-VRSDIQMIFQDPL---ASlnprmtIGEIIAEPLrtYH 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 106 SGERKSNVHKKVTQALDWADL-SHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQQTAKLLQRLKD 184
Cdd:PRK15079 130 PKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQR 209
|
170 180 190
....*....|....*....|....*....|..
gi 504819384 185 E-GVTIMISSHEAHTVEHIADHHIHIEHGNAL 215
Cdd:PRK15079 210 EmGLSLIFIAHDLAVVKHISDRVLVMYLGHAV 241
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
35-212 |
3.26e-16 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 75.39 E-value: 3.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 35 LTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNW-----KQAKAYIQKDI---------IYLHQQPYLFDASVTDNIA 100
Cdd:PRK10619 36 IIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLvrdkdGQLKVADKNQLrllrtrltmVFQHFNLWSHMTVLENVME 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 101 YGLYRSGERKSNVHKKVTQALDWADLSHLAH-RPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQQTAKLL 179
Cdd:PRK10619 116 APIQVLGLSKQEARERAVKYLAKVGIDERAQgKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIM 195
|
170 180 190
....*....|....*....|....*....|...
gi 504819384 180 QRLKDEGVTIMISSHEAHTVEHIADHHIHIEHG 212
Cdd:PRK10619 196 QQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQG 228
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
37-213 |
4.52e-16 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 74.23 E-value: 4.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 37 GQNGSGKTTLLKIMSGLLKPDSASinyqgLTLNWKQ--AKAYIQKDIIYLHQQPYLFD-ASVTDNIAYGLYRSGERKSNV 113
Cdd:PRK10771 32 GPSGAGKSTLLNLIAGFLTPASGS-----LTLNGQDhtTTPPSRRPVSMLFQENNLFShLTVAQNIGLGLNPGLKLNAAQ 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 114 HKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQQTAKLLQRLKDE-GVTIMIS 192
Cdd:PRK10771 107 REKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQErQLTLLMV 186
|
170 180
....*....|....*....|.
gi 504819384 193 SHEAHTVEHIADHHIHIEHGN 213
Cdd:PRK10771 187 SHSLEDAARIAPRSLVVADGR 207
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-204 |
5.21e-16 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 76.40 E-value: 5.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 4 LVSYKNLAITLSGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSAS--INYQGLTLNWKQAKAYIQKDI 81
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTWDgeIYWSGSPLKASNIRDTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 82 IYLHQQPYLF-DASVTDNIAYG--LYRSGERksnvhkkvtqaLDWADLSHLAH--------------RPAKQLSGGEKQR 144
Cdd:TIGR02633 81 VIIHQELTLVpELSVAENIFLGneITLPGGR-----------MAYNAMYLRAKnllrelqldadnvtRPVGDYGGGQQQL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 145 VALTRARILSPRLLLLDEPTASMDSTAKQQTAKLLQRLKDEGVTIMISSHEAHTVEHIAD 204
Cdd:TIGR02633 150 VEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCD 209
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
27-212 |
7.28e-16 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 73.52 E-value: 7.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 27 IPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNWKQAKAYIQKD---IIYLHQQPYLFDASVTDNIAYGL 103
Cdd:cd03290 24 IPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNrysVAYAAQKPWLLNATVEENITFGS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 104 YRSGERksnvHKKVTQA---------LDWADLSHLAHRpAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQQ 174
Cdd:cd03290 104 PFNKQR----YKAVTDAcslqpdidlLPFGDQTEIGER-GINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDH 178
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 504819384 175 --TAKLLQRLKDEGVTIMISSHEAHTVEHiADHHIHIEHG 212
Cdd:cd03290 179 lmQEGILKFLQDDKRTLVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
37-204 |
1.73e-15 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 74.23 E-value: 1.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 37 GQNGSGKTTLLKIMSGLLKPDSASINYQG--LTLNWKQAKAYIQKDIIYLHQQPYlfdASVtdniayglyrsgerksNVH 114
Cdd:PRK11308 48 GESGCGKSTLARLLTMIETPTGGELYYQGqdLLKADPEAQKLLRQKIQIVFQNPY---GSL----------------NPR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 115 KKVTQALDW-----ADLSHlAHRPAKQL--------------------SGGEKQRVALTRARILSPRLLLLDEPTASMDS 169
Cdd:PRK11308 109 KKVGQILEEpllinTSLSA-AERREKALammakvglrpehydryphmfSGGQRQRIAIARALMLDPDVVVADEPVSALDV 187
|
170 180 190
....*....|....*....|....*....|....*.
gi 504819384 170 TAKQQTAKLLQRLKDE-GVTIMISSHEAHTVEHIAD 204
Cdd:PRK11308 188 SVQAQVLNLMMDLQQElGLSYVFISHDLSVVEHIAD 223
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
35-205 |
1.78e-15 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 74.83 E-value: 1.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 35 LTGQNGSGKTTLLKIMSGLLKPDS--ASINYQGLTLNWKQAKAYIQKDIIYLHQQ----PYLfdaSVTDNIAYGlyrsGE 108
Cdd:NF040905 32 LCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGEVCRFKDIRDSEALGIVIIHQElaliPYL---SIAENIFLG----NE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 109 RKSN-------VHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRAriLSP--RLLLLDEPTASMDSTAKQQTAKLL 179
Cdd:NF040905 105 RAKRgvidwneTNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKA--LSKdvKLLILDEPTAALNEEDSAALLDLL 182
|
170 180
....*....|....*....|....*.
gi 504819384 180 QRLKDEGVTIMISSHEAHTVEHIADH 205
Cdd:NF040905 183 LELKAQGITSIIISHKLNEIRRVADS 208
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
37-203 |
2.12e-15 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 74.59 E-value: 2.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 37 GQNGSGKTTLLKIMSGLLKPdsasinYQGltlnwkqaKAYIQKDII--YLHQQPYLfDAS--VTDNIAYGLyrsGERKSN 112
Cdd:TIGR03719 38 GLNGAGKSTLLRIMAGVDKD------FNG--------EARPQPGIKvgYLPQEPQL-DPTktVRENVEEGV---AEIKDA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 113 VHK-----------------------KVTQALDWADLSHLAHR---------------PAKQLSGGEKQRVALTRARILS 154
Cdd:TIGR03719 100 LDRfneisakyaepdadfdklaaeqaELQEIIDAADAWDLDSQleiamdalrcppwdaDVTKLSGGERRRVALCRLLLSK 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 504819384 155 PRLLLLDEPTASMDStakQQTAKLLQRLKDEGVTIMISSHEAHTVEHIA 203
Cdd:TIGR03719 180 PDMLLLDEPTNHLDA---ESVAWLERHLQEYPGTVVAVTHDRYFLDNVA 225
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-204 |
3.16e-15 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 74.20 E-value: 3.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 1 MSTLVSYKNLAITLSGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLkPD---SASINYQGLTLNWKQAKAYI 77
Cdd:PRK13549 2 MEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEELQASNIRDTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 78 QKDIIYLHQQ----PYLfdaSVTDNIAYG--LYRSGERKSN-VHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRA 150
Cdd:PRK13549 81 RAGIAIIHQElalvKEL---SVLENIFLGneITPGGIMDYDaMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 504819384 151 RILSPRLLLLDEPTASMdsTAKqQTAKLL---QRLKDEGVTIMISSHEAHTVEHIAD 204
Cdd:PRK13549 158 LNKQARLLILDEPTASL--TES-ETAVLLdiiRDLKAHGIACIYISHKLNEVKAISD 211
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
25-212 |
4.12e-15 |
|
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: 73.70 E-value: 4.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 25 LDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASI-----NYQGLTLnwkqakAYIQKDIIYLHQQPYLFDASVTDNI 99
Cdd:COG5265 379 FEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRIlidgqDIRDVTQ------ASLRAAIGIVPQDTVLFNDTIAYNI 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 100 AYGlyrsgeRKSNVHKKVTQAldwADLSHLAH---------------RPAKqLSGGEKQRVALTRArIL-SPRLLLLDEP 163
Cdd:COG5265 453 AYG------RPDASEEEVEAA---ARAAQIHDfieslpdgydtrvgeRGLK-LSGGEKQRVAIART-LLkNPPILIFDEA 521
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 504819384 164 TASMDSTAKQ--QTAklLQRLKDEGVTIMIssheAH---TVEHiADHHIHIEHG 212
Cdd:COG5265 522 TSALDSRTERaiQAA--LREVARGRTTLVI----AHrlsTIVD-ADEILVLEAG 568
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
31-221 |
4.63e-15 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 72.01 E-value: 4.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 31 QCTLLTGQNGSGKTTLLKIMSGLLKP-----------DSASINYQGLTLN--WKQAKAYIQKDII---YLHQQPYLFDAS 94
Cdd:cd03236 27 QVLGLVGPNGIGKSTALKILAGKLKPnlgkfddppdwDEILDEFRGSELQnyFTKLLEGDVKVIVkpqYVDLIPKAVKGK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 95 VTDNiaygLYRSGERksNVHKKVTQALDwadLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQQ 174
Cdd:cd03236 107 VGEL----LKKKDER--GKLDELVDQLE---LRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLN 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 504819384 175 TAKLLQRLKDEGVTIMISSHEAHTVEHIADhHIHIEHGNA----LIRPPNS 221
Cdd:cd03236 178 AARLIRELAEDDNYVLVVEHDLAVLDYLSD-YIHCLYGEPgaygVVTLPKS 227
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
35-195 |
6.13e-15 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 73.16 E-value: 6.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 35 LTGQNGSGKTTLLKIMSGLLKPD---SASINYQGLTLNWKQAK---AYIQKDIIY---LHQQPYL-FDASVtdniaygly 104
Cdd:TIGR00955 56 VMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDAKEMRaisAYVQQDDLFiptLTVREHLmFQAHL--------- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 105 RSGERKSNVHKK--VTQALDWADLSHLAH------RPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQQTA 176
Cdd:TIGR00955 127 RMPRRVTKKEKRerVDEVLQALGLRKCANtrigvpGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVV 206
|
170
....*....|....*....
gi 504819384 177 KLLQRLKDEGVTIMISSHE 195
Cdd:TIGR00955 207 QVLKGLAQKGKTIICTIHQ 225
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
19-213 |
1.10e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 72.55 E-value: 1.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 19 VLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASInyqglTLNWKQAKAYIQKD----IIYLHQQPYLFDAS 94
Cdd:PRK11160 355 VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEI-----LLNGQPIADYSEAAlrqaISVVSQRVHLFSAT 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 95 VTDNIAYGLYRSGErksnvhKKVTQALDWADLSHLAHRPA----------KQLSGGEKQRVALTRARILSPRLLLLDEPT 164
Cdd:PRK11160 430 LRDNLLLAAPNASD------EALIEVLQQVGLEKLLEDDKglnawlgeggRQLSGGEQRRLGIARALLHDAPLLLLDEPT 503
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 504819384 165 ASMDSTAKQQTAKLLQRLKDEGVTIMIsSHEAHTVE-----HIADHHIHIEHGN 213
Cdd:PRK11160 504 EGLDAETERQILELLAEHAQNKTVLMI-THRLTGLEqfdriCVMDNGQIIEQGT 556
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
5-212 |
1.46e-14 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 72.36 E-value: 1.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 5 VSYKNLAITLSGKLVLNIKH--LDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNwKQAKAYIQKDII 82
Cdd:PRK11176 342 IEFRNVTFTYPGKEVPALRNinFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLR-DYTLASLRNQVA 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 83 YLHQQPYLFDASVTDNIAYGLYRSGERKSNVHK-KVTQALDWadLSHLAH-------RPAKQLSGGEKQRVALTRARILS 154
Cdd:PRK11176 421 LVSQNVHLFNDTIANNIAYARTEQYSREQIEEAaRMAYAMDF--INKMDNgldtvigENGVLLSGGQRQRIAIARALLRD 498
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 504819384 155 PRLLLLDEPTASMDSTAKQQTAKLLQRL-KDEgvTIMISSHEAHTVEHiADHHIHIEHG 212
Cdd:PRK11176 499 SPILILDEATSALDTESERAIQAALDELqKNR--TSLVIAHRLSTIEK-ADEILVVEDG 554
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-205 |
1.59e-14 |
|
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: 72.02 E-value: 1.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 1 MSTLVSYKNL--AITLSGKLVLNIKH--LDIPAHQCTLLTGQNGSGKT-TLLKIMsGLLkPDSA-----SINYQG---LT 67
Cdd:COG4172 3 SMPLLSVEDLsvAFGQGGGTVEAVKGvsFDIAAGETLALVGESGSGKSvTALSIL-RLL-PDPAahpsgSILFDGqdlLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 68 LNWKQAKAYIQKDIIYLHQQPY-----LFdaSVTDNIAYGLyrsgerksNVHKKVT------QALDWADLSHL--AHRPA 134
Cdd:COG4172 81 LSERELRRIRGNRIAMIFQEPMtslnpLH--TIGKQIAEVL--------RLHRGLSgaaaraRALELLERVGIpdPERRL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504819384 135 K----QLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQQTAKLLQRLKDE-GVTIMISSHEAHTVEHIADH 205
Cdd:COG4172 151 DayphQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRElGMALLLITHDLGVVRRFADR 226
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
5-199 |
1.83e-14 |
|
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: 69.83 E-value: 1.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 5 VSYKNLAITLSGKLVLNIKHL--DIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNwKQAKAYIQKDII 82
Cdd:cd03244 3 IEFKNVSLRYRPNLPPVLKNIsfSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDIS-KIGLHDLRSRIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 83 YLHQQPYLFDASVTDNIA-YGLYRSGERKS---NVH-KKVTQALDWADLSHLAHRPaKQLSGGEKQRVALTRARILSPRL 157
Cdd:cd03244 82 IIPQDPVLFSGTIRSNLDpFGEYSDEELWQaleRVGlKEFVESLPGGLDTVVEEGG-ENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 504819384 158 LLLDEPTASMDStakqQTAKLLQRLKDE---GVTIMISSHEAHTV 199
Cdd:cd03244 161 LVLDEATASVDP----ETDALIQKTIREafkDCTVLTIAHRLDTI 201
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
37-168 |
2.32e-14 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 71.69 E-value: 2.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 37 GQNGSGKTTLLKIMSGLLKPdsasinYQGltlnwkqaKAYIQKDII--YLHQQPYLfDAS--VTDNIAYGLyrsGERKSN 112
Cdd:PRK11819 40 GLNGAGKSTLLRIMAGVDKE------FEG--------EARPAPGIKvgYLPQEPQL-DPEktVRENVEEGV---AEVKAA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 113 VHK-----------------------KVTQALDWADLSHLAHR---------------PAKQLSGGEKQRVALTRARILS 154
Cdd:PRK11819 102 LDRfneiyaayaepdadfdalaaeqgELQEIIDAADAWDLDSQleiamdalrcppwdaKVTKLSGGERRRVALCRLLLEK 181
|
170
....*....|....
gi 504819384 155 PRLLLLDEPTASMD 168
Cdd:PRK11819 182 PDMLLLDEPTNHLD 195
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
8-209 |
2.66e-14 |
|
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: 69.09 E-value: 2.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 8 KNLAITLSGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGL--LKPDSASINYQGltlnwkqakayiqKDIIylh 85
Cdd:cd03217 4 KDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKG-------------EDIT--- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 86 qqpylfDASVTDNIAYGLYRSGERKSNVHK-KVTQALDWADLShlahrpakqLSGGEKQRVALTRARILSPRLLLLDEPT 164
Cdd:cd03217 68 ------DLPPEERARLGIFLAFQYPPEIPGvKNADFLRYVNEG---------FSGGEKKRNEILQLLLLEPDLAILDEPD 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 504819384 165 ASMDSTAKQQTAKLLQRLKDEGVTIMISSHEAHTVEHIADHHIHI 209
Cdd:cd03217 133 SGLDIDALRLVAEVINKLREEGKSVLIITHYQRLLDYIKPDRVHV 177
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
25-216 |
3.31e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 69.73 E-value: 3.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 25 LDIPAHQ-CTLLtGQNGSGKTTLLKIMSGLLKPDSASINYQG--LTlNWKQAKayIQKDIIYLHQQPYL---FDASVTDN 98
Cdd:COG1101 27 LTIEEGDfVTVI-GSNGAGKSTLLNAIAGSLPPDSGSILIDGkdVT-KLPEYK--RAKYIGRVFQDPMMgtaPSMTIEEN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 99 IAYGLYRSGER--KSNVHKKVTQ----ALDWADLShLAHR---PAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDS 169
Cdd:COG1101 103 LALAYRRGKRRglRRGLTKKRRElfreLLATLGLG-LENRldtKVGLLSGGQRQALSLLMATLTKPKLLLLDEHTAALDP 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 504819384 170 takqQTAKLLQRLKDEGV------TIMISsheahtvehiadHHIH--IEHGNALI 216
Cdd:COG1101 182 ----KTAALVLELTEKIVeennltTLMVT------------HNMEqaLDYGNRLI 220
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
37-212 |
3.37e-14 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 70.97 E-value: 3.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 37 GQNGSGKTTLLKIMSGLLKP------DSASIN-----YQGltlnwKQAKAYIQK----------DIIYLHQQPYLFDASV 95
Cdd:COG1245 106 GPNGIGKSTALKILSGELKPnlgdydEEPSWDevlkrFRG-----TELQDYFKKlangeikvahKPQYVDLIPKVFKGTV 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 96 TDNiaygLYRSGERKsnVHKKVTQALDwadLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQQT 175
Cdd:COG1245 181 REL----LEKVDERG--KLDELAEKLG---LENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNV 251
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 504819384 176 AKLLQRLKDEGVTIMIssheahtVEH-------IADhHIHIEHG 212
Cdd:COG1245 252 ARLIRELAEEGKYVLV-------VEHdlaildyLAD-YVHILYG 287
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
19-223 |
3.90e-14 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 70.91 E-value: 3.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 19 VLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQG---LTLNWKQAKAYIQKDIIYLHQQPYLFD-AS 94
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGqdvATLDADALAQLRREHFGFIFQRYHLLShLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 95 VTDNIAY-GLYRSGERKSNVHKKVT--QALDWADLSHlaHRPAkQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTA 171
Cdd:PRK10535 103 AAQNVEVpAVYAGLERKQRLLRAQEllQRLGLEDRVE--YQPS-QLSGGQQQRVSIARALMNGGQVILADEPTGALDSHS 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 504819384 172 KQQTAKLLQRLKDEGVTIMISSHEAHtVEHIADHHIHIEHGNALIRPPNSNN 223
Cdd:PRK10535 180 GEEVMAILHQLRDRGHTVIIVTHDPQ-VAAQAERVIEIRDGEIVRNPPAQEK 230
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
14-212 |
4.20e-14 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 70.96 E-value: 4.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 14 LSGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASInyqgltlnWKQakayiqKDIIYLHQQPYLFDA 93
Cdd:PTZ00243 670 LEPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV--------WAE------RSIAYVPQQAWIMNA 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 94 SVTDNIaygLYRSGERKSNVHKKVTQALDWADLSHLAH-------RPAKQLSGGEKQRVALTRARILSPRLLLLDEPTAS 166
Cdd:PTZ00243 736 TVRGNI---LFFDEEDAARLADAVRVSQLEADLAQLGGgleteigEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSA 812
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 504819384 167 MDSTAKQQTAK--LLQRLKdeGVTIMISSHEAHTVEHiADHHIHIEHG 212
Cdd:PTZ00243 813 LDAHVGERVVEecFLGALA--GKTRVLATHQVHVVPR-ADYVVALGDG 857
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
5-212 |
4.90e-14 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 70.81 E-value: 4.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 5 VSYKNLAITL--SGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQG--LTLNWKQAKAYI--- 77
Cdd:TIGR01257 929 VCVKNLVKIFepSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGkdIETNLDAVRQSLgmc 1008
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 78 -QKDIIYLHqqpylfdASVTDNIAYGLYRSGERKSNVHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSPR 156
Cdd:TIGR01257 1009 pQHNILFHH-------LTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAK 1081
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 504819384 157 LLLLDEPTASMDSTAKQQTAKLLQRLKdEGVTIMISSHEAHTVEHIADHHIHIEHG 212
Cdd:TIGR01257 1082 VVVLDEPTSGVDPYSRRSIWDLLLKYR-SGRTIIMSTHHMDEADLLGDRIAIISQG 1136
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
35-201 |
5.35e-14 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 70.83 E-value: 5.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 35 LTGQNGSGKTTLLKIMSGLLKPDSASI------NYQGLTLNWKQAKayiqkdIIYLHQQPYLFDASVTDNIAYGLY---- 104
Cdd:PTZ00265 416 FVGESGCGKSTILKLIERLYDPTEGDIiindshNLKDINLKWWRSK------IGVVSQDPLLFSNSIKNNIKYSLYslkd 489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 105 ---------------RSGERKSNVHKK--------VTQALDWADLSH--------------------------------- 128
Cdd:PTZ00265 490 lealsnyynedgndsQENKNKRNSCRAkcagdlndMSNTTDSNELIEmrknyqtikdsevvdvskkvlihdfvsalpdky 569
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504819384 129 --LAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQQTAKLLQRLK--DEGVTIMIsSHEAHTVEH 201
Cdd:PTZ00265 570 etLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITIII-AHRLSTIRY 645
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
25-204 |
6.43e-14 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 70.14 E-value: 6.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 25 LDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNWKQAKAYIQKDIIYLHQQPYLF-DASVTDNIAYGL 103
Cdd:PRK10982 19 LKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGISMVHQELNLVlQRSVMDNMWLGR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 104 YrsgERKSNV--HKKV---TQAL-DWADLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQQTAK 177
Cdd:PRK10982 99 Y---PTKGMFvdQDKMyrdTKAIfDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNHLFT 175
|
170 180
....*....|....*....|....*..
gi 504819384 178 LLQRLKDEGVTIMISSHEAHTVEHIAD 204
Cdd:PRK10982 176 IIRKLKERGCGIVYISHKMEEIFQLCD 202
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
35-195 |
6.61e-14 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 70.36 E-value: 6.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 35 LTGQNGSGKTTLLKIMSGLLKPDSASInYQGLTLnwkqakayiqkDIIYLHQQPYLFDA--SVTDNIAYGlyrsgerKSN 112
Cdd:PRK11147 350 LIGPNGCGKTTLLKLMLGQLQADSGRI-HCGTKL-----------EVAYFDQHRAELDPekTVMDNLAEG-------KQE 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 113 VhkkVTQALDWADLSHL---------AHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDStakqQTAKLLQRLK 183
Cdd:PRK11147 411 V---MVNGRPRHVLGYLqdflfhpkrAMTPVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDV----ETLELLEELL 483
|
170
....*....|....
gi 504819384 184 DE--GvTIMISSHE 195
Cdd:PRK11147 484 DSyqG-TVLLVSHD 496
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
25-215 |
6.85e-14 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 70.06 E-value: 6.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 25 LDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGL---TLNWKQAKAYIQKDIIYLHQQPYLF-DASVTDNIA 100
Cdd:PRK10070 49 LAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVdiaKISDAELREVRRKKIAMVFQSFALMpHMTVLDNTA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 101 YGLYRSGERKSNVHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQQTAKLLQ 180
Cdd:PRK10070 129 FGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELV 208
|
170 180 190
....*....|....*....|....*....|....*.
gi 504819384 181 RLK-DEGVTIMISSHEAHTVEHIADHHIHIEHGNAL 215
Cdd:PRK10070 209 KLQaKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVV 244
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
35-212 |
1.75e-13 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 68.83 E-value: 1.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 35 LTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNwKQAKAYIQKDIIYLHQQPYLFDASVTDNIAYG--------LYRS 106
Cdd:PRK13657 366 IVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIR-TVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGrpdatdeeMRAA 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 107 GERksnvhkkvTQALDWadlshLAHRPAK----------QLSGGEKQRVALTRARILSPRLLLLDEPTASMDST--AKQQ 174
Cdd:PRK13657 445 AER--------AQAHDF-----IERKPDGydtvvgergrQLSGGERQRLAIARALLKDPPILILDEATSALDVEteAKVK 511
|
170 180 190
....*....|....*....|....*....|....*...
gi 504819384 175 TAklLQRLKdEGVTIMISSHEAHTVEHiADHHIHIEHG 212
Cdd:PRK13657 512 AA--LDELM-KGRTTFIIAHRLSTVRN-ADRILVFDNG 545
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
16-194 |
2.69e-13 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 68.59 E-value: 2.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 16 GKLVLNIKHLDIPAHQ--------CTLLTGQ-------NGSGKTTLLKIMSGLLKPDSASINYQGLTL------NWKQAK 74
Cdd:PRK10789 312 GELDVNIRQFTYPQTDhpalenvnFTLKPGQmlgicgpTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLtklqldSWRSRL 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 75 AYIQkdiiylhQQPYLFDASVTDNIAYGLYRSGE-------RKSNVHKKVTQaLDWADLSHLAHRpAKQLSGGEKQRVAL 147
Cdd:PRK10789 392 AVVS-------QTPFLFSDTVANNIALGRPDATQqeiehvaRLASVHDDILR-LPQGYDTEVGER-GVMLSGGQKQRISI 462
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 504819384 148 TRARILSPRLLLLDEPTASMDSTAKQQtakLLQRLKD--EGVTIMISSH 194
Cdd:PRK10789 463 ARALLLNAEILILDDALSAVDGRTEHQ---ILHNLRQwgEGRTVIISAH 508
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
37-194 |
2.74e-13 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 67.26 E-value: 2.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 37 GQNGSGKTTLLKIMSGLLKPDSASINYQG--------LTLNWKQAKAYIQKDIIYLHQQP---YLFDASVTDNIAYGLYR 105
Cdd:PRK11701 39 GESGSGKTTLLNALSARLAPDAGEVHYRMrdgqlrdlYALSEAERRRLLRTEWGFVHQHPrdgLRMQVSAGGNIGERLMA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 106 SGERksNVHKKVTQALDW-----ADLSHLAHRPAkQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQQTAKLLQ 180
Cdd:PRK11701 119 VGAR--HYGDIRATAGDWlerveIDAARIDDLPT-TFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLR 195
|
170
....*....|....*
gi 504819384 181 RLKDE-GVTIMISSH 194
Cdd:PRK11701 196 GLVRElGLAVVIVTH 210
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
8-213 |
4.72e-13 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 66.55 E-value: 4.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 8 KNLAITLSGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNWKQAKAYIQKDIIYLHQQ 87
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 88 PYLFDASVTDNIAYGLYR-----SGERKSNvHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDE 162
Cdd:PRK10253 91 TTPGDITVQELVARGRYPhqplfTRWRKED-EEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 504819384 163 PTASMDSTAKQQTAKLLQRL-KDEGVTIMISSHEAHTVEHIADHHIHIEHGN 213
Cdd:PRK10253 170 PTTWLDISHQIDLLELLSELnREKGYTLAAVLHDLNQACRYASHLIALREGK 221
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
25-194 |
4.96e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 65.75 E-value: 4.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 25 LDIPAHQCTLLTGQNGSGKTTLLKIMSGLLK--PDSASINyqgltlnwkqakayIQKDIIYLhqqpylfDASVTDNIAyg 102
Cdd:COG2401 51 LEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVD--------------VPDNQFGR-------EASLIDAIG-- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 103 lyrsgeRKSNVHKKVtQALDWADLS--HLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQQTAKLLQ 180
Cdd:COG2401 108 ------RKGDFKDAV-ELLNAVGLSdaVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQ 180
|
170
....*....|....*
gi 504819384 181 RL-KDEGVTIMISSH 194
Cdd:COG2401 181 KLaRRAGITLVVATH 195
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
25-182 |
6.01e-13 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 67.18 E-value: 6.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 25 LDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNWKQAKayiQKDI--------IYLHQqpylfdaSVT 96
Cdd:PRK11650 25 LDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPA---DRDIamvfqnyaLYPHM-------SVR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 97 DNIAYGLYRSGERKSNVHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDstakqqtA 176
Cdd:PRK11650 95 ENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD-------A 167
|
170
....*....|...
gi 504819384 177 KL-------LQRL 182
Cdd:PRK11650 168 KLrvqmrleIQRL 180
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
86-200 |
6.29e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 67.75 E-value: 6.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 86 QQPYLFDASVTDNIAYGlyrsgeRKSNVHKKVTQALDWADLSHLAHR----------P-AKQLSGGEKQRVALTRARILS 154
Cdd:PTZ00265 1303 QEPMLFNMSIYENIKFG------KEDATREDVKRACKFAAIDEFIESlpnkydtnvgPyGKSLSGGQKQRIAIARALLRE 1376
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 504819384 155 PRLLLLDEPTASMDSTAKQQTAKLLQRLKDEG-VTIMISSHEAHTVE 200
Cdd:PTZ00265 1377 PKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdKTIITIAHRIASIK 1423
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
8-209 |
1.35e-12 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 64.97 E-value: 1.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 8 KNLAITLSGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGllKPD----SASINYQGLTLN----WKQAKAYIqk 79
Cdd:TIGR01978 4 KDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAG--HPSyevtSGTILFKGQDLLelepDERARAGL-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 80 diiYLHQQPYLFDASVTDNI----AYGLYRSGERK-----SNVHKKVTQALDWADLS-HLAHRPAKQ-LSGGEKQRVALT 148
Cdd:TIGR01978 80 ---FLAFQYPEEIPGVSNLEflrsALNARRSARGEepldlLDFEKLLKEKLALLDMDeEFLNRSVNEgFSGGEKKRNEIL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504819384 149 RARILSPRLLLLDEPTASMDSTAKQQTAKLLQRLKDEGVTIMISSHEAHTVEHIADHHIHI 209
Cdd:TIGR01978 157 QMALLEPKLAILDEIDSGLDIDALKIVAEGINRLREPDRSFLIITHYQRLLNYIKPDYVHV 217
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
131-212 |
1.59e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 66.27 E-value: 1.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 131 HRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQQTAKLLQRLKDE-GVTIMISSHEAHTVEHIADHHIHI 209
Cdd:PRK15134 420 HRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKhQLAYLFISHDLHVVRALCHQVIVL 499
|
...
gi 504819384 210 EHG 212
Cdd:PRK15134 500 RQG 502
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
10-185 |
1.63e-12 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 65.23 E-value: 1.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 10 LAITLSGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLL----KPDSASINyQGLTLNWKQAKAYIQKDIIYLH 85
Cdd:PRK13547 7 LHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLtgggAPRGARVT-GDVTLNGEPLAAIDAPRLARLR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 86 ------QQPyLFDASVTDNIAYGLY----RSGERKSNVHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRA----- 150
Cdd:PRK13547 86 avlpqaAQP-AFAFSAREIVLLGRYpharRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVlaqlw 164
|
170 180 190
....*....|....*....|....*....|....*....
gi 504819384 151 ----RILSPRLLLLDEPTASMDSTAKQQTAKLLQRLKDE 185
Cdd:PRK13547 165 pphdAAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARD 203
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
25-195 |
1.65e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 66.13 E-value: 1.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 25 LDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQgltlnwkqakayiqKDIIY--LHQQPYLFDA-SVTDNIAY 101
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYE--------------QDLIVarLQQDPPRNVEgTVYDFVAE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 102 GLYRSGERKSNVHK------------------KVTQALDWADLSHL--------------AHRPAKQLSGGEKQRVALTR 149
Cdd:PRK11147 90 GIEEQAEYLKRYHDishlvetdpseknlnelaKLQEQLDHHNLWQLenrinevlaqlgldPDAALSSLSGGWLRKAALGR 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 504819384 150 ARILSPRLLLLDEPTASMDSTAKQQtakLLQRLKDEGVTIMISSHE 195
Cdd:PRK11147 170 ALVSNPDVLLLDEPTNHLDIETIEW---LEGFLKTFQGSIIFISHD 212
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
37-212 |
1.79e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 65.99 E-value: 1.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 37 GQNGSGKTTLLKIMSGLLKP------DSASIN-----YQGLTL-NW------KQAKAyIQKdIIYLHQQPYLFDASVTDN 98
Cdd:PRK13409 106 GPNGIGKTTAVKILSGELIPnlgdyeEEPSWDevlkrFRGTELqNYfkklynGEIKV-VHK-PQYVDLIPKVFKGKVREL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 99 iaygLYRSGERKsnVHKKVTQALDwadLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQQTAKL 178
Cdd:PRK13409 184 ----LKKVDERG--KLDEVVERLG---LENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARL 254
|
170 180 190
....*....|....*....|....*....|....
gi 504819384 179 LQRLKdEGVTIMISSHEAHTVEHIADhHIHIEHG 212
Cdd:PRK13409 255 IRELA-EGKYVLVVEHDLAVLDYLAD-NVHIAYG 286
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
8-209 |
1.95e-12 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 64.32 E-value: 1.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 8 KNLAITLSGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGL--LKPDSASINYQG--LTlNW---KQAKAyiqkD 80
Cdd:COG0396 4 KNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGedIL-ELspdERARA----G 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 81 IIYLHQQPYLFDA-SVTD--NIAYGLyRSGERKSNV--HKKVTQALDWADLSH-LAHRPAKQ-LSGGEKQRVALTRARIL 153
Cdd:COG0396 79 IFLAFQYPVEIPGvSVSNflRTALNA-RRGEELSARefLKLLKEKMKELGLDEdFLDRYVNEgFSGGEKKRNEILQMLLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 504819384 154 SPRLLLLDEPTASMDSTAKQQTAKLLQRLKDEGVTIMISSHEAHTVEHIADHHIHI 209
Cdd:COG0396 158 EPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITHYQRILDYIKPDFVHV 213
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
35-205 |
1.97e-12 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 65.31 E-value: 1.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 35 LTGQNGSGKTTLLKIMSGLLKP------DSASINYQGLT-LNWKQAKAYIQKDIIYLHQQP--YLfDASVT--------- 96
Cdd:COG4170 38 LVGESGSGKSLIAKAICGITKDnwhvtaDRFRWNGIDLLkLSPRERRKIIGREIAMIFQEPssCL-DPSAKigdqlieai 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 97 DNIAYGLY---RSGERKSNV-----------HKKVTQALDWadlshlahrpakQLSGGEKQRVALTRARILSPRLLLLDE 162
Cdd:COG4170 117 PSWTFKGKwwqRFKWRKKRAiellhrvgikdHKDIMNSYPH------------ELTEGECQKVMIAMAIANQPRLLIADE 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 504819384 163 PTASMDSTAKQQTAKLLQRL-KDEGVTIMISSHEAHTVEHIADH 205
Cdd:COG4170 185 PTNAMESTTQAQIFRLLARLnQLQGTSILLISHDLESISQWADT 228
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
14-191 |
2.61e-12 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 65.42 E-value: 2.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 14 LSGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASI--NYQGLT-LNWKQAKAYIQKDiiylhqqpyl 90
Cdd:PRK10938 13 LSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERqsQFSHITrLSFEQLQKLVSDE---------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 91 FDASVTDNIAYGLYRSGERKSNV----HKKVTQALDWADL---SHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEP 163
Cdd:PRK10938 83 WQRNNTDMLSPGEDDTGRTTAEIiqdeVKDPARCEQLAQQfgiTALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEP 162
|
170 180
....*....|....*....|....*...
gi 504819384 164 TASMDSTAKQQTAKLLQRLKDEGVTIMI 191
Cdd:PRK10938 163 FDGLDVASRQQLAELLASLHQSGITLVL 190
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
31-217 |
3.02e-12 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 64.43 E-value: 3.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 31 QCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNWKQAkAYIQKDIIYLHQQP-----------YLFDASVTDNI 99
Cdd:PRK15112 40 QTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDY-SYRSQRIRMIFQDPstslnprqrisQILDFPLRLNT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 100 AYglyRSGERKsnvhKKVTQALDWADL--SHLAHRPaKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQQTAK 177
Cdd:PRK15112 119 DL---EPEQRE----KQIIETLRQVGLlpDHASYYP-HMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLIN 190
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 504819384 178 LLQRLKDE-GVTIMISSHEAHTVEHIADHHIHIEHGNALIR 217
Cdd:PRK15112 191 LMLELQEKqGISYIYVTQHLGMMKHISDQVLVMHQGEVVER 231
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
13-192 |
9.11e-12 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 61.89 E-value: 9.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 13 TLSGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPD---SASINYQGLTLnwKQAKAYIQKDIIYLHQQPy 89
Cdd:cd03233 16 GRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPY--KEFAEKYPGEIIYVSEED- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 90 LFDASVTdniayglyrsgerksnvhkkVTQALDWAdLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDS 169
Cdd:cd03233 93 VHFPTLT--------------------VRETLDFA-LRCKGNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDS 151
|
170 180
....*....|....*....|....
gi 504819384 170 TAKQQTAKLLQRLKDE-GVTIMIS 192
Cdd:cd03233 152 STALEILKCIRTMADVlKTTTFVS 175
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
4-168 |
1.46e-11 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 61.79 E-value: 1.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 4 LVSYKNLAITLSGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTlnwkQAKAYIQKDIIY 83
Cdd:PRK13543 11 LLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKT----ATRGDRSRFMAY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 84 LHQQPYL-FDASVTDNIAY--GL--YRSGERKSNvhkkvtqALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSPRLL 158
Cdd:PRK13543 87 LGHLPGLkADLSTLENLHFlcGLhgRRAKQMPGS-------ALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLW 159
|
170
....*....|
gi 504819384 159 LLDEPTASMD 168
Cdd:PRK13543 160 LLDEPYANLD 169
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
31-200 |
1.86e-11 |
|
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: 63.49 E-value: 1.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 31 QCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTlnwkqakayIQKDIIYLHQQ----PYlFDAsvTDNIAYG---L 103
Cdd:TIGR01257 1966 ECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKS---------ILTNISDVHQNmgycPQ-FDA--IDDLLTGrehL 2033
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 104 YRSGERKSNVHKKVTQALDWA----DLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQQTAKLL 179
Cdd:TIGR01257 2034 YLYARLRGVPAEEIEKVANWSiqslGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTI 2113
|
170 180
....*....|....*....|.
gi 504819384 180 QRLKDEGVTIMISSHEAHTVE 200
Cdd:TIGR01257 2114 VSIIREGRAVVLTSHSMEECE 2134
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
16-195 |
2.00e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 62.71 E-value: 2.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 16 GKLVLNIKHLDIPA--------HQCTLL--TGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNWKQAKAYIQKDIIYLH 85
Cdd:PRK10762 254 GEVRLKVDNLSGPGvndvsftlRKGEILgvSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLANGIVYIS 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 86 QQP----YLFDASVTDN-----IAYGLYRSGERKsnvHKKVTQAL-DWADLSHL----AHRPAKQLSGGEKQRVALTRAR 151
Cdd:PRK10762 334 EDRkrdgLVLGMSVKENmsltaLRYFSRAGGSLK---HADEQQAVsDFIRLFNIktpsMEQAIGLLSGGNQQKVAIARGL 410
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 504819384 152 ILSPRLLLLDEPTASMDSTAKQQTAKLLQRLKDEGVTIMISSHE 195
Cdd:PRK10762 411 MTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSE 454
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
21-197 |
2.52e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 63.07 E-value: 2.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 21 NIKhLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKP-DSASINYQGltlnwkqakayiqkDIIYLHQQPYLFDASVTDNI 99
Cdd:PLN03232 635 DIN-LEIPVGSLVAIVGGTGEGKTSLISAMLGELSHaETSSVVIRG--------------SVAYVPQVSWIFNATVRENI 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 100 AYGLYRSGER--KSNVHKKVTQALDW---ADLSHLAHRpAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQQ 174
Cdd:PLN03232 700 LFGSDFESERywRAIDVTALQHDLDLlpgRDLTEIGER-GVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQ 778
|
170 180
....*....|....*....|...
gi 504819384 175 TAKLLQRLKDEGVTIMISSHEAH 197
Cdd:PLN03232 779 VFDSCMKDELKGKTRVLVTNQLH 801
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
25-185 |
2.67e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 62.83 E-value: 2.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 25 LDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNWKQAKAYIQKDIIYLHQ------QPYLfdaSVTDN 98
Cdd:NF033858 22 LDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHRRAVCPRIAYMPQglgknlYPTL---SVFEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 99 IA-----YGLYRSgERksnvHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQ 173
Cdd:NF033858 99 LDffgrlFGQDAA-ER----RRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRR 173
|
170
....*....|..
gi 504819384 174 QTAKLLQRLKDE 185
Cdd:NF033858 174 QFWELIDRIRAE 185
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
2-214 |
4.81e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 61.64 E-value: 4.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 2 STLVSYKNLAITLSG----KLVLNIKHLDIPAHQCTLLTGQNGSGKT-TLLKIMSGLLKPD----SASINYQGLTL---N 69
Cdd:PRK15134 3 QPLLAIENLSVAFRQqqtvRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLlhaS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 70 WKQAKAYIQKDIIYLHQQPyLFDASVTDNIAYGLYR-----SGERKSNVHKKVTQALDWADLSHLAHRPAK---QLSGGE 141
Cdd:PRK15134 83 EQTLRGVRGNKIAMIFQEP-MVSLNPLHTLEKQLYEvlslhRGMRREAARGEILNCLDRVGIRQAAKRLTDyphQLSGGE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504819384 142 KQRVALTRARILSPRLLLLDEPTASMDSTAKQQTAKLLQRLKDE-GVTIMISSHEAHTVEHIADHHIHIEHGNA 214
Cdd:PRK15134 162 RQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNGRC 235
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
13-174 |
8.00e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 61.29 E-value: 8.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 13 TLSgklvlNIkHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSasinyqgltlnwkQAKAYIQKDIIYLHQQPYLFD 92
Cdd:PLN03130 632 TLS-----NI-NLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRS-------------DASVVIRGTVAYVPQVSWIFN 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 93 ASVTDNIAYGLYRSGERksnvhkkVTQALDWADLSH-LAHRPAKQL----------SGGEKQRVALTRARILSPRLLLLD 161
Cdd:PLN03130 693 ATVRDNILFGSPFDPER-------YERAIDVTALQHdLDLLPGGDLteigergvniSGGQKQRVSMARAVYSNSDVYIFD 765
|
170
....*....|...
gi 504819384 162 EPTASMDSTAKQQ 174
Cdd:PLN03130 766 DPLSALDAHVGRQ 778
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
133-212 |
8.80e-11 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 60.99 E-value: 8.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 133 PAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQQTAKLLQRLKDEGVTIMISSHEAHTVEHIADHHIHIEHG 212
Cdd:TIGR02633 400 PIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEG 479
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
37-195 |
9.16e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 61.05 E-value: 9.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 37 GQNGSGKTTLLKIMSGLLKpdSASINYQGLTLNWKQAKAYI-------QKDIIYLHqqpylfdASVTDNIAY-GLYR--- 105
Cdd:PLN03211 101 GPSGSGKSTLLNALAGRIQ--GNNFTGTILANNRKPTKQILkrtgfvtQDDILYPH-------LTVRETLVFcSLLRlpk 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 106 --SGERKSNVHKKVTQALDWADLSH--LAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQQTAKLLQR 181
Cdd:PLN03211 172 slTKQEKILVAESVISELGLTKCENtiIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGS 251
|
170
....*....|....
gi 504819384 182 LKDEGVTIMISSHE 195
Cdd:PLN03211 252 LAQKGKTIVTSMHQ 265
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
133-193 |
1.03e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 60.71 E-value: 1.03e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504819384 133 PAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQQTAKLLQRLKDEGVT-IMISS 193
Cdd:PRK13549 402 AIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAiIVISS 463
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
12-212 |
1.21e-10 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 58.49 E-value: 1.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 12 ITLSGKLVLNIKHLD--IPAHQCTLLTGQNGSGKTTLLKimsgllkpdsASINYQGLTLNWKQAKAYIQKDIIYLHQQPY 89
Cdd:cd03238 1 LTVSGANVHNLQNLDvsIPLNVLVVVTGVSGSGKSTLVN----------EGLYASGKARLISFLPKFSRNKLIFIDQLQF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 90 LFDAsvtdNIAYglyrsgerksnvhkkVTqaLDwadlshlahRPAKQLSGGEKQRVALTR--ARILSPRLLLLDEPTASM 167
Cdd:cd03238 71 LIDV----GLGY---------------LT--LG---------QKLSTLSGGELQRVKLASelFSEPPGTLFILDEPSTGL 120
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 504819384 168 DSTAKQQTAKLLQRLKDEGVTIMISSHEAHTVEHiADHHIHIEHG 212
Cdd:cd03238 121 HQQDINQLLEVIKGLIDLGNTVILIEHNLDVLSS-ADWIIDFGPG 164
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
12-194 |
1.30e-10 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 60.53 E-value: 1.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 12 ITLSGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPdsasinYQG-LTLNWKQAkayiqkdIIYLHQQPYL 90
Cdd:TIGR00954 460 VTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPV------YGGrLTKPAKGK-------LFYVPQRPYM 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 91 FDASVTDNIAYGLyrSGE---RKSNVHKKVTQALDWADLSHLAHRPA---------KQLSGGEKQRVALTRARILSPRLL 158
Cdd:TIGR00954 527 TLGTLRDQIIYPD--SSEdmkRRGLSDKDLEQILDNVQLTHILEREGgwsavqdwmDVLSGGEKQRIAMARLFYHKPQFA 604
|
170 180 190
....*....|....*....|....*....|....*.
gi 504819384 159 LLDEPTASMDSTAKQqtaKLLQRLKDEGVTIMISSH 194
Cdd:TIGR00954 605 ILDECTSAVSVDVEG---YMYRLCREFGITLFSVSH 637
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
5-212 |
1.78e-10 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 57.97 E-value: 1.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 5 VSYKNLAITLsGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNWKQAKAyiqkdiiyl 84
Cdd:cd03222 1 QLYPDCVKRY-GVFFLLVELGVVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVYKPQYI--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 85 hqqpylfdasvtdniayglyrsgerksnvhkkvtqaldwadlshlahrpakQLSGGEKQRVALTRARILSPRLLLLDEPT 164
Cdd:cd03222 71 ---------------------------------------------------DLSGGELQRVAIAAALLRNATFYLFDEPS 99
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 504819384 165 ASMDSTAKQQTAKLLQRLKDEGV-TIMISSHEAHTVEHIADhHIHIEHG 212
Cdd:cd03222 100 AYLDIEQRLNAARAIRRLSEEGKkTALVVEHDLAVLDYLSD-RIHVFEG 147
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
5-199 |
2.00e-10 |
|
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: 58.19 E-value: 2.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 5 VSYKNLAITLSGKL--VLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNwKQAKAYIQKDII 82
Cdd:cd03369 7 IEVENLSVRYAPDLppVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDIS-TIPLEDLRSSLT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 83 YLHQQPYLFDASVTDNI-AYGLYRSgerksnvhKKVTQALDWADlshlahrPAKQLSGGEKQRVALTRARILSPRLLLLD 161
Cdd:cd03369 86 IIPQDPTLFSGTIRSNLdPFDEYSD--------EEIYGALRVSE-------GGLNLSQGQRQLLCLARALLKRPRVLVLD 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 504819384 162 EPTASMDStakqQTAKLLQRLKDE---GVTIMISSHEAHTV 199
Cdd:cd03369 151 EATASIDY----ATDALIQKTIREeftNSTILTIAHRLRTI 187
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
35-203 |
3.11e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 59.48 E-value: 3.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 35 LTGQNGSGKTTLLKIMSGLLKPDSASINYQGL---TLNWKQAKAyIQKDIIYLHQQPYL-FDA--SVTDNIAYGLYRSGE 108
Cdd:PRK10261 355 LVGESGSGKSTTGRALLRLVESQGGEIIFNGQridTLSPGKLQA-LRRDIQFIFQDPYAsLDPrqTVGDSIMEPLRVHGL 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 109 RKSN-VHKKVTQALDWADL--SHlAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQQTAKLLQRL-KD 184
Cdd:PRK10261 434 LPGKaAAARVAWLLERVGLlpEH-AWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLqRD 512
|
170
....*....|....*....
gi 504819384 185 EGVTIMISSHEAHTVEHIA 203
Cdd:PRK10261 513 FGIAYLFISHDMAVVERIS 531
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
35-210 |
4.12e-10 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 59.03 E-value: 4.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 35 LTGQNGSGKTTLLKIMSGLLKPDSASINYQGltlNWKQAkayiqkdiiYLHQQPYLFDASVTDNIAYG--LYRSGERK-- 110
Cdd:PRK10636 32 LVGKNGCGKSTLLALLKNEISADGGSYTFPG---NWQLA---------WVNQETPALPQPALEYVIDGdrEYRQLEAQlh 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 111 -----------SNVHKKVTQALDW---ADLSHLAH----------RPAKQLSGGEKQRVALTRARILSPRLLLLDEPTAS 166
Cdd:PRK10636 100 danerndghaiATIHGKLDAIDAWtirSRAASLLHglgfsneqleRPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNH 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 504819384 167 MDSTAkqqTAKLLQRLKDEGVTIMISSHEAHTVEHIADHHIHIE 210
Cdd:PRK10636 180 LDLDA---VIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIE 220
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
31-195 |
5.51e-10 |
|
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: 56.87 E-value: 5.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 31 QCTLLTGQNGSGKTTLLKIMSGllKPDSASINYQgLTLNWKQAKAYIQKDIIYLHQQPYLFDASvtdniayglyrsgerk 110
Cdd:cd03232 34 TLTALMGESGAGKTTLLDVLAG--RKTAGVITGE-ILINGRPLDKNFQRSTGYVEQQDVHSPNL---------------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 111 snvhkKVTQALDW-ADLshlahrpaKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQQTAKLLQRLKDEGVTI 189
Cdd:cd03232 95 -----TVREALRFsALL--------RGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADSGQAI 161
|
....*.
gi 504819384 190 MISSHE 195
Cdd:cd03232 162 LCTIHQ 167
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
2-209 |
6.33e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 57.34 E-value: 6.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 2 STLVSYKNLAITLSGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGllKPD----SASINYQGLTLNWKQAKAYI 77
Cdd:CHL00131 5 KPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPAykilEGDILFKGESILDLEPEERA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 78 QKDIIYLHQQPYLFdASVTD----NIAYGLYRSGERKSNVH-----KKVTQALDWADLS-HLAHRPAKQ-LSGGEKQRVA 146
Cdd:CHL00131 83 HLGIFLAFQYPIEI-PGVSNadflRLAYNSKRKFQGLPELDpleflEIINEKLKLVGMDpSFLSRNVNEgFSGGEKKRNE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504819384 147 LTRARILSPRLLLLDEPTASMDSTAKQQTAKLLQRLKDEGVTIMISSHEAHTVEHIADHHIHI 209
Cdd:CHL00131 162 ILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHYQRLLDYIKPDYVHV 224
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
33-205 |
6.69e-10 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 58.20 E-value: 6.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 33 TL-LTGQNGSGKT-TLLKIMsGLLKPD---SASINYQG---LTLNWKQAKAYIQKDIIYLHQQPylfdasVTDNIAYglY 104
Cdd:PRK09473 44 TLgIVGESGSGKSqTAFALM-GLLAANgriGGSATFNGreiLNLPEKELNKLRAEQISMIFQDP------MTSLNPY--M 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 105 RSGERKSNV---HKKVTQA---------LDWADLSHLAHR----PaKQLSGGEKQRVALTRARILSPRLLLLDEPTASMD 168
Cdd:PRK09473 115 RVGEQLMEVlmlHKGMSKAeafeesvrmLDAVKMPEARKRmkmyP-HEFSGGMRQRVMIAMALLCRPKLLIADEPTTALD 193
|
170 180 190
....*....|....*....|....*....|....*....
gi 504819384 169 STAKQQTAKLLQRLKDEGVT--IMIsSHEAHTVEHIADH 205
Cdd:PRK09473 194 VTVQAQIMTLLNELKREFNTaiIMI-THDLGVVAGICDK 231
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
136-204 |
6.84e-10 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 57.89 E-value: 6.84e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 136 QLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQQTAKLLQRL-KDEGVTIMISSHEAHTVEHIAD 204
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLnQNNNTTILLISHDLQMLSQWAD 227
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
31-204 |
8.30e-10 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 58.06 E-value: 8.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 31 QCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNWKQAKAYIQkdiiylhqqpyLFDASVTDNIAYGLYRSGERK 110
Cdd:PRK10522 350 ELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRK-----------LFSAVFTDFHLFDQLLGPEGK 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 111 SNVHKKVTQALDWADLSH-LAHRPAK----QLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQQ-TAKLLQRLKD 184
Cdd:PRK10522 419 PANPALVEKWLERLKMAHkLELEDGRisnlKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREfYQVLLPLLQE 498
|
170 180
....*....|....*....|
gi 504819384 185 EGVTIMISSHEAHTVEHiAD 204
Cdd:PRK10522 499 MGKTIFAISHDDHYFIH-AD 517
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
37-196 |
9.09e-10 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 58.21 E-value: 9.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 37 GQNGSGKTTLLKIMSGLLKPDSAsinyqgltlnwkQAKayiqkdiiylhqqpyLFDASVT-DNIA--------------Y 101
Cdd:NF033858 299 GSNGCGKSTTMKMLTGLLPASEG------------EAW---------------LFGQPVDaGDIAtrrrvgymsqafslY 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 102 G-------------LYRSGERKsnVHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMD 168
Cdd:NF033858 352 GeltvrqnlelharLFHLPAAE--IAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
170 180 190
....*....|....*....|....*....|..
gi 504819384 169 STAKQQTAKLLQRL-KDEGVTIMISSH---EA 196
Cdd:NF033858 430 PVARDMFWRLLIELsREDGVTIFISTHfmnEA 461
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
5-197 |
9.96e-10 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 57.17 E-value: 9.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 5 VSYKNLaiTLSGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGltlnwkqakayiqkDIIYL 84
Cdd:cd03291 40 LFFSNL--CLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG--------------RISFS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 85 HQQPYLFDASVTDNIAYGLYRSGERKSNVHKKVTQALDWADLSHLAHRPAKQ----LSGGEKQRVALTRARILSPRLLLL 160
Cdd:cd03291 104 SQFSWIMPGTIKENIIFGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEggitLSGGQRARISLARAVYKDADLYLL 183
|
170 180 190
....*....|....*....|....*....|....*...
gi 504819384 161 DEPTASMD-STAKQQTAKLLQRLKDEGVTIMISSHEAH 197
Cdd:cd03291 184 DSPFGYLDvFTEKEIFESCVCKLMANKTRILVTSKMEH 221
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
30-210 |
1.16e-09 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 55.07 E-value: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 30 HQCTLLTGQNGSGKTTLLKIMSGLLKPDSasinyqgltlnwkqakayiqKDIIYLhqqpylfdasvtdniayglyrSGER 109
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPG--------------------GGVIYI---------------------DGED 40
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 110 KsnvhkkvTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDS------TAKQQTAKLLQRLK 183
Cdd:smart00382 41 I-------LEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAeqeallLLLEELRLLLLLKS 113
|
170 180 190
....*....|....*....|....*....|..
gi 504819384 184 DEGVTIMISSHE-----AHTVEHIADHHIHIE 210
Cdd:smart00382 114 EKNLTVILTTNDekdlgPALLRRRFDRRIVLL 145
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
25-212 |
1.26e-09 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 57.50 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 25 LDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNWKQAKAYIQK-DIIYlhQQPYLFDAsvtdniaygL 103
Cdd:COG4615 353 LTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLfSAVF--SDFHLFDR---------L 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 104 YrsGERKSNVHKKVTQALDWADLSHlahrpaK-----------QLSGGEKQRVALTRArILSPR-LLLLDEPTASMDSTA 171
Cdd:COG4615 422 L--GLDGEADPARARELLERLELDH------KvsvedgrfsttDLSQGQRKRLALLVA-LLEDRpILVFDEWAADQDPEF 492
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 504819384 172 KQQ-TAKLLQRLKDEGVTIMISSHEAHTVeHIADHHIHIEHG 212
Cdd:COG4615 493 RRVfYTELLPELKARGKTVIAISHDDRYF-DLADRVLKMDYG 533
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
113-213 |
2.12e-09 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 57.15 E-value: 2.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 113 VHKKVtQALDWADLSHLA-HRPAKQLSGGEKQRVALTR---ARILSPRLLLLDEPTASMDSTAKQQTAKLLQRLKDEGVT 188
Cdd:PRK00635 786 IHEKI-HALCSLGLDYLPlGRPLSSLSGGEIQRLKLAYellAPSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHT 864
|
90 100
....*....|....*....|....*..
gi 504819384 189 IMISSHEAHTVEhIADHHIHI--EHGN 213
Cdd:PRK00635 865 VVIIEHNMHVVK-VADYVLELgpEGGN 890
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
12-197 |
2.42e-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: 56.84 E-value: 2.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 12 ITLSGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGltlnwkqakayiqkDIIYLHQQPYLF 91
Cdd:TIGR01271 434 FSLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG--------------RISFSPQTSWIM 499
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 92 DASVTDNIAYGLYRSGERKSNVHKKVTQALDWADLSHLAHRPAKQ----LSGGEKQRVALTRARILSPRLLLLDEPTASM 167
Cdd:TIGR01271 500 PGTIKDNIIFGLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFTHL 579
|
170 180 190
....*....|....*....|....*....|.
gi 504819384 168 D-STAKQQTAKLLQRLKDEGVTIMISSHEAH 197
Cdd:TIGR01271 580 DvVTEKEIFESCLCKLMSNKTRILVTSKLEH 610
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
37-168 |
6.43e-09 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 55.33 E-value: 6.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 37 GQNGSGKTTLLKIMSGLLKPDSASINYqGLTLnwkqakayiqkDIIYLHQQPYLFDA--SVTDNIAYGL--YRSGERKSN 112
Cdd:TIGR03719 355 GPNGAGKSTLFRMITGQEQPDSGTIEI-GETV-----------KLAYVDQSRDALDPnkTVWEEISGGLdiIKLGKREIP 422
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 504819384 113 VHKKVTQ-ALDWADlshlAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMD 168
Cdd:TIGR03719 423 SRAYVGRfNFKGSD----QQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLD 475
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
35-212 |
8.24e-09 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 54.44 E-value: 8.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 35 LTGQNGSGKTTLLKIMSGLLKPDSASINYQGltlnwkqakayiQKDIIYLHQQpylFDASVT--DNIAYGLYRSGERKSN 112
Cdd:PRK13546 55 LVGINGSGKSTLSNIIGGSLSPTVGKVDRNG------------EVSVIAISAG---LSGQLTgiENIEFKMLCMGFKRKE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 113 VHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQQTAKLLQRLKDEGVTIMIS 192
Cdd:PRK13546 120 IKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEFKEQNKTIFFV 199
|
170 180
....*....|....*....|
gi 504819384 193 SHEAHTVEHIADHHIHIEHG 212
Cdd:PRK13546 200 SHNLGQVRQFCTKIAWIEGG 219
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
12-212 |
8.94e-09 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 53.80 E-value: 8.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 12 ITLSGKLVLNIK--HLDIPAHQCTLLTGQNGSGKTTLL---------------------KIMSGLLKPDSASInyQGLTl 68
Cdd:cd03270 1 IIVRGAREHNLKnvDVDIPRNKLVVITGVSGSGKSSLAfdtiyaegqrryveslsayarQFLGQMDKPDVDSI--EGLS- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 69 nwkQAKAYIQKDIiylHQQPYLFDASVTDniAYGLYRSGERKSNVHKKVTQALDwADLSHLA-HRPAKQLSGGEKQRVAL 147
Cdd:cd03270 78 ---PAIAIDQKTT---SRNPRSTVGTVTE--IYDYLRLLFARVGIRERLGFLVD-VGLGYLTlSRSAPTLSGGEAQRIRL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504819384 148 TRaRI---LSPRLLLLDEPTASMDSTAKQQTAKLLQRLKDEGVTIMISSHEAHTVEHiADHHIHI-----EHG 212
Cdd:cd03270 149 AT-QIgsgLTGVLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIRA-ADHVIDIgpgagVHG 219
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
40-204 |
1.13e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 54.53 E-value: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 40 GSGKTTLLKIMSGLLKPDSASINYQGLTLNWKQAKAYI------------QKDIIYLHqqpylfdaSVTDNIA------- 100
Cdd:PRK11288 289 GAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIragimlcpedrkAEGIIPVH--------SVADNINisarrhh 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 101 --YGLYRSGERKSNVHKKVTQALDWADLShlAHRPAKQLSGGEKQRVALtrARILSPRL--LLLDEPTASMDSTAKQQTA 176
Cdd:PRK11288 361 lrAGCLINNRWEAENADRFIRSLNIKTPS--REQLIMNLSGGNQQKAIL--GRWLSEDMkvILLDEPTRGIDVGAKHEIY 436
|
170 180
....*....|....*....|....*...
gi 504819384 177 KLLQRLKDEGVTIMISSHEAHTVEHIAD 204
Cdd:PRK11288 437 NVIYELAAQGVAVLFVSSDLPEVLGVAD 464
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
40-195 |
1.59e-08 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 54.26 E-value: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 40 GSGKTTLLKIMSGLLKPDSASINYQGLTLNWKQAKAYIQKDIIYLHQQPYLF----DASVTDNIAYGLYRSGERKSNVhk 115
Cdd:COG3845 294 GNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLGVAYIPEDRLGRglvpDMSVAENLILGRYRRPPFSRGG-- 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 116 kvtqALDWADLSHLAHR--------------PAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQQTAKLLQR 181
Cdd:COG3845 372 ----FLDRKAIRAFAEElieefdvrtpgpdtPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLE 447
|
170
....*....|....
gi 504819384 182 LKDEGVTIMISSHE 195
Cdd:COG3845 448 LRDAGAAVLLISED 461
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
35-199 |
2.86e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 53.71 E-value: 2.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 35 LTGQNGSGKTTLLKIMSGLLKPDSASInyqgltlnWKQAKAYI------QKDIIYLHQQPYLFDASVTDNIAyglyrsgE 108
Cdd:PLN03073 540 MVGPNGIGKSTILKLISGELQPSSGTV--------FRSAKVRMavfsqhHVDGLDLSSNPLLYMMRCFPGVP-------E 604
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 109 RKSNVHkkvtqaLDWADLS-HLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQqtaKLLQRLKDEGV 187
Cdd:PLN03073 605 QKLRAH------LGSFGVTgNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVE---ALIQGLVLFQG 675
|
170
....*....|..
gi 504819384 188 TIMISSHEAHTV 199
Cdd:PLN03073 676 GVLMVSHDEHLI 687
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
4-217 |
3.31e-08 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 52.49 E-value: 3.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 4 LVSYKNLAITLSGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGL--LKPDSASINYQGLTLNWKQAKAYIQKDI 81
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSPEDRAGEGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 82 IYLHQQP---------YLFDASVTdniAYGLYRsgerksnvHKKVTQALDWADL----SHLAHRPAKQL--------SGG 140
Cdd:PRK09580 81 FMAFQYPveipgvsnqFFLQTALN---AVRSYR--------GQEPLDRFDFQDLmeekIALLKMPEDLLtrsvnvgfSGG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504819384 141 EKQRVALTRARILSPRLLLLDEPTASMDSTAKQQTAKLLQRLKDEGVTIMISSHEAHTVEHIADHHIHIEHGNALIR 217
Cdd:PRK09580 150 EKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYQRILDYIKPDYVHVLYQGRIVK 226
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
33-194 |
3.81e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 51.80 E-value: 3.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 33 TLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNwKQAKAYIQkdiiYL-HQQPYLFDASVTDNIAY--GLYRSGEr 109
Cdd:PRK13541 29 TYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNIN-NIAKPYCT----YIgHNLGLKLEMTVFENLKFwsEIYNSAE- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 110 ksnvhkKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQQTAKLLQRLKDEGVTI 189
Cdd:PRK13541 103 ------TLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVMKANSGGIV 176
|
....*
gi 504819384 190 MISSH 194
Cdd:PRK13541 177 LLSSH 181
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
132-207 |
5.57e-08 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 52.71 E-value: 5.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 132 RPAKQLSGGEKQRVALtrARILSPR-----LLLLDEPTASMDSTAKQQTAKLLQRLKDEGVTIMISSHEAHTVEhIADHH 206
Cdd:TIGR00630 825 QPATTLSGGEAQRIKL--AKELSKRstgrtLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNLDVIK-TADYI 901
|
.
gi 504819384 207 I 207
Cdd:TIGR00630 902 I 902
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
17-204 |
7.50e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 52.48 E-value: 7.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 17 KLVLN-IKHLDIPAHQCTLLtGQNGSGKTTLLKIMSGLLKPDSASINY-QGLTLNWkqakaYIQkdiiylHQQPYL-FDA 93
Cdd:PRK10636 325 RIILDsIKLNLVPGSRIGLL-GRNGAGKSTLIKLLAGELAPVSGEIGLaKGIKLGY-----FAQ------HQLEFLrADE 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 94 SVTDNIAYGLYRSGERKSNVH--------KKVTQaldwadlshlahrPAKQLSGGEKQRVALTRARILSPRLLLLDEPTA 165
Cdd:PRK10636 393 SPLQHLARLAPQELEQKLRDYlggfgfqgDKVTE-------------ETRRFSGGEKARLVLALIVWQRPNLLLLDEPTN 459
|
170 180 190
....*....|....*....|....*....|....*....
gi 504819384 166 SMDSTAKQqtaKLLQRLKDEGVTIMISSHEAHTVEHIAD 204
Cdd:PRK10636 460 HLDLDMRQ---ALTEALIDFEGALVVVSHDRHLLRSTTD 495
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
8-168 |
9.34e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 52.17 E-value: 9.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 8 KNLAITLSGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSgLLKPDSASINYQGL----------------TLNWK 71
Cdd:PLN03073 181 ENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMA-MHAIDGIPKNCQILhveqevvgddttalqcVLNTD 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 72 QAKAYIQKDIIYLHQQPYLFDASVTDNIAYGLYRSGERKSNVHKKVTQ------ALD-----------WADLS---HLAH 131
Cdd:PLN03073 260 IERTQLLEEEAQLVAQQRELEFETETGKGKGANKDGVDKDAVSQRLEEiykrleLIDaytaearaasiLAGLSftpEMQV 339
|
170 180 190
....*....|....*....|....*....|....*..
gi 504819384 132 RPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMD 168
Cdd:PLN03073 340 KATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
136-195 |
1.18e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 51.71 E-value: 1.18e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 136 QLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQQTAKLLQRLKDEGVTIMISSHE 195
Cdd:PRK09700 409 ELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSE 468
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
20-212 |
1.25e-07 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 51.81 E-value: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 20 LNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGltlnwkqaKAYIQKDIIYLHQQpylfdASVTDNI 99
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG--------SAALIAISSGLNGQ-----LTGIENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 100 AYGLYRSGERKSNVHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQQTAKLL 179
Cdd:PRK13545 107 ELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKM 186
|
170 180 190
....*....|....*....|....*....|...
gi 504819384 180 QRLKDEGVTIMISSHEAHTVEHIADHHIHIEHG 212
Cdd:PRK13545 187 NEFKEQGKTIFFISHSLSQVKSFCTKALWLHYG 219
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
5-199 |
1.39e-07 |
|
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: 51.87 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 5 VSYKNLAITLSGKLVLNIKHLDIPAH--QCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNwKQAKAYIQKDII 82
Cdd:TIGR00957 1285 VEFRNYCLRYREDLDLVLRHINVTIHggEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIA-KIGLHDLRFKIT 1363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 83 YLHQQPYLFDASVTDNI-AYGLYRSGE-----RKSNVHKKVTQALDwaDLSHLAHRPAKQLSGGEKQRVALTRARILSPR 156
Cdd:TIGR00957 1364 IIPQDPVLFSGSLRMNLdPFSQYSDEEvwwalELAHLKTFVSALPD--KLDHECAEGGENLSVGQRQLVCLARALLRKTK 1441
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 504819384 157 LLLLDEPTASMDstakQQTAKLLQ---RLKDEGVTIMISSHEAHTV 199
Cdd:TIGR00957 1442 ILVLDEATAAVD----LETDNLIQstiRTQFEDCTVLTIAHRLNTI 1483
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
136-207 |
1.55e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 50.90 E-value: 1.55e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504819384 136 QLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQQTAKLLQRL-KDEGVTIMISSHEAHTVEHIAdHHI 207
Cdd:PRK11022 153 QLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELqQKENMALVLITHDLALVAEAA-HKI 224
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
35-215 |
1.84e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 51.01 E-value: 1.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 35 LTGQNGSGKT-TLLKIMSgLLKPDSASINYQGLTLNWK---------QAKAYIQK----DIIYLHQQP-------YLFDA 93
Cdd:PRK10261 47 IVGESGSGKSvTALALMR-LLEQAGGLVQCDKMLLRRRsrqvielseQSAAQMRHvrgaDMAMIFQEPmtslnpvFTVGE 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 94 SVTDNIAYGLYRSGERKSNVHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQ 173
Cdd:PRK10261 126 QIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQA 205
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 504819384 174 QTAKLLQRLKDE-GVTIMISSHEAHTVEHIADHHIHIEHGNAL 215
Cdd:PRK10261 206 QILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLVMYQGEAV 248
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
110-215 |
3.24e-07 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 50.12 E-value: 3.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 110 KSNVHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQQTAKLLQRLKDEGVTI 189
Cdd:NF000106 118 RKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATV 197
|
90 100
....*....|....*....|....*.
gi 504819384 190 MISSHEAHTVEHIADHHIHIEHGNAL 215
Cdd:NF000106 198 LLTTQYMEEAEQLAHELTVIDRGRVI 223
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
20-169 |
5.48e-07 |
|
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: 49.94 E-value: 5.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 20 LNIKHLDIPAHQCTLLTGQNGSGKTTLLkimSGLLKpdsasinyqglTLNWKQAKAYIQKDIIYLHQQPYLFDASVTDNI 99
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLL---SALLA-----------EMDKVEGHVHMKGSVAYVPQQAWIQNDSLRENI 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 100 AYGlyrsGERKSNVHKKVTQALdwADLSHLAHRPAK----------QLSGGEKQRVALTRARILSPRLLLLDEPTASMDS 169
Cdd:TIGR00957 720 LFG----KALNEKYYQQVLEAC--ALLPDLEILPSGdrteigekgvNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDA 793
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
132-207 |
5.58e-07 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 49.15 E-value: 5.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 132 RPAKQLSGGEKQRVALtrARILSPR-----LLLLDEPTASMDSTAKQQTAKLLQRLKDEGVTIMISSHEAHTVEhIADHH 206
Cdd:cd03271 165 QPATTLSGGEAQRIKL--AKELSKRstgktLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIK-CADWI 241
|
.
gi 504819384 207 I 207
Cdd:cd03271 242 I 242
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
137-193 |
1.16e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 48.57 E-value: 1.16e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 504819384 137 LSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQQTAKLLQRL--KDEGVtIMISS 193
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELakKDKGI-IIISS 449
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
37-168 |
1.21e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 48.73 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 37 GQNGSGKTTLLKIMSGLLKPDSASINyqgltlnWKQAKA--YIQKDiiylHQQPYLFDASVTDNIAYglYRSGERKSNVH 114
Cdd:PRK15064 352 GENGVGKTTLLRTLVGELEPDSGTVK-------WSENANigYYAQD----HAYDFENDLTLFDWMSQ--WRQEGDDEQAV 418
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 115 KKVtqaldwadLSHL------AHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMD 168
Cdd:PRK15064 419 RGT--------LGRLlfsqddIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMD 470
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
37-196 |
1.55e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.09 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 37 GQNGSGKTTLLKIMSGLlKPDSASinyQGLTLNWKQAKA-----YIQKDIIY----LHQQpYLFDASVTDNI------AY 101
Cdd:PRK10938 293 GPNGAGKSTLLSLITGD-HPQGYS---NDLTLFGRRRGSgetiwDIKKHIGYvsssLHLD-YRVSTSVRNVIlsgffdSI 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 102 GLYRS-GERKsnvHKKVTQaldWADLSHLAHRPAKQ----LSGGEkQRVAL-TRARILSPRLLLLDEPTASMDSTAKQQT 175
Cdd:PRK10938 368 GIYQAvSDRQ---QKLAQQ---WLDILGIDKRTADApfhsLSWGQ-QRLALiVRALVKHPTLLILDEPLQGLDPLNRQLV 440
|
170 180
....*....|....*....|..
gi 504819384 176 AKLLQRLKDEGVT-IMISSHEA 196
Cdd:PRK10938 441 RRFVDVLISEGETqLLFVSHHA 462
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
133-205 |
1.65e-06 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 48.48 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 133 PAKQLSGGEKQRVALtrARILSPR-----LLLLDEPTasmdstakqqT-------AKL---LQRLKDEGVTIMIssheah 197
Cdd:COG0178 823 PATTLSGGEAQRVKL--ASELSKRstgktLYILDEPT----------TglhfhdiRKLlevLHRLVDKGNTVVV------ 884
|
90
....*....|....
gi 504819384 198 tVEH----I--ADH 205
Cdd:COG0178 885 -IEHnldvIktADW 897
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
121-212 |
2.56e-06 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 47.70 E-value: 2.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 121 LDWADLShlahRPAKQLSGGEKQRVALTrARI---LSPRLLLLDEPTASMDSTAKQQTAKLLQRLKDEGVTIMISSHEAH 197
Cdd:TIGR00630 477 LDYLSLS----RAAGTLSGGEAQRIRLA-TQIgsgLTGVLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDED 551
|
90 100
....*....|....*....|
gi 504819384 198 TVEHiADHHIHI-----EHG 212
Cdd:TIGR00630 552 TIRA-ADYVIDIgpgagEHG 570
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
32-210 |
2.60e-06 |
|
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: 46.45 E-value: 2.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 32 CTLLTGQNGSGKTTLLK----IMSGLLKPDSASINYQGLTLNWKQAKAYIQKDIIYLHQQPYLF--DASVTDNIAYglYR 105
Cdd:cd03240 24 LTLIVGQNGAGKTTIIEalkyALTGELPPNSKGGAHDPKLIREGEVRAQVKLAFENANGKKYTItrSLAILENVIF--CH 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 106 SGErksnvhkkvtqaLDWadlshLAHRPAKQLSGGEKQ------RVALTRARILSPRLLLLDEPTASMDS-TAKQQTAKL 178
Cdd:cd03240 102 QGE------------SNW-----PLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEeNIEESLAEI 164
|
170 180 190
....*....|....*....|....*....|...
gi 504819384 179 LQRLKDEGV-TIMISSHEAHTVEHiADHHIHIE 210
Cdd:cd03240 165 IEERKSQKNfQLIVITHDEELVDA-ADHIYRVE 196
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
6-195 |
3.23e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 47.41 E-value: 3.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 6 SYKNLAITL---SGKLVLnIKHLD---IPAhQCTLLTGQNGSGKTTLLKIMS-----GLLKPDSASINYQGLTLNWKQAK 74
Cdd:TIGR00956 761 HWRNLTYEVkikKEKRVI-LNNVDgwvKPG-TLTALMGASGAGKTTLLNVLAervttGVITGGDRLVNGRPLDSSFQRSI 838
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 75 AYIQKDIIYLHQqpylfdASVTDNIAYGLYR------SGERKSNVHKKVTQAL---DWADLshLAHRPAKQLSGGEKQRV 145
Cdd:TIGR00956 839 GYVQQQDLHLPT------STVRESLRFSAYLrqpksvSKSEKMEYVEEVIKLLemeSYADA--VVGVPGEGLNVEQRKRL 910
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 504819384 146 ALTRARILSPRLLL-LDEPTASMDSTAKQQTAKLLQRLKDEGVTIMISSHE 195
Cdd:TIGR00956 911 TIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQ 961
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
37-168 |
4.45e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 47.04 E-value: 4.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 37 GQNGSGKTTLLKIMSGLLKPDSASINYqGLTLnwkqakayiqkDIIYLHQQPYLFDASVT---------DNIAYGLY--- 104
Cdd:PRK11819 357 GPNGAGKSTLFKMITGQEQPDSGTIKI-GETV-----------KLAYVDQSRDALDPNKTvweeisgglDIIKVGNReip 424
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504819384 105 ------RSGERKSNVHKKVtqaldwadlshlahrpaKQLSGGEKQRVALtrARILSP--RLLLLDEPTASMD 168
Cdd:PRK11819 425 srayvgRFNFKGGDQQKKV-----------------GVLSGGERNRLHL--AKTLKQggNVLLLDEPTNDLD 477
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
25-209 |
5.43e-06 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 45.04 E-value: 5.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 25 LDIPAHQCTLLTGQNGSGKTTLLKimsgllkpdsasinyqgltlnwkqakayiqkDIIYLhqqpyLFDASVTDNiaygly 104
Cdd:cd03227 16 VTFGEGSLTIITGPNGSGKSTILD-------------------------------AIGLA-----LGGAQSATR------ 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 105 rsgeRKSNVHKKVTQALDWADLSHLAHrpakQLSGGEKQRVALtrARILS-----PR-LLLLDEPTASMDSTAKQQTAKL 178
Cdd:cd03227 54 ----RRSGVKAGCIVAAVSAELIFTRL----QLSGGEKELSAL--ALILAlaslkPRpLYILDEIDRGLDPRDGQALAEA 123
|
170 180 190
....*....|....*....|....*....|.
gi 504819384 179 LQRLKDEGVTIMISSHEaHTVEHIADHHIHI 209
Cdd:cd03227 124 ILEHLVKGAQVIVITHL-PELAELADKLIHI 153
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
13-194 |
6.75e-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: 6.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 13 TLSGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSA----SINYQGLTLN-WKQAKAYIQkdiiylhQQ 87
Cdd:TIGR01271 1228 TEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEGEiqidGVSWNSVTLQtWRKAFGVIP-------QK 1300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 88 PYLFDASVTDNIAYGLYRSGERKSNVHKKVTQAldwadlSHLAHRPAKQ----------LSGGEKQRVALTRARILSPRL 157
Cdd:TIGR01271 1301 VFIFSGTFRKNLDPYEQWSDEEIWKVAEEVGLK------SVIEQFPDKLdfvlvdggyvLSNGHKQLMCLARSILSKAKI 1374
|
170 180 190
....*....|....*....|....*....|....*...
gi 504819384 158 LLLDEPTASMDSTAKQQTAKLL-QRLKDegVTIMISSH 194
Cdd:TIGR01271 1375 LLLDEPSAHLDPVTLQIIRKTLkQSFSN--CTVILSEH 1410
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
33-204 |
8.81e-06 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 44.95 E-value: 8.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 33 TLLTGQNGSGKTTLLKIMSGLLkpdsasinyqgltlnWKQAKAYIQKDIIYLHQQPYLFDASVTDNIAYG--LYRSgERK 110
Cdd:cd03279 31 FLICGPTGAGKSTILDAITYAL---------------YGKTPRYGRQENLRSVFAPGEDTAEVSFTFQLGgkKYRV-ERS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 111 SNV-HKKVTQA--LDWADLSHLAHRPAKQLSGGEKQRVALTRARILSP----------RLLLLDEPTASMDSTAKQQTAK 177
Cdd:cd03279 95 RGLdYDQFTRIvlLPQGEFDRFLARPVSTLSGGETFLASLSLALALSEvlqnrggarlEALFIDEGFGTLDPEALEAVAT 174
|
170 180
....*....|....*....|....*..
gi 504819384 178 LLQRLKDEGVTIMISSHeahtVEHIAD 204
Cdd:cd03279 175 ALELIRTENRMVGVISH----VEELKE 197
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
133-207 |
1.05e-05 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 45.83 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 133 PAKQLSGGEKQRVALtrARILSPR-----LLLLDEPTasmdstakqqT-------AKL---LQRLKDEGVTIMIssheah 197
Cdd:PRK00349 827 PATTLSGGEAQRVKL--AKELSKRstgktLYILDEPT----------TglhfediRKLlevLHRLVDKGNTVVV------ 888
|
90
....*....|....*.
gi 504819384 198 tVEH------IADHHI 207
Cdd:PRK00349 889 -IEHnldvikTADWII 903
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
115-212 |
1.13e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 45.98 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 115 KKVTQALDWADLSHLahrPAKQ----LSGGEKQRVALTRARILSPR---LLLLDEPTASMDSTAKQQTAKLLQRLKDEGV 187
Cdd:PRK00635 1677 QKPLQALIDNGLGYL---PLGQnlssLSLSEKIAIKIAKFLYLPPKhptLFLLDEIATSLDNQQKSALLVQLRTLVSLGH 1753
|
90 100
....*....|....*....|....*
gi 504819384 188 TIMISSHEAHTVEHiADHHIHIEHG 212
Cdd:PRK00635 1754 SVIYIDHDPALLKQ-ADYLIEMGPG 1777
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
137-193 |
1.35e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 45.55 E-value: 1.35e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 504819384 137 LSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQQTAKLLQRLKDEGVT-IMISS 193
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGvIVISS 462
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
33-196 |
1.78e-05 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 44.23 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 33 TLLTGQNGSGKTTLLK-IMSGLLKPDSASINYQGLTLNWKQAKAYI----------------QKDIIYLHQQPY------ 89
Cdd:COG0419 26 NLIVGPNGAGKSTILEaIRYALYGKARSRSKLRSDLINVGSEEASVelefehggkryrierrQGEFAEFLEAKPserkea 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 90 ---LFDASVTDNIAYGLYRSGERKSNVHKKVTQALDWAD--LSHLAH-RPAKQLSGGEKQRVALtrARILSprlLLLDep 163
Cdd:COG0419 106 lkrLLGLEIYEELKERLKELEEALESALEELAELQKLKQeiLAQLSGlDPIETLSGGERLRLAL--ADLLS---LILD-- 178
|
170 180 190
....*....|....*....|....*....|...
gi 504819384 164 TASMDSTAKQQTAKLLQRLKdegvtimISSHEA 196
Cdd:COG0419 179 FGSLDEERLERLLDALEELA-------IITHVI 204
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
21-72 |
2.92e-05 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 43.83 E-value: 2.92e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 504819384 21 NIKHLDIP---AHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASI---NYQGLTLNWKQ 72
Cdd:COG3950 13 GFEDLEIDfdnPPRLTVLVGENGSGKTTLLEAIALALSGLLSRLddvKFRKLLIRNGE 70
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
8-194 |
3.08e-05 |
|
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: 44.07 E-value: 3.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 8 KNLAI--TLSGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSA----SINYQGLTLN-WKQAKAYIQkd 80
Cdd:cd03289 6 KDLTAkyTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGDiqidGVSWNSVPLQkWRKAFGVIP-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 81 iiylhQQPYLFDASVTDNI-AYGLYRSGERKsnvhkKVTQALDWAdlSHLAHRPAKQ----------LSGGEKQRVALTR 149
Cdd:cd03289 84 -----QKVFIFSGTFRKNLdPYGKWSDEEIW-----KVAEEVGLK--SVIEQFPGQLdfvlvdggcvLSHGHKQLMCLAR 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 504819384 150 ARILSPRLLLLDEPTASMDSTAKQQTAKLLQRlKDEGVTIMISSH 194
Cdd:cd03289 152 SVLSKAKILLLDEPSAHLDPITYQVIRKTLKQ-AFADCTVILSEH 195
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
35-199 |
5.23e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 43.81 E-value: 5.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 35 LTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNwKQAKAYIQKDIIYLHQQPYLFDASVTDNIA-------YGLYRSG 107
Cdd:PLN03232 1267 VVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVA-KFGLTDLRRVLSIIPQSPVLFSGTVRFNIDpfsehndADLWEAL 1345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 108 ERksnVHKKVTQALDWADLSHLAHRPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDStakqQTAKLLQR-LKDE- 185
Cdd:PLN03232 1346 ER---AHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDV----RTDSLIQRtIREEf 1418
|
170
....*....|....*
gi 504819384 186 -GVTIMISSHEAHTV 199
Cdd:PLN03232 1419 kSCTMLVIAHRLNTI 1433
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
135-210 |
6.64e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.49 E-value: 6.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 135 KQLSGGEKQ------RVALTR--------ARILSPrlLLLDEPTASMDSTAKQQTAKLLQRLKDEGV-TIMISSHEAHTV 199
Cdd:PRK02224 780 EQLSGGERAlfnlslRCAIYRllaegiegDAPLPP--LILDEPTVFLDSGHVSQLVDLVESMRRLGVeQIVVVSHDDELV 857
|
90
....*....|.
gi 504819384 200 EHiADHHIHIE 210
Cdd:PRK02224 858 GA-ADDLVRVE 867
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
7-200 |
1.06e-04 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 42.38 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 7 YKNLAITLSGKLVLNIKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQgltlnwkqAKAYIQKDIIYLHQ 86
Cdd:pfam13304 115 AEELRLGLDVEERIELSLSELSDLISGLLLLSIISPLSFLLLLDEGLLLEDWAVLDLA--------ADLALFPDLKELLQ 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 87 QPYLFDASVTDNIAYGLYRSGERKSNVHKKVTQALDWADLSHLAHRPAKQLSGGEKQ---RVALTRARILSPRLLLLDEP 163
Cdd:pfam13304 187 RLVRGLKLADLNLSDLGEGIEKSLLVDDRLRERGLILLENGGGGELPAFELSDGTKRllaLLAALLSALPKGGLLLIDEP 266
|
170 180 190
....*....|....*....|....*....|....*..
gi 504819384 164 TASMDSTAKQQTAKLLQRLKDEGVTIMISSHEAHTVE 200
Cdd:pfam13304 267 ESGLHPKLLRRLLELLKELSRNGAQLILTTHSPLLLD 303
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
136-212 |
2.19e-04 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 41.22 E-value: 2.19e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504819384 136 QLSGGEKQRVALTRARILSPRLLLLDEPTASMDSTAKQQTAKLLQRL-KDEGVTIMISSHEAHTVEHIADHHIHIEHG 212
Cdd:PRK10418 140 EMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIvQKRALGMLLVTHDMGVVARLADDVAVMSHG 217
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
35-204 |
2.43e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 41.80 E-value: 2.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 35 LTGQNGSGKTTLLKIMSGLLKPDSASINyqgLTLNWKQAK------AYIQ--------------------KDIIYLhqqp 88
Cdd:PRK15064 32 LIGANGCGKSTFMKILGGDLEPSAGNVS---LDPNERLGKlrqdqfAFEEftvldtvimghtelwevkqeRDRIYA---- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 89 yLFDASVTDNIA----------YGLY----RSGERKSNVHKKVTQaldwadlsHLAhrPAKQLSGGEKQRVALTRARILS 154
Cdd:PRK15064 105 -LPEMSEEDGMKvadlevkfaeMDGYtaeaRAGELLLGVGIPEEQ--------HYG--LMSEVAPGWKLRVLLAQALFSN 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 504819384 155 PRLLLLDEPTASMDStakqQTAKLLQR-LKDEGVTIMISSHEAH---TV-EHIAD 204
Cdd:PRK15064 174 PDILLLDEPTNNLDI----NTIRWLEDvLNERNSTMIIISHDRHflnSVcTHMAD 224
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
25-58 |
3.39e-04 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 37.58 E-value: 3.39e-04
10 20 30
....*....|....*....|....*....|....
gi 504819384 25 LDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDS 58
Cdd:pfam13555 17 IPIDPRGNTLLTGPSGSGKSTLLDAIQTLLVPAK 50
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
131-181 |
3.55e-04 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 38.37 E-value: 3.55e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504819384 131 HRPAKQLSGGEKQRVA-------------LTRARILSPRLLLLDEPTASMDSTAKQQTAKLLQR 181
Cdd:pfam13558 27 YRRSGGLSGGEKQLLAylplaaalaaqygSAEGRPPAPRLVFLDEAFAKLDEENIRTALELLRA 90
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
21-232 |
5.83e-04 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 40.37 E-value: 5.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 21 NIKHLDIP-AHQCTLLTGQNGSGKTTLLKIMSGLLKPDSA----------SINYQG----LTLNWKQAKAYIQKDIIY-- 83
Cdd:COG3593 13 SIKDLSIElSDDLTVLVGENNSGKSSILEALRLLLGPSSSrkfdeedfylGDDPDLpeieIELTFGSLLSRLLRLLLKee 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 84 ----LHQQPYLFDASVTDNIA--------YGLYRSGERKSNVHKKVTQALDWAD-----LSHLAHRPAKQLSGGEKQRVA 146
Cdd:COG3593 93 dkeeLEEALEELNEELKEALKalnellseYLKELLDGLDLELELSLDELEDLLKslslrIEDGKELPLDRLGSGFQRLIL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 147 LTRARILS-------PRLLLLDEPTASMDSTAKQQTAKLLQRLKDEGVTIMISSHEAHTVEHIADHHIHIehgnaLIRPP 219
Cdd:COG3593 173 LALLSALAelkrapaNPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTHSPHLLSEVPLENIRR-----LRRDS 247
|
250
....*....|...
gi 504819384 220 NSNNVTMINTAKK 232
Cdd:COG3593 248 GGTTSTKLIDLDD 260
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
126-209 |
6.34e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.58 E-value: 6.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 126 LSHLA-HRPAKQLSGGEKQRVALtrARILSPRLL----LLDEPTASMDSTAKQQTAKLLQRLKDEGVTIMISSHEAHTVE 200
Cdd:PRK00635 465 LPYLTpERALATLSGGEQERTAL--AKHLGAELIgityILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDEQMIS 542
|
....*....
gi 504819384 201 hIADHHIHI 209
Cdd:PRK00635 543 -LADRIIDI 550
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
132-212 |
9.83e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 40.01 E-value: 9.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 132 RPAKQLSGGEKQRVALTRArI---LSPRLLLLDEPTASM---DstakqqTAKL---LQRLKDEGVTIMIssheahtVEH- 201
Cdd:COG0178 481 RSAGTLSGGEAQRIRLATQ-IgsgLVGVLYVLDEPSIGLhqrD------NDRLietLKRLRDLGNTVIV-------VEHd 546
|
90 100
....*....|....*....|.
gi 504819384 202 -----IADHHIHI-----EHG 212
Cdd:COG0178 547 edtirAADYIIDIgpgagEHG 567
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
37-199 |
1.21e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 39.72 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 37 GQNGSGKTTLLKIMSGLLKPDSASINYQGLTLNwKQAKAYIQKDIIYLHQQPYLFDASVTDNIA-------YGLYRSGER 109
Cdd:PLN03130 1272 GRTGAGKSSMLNALFRIVELERGRILIDGCDIS-KFGLMDLRKVLGIIPQAPVLFSGTVRFNLDpfnehndADLWESLER 1350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 110 K--SNVHKKVTQALDwADLSHlahrPAKQLSGGEKQRVALTRARILSPRLLLLDEPTASMDStakqQTAKLLQR-LKDE- 185
Cdd:PLN03130 1351 AhlKDVIRRNSLGLD-AEVSE----AGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDV----RTDALIQKtIREEf 1421
|
170
....*....|....*
gi 504819384 186 -GVTIMISSHEAHTV 199
Cdd:PLN03130 1422 kSCTMLIIAHRLNTI 1436
|
|
| RecF |
COG1195 |
Recombinational DNA repair ATPase RecF [Replication, recombination and repair]; |
21-47 |
2.80e-03 |
|
Recombinational DNA repair ATPase RecF [Replication, recombination and repair];
Pssm-ID: 440808 [Multi-domain] Cd Length: 352 Bit Score: 38.21 E-value: 2.80e-03
10 20
....*....|....*....|....*...
gi 504819384 21 NIKHLDI-PAHQCTLLTGQNGSGKTTLL 47
Cdd:COG1195 12 NYESLELeFSPGINVLVGPNGQGKTNLL 39
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
137-194 |
3.36e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 38.34 E-value: 3.36e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504819384 137 LSGGEKQ------RVALTRARILSPRLLLLDEPTASMDSTAKQQTAKLLQ-RLKDEGV---TIMISSH 194
Cdd:PRK01156 802 LSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTNLKDIIEySLKDSSDipqVIMISHH 869
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
21-47 |
3.62e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 37.99 E-value: 3.62e-03
10 20
....*....|....*....|....*..
gi 504819384 21 NIKHLDIPAHQCTLLTGQNGSGKTTLL 47
Cdd:COG4637 12 SLRDLELPLGPLTVLIGANGSGKSNLL 38
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
33-116 |
4.47e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 37.37 E-value: 4.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 33 TLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGL------------TLNWKQAKAYIQKDIIYLHQQPYLFDASVTDNia 100
Cdd:pfam13304 2 NVLIGPNGSGKSNLLEALRFLADFDALVIGLTDErsrnggiggipsLLNGIDPKEPIEFEISEFLEDGVRYRYGLDLE-- 79
|
90
....*....|....*.
gi 504819384 101 ygLYRSGERKSNVHKK 116
Cdd:pfam13304 80 --REDVEEKLSSKPTL 93
|
|
| COG4938 |
COG4938 |
Predicted ATPase [General function prediction only]; |
22-202 |
4.50e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443965 [Multi-domain] Cd Length: 277 Bit Score: 37.26 E-value: 4.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 22 IKHLDIPAHQCTLLTGQNGSGKTTLLKIMSGLLKPDSASINYQGLTLnwkqakAYIQKDIIYLHQQPYLFDASVTDNIA- 100
Cdd:COG4938 12 FKEAELELKPLTLLIGPNGSGKSTLIQALLLLLQSNFIYLPAERSGP------ARLYPSLVRELSDLGSRGEYTADFLAe 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504819384 101 YGLYRSGERKSNVHKKvtQALDWadLSHL--------AHRPAKQL-----SGGEKQRVA------------LTRARILSP 155
Cdd:COG4938 86 LENLEILDDKSKELLE--QVEEW--LEKIfpgkvevdASSDLVRLvfrpsGNGKRIPLSnvgsgvsellpiLLALLSAAK 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 504819384 156 R--LLLLDEPTASMDSTAKQQTAKLLQRLKDEGVTIMISSHEAHTVEHI 202
Cdd:COG4938 162 PgsLLIIEEPEAHLHPKAQSALAELLAELANSGVQVIIETHSDYILNGL 210
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
33-57 |
5.05e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 37.59 E-value: 5.05e-03
10 20
....*....|....*....|....*
gi 504819384 33 TLLTGQNGSGKTTLLKIMSGLLKPD 57
Cdd:COG4913 27 TLLTGDNGSGKSTLLDAIQTLLVPA 51
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
6-47 |
6.07e-03 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 36.71 E-value: 6.07e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 504819384 6 SYKNLAITLSGKLvlnikhldipahqcTLLTGQNGSGKTTLL 47
Cdd:pfam13476 8 SFRDQTIDFSKGL--------------TLITGPNGSGKTTIL 35
|
|
| |
