|
Name |
Accession |
Description |
Interval |
E-value |
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-251 |
2.33e-175 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 482.28 E-value: 2.33e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 1 MIEISKISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVLAKNLSIL 80
Cdd:COG4604 1 MIEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 81 RQENQFVSRLTVEELVGFGRYPYSKGRLTLDDKKVIDESLAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQDTEYVMLD 160
Cdd:COG4604 81 RQENHINSRLTVRELVAFGRFPYSKGRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 161 EPLNNLDMKHAVIMMKLLRKAADELGKTIIIVIHDINFASVYSDYILAMRNGQLYYHGSPKEIMKADIIEDIFDTPVDVK 240
Cdd:COG4604 161 EPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEIITPEVLSDIYDTDIEVE 240
|
250
....*....|.
gi 1943291881 241 ELDNKLIAMYY 251
Cdd:COG4604 241 EIDGKRICVYF 251
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-239 |
4.39e-101 |
|
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: 294.26 E-value: 4.39e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 1 MIEISKISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVLAKNLSIL 80
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 81 RQENQFVSRLTVEELVGFGRYPYSK--GRLTLDDKKVIDESLAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQDTEYVM 158
Cdd:COG1120 81 PQEPPAPFGLTVRELVALGRYPHLGlfGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 159 LDEPLNNLDMKHAVIMMKLLRKAADELGKTIIIVIHDINFASVYSDYILAMRNGQLYYHGSPKEIMKADIIEDIFDTPVD 238
Cdd:COG1120 161 LDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLTPELLEEVYGVEAR 240
|
.
gi 1943291881 239 V 239
Cdd:COG1120 241 V 241
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-239 |
1.57e-77 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 234.52 E-value: 1.57e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 1 MIEISKISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVLAKNLSIL 80
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 81 RQENQFVSRLTVEELVGFGRYPYSK--GRLTLDDKKVIDESLAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQDTEYVM 158
Cdd:PRK11231 82 PQHHLTPEGITVRELVAYGRSPWLSlwGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 159 LDEPLNNLDMKHAVIMMKLLRKAADElGKTIIIVIHDINFASVYSDYILAMRNGQLYYHGSPKEIMKADIIEDIFDTPVD 238
Cdd:PRK11231 162 LDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTPGLLRTVFDVEAE 240
|
.
gi 1943291881 239 V 239
Cdd:PRK11231 241 I 241
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
3-218 |
1.46e-68 |
|
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: 209.21 E-value: 1.46e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 3 EISKISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVLAKNLSILRQ 82
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 83 enqfvsrltveelvgfgrypyskgrltlddkkvideSLAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQDTEYVMLDEP 162
Cdd:cd03214 81 ------------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEP 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1943291881 163 LNNLDMKHAVIMMKLLRKAADELGKTIIIVIHDINFASVYSDYILAMRNGQLYYHG 218
Cdd:cd03214 125 TSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-243 |
1.70e-66 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 206.09 E-value: 1.70e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 1 MIEISKISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDV--LAKNLS 78
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRRIgyVPQRAE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 79 ILRQenqFvsRLTVEELVGFGRYPYSK--GRLTLDDKKVIDESLAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQDTEY 156
Cdd:COG1121 86 VDWD---F--PITVRDVVLMGRYGRRGlfRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 157 VMLDEPLNNLDMKHAVIMMKLLRKAADElGKTIIIVIHDINFASVYSDYILAMrNGQLYYHGSPKEIMKADIIEDIFDTP 236
Cdd:COG1121 161 LLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLL-NRGLVAHGPPEEVLTPENLSRAYGGP 238
|
....*..
gi 1943291881 237 VDVKELD 243
Cdd:COG1121 239 VALLAHG 245
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-239 |
9.82e-66 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 204.58 E-value: 9.82e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 1 MIEISKISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVLAKNLSIL 80
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 81 RQEnqfvSRL----TVEELVGFGRYPYskGRLTLDDKKVIDESLAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQ---- 152
Cdd:COG4559 81 PQH----SSLafpfTVEEVVALGRAPH--GSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAQlwep 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 153 ---DTEYVMLDEPLNNLDMKHAVIMMKLLRKAADElGKTIIIVIHDINFASVYSDYILAMRNGQLYYHGSPKEIMKADII 229
Cdd:COG4559 155 vdgGPRWLFLDEPTSALDLAHQHAVLRLARQLARR-GGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLTDELL 233
|
250
....*....|
gi 1943291881 230 EDIFDTPVDV 239
Cdd:COG4559 234 ERVYGADLRV 243
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-239 |
1.10e-65 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 204.62 E-value: 1.10e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 1 MIEISKISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVLAKNLSIL 80
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 81 RQENQFVSRLTVEELVGFGRYPYSKGRltLDDKKVIDESLAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQDTE----- 155
Cdd:PRK13548 82 PQHSSLSFPFTVEEVVAMGRAPHGLSR--AEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQLWEpdgpp 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 156 -YVMLDEPLNNLDMKHAVIMMKLLRKAADELGKTIIIVIHDINFASVYSDYILAMRNGQLYYHGSPKEIMKADIIEDIFD 234
Cdd:PRK13548 160 rWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVLTPETLRRVYG 239
|
....*
gi 1943291881 235 TPVDV 239
Cdd:PRK13548 240 ADVLV 244
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
15-239 |
8.66e-62 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 195.01 E-value: 8.66e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 15 TVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVLAKNLSILRQENQFVSRLTVEE 94
Cdd:PRK10575 25 TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQLPAAEGMTVRE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 95 LVGFGRYPY--SKGRLTLDDKKVIDESLAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQDTEYVMLDEPLNNLDMKHAV 172
Cdd:PRK10575 105 LVAIGRYPWhgALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQV 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1943291881 173 IMMKLLRKAADELGKTIIIVIHDINFASVYSDYILAMRNGQLYYHGSPKEIMKADIIEDIFDTPVDV 239
Cdd:PRK10575 185 DVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETLEQIYGIPMGI 251
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
3-218 |
7.42e-59 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 185.43 E-value: 7.42e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 3 EISKISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDV--LAKNLSIL 80
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKRIgyVPQRRSID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 81 RQenqfvSRLTVEELVGFGRYPYSK--GRLTLDDKKVIDESLAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQDTEYVM 158
Cdd:cd03235 81 RD-----FPISVRDVVLMGLYGHKGlfRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 159 LDEPLNNLDMKHAVIMMKLLRKAADElGKTIIIVIHDINFASVYSDYILAMrNGQLYYHG 218
Cdd:cd03235 156 LDEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLL-NRTVVASG 213
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-233 |
1.10e-57 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 183.34 E-value: 1.10e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 2 IEISKISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVLAKnLSILR 81
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRR-IGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 82 QENQFVSRLTVEELVGF-GRYpysKGRLTLDDKKVIDESLAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQDTEYVMLD 160
Cdd:COG1131 80 QEPALYPDLTVRENLRFfARL---YGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1943291881 161 EPLNNLDMKHAVIMMKLLRKAADElGKTIIIVIHDINFASVYSDYILAMRNGQLYYHGSPKEImKADIIEDIF 233
Cdd:COG1131 157 EPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL-KARLLEDVF 227
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-225 |
2.58e-57 |
|
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: 182.15 E-value: 2.58e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 2 IEISKISKHYQD-ITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVLAKNLSIL 80
Cdd:COG1122 1 IELENLSFSYPGgTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 81 RQ--ENQFVSRlTVEELVGFGryPYSKGrltLDDKKV---IDESLAFLNLTEFRHRYLDELSGGQRQRtyVAM--VLCQD 153
Cdd:COG1122 81 FQnpDDQLFAP-TVEEDVAFG--PENLG---LPREEIrerVEEALELVGLEHLADRPPHELSGGQKQR--VAIagVLAME 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1943291881 154 TEYVMLDEPLNNLDMKHAVIMMKLLRKAADElGKTIIIVIHDINFASVYSDYILAMRNGQLYYHGSPKEIMK 225
Cdd:COG1122 153 PEVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFS 223
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-233 |
7.55e-57 |
|
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: 181.59 E-value: 7.55e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 1 MIEISKISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVLaKNLSIL 80
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREAR-RQIGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 81 RQENQFVSRLTVEELVGFgrypYSKGRLTLDD--KKVIDESLAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQDTEYVM 158
Cdd:COG4555 80 PDERGLYDRLTVRENIRY----FAELYGLFDEelKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1943291881 159 LDEPLNNLDMKHAVIMMKLLRKAADElGKTIIIVIHDINFASVYSDYILAMRNGQLYYHGSPKEIMKA---DIIEDIF 233
Cdd:COG4555 156 LDEPTNGLDVMARRLLREILRALKKE-GKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEigeENLEDAF 232
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
11-233 |
1.43e-55 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 179.03 E-value: 1.43e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 11 YQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVLAKNLSILRQENQFVSRL 90
Cdd:PRK10253 17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 91 TVEELVGFGRYPYSK--GRLTLDDKKVIDESLAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQDTEYVMLDEPLNNLDM 168
Cdd:PRK10253 97 TVQELVARGRYPHQPlfTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDI 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1943291881 169 KHAVIMMKLLRKAADELGKTIIIVIHDINFASVYSDYILAMRNGQLYYHGSPKEIMKADIIEDIF 233
Cdd:PRK10253 177 SHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERIY 241
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-234 |
1.06e-54 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 176.02 E-value: 1.06e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 1 MIEISKISKHYQ-DITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVLAKnlsi 79
Cdd:COG3638 2 MLELRNLSKRYPgGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRR---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 80 LR-------QENQFVSRLTVEELVGFGRYPYSK------GRLTLDDKKVIDESLAFLNLTEFRHRYLDELSGGQRQRTYV 146
Cdd:COG3638 78 LRrrigmifQQFNLVPRLSVLTNVLAGRLGRTStwrsllGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 147 AMVLCQDTEYVMLDEPLNNLDMKHAVIMMKLLRKAADELGKTIIIVIHDINFASVYSDYILAMRNGQLYYHGSPKEImKA 226
Cdd:COG3638 158 ARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAEL-TD 236
|
....*...
gi 1943291881 227 DIIEDIFD 234
Cdd:COG3638 237 AVLREIYG 244
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
3-213 |
1.06e-53 |
|
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: 172.27 E-value: 1.06e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 3 EISKISKHYQD--ITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVLAKNLSIL 80
Cdd:cd03225 1 ELKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 81 RQ--ENQFVsRLTVEELVGFGryPYSKGRLTLDDKKVIDESLAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQDTEYVM 158
Cdd:cd03225 81 FQnpDDQFF-GPTVEEEVAFG--LENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1943291881 159 LDEPLNNLDMKHAVIMMKLLRKAADElGKTIIIVIHDINFASVYSDYILAMRNGQ 213
Cdd:cd03225 158 LDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-239 |
7.03e-53 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 176.19 E-value: 7.03e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 1 MIEISKISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVLAKNLSIL 80
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 81 RQENQFVSRLTVEELVGFGRYPYSK--GRLTLDDKKVIDESLAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQDTEYVM 158
Cdd:PRK09536 83 PQDTSLSFEFDVRQVVEMGRTPHRSrfDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 159 LDEPLNNLDMKHAVIMMKLLRKAADElGKTIIIVIHDINFASVYSDYILAMRNGQLYYHGSPKEIMKADIIEDIFDTPVD 238
Cdd:PRK09536 163 LDEPTASLDINHQVRTLELVRRLVDD-GKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADTLRAAFDARTA 241
|
.
gi 1943291881 239 V 239
Cdd:PRK09536 242 V 242
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-228 |
2.15e-52 |
|
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: 170.17 E-value: 2.15e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 1 MIEISKISKHY-QDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDsdvlAKNLSI 79
Cdd:TIGR02315 1 MLEVENLSKVYpNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLR----GKKLRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 80 LR-------QENQFVSRLTVEELVGFGRYPYSK------GRLTLDDKKVIDESLAFLNLTEFRHRYLDELSGGQRQRTYV 146
Cdd:TIGR02315 77 LRrrigmifQHYNLIERLTVLENVLHGRLGYKPtwrsllGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 147 AMVLCQDTEYVMLDEPLNNLDMKHAVIMMKLLRKAADELGKTIIIVIHDINFASVYSDYILAMRNGQLYYHGSPKEIMKA 226
Cdd:TIGR02315 157 ARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDDE 236
|
..
gi 1943291881 227 DI 228
Cdd:TIGR02315 237 VL 238
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-233 |
2.75e-51 |
|
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: 167.36 E-value: 2.75e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 2 IEISKISKHY-QDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVaatdSDVLAKNLSIL 80
Cdd:cd03256 1 IEVENLSKTYpNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDI----NKLKGKALRQL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 81 R-------QENQFVSRLTVEELVGFGRYPYSK------GRLTLDDKKVIDESLAFLNLTEFRHRYLDELSGGQRQRTYVA 147
Cdd:cd03256 77 RrqigmifQQFNLIERLSVLENVLSGRLGRRStwrslfGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 148 MVLCQDTEYVMLDEPLNNLDMKHAVIMMKLLRKAADELGKTIIIVIHDINFASVYSDYILAMRNGQLYYHGSPKEImKAD 227
Cdd:cd03256 157 RALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL-TDE 235
|
....*.
gi 1943291881 228 IIEDIF 233
Cdd:cd03256 236 VLDEIY 241
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-214 |
1.19e-50 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 165.22 E-value: 1.19e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 1 MIEISKISKHYQD----ITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVLAKn 76
Cdd:COG1136 4 LLELRNLTKSYGTgegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELAR- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 77 lsiLRQEN-----QF---VSRLTVEELVGFGRYPysKGRLTLDDKKVIDESLAFLNLTEFRHRYLDELSGGQRQRTYVAM 148
Cdd:COG1136 83 ---LRRRHigfvfQFfnlLPELTALENVALPLLL--AGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1943291881 149 VLCQDTEYVMLDEPLNNLDMKHAVIMMKLLRKAADELGKTIIIVIHDINFASvYSDYILAMRNGQL 214
Cdd:COG1136 158 ALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAA-RADRVIRLRDGRI 222
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-214 |
9.02e-50 |
|
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: 162.66 E-value: 9.02e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 2 IEISKISKHYQD----ITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVLA--- 74
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 75 -KNLSILRQENQFVSRLTVEELVgfgRYP-YSKGRLTLDDKKVIDESLAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQ 152
Cdd:cd03255 81 rRHIGFVFQSFNLLPDLTALENV---ELPlLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALAN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1943291881 153 DTEYVMLDEPLNNLDMKHAVIMMKLLRKAADELGKTIIIVIHDINFASvYSDYILAMRNGQL 214
Cdd:cd03255 158 DPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAE-YADRIIELRDGKI 218
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-227 |
4.11e-48 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 158.76 E-value: 4.11e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 1 MIEISKISKHYQDITVldNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDvlAKNLSIL 80
Cdd:COG3840 1 MLRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPA--ERPVSML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 81 RQENQFVSRLTVEELVGFGRYPysKGRLTLDDKKVIDESLAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQDTEYVMLD 160
Cdd:COG3840 77 FQENNLFPHLTVAQNIGLGLRP--GLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1943291881 161 EPLNNLD--MKHAviMMKLLRKAADELGKTIIIVIHDINFASVYSDYILAMRNGQLYYHGSPKEIMKAD 227
Cdd:COG3840 155 EPFSALDpaLRQE--MLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGE 221
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-214 |
1.44e-47 |
|
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: 156.53 E-value: 1.44e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 2 IEISKISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVaaTDSDVLAKNLSILR 81
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV--TGVPPERRNIGMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 82 QENQFVSRLTVEELVGFGryPYSKGRLTLDDKKVIDESLAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQDTEYVMLDE 161
Cdd:cd03259 79 QDYALFPHLTVAENIAFG--LKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1943291881 162 PLNNLDMKHAVIMMKLLRKAADELGKTIIIVIHDINFASVYSDYILAMRNGQL 214
Cdd:cd03259 157 PLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRI 209
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-227 |
1.33e-46 |
|
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: 154.97 E-value: 1.33e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 2 IEISKISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAA---TDSDVLAKNLS 78
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGlseAELYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 79 ILRQENQFVSRLTVEELVGFGRYPYSKGRLTLDDKKVIdESLAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQDTEYVM 158
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFPLREHTRLSEEEIREIVL-EKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1943291881 159 LDEPLNNLDMKHAVIMMKLLRKAADELGKTIIIVIHDINFASVYSDYILAMRNGQLYYHGSPKEIMKAD 227
Cdd:cd03261 160 YDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRASD 228
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-213 |
5.67e-46 |
|
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: 151.57 E-value: 5.67e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 2 IEISKISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVLA--KNLSI 79
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPlrRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 80 LRQENQFVSRLTVEELVGFGrypyskgrltlddkkvideslaflnltefrhryldeLSGGQRQRTYVAMVLCQDTEYVML 159
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG------------------------------------LSGGQQQRVALARALAMDPDVLLL 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1943291881 160 DEPLNNLDMKHAVIMMKLLRKAADELGKTIIIVIHDINFASVYSDYILAMRNGQ 213
Cdd:cd03229 125 DEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
2-225 |
6.84e-46 |
|
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: 152.98 E-value: 6.84e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 2 IEISKISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVLAKnLSILR 81
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIAR-LGIGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 82 --QENQFVSRLTVEELV----------GFGRYPYSKGRLTLDDKkvIDESLAFLNLTEFRHRYLDELSGGQRQRTYVAMV 149
Cdd:cd03219 80 tfQIPRLFPELTVLENVmvaaqartgsGLLLARARREEREARER--AEELLERVGLADLADRPAGELSYGQQRRLEIARA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1943291881 150 LCQDTEYVMLDEPLNNLDMKHAVIMMKLLRKAADElGKTIIIVIHDINFASVYSDYILAMRNGQLYYHGSPKEIMK 225
Cdd:cd03219 158 LATDPKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
11-200 |
2.75e-45 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 150.08 E-value: 2.75e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 11 YQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGmdvaatdsdvlAKNLSILRQENQFVSRL 90
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-----------GARVAYVPQRSEVPDSL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 91 --TVEELVGFGRYPY--SKGRLTLDDKKVIDESLAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQDTEYVMLDEPLNNL 166
Cdd:NF040873 71 plTVRDLVAMGRWARrgLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGL 150
|
170 180 190
....*....|....*....|....*....|....
gi 1943291881 167 DMKHAVIMMKLLRKAADElGKTIIIVIHDINFAS 200
Cdd:NF040873 151 DAESRERIIALLAEEHAR-GATVVVVTHDLELVR 183
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-224 |
5.95e-45 |
|
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: 157.37 E-value: 5.95e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 1 MIEISKISKHY-----QDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVLAK 75
Cdd:COG1123 260 LLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 76 nlsiLRQENQFV---------SRLTVEELVGFGryPYSKGRLTLDD-KKVIDESLAFLNL-TEFRHRYLDELSGGQRQRT 144
Cdd:COG1123 340 ----LRRRVQMVfqdpysslnPRMTVGDIIAEP--LRLHGLLSRAErRERVAELLERVGLpPDLADRYPHELSGGQRQRV 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 145 YVAMVLCQDTEYVMLDEPLNNLDMKHAVIMMKLLRKAADELGKTIIIVIHDINFASVYSDYILAMRNGQLYYHGSPKEIM 224
Cdd:COG1123 414 AIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVF 493
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-214 |
3.29e-44 |
|
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: 146.77 E-value: 3.29e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 2 IEISKISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVLaKNLSILR 81
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVK-RRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 82 QENQFVSRLTVEELVgfgrypyskgrltlddkkvideslaflnltefrhryldELSGGQRQRTYVAMVLCQDTEYVMLDE 161
Cdd:cd03230 80 EEPSLYENLTVRENL--------------------------------------KLSGGMKQRLALAQALLHDPELLILDE 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1943291881 162 PLNNLDMKHAVIMMKLLRKAADElGKTIIIVIHDINFASVYSDYILAMRNGQL 214
Cdd:cd03230 122 PTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-225 |
2.42e-43 |
|
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: 147.11 E-value: 2.42e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 1 MIEISKISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVLAKnLSIL 80
Cdd:COG0411 4 LLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIAR-LGIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 81 R--QENQFVSRLTVEE--LVGF---GRYPYSKGRLTL-----DDKKVIDES---LAFLNLTEFRHRYLDELSGGQRQRTY 145
Cdd:COG0411 83 RtfQNPRLFPELTVLEnvLVAAharLGRGLLAALLRLprarrEEREARERAeelLERVGLADRADEPAGNLSYGQQRRLE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 146 VAMVLCQDTEYVMLDEP---LNNLDMKHaviMMKLLRKAADELGKTIIIVIHDINFASVYSDYILAMRNGQLYYHGSPKE 222
Cdd:COG0411 163 IARALATEPKLLLLDEPaagLNPEETEE---LAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAE 239
|
...
gi 1943291881 223 IMK 225
Cdd:COG0411 240 VRA 242
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-246 |
8.11e-43 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 146.44 E-value: 8.11e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 2 IEISKISKHYQ-----DITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDsdvlAKN 76
Cdd:TIGR04521 1 IKLKNVSYIYQpgtpfEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKK----KKK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 77 LSILRQ---------ENQFVSRlTVEELVGFG--RYPYSKGRLtldDKKVIdESLAFLNLTEfrhRYLD----ELSGGQR 141
Cdd:TIGR04521 77 LKDLRKkvglvfqfpEHQLFEE-TVYKDIAFGpkNLGLSEEEA---EERVK-EALELVGLDE---EYLErspfELSGGQM 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 142 QRTYVAMVLCQDTEYVMLDEPLNNLDMKHAVIMMKLLRKAADELGKTIIIVIHDINFASVYSDYILAMRNGQLYYHGSPK 221
Cdd:TIGR04521 149 RRVAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPR 228
|
250 260
....*....|....*....|....*..
gi 1943291881 222 EI-MKADIIEDI-FDTPvDVKELDNKL 246
Cdd:TIGR04521 229 EVfSDVDELEKIgLDVP-EITELARKL 254
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-227 |
2.40e-42 |
|
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: 143.97 E-value: 2.40e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 1 MIEISKISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVLA---KNL 77
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYelrRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 78 SILRQENQFVSRLTVEELVGFG-RYpysKGRLTLDD-KKVIDESLAFLNLTEFRHRYLDELSGGQRQRtyV----AMVLc 151
Cdd:COG1127 85 GMLFQGGALFDSLTVFENVAFPlRE---HTDLSEAEiRELVLEKLELVGLPGAADKMPSELSGGMRKR--ValarALAL- 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1943291881 152 qDTEYVMLDEPLNNLDMKHAVIMMKLLRKAADELGKTIIIVIHDINFASVYSDYILAMRNGQLYYHGSPKEIMKAD 227
Cdd:COG1127 159 -DPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASD 233
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-224 |
4.51e-42 |
|
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: 143.60 E-value: 4.51e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 2 IEISKISKHYQDIT-VLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVLAKNLSIL 80
Cdd:cd03295 1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 81 RQENQFVSRLTVEELVGFgrYPYSKGRLTLDDKKVIDESLAFLNL--TEFRHRYLDELSGGQRQRTYVAMVLCQDTEYVM 158
Cdd:cd03295 81 IQQIGLFPHMTVEENIAL--VPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1943291881 159 LDEPLNNLDMKHAVIMMKLLRKAADELGKTIIIVIHDINFASVYSDYILAMRNGQLYYHGSPKEIM 224
Cdd:cd03295 159 MDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
2-218 |
1.79e-41 |
|
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: 141.09 E-value: 1.79e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 2 IEISKISKHYQDITVldNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAAtdSDVLAKNLSILR 81
Cdd:cd03298 1 VRLDKIRFSYGEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTA--APPADRPVSMLF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 82 QENQFVSRLTVEELVGFGRYPysKGRLTLDDKKVIDESLAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQDTEYVMLDE 161
Cdd:cd03298 77 QENNLFAHLTVEQNVGLGLSP--GLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1943291881 162 PLNNLDMKHAVIMMKLLRKAADELGKTIIIVIHDINFASVYSDYILAMRNGQLYYHG 218
Cdd:cd03298 155 PFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-218 |
4.36e-41 |
|
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: 140.33 E-value: 4.36e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 1 MIEISKISKHYQD----ITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDsdvlAKN 76
Cdd:cd03257 1 LLEVKNLSVSFPTgggsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLS----RRL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 77 LSILRQENQFVS---------RLTVEELVGFGRYPYSKGRLTLDDKKVIDESLAFLNLTE-FRHRYLDELSGGQRQRTYV 146
Cdd:cd03257 77 RKIRRKEIQMVFqdpmsslnpRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEeVLNRYPHELSGGQRQRVAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1943291881 147 AMVLCQDTEYVMLDEPLNNLDMKHAVIMMKLLRKAADELGKTIIIVIHDINFASVYSDYILAMRNGQLYYHG 218
Cdd:cd03257 157 ARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-226 |
2.28e-40 |
|
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: 145.43 E-value: 2.28e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 1 MIEISKISKHY--QDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPE---SGMVSVNGMDVAATDSDVLAK 75
Cdd:COG1123 4 LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 76 NLSILRQE--NQFVSrLTVEELVGFGrypYSKGRLTLDD-KKVIDESLAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQ 152
Cdd:COG1123 84 RIGMVFQDpmTQLNP-VTVGDQIAEA---LENLGLSRAEaRARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1943291881 153 DTEYVMLDEPLNNLDMKHAVIMMKLLRKAADELGKTIIIVIHDINFASVYSDYILAMRNGQLYYHGSPKEIMKA 226
Cdd:COG1123 160 DPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAA 233
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-211 |
2.85e-40 |
|
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: 137.99 E-value: 2.85e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 2 IEISKISKHYQD----ITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVlaknl 77
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPDR----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 78 SILRQENQFVSRLTVEELVGFGryPYSKGRLTLDDKKVIDESLAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQDTEYV 157
Cdd:cd03293 76 GYVFQQDALLPWLTVLDNVALG--LELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1943291881 158 MLDEPLNNLDMKHAVIMMKLLRKAADELGKTIIIVIHDINFASVYSDYILAMRN 211
Cdd:cd03293 154 LLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSA 207
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-223 |
1.47e-39 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 139.85 E-value: 1.47e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 1 MIEISKISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVaatdSDVLA--KNLS 78
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDV----TGLPPekRNVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 79 ILRQE-----NqfvsrLTVEELVGFGrypyskgrltLDDKKV--------IDESLAFLNLTEFRHRYLDELSGGQRQRty 145
Cdd:COG3842 81 MVFQDyalfpH-----LTVAENVAFG----------LRMRGVpkaeirarVAELLELVGLEGLADRYPHQLSGGQQQR-- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 146 VAM---------VLcqdteyvMLDEPLNNLDMKHAVIMMKLLRKAADELGKTIIIVIHDINFASVYSDYILAMRNGQLYY 216
Cdd:COG3842 144 VALaralapeprVL-------LLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQ 216
|
....*..
gi 1943291881 217 HGSPKEI 223
Cdd:COG3842 217 VGTPEEI 223
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-223 |
2.56e-39 |
|
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: 136.21 E-value: 2.56e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 2 IEISKISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVaaTDSDVLAKNLSILR 81
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI--TNLPPHKRPVNTVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 82 QENQFVSRLTVEELVGFGRypyskgRLTLDDKKVI----DESLAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQDTEYV 157
Cdd:cd03300 79 QNYALFPHLTVFENIAFGL------RLKKLPKAEIkervAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1943291881 158 MLDEPLNNLDMKHAVIMMKLLRKAADELGKTIIIVIHDINFASVYSDYILAMRNGQLYYHGSPKEI 223
Cdd:cd03300 153 LLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-223 |
4.26e-39 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 138.74 E-value: 4.26e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 2 IEISKISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAAtdsdvlakNLSIlr 81
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFT--------NLPP-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 82 QENQ--FVSR-------LTVEELVGFG--RYPYSKGRLtlddKKVIDESLAFLNLTEFRHRYLDELSGGQRQRTYVAMVL 150
Cdd:COG1118 73 RERRvgFVFQhyalfphMTVAENIAFGlrVRPPSKAEI----RARVEELLELVQLEGLADRYPSQLSGGQRQRVALARAL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1943291881 151 CQDTEYVMLDEPLNNLDMKHAVIMMKLLRKAADELGKTIIIVIHDINFASVYSDYILAMRNGQLYYHGSPKEI 223
Cdd:COG1118 149 AVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEV 221
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-224 |
4.99e-39 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 135.61 E-value: 4.99e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 1 MIEISKISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVlaknlSIL 80
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDE-----RLI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 81 RQE-----NQF--VSRLTVEELVGFGryP-YSKGRLTLDDKKVIDESLAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQ 152
Cdd:PRK09493 76 RQEagmvfQQFylFPHLTALENVMFG--PlRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1943291881 153 DTEYVMLDEPLNNLD--MKHAVimMKLLRKAADElGKTIIIVIHDINFASVYSDYILAMRNGQLYYHGSPKEIM 224
Cdd:PRK09493 154 KPKLMLFDEPTSALDpeLRHEV--LKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLI 224
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-214 |
6.76e-39 |
|
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: 135.32 E-value: 6.76e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 1 MIEISKISKHY----QDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVLAKN 76
Cdd:COG1124 1 MLEVRNLSVSYgqggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 77 LSILRQeNQFVS---RLTVEELVgfgRYPYSKGRLTLDDKKvIDESLAFLNLT-EFRHRYLDELSGGQRQRTYVAMVLCQ 152
Cdd:COG1124 81 VQMVFQ-DPYASlhpRHTVDRIL---AEPLRIHGLPDREER-IAELLEQVGLPpSFLDRYPHQLSGGQRQRVAIARALIL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1943291881 153 DTEYVMLDEPLNNLDMKHAVIMMKLLRKAADELGKTIIIVIHDINFASVYSDYILAMRNGQL 214
Cdd:COG1124 156 EPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRI 217
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-212 |
6.76e-39 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 135.60 E-value: 6.76e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 1 MIEISKISKHYQ----DITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVlakn 76
Cdd:COG1116 7 ALELRGVSKRFPtgggGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPDR---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 77 lSILRQEnqfvSRL----TVEELVGFGryPYSKGRLTLDDKKVIDESLAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQ 152
Cdd:COG1116 83 -GVVFQE----PALlpwlTVLDNVALG--LELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALAN 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1943291881 153 DTEYVMLDEPLNNLDMKHAVIMMKLLRKAADELGKTIIIVIHDINFAsVY-SDYILAMRNG 212
Cdd:COG1116 156 DPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEA-VFlADRVVVLSAR 215
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
12-245 |
1.80e-38 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 134.20 E-value: 1.80e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 12 QDITV---LDNITTTIQRGGITSIIGPNGAGKSTLLSVI-GrlLLPESGMVSVNGMDVAATDSDVLAKNLSILRQENQFV 87
Cdd:COG4138 4 NDVAVagrLGPISAQVNAGELIHLIGPNGAGKSTLLARMaG--LLPGQGEILLNGRPLSDWSAAELARHRAYLSQQQSPP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 88 SRLTVEELVGFGrypYSKGRLTLDDKKVIDESLAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQ-------DTEYVMLD 160
Cdd:COG4138 82 FAMPVFQYLALH---QPAGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 161 EPLNNLDMKHAVIMMKLLRKAAdELGKTIIIVIHDINFASVYSDYILAMRNGQLYYHGSPKEIMKADIIEDIFDTPVDVK 240
Cdd:COG4138 159 EPMNSLDVAQQAALDRLLRELC-QQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMTPENLSEVFGVKFRRL 237
|
....*
gi 1943291881 241 ELDNK 245
Cdd:COG4138 238 EVEGH 242
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-236 |
3.00e-38 |
|
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: 133.62 E-value: 3.00e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 2 IEISKISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDvaATDSDVLAKNLSILR 81
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGED--ATDVPVQERNVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 82 QENQFVSRLTVEELVGFG-RYPYSKGRLTLDD-KKVIDESLAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQDTEYVML 159
Cdd:cd03296 81 QHYALFRHMTVFDNVAFGlRVKPRSERPPEAEiRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1943291881 160 DEPLNNLDMKHAVIMMKLLRKAADELGKTIIIVIHDINFASVYSDYILAMRNGQLYYHGSPkeimkadiiEDIFDTP 236
Cdd:cd03296 161 DEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTP---------DEVYDHP 228
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-195 |
4.28e-38 |
|
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: 132.22 E-value: 4.28e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 1 MIEISKISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVlAKNLSIL 80
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDY-RRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 81 RQENQFVSRLTVEELVGFgrypYSKGRLTLDDKKVIDESLAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQDTEYVMLD 160
Cdd:COG4133 81 GHADGLKPELTVRENLRF----WAALYGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLD 156
|
170 180 190
....*....|....*....|....*....|....*.
gi 1943291881 161 EPLNNLDmKHAV-IMMKLLRKAADElGKTIIIVIHD 195
Cdd:COG4133 157 EPFTALD-AAGVaLLAELIAAHLAR-GGAVLLTTHQ 190
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-213 |
1.84e-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: 128.90 E-value: 1.84e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 3 EISKISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVLAKNLSilrq 82
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIG---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 83 enqfvsrltveelvgfgrypyskgrltlddkkvideslaflnltefrhrYLDELSGGQRQRTYVAMVLCQDTEYVMLDEP 162
Cdd:cd00267 77 -------------------------------------------------YVPQLSGGQRQRVALARALLLNPDLLLLDEP 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1943291881 163 LNNLDMKHAVIMMKLLRKAADElGKTIIIVIHDINFASVYSDYILAMRNGQ 213
Cdd:cd00267 108 TSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-223 |
2.85e-37 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 130.88 E-value: 2.85e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 1 MIEISKISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVLAknlsiL 80
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDINK-----L 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 81 RQE--------NQFvSRLTVEELVGFGryP-YSKGRltlDDKKVIDESLAFLN---LTEFRHRYLDELSGGQRQRtyVAM 148
Cdd:COG1126 76 RRKvgmvfqqfNLF-PHLTVLENVTLA--PiKVKKM---SKAEAEERAMELLErvgLADKADAYPAQLSGGQQQR--VAI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 149 V--LCQDTEyVML-DEPLNNLD--MKHAVimMKLLRKAADElGKTIIIVIHDINFASVYSDYILAMRNGQLYYHGSPKEI 223
Cdd:COG1126 148 AraLAMEPK-VMLfDEPTSALDpeLVGEV--LDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEF 223
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-223 |
5.25e-37 |
|
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: 129.55 E-value: 5.25e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 2 IEISKISKHY--QDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVaATDSDVLAKNLSI 79
Cdd:cd03263 1 LQIRNLTKTYkkGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI-RTDRKAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 80 LRQENQFVSRLTVEELVGFgrypYS--KGRLTLDDKKVIDESLAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQDTEYV 157
Cdd:cd03263 80 CPQFDALFDELTVREHLRF----YArlKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1943291881 158 MLDEPLNNLDMKHAVIMMKLLRKAADelGKTIIIVIHDINFASVYSDYILAMRNGQLYYHGSPKEI 223
Cdd:cd03263 156 LLDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
17-164 |
1.94e-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: 1.94e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 17 LDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVLAKNLSILRQENQFVSRLTVEELV 96
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1943291881 97 GFGRYPYSKGRLTLDDKkvIDESLAFLNLTEFRHRYLD----ELSGGQRQRTYVAMVLCQDTEYVMLDEPLN 164
Cdd:pfam00005 81 RLGLLLKGLSKREKDAR--AEEALEKLGLGDLADRPVGerpgTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
15-237 |
2.40e-36 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 129.56 E-value: 2.40e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 15 TVLDNITTTIQRGGITSIIGPNGAGKSTLLSVI-GRLLLPE-------SGMVSVNGMDVAATDSDVLAKNLSILRQENQF 86
Cdd:PRK13547 15 AILRDLSLRIEPGRVTALLGRNGAGKSTLLKALaGDLTGGGaprgarvTGDVTLNGEPLAAIDAPRLARLRAVLPQAAQP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 87 VSRLTVEELVGFGRYPYSK--GRLTLDDKKVIDESLAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQ---------DTE 155
Cdd:PRK13547 95 AFAFSAREIVLLGRYPHARraGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAQlwpphdaaqPPR 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 156 YVMLDEPLNNLDMKHAVIMMKLLRKAADELGKTIIIVIHDINFASVYSDYILAMRNGQLYYHGSPKEIMKADIIEDIFDT 235
Cdd:PRK13547 175 YLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVLTPAHIARCYGF 254
|
..
gi 1943291881 236 PV 237
Cdd:PRK13547 255 AV 256
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
2-225 |
5.51e-36 |
|
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: 127.45 E-value: 5.51e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 2 IEISKISKHYQDItVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVaaTDSDVLAKNLSILR 81
Cdd:cd03299 1 LKVENLSKDWKEF-KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDI--TNLPPEKRDISYVP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 82 QENQFVSRLTVEELVGFGRypyskgRLTLDDKKVIDESL----AFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQDTEYV 157
Cdd:cd03299 78 QNYALFPHMTVYKNIAYGL------KKRKVDKKEIERKVleiaEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKIL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1943291881 158 MLDEPLNNLDMKHAVIMMKLLRKAADELGKTIIIVIHDINFASVYSDYILAMRNGQLYYHGSPKEIMK 225
Cdd:cd03299 152 LLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFK 219
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-214 |
6.77e-36 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 127.09 E-value: 6.77e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 1 MIEISKISKHY-QDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVLAK---N 76
Cdd:COG2884 1 MIRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYlrrR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 77 LSILRQENQFVSRLTVEELVGFG-RYPYSKGRltlDDKKVIDESLAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQDTE 155
Cdd:COG2884 81 IGVVFQDFRLLPDRTVYENVALPlRVTGKSRK---EIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1943291881 156 YVMLDEPLNNLDMKHAVIMMKLLRKAAdELGKTIIIVIHDINFASVYSDYILAMRNGQL 214
Cdd:COG2884 158 LLLADEPTGNLDPETSWEIMELLEEIN-RRGTTVLIATHDLELVDRMPKRVLELEDGRL 215
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
3-214 |
1.31e-35 |
|
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: 125.83 E-value: 1.31e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 3 EISKIS-KHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDsdvLAKNLSILR 81
Cdd:cd03226 1 RIENISfSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKE---RRKSIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 82 QE--NQFVSRlTVEELVGFGRYPYSkgrltlDDKKVIDESLAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQDTEYVML 159
Cdd:cd03226 78 QDvdYQLFTD-SVREELLLGLKELD------AGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIF 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1943291881 160 DEPLNNLDMKHAVIMMKLLRKAADElGKTIIIVIHDINFASVYSDYILAMRNGQL 214
Cdd:cd03226 151 DEPTSGLDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
2-224 |
2.95e-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: 125.24 E-value: 2.95e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 2 IEISKISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVLAKN-LSIL 80
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAgIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 81 RQENQFVSRLTVEE--LVGFGRYPYSKGRLTLDdkKVIDEslaFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQDTEYVM 158
Cdd:cd03224 81 PEGRRIFPELTVEEnlLLGAYARRRAKRKARLE--RVYEL---FPRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1943291881 159 LDEPLNNLDMKHAVIMMKLLRKAADElGKTIIIVIHDINFASVYSDYILAMRNGQLYYHGSPKEIM 224
Cdd:cd03224 156 LDEPSEGLAPKIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELL 220
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-243 |
1.11e-34 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 124.43 E-value: 1.11e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 1 MIEISKISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGM-VSVNGMDVAATDSDVLAKNLSI 79
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERRGGEDVWELRKRIGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 80 L--RQENQFVSRLTVEELV--GF----GRYPyskgRLTLDDKKVIDESLAFLNLTEFRHRYLDELSGGQRQRTYVAMVLC 151
Cdd:COG1119 83 VspALQLRFPRDETVLDVVlsGFfdsiGLYR----EPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 152 QDTEYVMLDEPLNNLDMKHAVIMMKLLRKAADELGKTIIIVIHDIN--FASVysDYILAMRNGQLYYHGSPKEIMKADII 229
Cdd:COG1119 159 KDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEeiPPGI--THVLLLKDGRVVAAGPKEEVLTSENL 236
|
250
....*....|....
gi 1943291881 230 EDIFDTPVDVKELD 243
Cdd:COG1119 237 SEAFGLPVEVERRD 250
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-223 |
1.98e-34 |
|
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: 123.25 E-value: 1.98e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 2 IEISKISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAaTDSDVLAKNLSILR 81
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVV-REPREVRRRIGIVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 82 QENQFVSRLT-VEELVGFGR-YPYSKGRLtlddKKVIDESLAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQDTEYVML 159
Cdd:cd03265 80 QDLSVDDELTgWENLYIHARlYGVPGAER----RERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1943291881 160 DEPLNNLDMKHAVIMMKLLRKAADELGKTIIIVIHDINFASVYSDYILAMRNGQLYYHGSPKEI 223
Cdd:cd03265 156 DEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-240 |
3.45e-34 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 123.97 E-value: 3.45e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 2 IEISKISKHYQDIT--VLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVA-ATDSDVLAKnLS 78
Cdd:PRK13635 6 IRVEHISFRYPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSeETVWDVRRQ-VG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 79 ILRQ--ENQFVSRlTVEELVGFGRYPYSKGRLTLDDKkvIDESLAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQDTEY 156
Cdd:PRK13635 85 MVFQnpDNQFVGA-TVQDDVAFGLENIGVPREEMVER--VDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 157 VMLDEPLNNLDMKHAVIMMKLLRKAADELGKTIIIVIHDINFASvYSDYILAMRNGQLYYHGSPKEIMKA--DIIEDIFD 234
Cdd:PRK13635 162 IILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAA-QADRVIVMNKGEILEEGTPEEIFKSghMLQEIGLD 240
|
....*.
gi 1943291881 235 TPVDVK 240
Cdd:PRK13635 241 VPFSVK 246
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-223 |
3.50e-34 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 125.57 E-value: 3.50e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 1 MIEISKISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVaaTDSDVLAKNLSIL 80
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDV--TDLPPKDRNIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 81 RQenQFV--SRLTVEELVGFG----RYPysKGRLtldDKKViDESLAFLNLTEFRHRYLDELSGGQRQRtyVAM--VLCQ 152
Cdd:COG3839 81 FQ--SYAlyPHMTVYENIAFPlklrKVP--KAEI---DRRV-REAAELLGLEDLLDRKPKQLSGGQRQR--VALgrALVR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1943291881 153 DTEYVMLDEPLNNLDMKHAVIMMKLLRKAADELGKTIIIVIHDINFASVYSDYILAMRNGQLYYHGSPKEI 223
Cdd:COG3839 151 EPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEEL 221
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-223 |
1.05e-33 |
|
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: 121.53 E-value: 1.05e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 1 MIEISKISKHYQD----ITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDsdvlAKN 76
Cdd:cd03258 1 MIELKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLS----GKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 77 LSILRQE--------NQFVSRlTVEELVGfgrYP-----YSKGRLtlddKKVIDESLAFLNLTEFRHRYLDELSGGQRQR 143
Cdd:cd03258 77 LRKARRRigmifqhfNLLSSR-TVFENVA---LPleiagVPKAEI----EERVLELLELVGLEDKADAYPAQLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 144 TYVAMVLCQDTEYVMLDEPLNNLDMKHAVIMMKLLRKAADELGKTIIIVIHDINFASVYSDYILAMRNGQLYYHGSPKEI 223
Cdd:cd03258 149 VGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEV 228
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-214 |
1.06e-33 |
|
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: 121.10 E-value: 1.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 2 IEISKISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDsdvlaKNLSILR 81
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDK-----KNINELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 82 QENQFV-------SRLTVEELVGFGrypySKGRLTLDDKKVIDESLAFLN---LTEFRHRYLDELSGGQRQRTYVAMVLC 151
Cdd:cd03262 76 QKVGMVfqqfnlfPHLTVLENITLA----PIKVKGMSKAEAEERALELLEkvgLADKADAYPAQLSGGQQQRVAIARALA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1943291881 152 QDTEYVMLDEPLNNLD--MKHAVimMKLLRKAADElGKTIIIVIHDINFASVYSDYILAMRNGQL 214
Cdd:cd03262 152 MNPKVMLFDEPTSALDpeLVGEV--LDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-223 |
1.66e-33 |
|
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: 120.75 E-value: 1.66e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 2 IEISKISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLL-----LPESGMVSVNGMDVAATDSDVLA-- 74
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIYDLDVDVLElr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 75 KNLSILRQE-NQFvsRLTVEELVGFG-RYPYSKGRLTLDDkkVIDESLAFLNLTEFRHRYLD--ELSGGQRQRTYVAMVL 150
Cdd:cd03260 81 RRVGMVFQKpNPF--PGSIYDNVAYGlRLHGIKLKEELDE--RVEEALRKAALWDEVKDRLHalGLSGGQQQRLCLARAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1943291881 151 CQDTEYVMLDEPLNNLDMKHAVIMMKLLRKAADELgkTIIIVIHDINFASVYSDYILAMRNGQLYYHGSPKEI 223
Cdd:cd03260 157 ANEPEVLLLDEPTSALDPISTAKIEELIAELKKEY--TIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-236 |
1.97e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 122.02 E-value: 1.97e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 1 MIEISKISKHYQDIT--VLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVLAKNLS 78
Cdd:PRK13632 7 MIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 79 ILRQ--ENQFVSrLTVEELVGFG----RYPYSKGrltlddKKVIDESLAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQ 152
Cdd:PRK13632 87 IIFQnpDNQFIG-ATVEDDIAFGlenkKVPPKKM------KDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 153 DTEYVMLDEPLNNLDMKHAVIMMKLLRKAADELGKTIIIVIHDINFAsVYSDYILAMRNGQLYYHGSPKEIMK-ADIIED 231
Cdd:PRK13632 160 NPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEA-ILADKVIVFSEGKLIAQGKPKEILNnKEILEK 238
|
....*.
gi 1943291881 232 I-FDTP 236
Cdd:PRK13632 239 AkIDSP 244
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-227 |
2.52e-33 |
|
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: 126.41 E-value: 2.52e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 2 IEISKISKHY-QDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVLAKNLSIL 80
Cdd:COG4988 337 IELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 81 RQENQFVSrLTVEELVGFGRYPYSkgrltlDDKkvIDESLAFLNLTEFRHRY---LDE--------LSGGQRQRTYVAMV 149
Cdd:COG4988 417 PQNPYLFA-GTIRENLRLGRPDAS------DEE--LEAALEAAGLDEFVAALpdgLDTplgeggrgLSGGQAQRLALARA 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1943291881 150 LCQDTEYVMLDEPLNNLDMKHAVIMMKLLRKAADelGKTIIIVIHDINFAsVYSDYILAMRNGQLYYHGSPKEIMKAD 227
Cdd:COG4988 488 LLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALL-AQADRILVLDDGRIVEQGTHEELLAKN 562
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
23-214 |
3.66e-33 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 119.58 E-value: 3.66e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 23 TIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVaaTDSDVLAKNLSILRQENQFVSRLTVEELVGFGRYP 102
Cdd:TIGR01277 20 NVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSH--TGLAPYQRPVSMLFQENNLFAHLTVRQNIGLGLHP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 103 YSKgrLTLDDKKVIDESLAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQDTEYVMLDEPLNNLDMKHAVIMMKLLRKAA 182
Cdd:TIGR01277 98 GLK--LNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQLC 175
|
170 180 190
....*....|....*....|....*....|..
gi 1943291881 183 DELGKTIIIVIHDINFASVYSDYILAMRNGQL 214
Cdd:TIGR01277 176 SERQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-218 |
4.14e-33 |
|
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: 119.22 E-value: 4.14e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 2 IEISKISKHYQDITVLDNITTTIQRGgITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAAtDSDVLAKNLSILR 81
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 82 QENQFVSRLTVEELVGfgrypYS---KGRLTLDDKKVIDESLAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQDTEYVM 158
Cdd:cd03264 79 QEFGVYPNFTVREFLD-----YIawlKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILI 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 159 LDEPLNNLDMKHAVIMMKLLRKAADElgKTIIIVIHDINFASVYSDYILAMRNGQLYYHG 218
Cdd:cd03264 154 VDEPTAGLDPEERIRFRNLLSELGED--RIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-227 |
5.69e-33 |
|
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: 126.10 E-value: 5.69e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 2 IEISKISKHY--QDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVLAKNLSI 79
Cdd:COG2274 474 IELENVSFRYpgDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 80 LRQENQFVSRlTVEELVGFgrypyskGRLTLDDKKVIdESLAFLNLTEF-------RHRYLDE----LSGGQRQRTYVAM 148
Cdd:COG2274 554 VLQDVFLFSG-TIRENITL-------GDPDATDEEII-EAARLAGLHDFiealpmgYDTVVGEggsnLSGGQRQRLAIAR 624
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1943291881 149 VLCQDTEYVMLDEPLNNLDMKHAVIMMKLLRKAADelGKTIIIVIHDINFASvYSDYILAMRNGQLYYHGSPKEIMKAD 227
Cdd:COG2274 625 ALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTIR-LADRIIVLDKGRIVEDGTHEELLARK 700
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-214 |
7.57e-33 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 118.77 E-value: 7.57e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 2 IEISKISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVLAKNLSILR 81
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 82 QENQFVSRlTVEELVgfgRYPYSKGRLTLDDKKVIDeSLAFLNLTE-FRHRYLDELSGGQRQRTYVAMVLCQDTEYVMLD 160
Cdd:COG4619 81 QEPALWGG-TVRDNL---PFPFQLRERKFDRERALE-LLERLGLPPdILDKPVERLSGGERQRLALIRALLLQPDVLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1943291881 161 EPLNNLD--MKHAVImmKLLRKAADELGKTIIIVIHDINFASVYSDYILAMRNGQL 214
Cdd:COG4619 156 EPTSALDpeNTRRVE--ELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-246 |
8.96e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 120.48 E-value: 8.96e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 1 MIEISKISKHYQDIT-VLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDvaATDSDVLA---KN 76
Cdd:PRK13644 1 MIRLENVSYSYPDGTpALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGID--TGDFSKLQgirKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 77 LSILRQ--ENQFVSRlTVEELVGFGryPYSKGRLTLDDKKVIDESLAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQDT 154
Cdd:PRK13644 79 VGIVFQnpETQFVGR-TVEEDLAFG--PENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 155 EYVMLDEPLNNLDMKHAVIMMKLLRKaADELGKTIIIVIHDINFASVySDYILAMRNGQLYYHGSPKEIMKADIIEDIFD 234
Cdd:PRK13644 156 ECLIFDEVTSMLDPDSGIAVLERIKK-LHEKGKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGEPENVLSDVSLQTLGL 233
|
250
....*....|..
gi 1943291881 235 TPVDVKELDNKL 246
Cdd:PRK13644 234 TPPSLIELAENL 245
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1-224 |
1.15e-32 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 118.92 E-value: 1.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 1 MIEISKISKHYQDITVldNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDvlAKNLSIL 80
Cdd:PRK10771 1 MLKLTDITWLYHHLPM--RFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVSML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 81 RQENQFVSRLTVEELVGFGRYPyskG-RLTLDDKKVIDESLAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQDTEYVML 159
Cdd:PRK10771 77 FQENNLFSHLTVAQNIGLGLNP---GlKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1943291881 160 DEPLNNLDMKHAVIMMKLLRKAADELGKTIIIVIHDINFASVYSDYILAMRNGQLYYHGSPKEIM 224
Cdd:PRK10771 154 DEPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELL 218
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2-225 |
1.33e-32 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 121.75 E-value: 1.33e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 2 IEISKISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVaaTDSDVLAKNLSILR 81
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDV--THRSIQQRDICMVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 82 QENQFVSRLTVEELVGFGRYpySKGRLTLDDKKVIDESLAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQDTEYVMLDE 161
Cdd:PRK11432 85 QSYALFPHMSLGENVGYGLK--MLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1943291881 162 PLNNLDMKHAVIMMKLLRKAADELGKTIIIVIHDINFASVYSDYILAMRNGQLYYHGSPKEIMK 225
Cdd:PRK11432 163 PLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYR 226
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-214 |
1.67e-32 |
|
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: 117.74 E-value: 1.67e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 2 IEISKISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVaaTDSDVLAKNLSILR 81
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDV--TDLPPKDRDIAMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 82 QENQFVSRLTVEELVGFGRypyskgRLTLDDKKVIDESL----AFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQDTEYV 157
Cdd:cd03301 79 QNYALYPHMTVYDNIAFGL------KLRKVPKDEIDERVrevaELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVF 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1943291881 158 MLDEPLNNLDMKHAVIMMKLLRKAADELGKTIIIVIHDINFASVYSDYILAMRNGQL 214
Cdd:cd03301 153 LMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-226 |
6.06e-32 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 118.65 E-value: 6.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 1 MIEISKISKHYQDITV-LDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVLAKN--- 76
Cdd:COG1125 1 MIEFENVTKRYPDGTVaVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVELRRRigy 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 77 ----------LSILrqENqfVSrlTVEELVGfgrypYSKGRLtlddKKVIDESLAFLNL--TEFRHRYLDELSGGQRQRT 144
Cdd:COG1125 81 viqqiglfphMTVA--EN--IA--TVPRLLG-----WDKERI----RARVDELLELVGLdpEEYRDRYPHELSGGQQQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 145 YVAMVLCQDTEYVMLDEPLNNLDmkhAVIMMKL---LRKAADELGKTIIIVIHDINFASVYSDYILAMRNGQLYYHGSPK 221
Cdd:COG1125 146 GVARALAADPPILLMDEPFGALD---PITREQLqdeLLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPE 222
|
....*
gi 1943291881 222 EIMKA 226
Cdd:COG1125 223 EILAN 227
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-213 |
6.47e-32 |
|
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: 115.17 E-value: 6.47e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 2 IEISKISKHYQD--ITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVLAKNLSI 79
Cdd:cd03228 1 IEFKNVSFSYPGrpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 80 LRQENQFVSRlTVEElvgfgrypyskgrltlddkkvideslaflNLtefrhryldeLSGGQRQRTYVAMVLCQDTEYVML 159
Cdd:cd03228 81 VPQDPFLFSG-TIRE-----------------------------NI----------LSGGQRQRIAIARALLRDPPILIL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1943291881 160 DEPLNNLDMKHAVIMMKLLRKAADelGKTIIIVIHDInfASV-YSDYILAMRNGQ 213
Cdd:cd03228 121 DEATSALDPETEALILEALRALAK--GKTVIVIAHRL--STIrDADRIIVLDDGR 171
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
10-237 |
1.52e-31 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 116.19 E-value: 1.52e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 10 HYQDITV---LDNITTTIQRGGITSIIGPNGAGKSTLLSVI-GrlLLPESGMVSVNGMDVAATDSDVLAKNLSILRQENQ 85
Cdd:PRK03695 2 QLNDVAVstrLGPLSAEVRAGEILHLVGPNGAGKSTLLARMaG--LLPGSGSIQFAGQPLEAWSAAELARHRAYLSQQQT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 86 FVSRLTVeelvgfgrYPY-----SKGRLTLDDKKVIDESLAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQ-------D 153
Cdd:PRK03695 80 PPFAMPV--------FQYltlhqPDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdinpA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 154 TEYVMLDEPLNNLDMKHAVIMMKLLRKAAdELGKTIIIVIHDINFASVYSDYILAMRNGQLYYHGSPKEIMKADIIEDIF 233
Cdd:PRK03695 152 GQLLLLDEPMNSLDVAQQAALDRLLSELC-QQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPENLAQVF 230
|
....
gi 1943291881 234 DTPV 237
Cdd:PRK03695 231 GVNF 234
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-230 |
3.99e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 115.99 E-value: 3.99e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 2 IEISKISKHYQDIT-VLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVLAKNLSIL 80
Cdd:PRK13647 5 IEVEDLHFRYKDGTkALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 81 RQ--ENQFVSrLTVEELVGFGryPYSKGrltLDDKKV---IDESLAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQDTE 155
Cdd:PRK13647 85 FQdpDDQVFS-STVWDDVAFG--PVNMG---LDKDEVerrVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1943291881 156 YVMLDEPLNNLDMKHAVIMMKLLRKAADElGKTIIIVIHDINFASVYSDYILAMRNGQLYYHGSPKEIMKADIIE 230
Cdd:PRK13647 159 VIVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDEDIVE 232
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-223 |
4.20e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 116.10 E-value: 4.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 1 MIEISKISKHYQDIT-VLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNG--MDVAATDSDVLAKNL 77
Cdd:PRK13636 5 ILKVEELNYNYSDGThALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 78 SILRQ--ENQFVSRlTVEELVGFGryPYSKGRLTLDDKKVIDESLAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQDTE 155
Cdd:PRK13636 85 GMVFQdpDNQLFSA-SVYQDVSFG--AVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPK 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1943291881 156 YVMLDEPLNNLDMKHAVIMMKLLRKAADELGKTIIIVIHDINFASVYSDYILAMRNGQLYYHGSPKEI 223
Cdd:PRK13636 162 VLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEV 229
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-223 |
5.13e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 115.56 E-value: 5.13e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 1 MIEISKISKHYQDIT-VLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVLA--KNL 77
Cdd:PRK13639 1 ILETRDLKYSYPDGTeALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLEvrKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 78 SILRQ--ENQFVSRlTVEELVGFGryPYSKGRLTLDDKKVIDESLAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQDTE 155
Cdd:PRK13639 81 GIVFQnpDDQLFAP-TVEEDVAFG--PLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1943291881 156 YVMLDEPLNNLDMKHAVIMMKLLRKAADElGKTIIIVIHDINFASVYSDYILAMRNGQLYYHGSPKEI 223
Cdd:PRK13639 158 IIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEV 224
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
2-240 |
8.66e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 115.50 E-value: 8.66e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 2 IEISKISKHYQDIT-----VLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDvlaKN 76
Cdd:PRK13634 3 ITFQKVEHRYQYKTpferrALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKN---KK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 77 LSILRQ---------ENQFVSRlTVEELVGFGryPYSKGRLTLDDKKVIDESLAFLNLTE-FRHRYLDELSGGQRQRTYV 146
Cdd:PRK13634 80 LKPLRKkvgivfqfpEHQLFEE-TVEKDICFG--PMNFGVSEEDAKQKAREMIELVGLPEeLLARSPFELSGGQMRRVAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 147 AMVLCQDTEYVMLDEPLNNLDMKHAVIMMKLLRKAADELGKTIIIVIHDINFASVYSDYILAMRNGQLYYHGSPKEIM-K 225
Cdd:PRK13634 157 AGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFaD 236
|
250
....*....|....*.
gi 1943291881 226 ADIIEDI-FDTPVDVK 240
Cdd:PRK13634 237 PDELEAIgLDLPETVK 252
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-214 |
1.38e-30 |
|
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: 112.89 E-value: 1.38e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 2 IEISKISKHY-QDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVLAK---NL 77
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYlrrKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 78 SILRQENQFVSRLTVEELVGFG-RYPYSKGRLTlddKKVIDESLAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQDTEY 156
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFAlEVTGVPPREI---RKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1943291881 157 VMLDEPLNNLDMKHAVIMMKLLRKaADELGKTIIIVIHDINFASVYSDYILAMRNGQL 214
Cdd:cd03292 158 LIADEPTGNLDPDTTWEIMNLLKK-INKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-227 |
3.07e-30 |
|
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: 117.94 E-value: 3.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 2 IEISKISKHY--QDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVLAKNLSI 79
Cdd:COG4987 334 LELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 80 LRQENQFVSRlTVEE--LVGfgrypyskgRLTLDDKKVIdESLAFLNLTEFRHRY-------LDE----LSGGQRQRTYV 146
Cdd:COG4987 414 VPQRPHLFDT-TLREnlRLA---------RPDATDEELW-AALERVGLGDWLAALpdgldtwLGEggrrLSGGERRRLAL 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 147 AMVLCQDTEYVMLDEPLNNLDMKHAVIMMKLLRKAADelGKTIIIVIHDINFASVYsDYILAMRNGQLYYHGSPKEIMKA 226
Cdd:COG4987 483 ARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRLAGLERM-DRILVLEDGRIVEQGTHEELLAQ 559
|
.
gi 1943291881 227 D 227
Cdd:COG4987 560 N 560
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-197 |
8.91e-30 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 113.63 E-value: 8.91e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 1 MIEISKISKHY----QDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSdvlaKN 76
Cdd:COG1135 1 MIELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSE----RE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 77 LSILRQE--------NQFVSRlTVEELVGFgryP-----YSKGRLtldDKKViDESLAFLNLTEFRHRYLDELSGGQRQR 143
Cdd:COG1135 77 LRAARRKigmifqhfNLLSSR-TVAENVAL---PleiagVPKAEI---RKRV-AELLELVGLSDKADAYPSQLSGGQKQR 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1943291881 144 TYVAMVLCQDTEYVMLDEPLNNLDMK--HAVImmKLLRKAADELGKTIIIVIHDIN 197
Cdd:COG1135 149 VGIARALANNPKVLLCDEATSALDPEttRSIL--DLLKDINRELGLTIVLITHEMD 202
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-222 |
9.31e-30 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 112.03 E-value: 9.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 1 MIEISKISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLL----LPESgMVSVNGMDVAATDSdvLAKN 76
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdkSAGS-HIELLGRTVQREGR--LARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 77 LSILR-------QENQFVSRLTVEE--LVG-FGRYPYSKGRL---TLDDKKVIDESLAFLNLTEFRHRYLDELSGGQRQR 143
Cdd:PRK09984 81 IRKSRantgyifQQFNLVNRLSVLEnvLIGaLGSTPFWRTCFswfTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1943291881 144 TYVAMVLCQDTEYVMLDEPLNNLDMKHAVIMMKLLRKAADELGKTIIIVIHDINFASVYSDYILAMRNGQLYYHGSPKE 222
Cdd:PRK09984 161 VAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQ 239
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-224 |
9.60e-30 |
|
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: 111.23 E-value: 9.60e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 1 MIEISKISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVLAKN-LSI 79
Cdd:COG0410 3 MLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLgIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 80 LRQENQFVSRLTVEE--LVgfgrypyskGRLTLDDKKVIDESLA-----FLNLTEFRHRYLDELSGGQRQRTYVAMVLCQ 152
Cdd:COG0410 83 VPEGRRIFPSLTVEEnlLL---------GAYARRDRAEVRADLErvyelFPRLKERRRQRAGTLSGGEQQMLAIGRALMS 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1943291881 153 DTEYVMLDEPLNNLdmkhA-VI---MMKLLRKAADElGKTIIIVIHDINFASVYSDYILAMRNGQLYYHGSPKEIM 224
Cdd:COG0410 154 RPKLLLLDEPSLGL----ApLIveeIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELL 224
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
15-233 |
1.08e-29 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 112.28 E-value: 1.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 15 TVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVaatdSDVLAKNLSILRQENQFVS---RLT 91
Cdd:PRK15056 21 TALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPT----RQALQKNLVAYVPQSEEVDwsfPVL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 92 VEELVGFGRYPYSK--GRLTLDDKKVIDESLAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQDTEYVMLDEPLNNLDMK 169
Cdd:PRK15056 97 VEDVVMMGRYGHMGwlRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVK 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1943291881 170 HAVIMMKLLRKAADElGKTIIIVIHDINFASVYSDYILaMRNGQLYYHGSPKEIMKADIIEDIF 233
Cdd:PRK15056 177 TEARIISLLRELRDE-GKTMLVSTHNLGSVTEFCDYTV-MVKGTVLASGPTETTFTAENLELAF 238
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-223 |
3.44e-29 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 112.73 E-value: 3.44e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 2 IEISKISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVaatdSDVLAKNlsilR 81
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDI----THVPAEN----R 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 82 QENQ-FVS-----RLTVEELVGFGrypyskgrltLDDKKV--------IDESLAFLNLTEFRHRYLDELSGGQRQRTYVA 147
Cdd:PRK09452 87 HVNTvFQSyalfpHMTVFENVAFG----------LRMQKTpaaeitprVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1943291881 148 MVLCQDTEYVMLDEPLNNLDMKHAVIMMKLLRKAADELGKTIIIVIHDINFASVYSDYILAMRNGQLYYHGSPKEI 223
Cdd:PRK09452 157 RAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREI 232
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-218 |
5.59e-29 |
|
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: 108.52 E-value: 5.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 2 IEISKISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVLAknlsILR 81
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRIG----YLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 82 QENQFVSRLTV-EELVGFGRYpysKGRLTLDDKKVIDESLAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQDTEYVMLD 160
Cdd:cd03269 77 EERGLYPKMKViDQLVYLAQL---KGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1943291881 161 EPLNNLDMKHAVIMMKLLRKAADElGKTIIIVIHDINFASVYSDYILAMRNGQLYYHG 218
Cdd:cd03269 154 EPFSGLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-225 |
5.65e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 110.56 E-value: 5.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 1 MIEISKISKHYQD------ITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAatdsdvLA 74
Cdd:PRK13633 4 MIKCKNVSYKYESneesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTS------DE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 75 KNLSILRQ---------ENQFVSRLtVEELVGFGryPYSKGRLTLDDKKVIDESLAFLNLTEFRHRYLDELSGGQRQRTY 145
Cdd:PRK13633 78 ENLWDIRNkagmvfqnpDNQIVATI-VEEDVAFG--PENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 146 VAMVLCQDTEYVMLDEPLNNLDMKHAVIMMKLLRKAADELGKTIIIVIHDINFAsVYSDYILAMRNGQLYYHGSPKEIMK 225
Cdd:PRK13633 155 IAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEA-VEADRIIVMDSGKVVMEGTPKEIFK 233
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
7-218 |
6.86e-29 |
|
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: 108.54 E-value: 6.86e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 7 ISKHYQDITVldNITTTIQrGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNG---------MDVAATDSDVlaknl 77
Cdd:cd03297 6 IEKRLPDFTL--KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfdsrkkINLPPQQRKI----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 78 SILRQENQFVSRLTVEELVGFGrypySKGRLTLDDKKVIDESLAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQDTEYV 157
Cdd:cd03297 78 GLVFQQYALFPHLNVRENLAFG----LKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1943291881 158 MLDEPLNNLDMKHAVIMMKLLRKAADELGKTIIIVIHDINFASVYSDYILAMRNGQLYYHG 218
Cdd:cd03297 154 LLDEPFSALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-218 |
6.89e-29 |
|
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: 108.61 E-value: 6.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 1 MIEISKISKHYQD----ITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVLAkN 76
Cdd:cd03266 1 MITADALTKRFRDvkktVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARR-R 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 77 LSILRQENQFVSRLTVEELVG-FGRYPYSKGRltlDDKKVIDESLAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQDTE 155
Cdd:cd03266 80 LGFVSDSTGLYDRLTARENLEyFAGLYGLKGD---ELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1943291881 156 YVMLDEPLNNLDMKHAVIMMKLLRKAADElGKTIIIVIHDINFASVYSDYILAMRNGQLYYHG 218
Cdd:cd03266 157 VLLLDEPTTGLDVMATRALREFIRQLRAL-GKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
19-224 |
1.33e-28 |
|
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: 109.27 E-value: 1.33e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 19 NITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAA-TDSDVLA---KNLSILRQENQFVSRLTVEE 94
Cdd:cd03294 42 DVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAmSRKELRElrrKKISMVFQSFALLPHRTVLE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 95 LVGFGRYpySKGRLTLDDKKVIDESLAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQDTEYVMLDEPLNNLDMKHAVIM 174
Cdd:cd03294 122 NVAFGLE--VQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREM 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1943291881 175 MKLLRKAADELGKTIIIVIHDINFASVYSDYILAMRNGQLYYHGSPKEIM 224
Cdd:cd03294 200 QDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEIL 249
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
7-215 |
1.60e-28 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 107.82 E-value: 1.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 7 ISKHYQD----ITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVLAK----NLS 78
Cdd:TIGR02211 7 LGKRYQEgkldTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAKlrnkKLG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 79 ILRQENQFVSRLTVEELVGFgryPYSKGRLTLDDKKviDESLAFLNLTEFRHR---YLDELSGGQRQRTYVAMVLCQDTE 155
Cdd:TIGR02211 87 FIYQFHHLLPDFTALENVAM---PLLIGKKSVKEAK--ERAYEMLEKVGLEHRinhRPSELSGGERQRVAIARALVNQPS 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 156 YVMLDEPLNNLDMKHAVIMMKLLRKAADELGKTIIIVIHDINFASVYsDYILAMRNGQLY 215
Cdd:TIGR02211 162 LVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKL-DRVLEMKDGQLF 220
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-223 |
2.56e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 108.67 E-value: 2.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 1 MIEISKISKHY---QDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVLAKNL 77
Cdd:PRK13650 4 IIEVKNLTFKYkedQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 78 SILRQ--ENQFVSRlTVEELVGFGRYpySKGRLTLDDKKVIDESLAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQDTE 155
Cdd:PRK13650 84 GMVFQnpDNQFVGA-TVEDDVAFGLE--NKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1943291881 156 YVMLDEPLNNLDMKHAVIMMKLLRKAADELGKTIIIVIHDINFASVySDYILAMRNGQLYYHGSPKEI 223
Cdd:PRK13650 161 IIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVAL-SDRVLVMKNGQVESTSTPREL 227
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-218 |
2.91e-28 |
|
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: 106.53 E-value: 2.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 2 IEISKISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVlaKNLSILR 81
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEAL--RRIGALI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 82 QENQFVSRLTVEELVgfgrypYSKGRLTLDDKKVIDESLAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQDTEYVMLDE 161
Cdd:cd03268 79 EAPGFYPNLTARENL------RLLARLLGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1943291881 162 PLNNLDMKHAVIMMKLLRKAADElGKTIIIVIHDINFASVYSDYILAMRNGQLYYHG 218
Cdd:cd03268 153 PTNGLDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-209 |
5.08e-28 |
|
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: 111.61 E-value: 5.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 2 IEISKISKHYQDIT-VLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVLAKNLSIL 80
Cdd:TIGR02857 322 LEFSGVSVAYPGRRpALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 81 RQENQFVSRlTVEELVGFGRyPYSKGRLtlddkkvIDESLAFLNLTEF-------RHRYLDE----LSGGQRQRTYVAMV 149
Cdd:TIGR02857 402 PQHPFLFAG-TIAENIRLAR-PDASDAE-------IREALERAGLDEFvaalpqgLDTPIGEggagLSGGQAQRLALARA 472
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 150 LCQDTEYVMLDEPLNNLDMKHAVIMMKLLRKAADelGKTIIIVIHDINFASVYsDYILAM 209
Cdd:TIGR02857 473 FLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAALA-DRIVVL 529
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-223 |
7.02e-28 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 109.02 E-value: 7.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 2 IEISKISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVaatdSDVLAKN--LSI 79
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDV----SRLHARDrkVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 80 LRQENQFVSRLTVEELVGFG--RYPYSKgRLTLD--DKKVIdESLAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQDTE 155
Cdd:PRK10851 79 VFQHYALFRHMTVFDNIAFGltVLPRRE-RPNAAaiKAKVT-QLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQ 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1943291881 156 YVMLDEPLNNLDMKHAVIMMKLLRKAADELGKTIIIVIHDINFASVYSDYILAMRNGQLYYHGSPKEI 223
Cdd:PRK10851 157 ILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
17-228 |
1.07e-27 |
|
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: 106.01 E-value: 1.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 17 LDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSD--VLAKNLSILrqenqfvSRLTVEE 94
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDrmVVFQNYSLL-------PWLTVRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 95 LVGFGRYPYSKGRLTLDDKKVIDESLAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQDTEYVMLDEPLNNLDMKHAVIM 174
Cdd:TIGR01184 74 NIALAVDRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1943291881 175 MKLLRKAADELGKTIIIVIHDINFASVYSDYILAMRNGQLYYHGspkEIMKADI 228
Cdd:TIGR01184 154 QEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIG---QILEVPF 204
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
15-218 |
2.71e-27 |
|
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: 103.78 E-value: 2.71e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 15 TVLDNITTTIQRGGITSIIGPNGAGKSTLLSVI-GRLLLPE-SGMVSVNGMDVaatDSDVLAKNLSILRQENQFVSRLTV 92
Cdd:cd03213 23 QLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALaGRRTGLGvSGEVLINGRPL---DKRSFRKIIGYVPQDDILHPTLTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 93 EELVGFgrypyskgrltlddkkvideslaflnltefrHRYLDELSGGQRQRTYVAMVLCQDTEYVMLDEPLNNLDMKHAV 172
Cdd:cd03213 100 RETLMF-------------------------------AAKLRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSAL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1943291881 173 IMMKLLRKAADElGKTIIIVIHDINfASVYS--DYILAMRNGQLYYHG 218
Cdd:cd03213 149 QVMSLLRRLADT-GRTIICSIHQPS-SEIFElfDKLLLLSQGRVIYFG 194
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-247 |
2.92e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 106.04 E-value: 2.92e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 2 IEISKISKHYQD--ITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPES---GMVSVNGMDVAA-TDSDVLAK 75
Cdd:PRK13640 6 VEFKHVSFTYPDskKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITLTAkTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 76 nLSILRQ--ENQFVSRlTVEELVGFGRYPYSKGRLTLddKKVIDESLAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQD 153
Cdd:PRK13640 86 -VGIVFQnpDNQFVGA-TVGDDVAFGLENRAVPRPEM--IKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 154 TEYVMLDEPLNNLDMKHAVIMMKLLRKAADELGKTIIIVIHDINFASVySDYILAMRNGQLYYHGSPKEIM-KADIIEDI 232
Cdd:PRK13640 162 PKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANM-ADQVLVLDDGKLLAQGSPVEIFsKVEMLKEI 240
|
250
....*....|....*.
gi 1943291881 233 -FDTPVdVKELDNKLI 247
Cdd:PRK13640 241 gLDIPF-VYKLKNKLK 255
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
16-218 |
6.15e-27 |
|
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: 103.50 E-value: 6.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 16 VLDNITTTIQRGGITSIIGPNGAGKSTLLSVI-GRLLLPE--SGMVSVNGMDVaatDSDVLAKNLSILRQENQFVSRLTV 92
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAIsGRVEGGGttSGQILFNGQPR---KPDQFQKCVAYVRQDDILLPGLTV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 93 EELVGF-----GRYPYSKGRltlDDKKVIDESLAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQDTEYVMLDEPLNNLD 167
Cdd:cd03234 99 RETLTYtailrLPRKSSDAI---RKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1943291881 168 MKHAVIMMKLLRKAADElGKTIIIVIHDINfASVYS--DYILAMRNGQLYYHG 218
Cdd:cd03234 176 SFTALNLVSTLSQLARR-NRIVILTIHQPR-SDLFRlfDRILLLSSGEIVYSG 226
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
32-223 |
6.27e-27 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 106.04 E-value: 6.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 32 IIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVaatdSDVLAKNLSI--LRQENQFVSRLTVEELVGFGRYPYSKGRLT 109
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDV----TNVPPHLRHInmVFQSYALFPHMTVEENVAFGLKMRKVPRAE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 110 LDDKkvIDESLAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQDTEYVMLDEPLNNLDMKHAVIMMKLLRKAADELGKTI 189
Cdd:TIGR01187 77 IKPR--VLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITF 154
|
170 180 190
....*....|....*....|....*....|....
gi 1943291881 190 IIVIHDINFASVYSDYILAMRNGQLYYHGSPKEI 223
Cdd:TIGR01187 155 VFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEI 188
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
1-214 |
7.92e-27 |
|
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: 104.50 E-value: 7.92e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 1 MIEISKISKHY---------QDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSd 71
Cdd:TIGR02769 2 LLEVRDVTHTYrtgglfgakQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDR- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 72 vlaKNLSILRQENQFV---------SRLTVEELVGFGRYPYskgrLTLDDKKVIDESLAFLNLTEFR----HRYLDELSG 138
Cdd:TIGR02769 81 ---KQRRAFRRDVQLVfqdspsavnPRMTVRQIIGEPLRHL----TSLDESEQKARIAELLDMVGLRsedaDKLPRQLSG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1943291881 139 GQRQRTYVAMVLCQDTEYVMLDEPLNNLDMKHAVIMMKLLRKAADELGKTIIIVIHDINFASVYSDYILAMRNGQL 214
Cdd:TIGR02769 154 GQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-236 |
8.58e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 104.79 E-value: 8.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 1 MIEISKISKHYQ---DITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVLAKNL 77
Cdd:PRK13642 4 ILEVENLVFKYEkesDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 78 SILRQ--ENQFVSRlTVEELVGFGRYpySKGRLTLDDKKVIDESLAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQDTE 155
Cdd:PRK13642 84 GMVFQnpDNQFVGA-TVEDDVAFGME--NQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 156 YVMLDEPLNNLDMKHAVIMMKLLRKAADELGKTIIIVIHDINFASVySDYILAMRNGQLYYHGSPKEIMKA--DIIEDIF 233
Cdd:PRK13642 161 IIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATseDMVEIGL 239
|
...
gi 1943291881 234 DTP 236
Cdd:PRK13642 240 DVP 242
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-240 |
9.99e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 104.06 E-value: 9.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 1 MIEISKISKHYQDIT--VLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVLAKNLS 78
Cdd:PRK13648 7 IIVFKNVSFQYQSDAsfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 79 ILRQ--ENQFVSRlTVEELVGFG----RYPYSKGrltlddKKVIDESLAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQ 152
Cdd:PRK13648 87 IVFQnpDNQFVGS-IVKYDVAFGlenhAVPYDEM------HRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 153 DTEYVMLDEPLNNLDMKHAVIMMKLLRKAADELGKTIIIVIHDINFAsVYSDYILAMRNGQLYYHGSPKEIMK-ADIIED 231
Cdd:PRK13648 160 NPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEA-MEADHVIVMNKGTVYKEGTPTEIFDhAEELTR 238
|
250
....*....|
gi 1943291881 232 I-FDTPVDVK 240
Cdd:PRK13648 239 IgLDLPFPIK 248
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-214 |
1.02e-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: 103.28 E-value: 1.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 1 MIEISKISKHYQD----ITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSD----V 72
Cdd:COG4181 8 IIELRGLTKTVGTgageLTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDararL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 73 LAKNLSILRQENQFVSRLT-VE------ELVGFGrypyskgrltlDDKKVIDESLAFLNLTEFRHRYLDELSGGQRQRTY 145
Cdd:COG4181 88 RARHVGFVFQSFQLLPTLTaLEnvmlplELAGRR-----------DARARARALLERVGLGHRLDHYPAQLSGGEQQRVA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1943291881 146 VAMVLCQDTEYVMLDEPLNNLDMKHAVIMMKLLRKAADELGKTIIIVIHDINFASvYSDYILAMRNGQL 214
Cdd:COG4181 157 LARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAA-RCDRVLRLRAGRL 224
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1-225 |
1.08e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 104.82 E-value: 1.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 1 MIEISKISKHYQDIT-----VLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDV--- 72
Cdd:PRK13643 1 MIKFEKVNYTYQPNSpfasrALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeik 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 73 -LAKNLSILRQ--ENQFVSRlTVEELVGFGryPYSKGRLTLDDKKVIDESLAFLNLT-EFRHRYLDELSGGQRQRTYVAM 148
Cdd:PRK13643 81 pVRKKVGVVFQfpESQLFEE-TVLKDVAFG--PQNFGIPKEKAEKIAAEKLEMVGLAdEFWEKSPFELSGGQMRRVAIAG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1943291881 149 VLCQDTEYVMLDEPLNNLDMKHAVIMMKLLrKAADELGKTIIIVIHDINFASVYSDYILAMRNGQLYYHGSPKEIMK 225
Cdd:PRK13643 158 ILAMEPEVLVLDEPTAGLDPKARIEMMQLF-ESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQ 233
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-223 |
1.09e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 104.50 E-value: 1.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 1 MIEISKISKHYQ-DITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVLAKNLSI 79
Cdd:PRK13652 3 LIETRDLCYSYSgSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 80 LRQ--ENQFVSRlTVEELVGFGryPYSKGrltLDDKKV---IDESLAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQDT 154
Cdd:PRK13652 83 VFQnpDDQIFSP-TVEQDIAFG--PINLG---LDEETVahrVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1943291881 155 EYVMLDEPLNNLDMKHAVIMMKLLRKAADELGKTIIIVIHDINFASVYSDYILAMRNGQLYYHGSPKEI 223
Cdd:PRK13652 157 QVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
1-213 |
2.18e-26 |
|
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: 101.94 E-value: 2.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 1 MIEISKISKHYQ-DITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVLAK---N 76
Cdd:TIGR02673 1 MIEFHNVSKAYPgGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLlrrR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 77 LSILRQENQFVSRLTVEELVGFG-RYPYSKGRltlDDKKVIDESLAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQDTE 155
Cdd:TIGR02673 81 IGVVFQDFRLLPDRTVYENVALPlEVRGKKER---EIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1943291881 156 YVMLDEPLNNLDMKHAVIMMKLLRKAADeLGKTIIIVIHDINFASVYSDYILAMRNGQ 213
Cdd:TIGR02673 158 LLLADEPTGNLDPDLSERILDLLKRLNK-RGTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-223 |
2.23e-26 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 105.30 E-value: 2.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 1 MIEISKISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSdvLAKNLSIL 80
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPP--YQRPINMM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 81 RQENQFVSRLTVEELVGFGrypYSKGRLTLDD-KKVIDESLAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQDTEYVML 159
Cdd:PRK11607 97 FQSYALFPHMTVEQNIAFG---LKQDKLPKAEiASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1943291881 160 DEPLNNLDMKHAVIMMKLLRKAADELGKTIIIVIHDINFASVYSDYILAMRNGQLYYHGSPKEI 223
Cdd:PRK11607 174 DEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-230 |
2.25e-26 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 103.55 E-value: 2.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 1 MIEISKISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVLA---KNL 77
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLLAlrqQVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 78 SILRQENQFVSRLTVEELVGFgrypySKGRLTLDDKKV---IDESLAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQDT 154
Cdd:PRK13638 81 TVFQDPEQQIFYTDIDSDIAF-----SLRNLGVPEAEItrrVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1943291881 155 EYVMLDEPLNNLDMKHAVIMMKLLRKAADElGKTIIIVIHDINFASVYSDYILAMRNGQLYYHGSPKEIM-KADIIE 230
Cdd:PRK13638 156 RYLLLDEPTAGLDPAGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFaCTEAME 231
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
17-225 |
2.86e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 103.37 E-value: 2.86e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 17 LDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDvlaKNLSILRQ---------ENQFV 87
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGN---KNLKKLRKkvslvfqfpEAQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 88 SRlTVEELVGFGryPYSKGrltLDDKKVIDESLAFLNLTEFRHRYLD----ELSGGQRQRTYVAMVLCQDTEYVMLDEPL 163
Cdd:PRK13641 100 EN-TVLKDVEFG--PKNFG---FSEDEAKEKALKWLKKVGLSEDLISkspfELSGGQMRRVAIAGVMAYEPEILCLDEPA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1943291881 164 NNLDMKHAVIMMKLLrKAADELGKTIIIVIHDINFASVYSDYILAMRNGQLYYHGSPKEIMK 225
Cdd:PRK13641 174 AGLDPEGRKEMMQLF-KDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFS 234
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
2-227 |
3.33e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 103.32 E-value: 3.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 2 IEISKISKHYQDIT-----VLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDvlaKN 76
Cdd:PRK13646 3 IRFDNVSYTYQKGTpyehqAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKD---KY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 77 LSILRQENQFV-----SRL---TVEELVGFGryPYSKGrltLDDKKVIDESLAFLNLTEFRHRYLD----ELSGGQRQRT 144
Cdd:PRK13646 80 IRPVRKRIGMVfqfpeSQLfedTVEREIIFG--PKNFK---MNLDEVKNYAHRLLMDLGFSRDVMSqspfQMSGGQMRKI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 145 YVAMVLCQDTEYVMLDEPLNNLDMKHAVIMMKLLRKAADELGKTIIIVIHDINFASVYSDYILAMRNGQLYYHGSPKEIM 224
Cdd:PRK13646 155 AIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELF 234
|
...
gi 1943291881 225 KAD 227
Cdd:PRK13646 235 KDK 237
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-223 |
3.45e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 103.26 E-value: 3.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 1 MIEISKISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDV-------- 72
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRRigylpeer 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 73 -LAKNLSILRQenqfvsrltveeLVGFGRYpysKGrLTLDD-KKVIDESLAFLNLTEFRHRYLDELSGGQRQRT-YVAMV 149
Cdd:COG4152 81 gLYPKMKVGEQ------------LVYLARL---KG-LSKAEaKRRADEWLERLGLGDRANKKVEELSKGNQQKVqLIAAL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1943291881 150 LCqDTEYVMLDEPLNNLDMKHAVIMMKLLRKAADElGKTIIIVIHDINFASVYSDYILAMRNGQLYYHGSPKEI 223
Cdd:COG4152 145 LH-DPELLILDEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI 216
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
3-228 |
4.36e-26 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 101.45 E-value: 4.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 3 EISKISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLL-SVIGrLLLPESGMVSVNGMDVAATDSDVLAKN-LSIL 80
Cdd:TIGR03410 2 EVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLkTLMG-LLPVKSGSIRLDGEDITKLPPHERARAgIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 81 RQENQFVSRLTVEE--LVGFGRYPYSKgrltlddKKVIDESLA-FLNLTEFRHRYLDELSGGQRQRTYVAMVLCQDTEYV 157
Cdd:TIGR03410 81 PQGREIFPRLTVEEnlLTGLAALPRRS-------RKIPDEIYElFPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1943291881 158 MLDEPLNNLdmKHAVI--MMKLLRKAADELGKTIIIVIHDINFASVYSDYILAMRNGQLYYHGSPKEIMKADI 228
Cdd:TIGR03410 154 LLDEPTEGI--QPSIIkdIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDELDEDKV 224
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-196 |
1.33e-25 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 101.09 E-value: 1.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 1 MIEISKISKHY----QDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSD--VLA 74
Cdd:COG4525 3 MLTVRHVSVRYpgggQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADrgVVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 75 KNLSILrqenqfvSRLTVEELVGFGrypyskgrLTL------DDKKVIDESLAFLNLTEFRHRYLDELSGGQRQRTYVAM 148
Cdd:COG4525 83 QKDALL-------PWLNVLDNVAFG--------LRLrgvpkaERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIAR 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1943291881 149 VLCQDTEYVMLDEPLNNLDMKHAVIMMKLLRKAADELGKTIIIVIHDI 196
Cdd:COG4525 148 ALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSV 195
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
16-224 |
2.00e-25 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 104.44 E-value: 2.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 16 VLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVLAKNLSILRQENQFVSRLTVEEL 95
Cdd:TIGR01846 472 VLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNI 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 96 vgfgrypySKGRLTLDDKKVIDES-----LAFLnlTEFRHRY---LDE----LSGGQRQRTYVAMVLCQDTEYVMLDEPL 163
Cdd:TIGR01846 552 --------ALCNPGAPFEHVIHAAklagaHDFI--SELPQGYnteVGEkganLSGGQRQRIAIARALVGNPRILIFDEAT 621
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1943291881 164 NNLDMKHAVIMMKLLRKAADelGKTIIIVIHDINfASVYSDYILAMRNGQLYYHGSPKEIM 224
Cdd:TIGR01846 622 SALDYESEALIMRNMREICR--GRTVIIIAHRLS-TVRACDRIIVLEKGQIAESGRHEELL 679
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2-214 |
2.91e-25 |
|
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: 99.20 E-value: 2.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 2 IEISKISKHY--QDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVLAKNLSI 79
Cdd:cd03245 3 IEFRNVSFSYpnQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 80 LRQENQFVSRlTVEELVGFGRyPYSkgrltlDDKKVIdESLAFLNLTEF--RH-RYLD--------ELSGGQRQRTYVAM 148
Cdd:cd03245 83 VPQDVTLFYG-TLRDNITLGA-PLA------DDERIL-RAAELAGVTDFvnKHpNGLDlqigergrGLSGGQRQAVALAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1943291881 149 VLCQDTEYVMLDEPLNNLDMKHAVIMMKLLRKAADelGKTIIIVIHDINFASVySDYILAMRNGQL 214
Cdd:cd03245 154 ALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLG--DKTLIIITHRPSLLDL-VDRIIVMDSGRI 216
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-194 |
4.76e-25 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 101.03 E-value: 4.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 1 MIEISKISKHYQ----DITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDsdvlAKN 76
Cdd:PRK11153 1 MIELKNISKVFPqggrTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALS----EKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 77 LSILRQE--------NQFVSRlTVEELVGFgryPyskgrLTLD-------DKKViDESLAFLNLTEFRHRYLDELSGGQR 141
Cdd:PRK11153 77 LRKARRQigmifqhfNLLSSR-TVFDNVAL---P-----LELAgtpkaeiKARV-TELLELVGLSDKADRYPAQLSGGQK 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1943291881 142 QRTYVAMVLCQDTEYVMLDEPLNNLDMKHAVIMMKLLRKAADELGKTIIIVIH 194
Cdd:PRK11153 147 QRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITH 199
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-199 |
8.76e-25 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 98.62 E-value: 8.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 1 MIEISKISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSD--VLAKNLS 78
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAErgVVFQNEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 79 ILRQENqfvsrltVEELVGFGRYPYSKGRltLDDKKVIDESLAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQDTEYVM 158
Cdd:PRK11248 81 LLPWRN-------VQDNVAFGLQLAGVEK--MQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1943291881 159 LDEPLNNLDMKHAVIMMKLLRKAADELGKTIIIVIHDINFA 199
Cdd:PRK11248 152 LDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEA 192
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-223 |
9.24e-25 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 98.67 E-value: 9.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 1 MIEISKISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVLAKNL-SI 79
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLSQQKGLiRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 80 LRQENQFVSRltveelvGFGRYPYskgRLTLDD--------KKVIDES--------LAFLNLTEFRHRYLDELSGGQRQR 143
Cdd:PRK11264 83 LRQHVGFVFQ-------NFNLFPH---RTVLENiiegpvivKGEPKEEatararelLAKVGLAGKETSYPRRLSGGQQQR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 144 TYVAMVLCQDTEYVMLDEPLNNLDMKHAVIMMKLLRKAADElGKTIIIVIHDINFASVYSDYILAMRNGQLYYHGSPKEI 223
Cdd:PRK11264 153 VAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKAL 231
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
17-223 |
1.19e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 99.31 E-value: 1.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 17 LDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVlaKNLSILRQENQFVSRL------ 90
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKI--KEVKRLRKEIGLVFQFpeyqlf 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 91 --TVEELVGFGryPYSKGRLTLDDKKVIDESLAFLNL-TEFRHRYLDELSGGQRQRTYVAMVLCQDTEYVMLDEPLNNLD 167
Cdd:PRK13645 105 qeTIEKDIAFG--PVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLD 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1943291881 168 MKHAVIMMKLLRKAADELGKTIIIVIHDINFASVYSDYILAMRNGQLYYHGSPKEI 223
Cdd:PRK13645 183 PKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEI 238
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
2-232 |
1.19e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 99.05 E-value: 1.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 2 IEISKISKHYQDIT-----VLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDvlaKN 76
Cdd:PRK13649 3 INLQNVSYTYQAGTpfegrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKN---KD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 77 LSILRQ---------ENQFVSRlTVEELVGFGryPYSKGRLTLDDKKVIDESLAFLNLTE-FRHRYLDELSGGQRQRTYV 146
Cdd:PRK13649 80 IKQIRKkvglvfqfpESQLFEE-TVLKDVAFG--PQNFGVSQEEAEALAREKLALVGISEsLFEKNPFELSGGQMRRVAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 147 AMVLCQDTEYVMLDEPLNNLDMKHAVIMMKLLRKaADELGKTIIIVIHDINFASVYSDYILAMRNGQLYYHGSPKEIM-K 225
Cdd:PRK13649 157 AGILAMEPKILVLDEPTAGLDPKGRKELMTLFKK-LHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFqD 235
|
....*..
gi 1943291881 226 ADIIEDI 232
Cdd:PRK13649 236 VDFLEEK 242
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
11-218 |
1.84e-24 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 97.40 E-value: 1.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 11 YQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMdVAATDSDVLAKNLS-ILRQENQFVSR 89
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGL-VPWKRRKKFLRRIGvVFGQKTQLWWD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 90 LTVEELVGFGRYPYSkgrltLDD---KKVIDESLAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQDTEYVMLDEPLNNL 166
Cdd:cd03267 110 LPVIDSFYLLAAIYD-----LPParfKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGL 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1943291881 167 DM--KHAVimMKLLRKAADELGKTIIIVIHDINFASVYSDYILAMRNGQLYYHG 218
Cdd:cd03267 185 DVvaQENI--RNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
2-224 |
2.30e-24 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 97.73 E-value: 2.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 2 IEISKISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAAT-DSD--------- 71
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrDKDgqlkvadkn 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 72 ---VLAKNLSILRQENQFVSRLTVEE--------LVGFGRYPYSKGRLTLDDKKVIDESLaflnltefRHRYLDELSGGQ 140
Cdd:PRK10619 86 qlrLLRTRLTMVFQHFNLWSHMTVLEnvmeapiqVLGLSKQEARERAVKYLAKVGIDERA--------QGKYPVHLSGGQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 141 RQRTYVAMVLCQDTEYVMLDEPLNNLDMKHAVIMMKLLRKAADElGKTIIIVIHDINFASVYSDYILAMRNGQLYYHGSP 220
Cdd:PRK10619 158 QQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAP 236
|
....
gi 1943291881 221 KEIM 224
Cdd:PRK10619 237 EQLF 240
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
7-224 |
2.44e-24 |
|
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: 99.42 E-value: 2.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 7 ISKHYQDITvLDnITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVL----AKNLSILRQ 82
Cdd:TIGR02142 5 FSKRLGDFS-LD-ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFlppeKRRIGYVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 83 ENQFVSRLTVEELVGFGRYpyskgRLTLDDKKVIDESL-AFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQDTEYVMLDE 161
Cdd:TIGR02142 83 EARLFPHLSVRGNLRYGMK-----RARPSERRISFERViELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1943291881 162 PLNNLDMKHAVIMMKLLRKAADELGKTIIIVIHDINFASVYSDYILAMRNGQLYYHGSPKEIM 224
Cdd:TIGR02142 158 PLAALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVW 220
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2-225 |
2.59e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 98.62 E-value: 2.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 2 IEISKISKHYQ-----DITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMV----------SVNGMDVA 66
Cdd:PRK13651 3 IKVKNIVKIFNkklptELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 67 ATDSDVLA-------KNLSILRQEN----QFVS----RLTVEELVGFGryPYSKGRLTLDDKKVIDESLAFLNLTEfrhR 131
Cdd:PRK13651 83 VLEKLVIQktrfkkiKKIKEIRRRVgvvfQFAEyqlfEQTIEKDIIFG--PVSMGVSKEEAKKRAAKYIELVGLDE---S 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 132 YLD----ELSGGQRQRTYVAMVLCQDTEYVMLDEPLNNLDMKHAVIMMKLLRKAADElGKTIIIVIHDINFASVYSDYIL 207
Cdd:PRK13651 158 YLQrspfELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTI 236
|
250
....*....|....*...
gi 1943291881 208 AMRNGQLYYHGSPKEIMK 225
Cdd:PRK13651 237 FFKDGKIIKDGDTYDILS 254
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
17-220 |
3.12e-24 |
|
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: 101.24 E-value: 3.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 17 LDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVaATDSDVLAKNLSILRQENQFVSRLTVEELV 96
Cdd:TIGR01257 946 VDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHHLTVAEHI 1024
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 97 GFgrYPYSKGRlTLDDKKVidESLAFLNLTEFRHRYLDE---LSGGQRQRTYVAMVLCQDTEYVMLDEPLNNLDMKHAVI 173
Cdd:TIGR01257 1025 LF--YAQLKGR-SWEEAQL--EMEAMLEDTGLHHKRNEEaqdLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRS 1099
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1943291881 174 MMKLLRKAADelGKTIIIVIHDINFASVYSDYILAMRNGQLYYHGSP 220
Cdd:TIGR01257 1100 IWDLLLKYRS--GRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-214 |
3.56e-24 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 100.95 E-value: 3.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 1 MIEISKISKHYQ----DITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVLAKn 76
Cdd:PRK10535 4 LLELKDIRRSYPsgeeQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQ- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 77 lsiLRQEN--------QFVSRLTVEELV-------GFGRypysKGRltlddKKVIDESLAFLNLTEFRHRYLDELSGGQR 141
Cdd:PRK10535 83 ---LRREHfgfifqryHLLSHLTAAQNVevpavyaGLER----KQR-----LLRAQELLQRLGLEDRVEYQPSQLSGGQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1943291881 142 QRTYVAMVLCQDTEYVMLDEPLNNLDMKHAVIMMKLLRKAADElGKTIIIVIHDINFASvYSDYILAMRNGQL 214
Cdd:PRK10535 151 QRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDR-GHTVIIVTHDPQVAA-QAERVIEIRDGEI 221
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-226 |
7.99e-24 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 96.02 E-value: 7.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 1 MIEISKISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVA-ATDSD-----VLA 74
Cdd:COG4598 8 ALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRlKPDRDgelvpADR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 75 KNLSILRQENQFV-------SRLTVEELVGFGryP-YSKGRltlDDKKVIDESLAFLN---LTEFRHRYLDELSGGQRQR 143
Cdd:COG4598 88 RQLQRIRTRLGMVfqsfnlwSHMTVLENVIEA--PvHVLGR---PKAEAIERAEALLAkvgLADKRDAYPAHLSGGQQQR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 144 TYVAMVLCQDTEyVML-DEPLNNLD--MKHAVImmKLLRKAADElGKTIIIVIHDINFASVYSDYILAMRNGQLYYHGSP 220
Cdd:COG4598 163 AAIARALAMEPE-VMLfDEPTSALDpeLVGEVL--KVMRDLAEE-GRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPP 238
|
....*.
gi 1943291881 221 KEIMKA 226
Cdd:COG4598 239 AEVFGN 244
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-232 |
1.37e-23 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 98.55 E-value: 1.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 1 MIEISKISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVA-ATDSDVLAKNLSI 79
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRfRSPRDAQAAGIAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 80 LRQENQFVSRLTVEELVGFGRYPYSKGRltLDDKKVIDESLAFLNLTEFR---HRYLDELSGGQRQrtyvaMV-----LC 151
Cdd:COG1129 84 IHQELNLVPNLSVAENIFLGREPRRGGL--IDWRAMRRRARELLARLGLDidpDTPVGDLSVAQQQ-----LVeiaraLS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 152 QDTEYVMLDEPLNNLDMKHAVIMMKLLRKAADElGKTIIIVIHDIN--FAsvYSDYILAMRNGQLYYHGSPKEIMKADII 229
Cdd:COG1129 157 RDARVLILDEPTASLTEREVERLFRIIRRLKAQ-GVAIIYISHRLDevFE--IADRVTVLRDGRLVGTGPVAELTEDELV 233
|
...
gi 1943291881 230 EDI 232
Cdd:COG1129 234 RLM 236
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-224 |
1.43e-23 |
|
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: 94.92 E-value: 1.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 2 IEISKISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVLA-KNLSIL 80
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRArLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 81 RQENQFVSRLTVEE---LVGFGRYPYSKGRltlddKKVIDESLAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQDTEYV 157
Cdd:cd03218 81 PQEASIFRKLTVEEnilAVLEIRGLSKKER-----EEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1943291881 158 MLDEPLNNLDMKhAVIMMKLLRKAADELGktIIIVIHDIN----FASVYSDYIlaMRNGQLYYHGSPKEIM 224
Cdd:cd03218 156 LLDEPFAGVDPI-AVQDIQKIIKILKDRG--IGVLITDHNvretLSITDRAYI--IYEGKVLAEGTPEEIA 221
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-197 |
1.93e-23 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 94.09 E-value: 1.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 1 MIEISKISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPE---SGMVSVNGMDVaaTDSDVLAKNL 77
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRL--TALPAEQRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 78 SILRQENQFVSRLTVEELVGFGrYPYSKGRLtlDDKKVIDESLAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQDTEYV 157
Cdd:COG4136 79 GILFQDDLLFPHLSVGENLAFA-LPPTIGRA--QRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRAL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1943291881 158 MLDEPLNNLDMKHAVIMMKLLRKAADELGKTIIIVIHDIN 197
Cdd:COG4136 156 LLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEE 195
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1-214 |
2.30e-23 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 94.50 E-value: 2.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 1 MIEISKISKHYQD----ITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDV----AATDSDV 72
Cdd:PRK11629 5 LLQCDNLCKRYQEgsvqTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMsklsSAAKAEL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 73 LAKNLSILRQENQFVSRLTVEELVGFGRYPYSKGRLTLDDKKVidESLAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQ 152
Cdd:PRK11629 85 RNQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRAL--EMLAAVGLEHRANHRPSELSGGERQRVAIARALVN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1943291881 153 DTEYVMLDEPLNNLDMKHAVIMMKLLRKAADELGKTIIIVIHDINFASVYSDYiLAMRNGQL 214
Cdd:PRK11629 163 NPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQ-LEMRDGRL 223
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
2-225 |
2.53e-23 |
|
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: 94.21 E-value: 2.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 2 IEISKISKHY-QDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVLAKNLSIL 80
Cdd:cd03254 3 IEFENVNFSYdEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 81 RQENQFVSRLTVEELvgfgRYpyskGRLTLDDKKVIdESLAFLNLTEF-------RHRYLDE----LSGGQRQRTYVAMV 149
Cdd:cd03254 83 LQDTFLFSGTIMENI----RL----GRPNATDEEVI-EAAKEAGAHDFimklpngYDTVLGEnggnLSQGERQLLAIARA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1943291881 150 LCQDTEYVMLDEPLNNLDmkhaVIMMKLLRKAADEL--GKTIIIVIHDINfASVYSDYILAMRNGQLYYHGSPKEIMK 225
Cdd:cd03254 154 MLRDPKILILDEATSNID----TETEKLIQEALEKLmkGRTSIIIAHRLS-TIKNADKILVLDDGKIIEEGTHDELLA 226
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
15-226 |
3.67e-23 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 97.80 E-value: 3.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 15 TVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVLAKNLSILRQENQFVSRLTVEE 94
Cdd:TIGR01842 332 PTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTVAEN 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 95 LVGFGRYPyskgrltlDDKKVIDESLA------FLNLTEFRHRYLDE----LSGGQRQRTYVAMVLCQDTEYVMLDEPLN 164
Cdd:TIGR01842 412 IARFGENA--------DPEKIIEAAKLagvhelILRLPDGYDTVIGPggatLSGGQRQRIALARALYGDPKLVVLDEPNS 483
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1943291881 165 NLDMKHAVIMMKLLrKAADELGKTIIIVIHDINFASVySDYILAMRNGQLYYHGSPKEIMKA 226
Cdd:TIGR01842 484 NLDEEGEQALANAI-KALKARGITVVVITHRPSLLGC-VDKILVLQDGRIARFGERDEVLAK 543
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-223 |
4.30e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 94.21 E-value: 4.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 2 IEISKISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRL--LLPE---SGMVSVNGMDVAATDSDVLAKN 76
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLieLYPEarvSGEVYLDGQDIFKMDVIELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 77 LSILRQENQFVSRLTVEELVGFG----RYPYSKGRLtlddKKVIDESLAFLNLTEFRHRYLD----ELSGGQRQRTYVAM 148
Cdd:PRK14247 84 VQMVFQIPNPIPNLSIFENVALGlklnRLVKSKKEL----QERVRWALEKAQLWDEVKDRLDapagKLSGGQQQRLCIAR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1943291881 149 VLCQDTEYVMLDEPLNNLDMKHAVIMMKLLRKAADELgkTIIIVIHDINFASVYSDYILAMRNGQLYYHGSPKEI 223
Cdd:PRK14247 160 ALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDM--TIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREV 232
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-223 |
5.12e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 94.07 E-value: 5.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 1 MIEISKISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRL--LLPE---SGMVSVNGMDVAA--TDSDVL 73
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndLNPEvtiTGSIVYNGHNIYSprTDTVDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 74 AKNLS-ILRQENQFvsRLTVEELVGFG-RYPYSKGRLTLDdkKVIDESLAFLNL-TEFRHRYLDE---LSGGQRQRTYVA 147
Cdd:PRK14239 85 RKEIGmVFQQPNPF--PMSIYENVVYGlRLKGIKDKQVLD--EAVEKSLKGASIwDEVKDRLHDSalgLSGGQQQRVCIA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1943291881 148 MVLCQDTEYVMLDEPLNNLDMKHAVIMMKLLRKAADELgkTIIIVIHDINFASVYSDYILAMRNGQLYYHGSPKEI 223
Cdd:PRK14239 161 RVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQM 234
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
8-230 |
5.75e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 95.30 E-value: 5.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 8 SKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSV----NGMDVAATDSDVLA-----KNLS 78
Cdd:PRK13631 33 EKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyIGDKKNNHELITNPyskkiKNFK 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 79 ILRQENQFVSRL--------TVEELVGFGryPYSKGRLTLDDKKVIDESLAFLNLTE-FRHRYLDELSGGQRQRTYVAMV 149
Cdd:PRK13631 113 ELRRRVSMVFQFpeyqlfkdTIEKDIMFG--PVALGVKKSEAKKLAKFYLNKMGLDDsYLERSPFGLSGGQKRRVAIAGI 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 150 LCQDTEYVMLDEPLNNLDMKHAVIMMKLLRKAADElGKTIIIVIHDINFASVYSDYILAMRNGQLYYHGSPKEI-MKADI 228
Cdd:PRK13631 191 LAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIfTDQHI 269
|
..
gi 1943291881 229 IE 230
Cdd:PRK13631 270 IN 271
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
17-232 |
6.28e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 94.34 E-value: 6.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 17 LDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVaaTDSDVlakNLSILRQENQFVSRL------ 90
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDI--TDKKV---KLSDIRKKVGLVFQYpeyqlf 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 91 --TVEELVGFGryPYSKGRLTLDDKKVIDESLAFLNLT--EFRHRYLDELSGGQRQRTYVAMVLCQDTEYVMLDEPLNNL 166
Cdd:PRK13637 98 eeTIEKDIAFG--PINLGLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1943291881 167 DMKHAVIMMKLLRKAADELGKTIIIVIHDINFASVYSDYILAMRNGQLYYHGSPKEIMK-ADIIEDI 232
Cdd:PRK13637 176 DPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKeVETLESI 242
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
2-226 |
6.71e-23 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 97.24 E-value: 6.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 2 IEISKISKHY--QDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVLAKNLSI 79
Cdd:TIGR03375 464 IEFRNVSFAYpgQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADLRRNIGY 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 80 LRQEnqfvSRL---TVEELVGFGRyPYskgrltLDDKKVIdESLAFLNLTEF--RH-----RYLDE----LSGGQRQRTY 145
Cdd:TIGR03375 544 VPQD----PRLfygTLRDNIALGA-PY------ADDEEIL-RAAELAGVTEFvrRHpdgldMQIGErgrsLSGGQRQAVA 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 146 VAMVLCQDTEYVMLDEPLNNLDMKHAVIMMKLLRKAAdeLGKTIIIVIHDINFASVySDYILAMRNGQLYYHGSPKEIMK 225
Cdd:TIGR03375 612 LARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWL--AGKTLVLVTHRTSLLDL-VDRIIVMDNGRIVADGPKDQVLE 688
|
.
gi 1943291881 226 A 226
Cdd:TIGR03375 689 A 689
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-227 |
7.05e-23 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 96.77 E-value: 7.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 2 IEISKISKHYQ-DITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVLAKNLSIL 80
Cdd:COG1132 340 IEFENVSFSYPgDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 81 RQENQFVSRlTVEELVGFgrypyskGRLTLDDKKVIdESLAFLNLTEFRHRyLDE------------LSGGQRQRTYVAM 148
Cdd:COG1132 420 PQDTFLFSG-TIRENIRY-------GRPDATDEEVE-EAAKAAQAHEFIEA-LPDgydtvvgergvnLSGGQRQRIAIAR 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 149 VLCQDTEYVMLDEPLNNLDMKHAvimmKLLRKAADEL--GKTIIIVIHdiNFASV-YSDYILAMRNGQLYYHGSPKEIMK 225
Cdd:COG1132 490 ALLKDPPILILDEATSALDTETE----ALIQEALERLmkGRTTIVIAH--RLSTIrNADRILVLDDGRIVEQGTHEELLA 563
|
..
gi 1943291881 226 AD 227
Cdd:COG1132 564 RG 565
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-224 |
7.77e-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: 96.80 E-value: 7.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 1 MIEISKISKHYQD-----ITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMD--VAATDSDVL 73
Cdd:TIGR03269 279 IIKVRNVSKRYISvdrgvVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGDewVDMTKPGPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 74 AKN-----LSILRQENQFVSRLTV----EELVGFgRYPYSKGRLtlddKKVI-------DESLAflnlTEFRHRYLDELS 137
Cdd:TIGR03269 359 GRGrakryIGILHQEYDLYPHRTVldnlTEAIGL-ELPDELARM----KAVItlkmvgfDEEKA----EEILDKYPDELS 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 138 GGQRQRTYVAMVLCQDTEYVMLDEPLNNLDMKHAVIMMKLLRKAADELGKTIIIVIHDINFASVYSDYILAMRNGQLYYH 217
Cdd:TIGR03269 430 EGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKI 509
|
....*..
gi 1943291881 218 GSPKEIM 224
Cdd:TIGR03269 510 GDPEEIV 516
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-195 |
1.24e-22 |
|
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: 96.28 E-value: 1.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 2 IEISKISKHY-QDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVLAKNLSIL 80
Cdd:TIGR02868 335 LELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVC 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 81 RQ----------ENQFVSRLTV--EEL------VGFGRYPYSkgrltLDD--KKVIDESLAFlnltefrhryldeLSGGQ 140
Cdd:TIGR02868 415 AQdahlfdttvrENLRLARPDAtdEELwaalerVGLADWLRA-----LPDglDTVLGEGGAR-------------LSGGE 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1943291881 141 RQRTYVAMVLCQDTEYVMLDEPLNNLDMKHAVIMMKLLRKAADelGKTIIIVIHD 195
Cdd:TIGR02868 477 RQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALS--GRTVVLITHH 529
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
16-226 |
1.41e-22 |
|
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: 92.55 E-value: 1.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 16 VLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVLAKNLSILRQENQFVSRlTVEEL 95
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGVVLQENVLFNR-SIRDN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 96 VGFGRYPYSKGRLtLDDKKVIDESLAFLNLTEFRHRYLDE----LSGGQRQRTYVAMVLCQDTEYVMLDEPLNNLDMKHA 171
Cdd:cd03252 96 IALADPGMSMERV-IEAAKLAGAHDFISELPEGYDTIVGEqgagLSGGQRQRIAIARALIHNPRILIFDEATSALDYESE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1943291881 172 VIMMKLLRKAADelGKTIIIVIHDINfASVYSDYILAMRNGQLYYHGSPKEIMKA 226
Cdd:cd03252 175 HAIMRNMHDICA--GRTVIIIAHRLS-TVKNADRIIVMEKGRIVEQGSHDELLAE 226
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-237 |
1.59e-22 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 92.91 E-value: 1.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 1 MIEISKISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVL---AKNL 77
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRKRM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 78 SILRQENQFVSRLTVEELVGF-----GRYPYSKGRLTLDDKkvidesLAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQ 152
Cdd:PRK11831 87 SMLFQSGALFTDMNVFDNVAYplrehTQLPAPLLHSTVMMK------LEAVGLRGAAKLMPSELSGGMARRAALARAIAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 153 DTEYVMLDEPLNNLDmkhaVIMMKLLRKAADE----LGKTIIIVIHDINFASVYSDYILAMRNGQLYYHGSPKEIMKAD- 227
Cdd:PRK11831 161 EPDLIMFDEPFVGQD----PITMGVLVKLISElnsaLGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPd 236
|
250
....*....|....*
gi 1943291881 228 -----IIEDIFDTPV 237
Cdd:PRK11831 237 prvrqFLDGIADGPV 251
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-214 |
2.20e-22 |
|
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: 89.80 E-value: 2.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 2 IEISKISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVaATDSDVLAKNLSIlr 81
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEV-SFASPRDARRAGI-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 82 qenQFVSrltveelvgfgrypyskgrltlddkkvideslaflnltefrhryldELSGGQRQRTYVAMVLCQDTEYVMLDE 161
Cdd:cd03216 78 ---AMVY----------------------------------------------QLSVGERQMVEIARALARNARLLILDE 108
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1943291881 162 PLNNLDMKHAVIMMKLLRKAADElGKTIIIVIHDINFASVYSDYILAMRNGQL 214
Cdd:cd03216 109 PTAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-218 |
2.82e-22 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 91.61 E-value: 2.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 2 IEISKISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSV--NGMDVAATDSDvlaKNLSI 79
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIagNHFDFSKTPSD---KAIRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 80 LRQENQFV-------SRLTV-EELVgfgRYPYSKGRLTLDD-KKVIDESLAFLNLTEFRHRYLDELSGGQRQRTYVAMVL 150
Cdd:PRK11124 80 LRRNVGMVfqqynlwPHLTVqQNLI---EAPCRVLGLSKDQaLARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1943291881 151 CQDTEYVMLDEPLNNLDMKHAVIMMKLLRKAAdELGKTIIIVIHDINFASVYSDYILAMRNGQLYYHG 218
Cdd:PRK11124 157 MMEPQVLLFDEPTAALDPEITAQIVSIIRELA-ETGITQVIVTHEVEVARKTASRVVYMENGHIVEQG 223
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-228 |
4.04e-22 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 92.97 E-value: 4.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 2 IEISKISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVLAKnLSILR 81
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARAR-IGVVP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 82 QENQFVSRLTVEE-LVGFGRYPYSKGRltlDDKKVIDESLAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQDTEYVMLD 160
Cdd:PRK13536 121 QFDNLDLEFTVREnLLVFGRYFGMSTR---EIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILD 197
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 161 EPLNNLDmKHA--VIMMKLlrKAADELGKTIIIVIHDINFASVYSDYILAMRNGQLYYHGSPKEIMKADI 228
Cdd:PRK13536 198 EPTTGLD-PHArhLIWERL--RSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDEHI 264
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
13-212 |
4.50e-22 |
|
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: 90.85 E-value: 4.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 13 DITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMV---SVNGMDVAATDSDVLAKNLSILRQENQFVSR 89
Cdd:cd03290 13 GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsNKNESEPSFEATRSRNRYSVAYAAQKPWLLN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 90 LTVEELVGFGRyPYSKGRLtlddKKVID--------ESLAFLNLTEFRHRYLDeLSGGQRQRTYVAMVLCQDTEYVMLDE 161
Cdd:cd03290 93 ATVEENITFGS-PFNKQRY----KAVTDacslqpdiDLLPFGDQTEIGERGIN-LSGGQRQRICVARALYQNTNIVFLDD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1943291881 162 PLNNLDMKHAVIMMK--LLRKAADElGKTIIIVIHDINFAsVYSDYILAMRNG 212
Cdd:cd03290 167 PFSALDIHLSDHLMQegILKFLQDD-KRTLVLVTHKLQYL-PHADWIIAMKDG 217
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-249 |
6.38e-22 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 94.08 E-value: 6.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 1 MIEISKISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVLAKN-LSI 79
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLgIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 80 LRQENQFVSRLTVEELVGFGRYPYSK-GRLTLDDKKVIDESLAFLNLTEFRHRYLDE----LSGGQRQRTYVAMVLCQDT 154
Cdd:PRK09700 85 IYQELSVIDELTVLENLYIGRHLTKKvCGVNIIDWREMRVRAAMMLLRVGLKVDLDEkvanLSISHKQMLEIAKTLMLDA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 155 EYVMLDEP---LNNLDMKHAVIMMKLLRKAadelGKTIIIVIHDINFASVYSDYILAMRNGQLYYHGSPKEIMKADIIED 231
Cdd:PRK09700 165 KVIIMDEPtssLTNKEVDYLFLIMNQLRKE----GTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSNDDIVRL 240
|
250
....*....|....*...
gi 1943291881 232 IFDtpvdvKELDNKLIAM 249
Cdd:PRK09700 241 MVG-----RELQNRFNAM 253
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1-224 |
6.54e-22 |
|
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: 92.86 E-value: 6.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 1 MIEIsKISKHYQDITvLDnITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDV--AATDSDVLA--KN 76
Cdd:COG4148 2 MLEV-DFRLRRGGFT-LD-VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLqdSARGIFLPPhrRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 77 LSILRQENQFVSRLTVEELVGFG--RYPYSKGRLTLDDkkVIDeslaFLNLTEFRHRYLDELSGGQRQRtyVAMV--LCQ 152
Cdd:COG4148 79 IGYVFQEARLFPHLSVRGNLLYGrkRAPRAERRISFDE--VVE----LLGIGHLLDRRPATLSGGERQR--VAIGraLLS 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1943291881 153 DTEYVMLDEPLNNLDM--KHAVimMKLLRKAADELGKTIIIVIHDINFASVYSDYILAMRNGQLYYHGSPKEIM 224
Cdd:COG4148 151 SPRLLLMDEPLAALDLarKAEI--LPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVL 222
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
12-198 |
6.83e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 90.95 E-value: 6.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 12 QDITV-------LDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVLAkNLSILRQ-- 82
Cdd:COG4674 14 EDLTVsfdgfkaLNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGLDEHEIA-RLGIGRKfq 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 83 -----ENqfvsrLTVEE-L---VGFGRYPYS--KGRLTLDDKKVIDESLAFLNLTEFRHRYLDELSGGQRQRTYVAMVLC 151
Cdd:COG4674 93 kptvfEE-----LTVFEnLelaLKGDRGVFAslFARLTAEERDRIEEVLETIGLTDKADRLAGLLSHGQKQWLEIGMLLA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1943291881 152 QDTEYVMLDEPLNNldMKHAVIMM--KLLRKAADElgKTIIIVIHDINF 198
Cdd:COG4674 168 QDPKLLLLDEPVAG--MTDAETERtaELLKSLAGK--HSVVVVEHDMEF 212
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-219 |
9.38e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 93.59 E-value: 9.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 1 MIEISKISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVsvngmdvaatdsdVLAKNLSI- 79
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV-------------KLGETVKIg 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 80 -LRQEN-QFVSRLTVEELVgfgrypySKGRLTLDDKKVIDESLAFLnlteFR----HRYLDELSGGQRQRTYVAMVLCQD 153
Cdd:COG0488 382 yFDQHQeELDPDKTVLDEL-------RDGAPGGTEQEVRGYLGRFL----FSgddaFKPVGVLSGGEKARLALAKLLLSP 450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1943291881 154 TEYVMLDEPLNNLDMKhaviMMKLLRKAADELGKTIIIVIHDINFASVYSDYILAMRNGQLY-YHGS 219
Cdd:COG0488 451 PNVLLLDEPTNHLDIE----TLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVReYPGG 513
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-218 |
1.31e-21 |
|
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: 88.52 E-value: 1.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 2 IEISKISKHY--QDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDsDVLAKNLSI 79
Cdd:cd03247 1 LSINNVSFSYpeQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 80 LRQEnqfvsrltveelvgfgrypyskgrltlddkkvideslAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQDTEYVML 159
Cdd:cd03247 80 LNQR-------------------------------------PYLFDTTLRNNLGRRFSGGERQRLALARILLQDAPIVLL 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 160 DEPLNNLDMKHAVIMMKLLRKAADElgKTIIIVIHdiNFASV-YSDYILAMRNGQLYYHG 218
Cdd:cd03247 123 DEPTVGLDPITERQLLSLIFEVLKD--KTLIWITH--HLTGIeHMDKILFLENGKIIMQG 178
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
11-218 |
1.35e-21 |
|
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: 89.51 E-value: 1.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 11 YQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGmdvaaTDSDVLAKNLSilrqenqFVSRL 90
Cdd:cd03220 32 VGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG-----RVSSLLGLGGG-------FNPEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 91 TVEELVGF-GRYpysKGRLTLDDKKVIDESLAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQDTEYVMLDEPLNNLD-- 167
Cdd:cd03220 100 TGRENIYLnGRL---LGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDaa 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1943291881 168 -MKHAVIMMKLLRKAadelGKTIIIVIHDINFASVYSDYILAMRNGQLYYHG 218
Cdd:cd03220 177 fQEKCQRRLRELLKQ----GKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-226 |
1.44e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 90.11 E-value: 1.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 1 MIEISKISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLL------LPESGMVSVNGMDVAATDSDVLA 74
Cdd:PRK14246 10 VFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIeiydskIKVDGKVLYFGKDIFQIDAIKLR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 75 KNLSILRQENQFVSRLTVEELVGfgrYPY-SKG-RLTLDDKKVIDESLAFLNLTEFRHRYLD----ELSGGQRQRTYVAM 148
Cdd:PRK14246 90 KEVGMVFQQPNPFPHLSIYDNIA---YPLkSHGiKEKREIKKIVEECLRKVGLWKEVYDRLNspasQLSGGQQQRLTIAR 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1943291881 149 VLCQDTEYVMLDEPLNNLDMKHAVIMMKLLRKAADELgkTIIIVIHDINFASVYSDYILAMRNGQLYYHGSPKEIMKA 226
Cdd:PRK14246 167 ALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEI--AIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTS 242
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
26-234 |
1.56e-21 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 89.52 E-value: 1.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 26 RGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGmdvaaTDSDVLAKNLSILRQENQFV--SRLTVEELVGFGRypy 103
Cdd:TIGR03771 5 KGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAG-----ASPGKGWRHIGYVPQRHEFAwdFPISVAHTVMSGR--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 104 sKGRLTL------DDKKVIDESLAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQDTEYVMLDEPLNNLDMKHAVIMMKL 177
Cdd:TIGR03771 77 -TGHIGWlrrpcvADFAAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLTEL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1943291881 178 LRKAADElGKTIIIVIHDINFASVYSDYILAMrNGQLYYHGSPKEIMKADIIEDIFD 234
Cdd:TIGR03771 156 FIELAGA-GTAILMTTHDLAQAMATCDRVVLL-NGRVIADGTPQQLQDPAPWMTTFG 210
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-218 |
1.62e-21 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 89.69 E-value: 1.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 2 IEISKISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGM------DVAATDSDVLAK 75
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfdfsqKPSEKAIRLLRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 76 NLSILRQENQFVSRLTVEE-LVgfgRYPYSKgrLTLDDKKVIDES---LAFLNLTEFRHRYLDELSGGQRQRTYVAMVLC 151
Cdd:COG4161 83 KVGMVFQQYNLWPHLTVMEnLI---EAPCKV--LGLSKEQAREKAmklLARLRLTDKADRFPLHLSGGQQQRVAIARALM 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1943291881 152 QDTEYVMLDEPLNNLDMKHAVIMMKLLRKAAdELGKTIIIVIHDINFASVYSDYILAMRNGQLYYHG 218
Cdd:COG4161 158 MEPQVLLFDEPTAALDPEITAQVVEIIRELS-QTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQG 223
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-242 |
1.90e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 90.63 E-value: 1.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 2 IEISKISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVaATDSDVLAKNLSILR 81
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPV-PSRARHARQRVGVVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 82 QENQFVSRLTV-EELVGFGRYpysKGRLTLDDKKVIDESLAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQDTEYVMLD 160
Cdd:PRK13537 87 QFDNLDPDFTVrENLLVFGRY---FGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 161 EPLNNLDMKHAVIMMKLLRKAADElGKTIIIVIHDINFASVYSDYILAMRNGQLYYHGSPKEIMKA----DIIEDIFDTP 236
Cdd:PRK13537 164 EPTTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIESeigcDVIEIYGPDP 242
|
....*.
gi 1943291881 237 VDVKEL 242
Cdd:PRK13537 243 VALRDE 248
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-230 |
2.46e-21 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 92.40 E-value: 2.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 1 MIEISKISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDS-DVLAKNLSI 79
Cdd:COG3845 5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPrDAIALGIGM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 80 LRQENQFVSRLTVEELVGFGRYPysKGRLTLDDKKVIDESLAFLNLTEFR---HRYLDELSGGQRQRTYVAMVLCQDTEY 156
Cdd:COG3845 85 VHQHFMLVPNLTVAENIVLGLEP--TKGGRLDRKAARARIRELSERYGLDvdpDAKVEDLSVGEQQRVEILKALYRGARI 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1943291881 157 VMLDEPLNNLDMKHAVIMMKLLRKAADElGKTIIIVIHDINFASVYSDYILAMRNGQLYYHGSPKEIMKADIIE 230
Cdd:COG3845 163 LILDEPTAVLTPQEADELFEILRRLAAE-GKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAETSEEELAE 235
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-226 |
3.33e-21 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 88.99 E-value: 3.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 1 MIEISKISKHY----------------------QDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMV 58
Cdd:COG1134 4 MIEVENVSKSYrlyhepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 59 SVNGmDVAAtdsdVLAKNLSilrqenqFVSRLTVEELVgfgrypYSKGRL---TLDD-KKVIDESLAFLNLTEFRHRYLD 134
Cdd:COG1134 84 EVNG-RVSA----LLELGAG-------FHPELTGRENI------YLNGRLlglSRKEiDEKFDEIVEFAELGDFIDQPVK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 135 ELSGGQRQRTYVAMVLCQDTEYVMLDEPLnnldmkhAVIMMKLLRKAADEL------GKTIIIVIHDINFASVYSDYILA 208
Cdd:COG1134 146 TYSSGMRARLAFAVATAVDPDILLVDEVL-------AVGDAAFQKKCLARIrelresGRTVIFVSHSMGAVRRLCDRAIW 218
|
250
....*....|....*...
gi 1943291881 209 MRNGQLYYHGSPKEIMKA 226
Cdd:COG1134 219 LEKGRLVMDGDPEEVIAA 236
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
8-213 |
7.08e-21 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 87.14 E-value: 7.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 8 SKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMdVAatdsdvlaknlsilrqenqFV 87
Cdd:cd03250 12 SGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS-IA-------------------YV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 88 S------RLTVEELVGFGrYPYSKGRLtlddKKVID--------ESLAFLNLTEfrhryLDE----LSGGQRQRTYVAMV 149
Cdd:cd03250 72 SqepwiqNGTIRENILFG-KPFDEERY----EKVIKacalepdlEILPDGDLTE-----IGEkginLSGGQKQRISLARA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1943291881 150 LCQDTEYVMLDEPLNNLDMKHAV-IMMKLLRKAAdELGKTIIIVIHDINFASvYSDYILAMRNGQ 213
Cdd:cd03250 142 VYSDADIYLLDDPLSAVDAHVGRhIFENCILGLL-LNNKTRILVTHQLQLLP-HADQIVVLDNGR 204
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
16-226 |
1.60e-20 |
|
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: 90.19 E-value: 1.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 16 VLDNITTTIQRGGITSIIGPNGAGKSTLlsviGRLLL----PESGMVSVNGMDVAATDSDVLAKNLSILRQENQFVSRlT 91
Cdd:COG4618 347 ILRGVSFSLEPGEVLGVIGPSGSGKSTL----ARLLVgvwpPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDG-T 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 92 VEELVGfgRYPyskgrlTLDDKKVIDE-SLAflNLTE----FRHRY---LDE----LSGGQRQRTYVAMVLCQDTEYVML 159
Cdd:COG4618 422 IAENIA--RFG------DADPEKVVAAaKLA--GVHEmilrLPDGYdtrIGEggarLSGGQRQRIGLARALYGDPRLVVL 491
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1943291881 160 DEPLNNLDmkhAVIMMKLLR--KAADELGKTIIIVIHDINFASVySDYILAMRNGQLYYHGSPKEIMKA 226
Cdd:COG4618 492 DEPNSNLD---DEGEAALAAaiRALKARGATVVVITHRPSLLAA-VDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
7-194 |
2.26e-20 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 89.59 E-value: 2.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 7 ISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVA-ATDSDVLAKNLSILRQENQ 85
Cdd:PRK11288 10 IGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfASTTAALAAGVAIIYQELH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 86 FVSRLTVEELVGFGRYPYSKGrltlddkkVIDESLaflnLTEFRHRYLDE-------------LSGGQRQRTYVAMVLCQ 152
Cdd:PRK11288 90 LVPEMTVAENLYLGQLPHKGG--------IVNRRL----LNYEAREQLEHlgvdidpdtplkyLSIGQRQMVEIAKALAR 157
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1943291881 153 DTEYVMLDEPLNNLDMKHAVIMMKLLRKAADElGKTIIIVIH 194
Cdd:PRK11288 158 NARVIAFDEPTSSLSAREIEQLFRVIRELRAE-GRVILYVSH 198
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
24-224 |
2.41e-20 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 88.94 E-value: 2.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 24 IQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVA----ATDSDVLAKNLSILRQENQFVSRLTVEELVGFG 99
Cdd:PRK10070 51 IEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAkisdAELREVRRKKIAMVFQSFALMPHMTVLDNTAFG 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 100 RYPYSKGRLTLDDKKVidESLAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQDTEYVMLDEPLNNLDMKHAVIMMKLLR 179
Cdd:PRK10070 131 MELAGINAEERREKAL--DALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELV 208
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1943291881 180 KAADELGKTIIIVIHDINFASVYSDYILAMRNGQLYYHGSPKEIM 224
Cdd:PRK10070 209 KLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-227 |
3.16e-20 |
|
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: 86.13 E-value: 3.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 2 IEISKISKHYQD--ITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVLAKNLSI 79
Cdd:cd03251 1 VEFKNVTFRYPGdgPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 80 LRQENqFVSRLTVEELVGFgrypyskGRLTLDDKKVIDESLAfLNLTEFRHRYLD-----------ELSGGQRQRTYVAM 148
Cdd:cd03251 81 VSQDV-FLFNDTVAENIAY-------GRPGATREEVEEAARA-ANAHEFIMELPEgydtvigergvKLSGGQRQRIAIAR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 149 VLCQDTEYVMLDEPLNNLDMKHAvimmKLLRKAADEL--GKTIIIVIH---DINFAsvysDYILAMRNGQLYYHGSPKEI 223
Cdd:cd03251 152 ALLKDPPILILDEATSALDTESE----RLVQAALERLmkNRTTFVIAHrlsTIENA----DRIVVLEDGKIVERGTHEEL 223
|
....
gi 1943291881 224 MKAD 227
Cdd:cd03251 224 LAQG 227
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
15-222 |
4.05e-20 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 88.95 E-value: 4.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 15 TVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPE---SGMVSVNGMDVaatDSDVLAKNLSILRQENQFVSRLT 91
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPI---DAKEMRAISAYVQQDDLFIPTLT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 92 VEELVGF------GRYPYSKGRltlddKKVIDESLAFLNLTEFRH------RYLDELSGGQRQRTYVAMVLCQDTEYVML 159
Cdd:TIGR00955 116 VREHLMFqahlrmPRRVTKKEK-----RERVDEVLQALGLRKCANtrigvpGRVKGLSGGERKRLAFASELLTDPPLLFC 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1943291881 160 DEPLNNLD--MKHAVImmKLLRKAADElGKTIIIVIHDINfASVYS--DYILAMRNGQLYYHGSPKE 222
Cdd:TIGR00955 191 DEPTSGLDsfMAYSVV--QVLKGLAQK-GKTIICTIHQPS-SELFElfDKIILMAEGRVAYLGSPDQ 253
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-213 |
5.57e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 85.91 E-value: 5.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 1 MIEISKISKHYQ-----DITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVLAK 75
Cdd:COG1101 1 MLELKNLSKTFNpgtvnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 76 NLSILRQENQF--VSRLTVEE----------LVGFGRypyskgRLTLDDKKVIDESLAFLNL-TEFRhryLDE----LSG 138
Cdd:COG1101 81 YIGRVFQDPMMgtAPSMTIEEnlalayrrgkRRGLRR------GLTKKRRELFRELLATLGLgLENR---LDTkvglLSG 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1943291881 139 GQRQRTYVAMVLCQDTEYVMLDEPLNNLDMKHAVIMMKLLRKAADELGKTIIIVIHDINFASVYSDYILAMRNGQ 213
Cdd:COG1101 152 GQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGR 226
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-214 |
8.37e-20 |
|
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: 83.42 E-value: 8.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 2 IEISKISKHYQDIT--VLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVLAKNLSI 79
Cdd:cd03246 1 LEVENVSFRYPGAEppVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 80 LRQEnqfvsrltVEELVGfgrypyskgrlTLDDkkvideslaflNLtefrhryldeLSGGQRQRTYVAMVLCQDTEYVML 159
Cdd:cd03246 81 LPQD--------DELFSG-----------SIAE-----------NI----------LSGGQRQRLGLARALYGNPRILVL 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1943291881 160 DEPLNNLDMK------HAVIMMKLlrkaadeLGKTIIIVIHDIN-FASVysDYILAMRNGQL 214
Cdd:cd03246 121 DEPNSHLDVEgeralnQAIAALKA-------AGATRIVIAHRPEtLASA--DRILVLEDGRV 173
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-213 |
3.96e-19 |
|
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: 80.96 E-value: 3.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 2 IEISKISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVngmdvaatdsdvlAKNLSILr 81
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW-------------GSTVKIG- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 82 qenqfvsrltveelvgfgrypyskgrltlddkkvideslaflnltefrhrYLDELSGGQRQRTYVAMVLCQDTEYVMLDE 161
Cdd:cd03221 67 --------------------------------------------------YFEQLSGGEKMRLALAKLLLENPNLLLLDE 96
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1943291881 162 PLNNLDMKHAvimmKLLRKAADELGKTIIIVIHDINFASVYSDYILAMRNGQ 213
Cdd:cd03221 97 PTNHLDLESI----EALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
2-227 |
4.82e-19 |
|
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: 85.92 E-value: 4.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 2 IEISKISKHY--QDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVLAKNLSI 79
Cdd:TIGR02203 331 VEFRNVTFRYpgRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVAL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 80 LRQeNQFVSRLTVEELVGFGRypyskgRLTLDDKKvIDESLAFLNLTEFRHRyLDE------------LSGGQRQRTYVA 147
Cdd:TIGR02203 411 VSQ-DVVLFNDTIANNIAYGR------TEQADRAE-IERALAAAYAQDFVDK-LPLgldtpigengvlLSGGQRQRLAIA 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 148 MVLCQDTEYVMLDEPLNNLDMKHAvimmKLLRKAADEL--GKTIIIVIHDINFASvYSDYILAMRNGQLYYHGSPKEIMK 225
Cdd:TIGR02203 482 RALLKDAPILILDEATSALDNESE----RLVQAALERLmqGRTTLVIAHRLSTIE-KADRIVVMDDGRIVERGTHNELLA 556
|
..
gi 1943291881 226 AD 227
Cdd:TIGR02203 557 RN 558
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
2-227 |
5.36e-19 |
|
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: 82.97 E-value: 5.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 2 IEISKISKHY---QDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVLAKNLS 78
Cdd:cd03249 1 IEFKNVSFRYpsrPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 79 ILRQENQFVSRlTVEELVGFGRYPyskgRLTLDDKKVIDESLAFLNLTEFRHRYLDE-------LSGGQRQRTYVAMVLC 151
Cdd:cd03249 81 LVSQEPVLFDG-TIAENIRYGKPD----ATDEEVEEAAKKANIHDFIMSLPDGYDTLvgergsqLSGGQKQRIAIARALL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1943291881 152 QDTEYVMLDEPLNNLDMKHAVIMMKLLRKAAdeLGKTIIIVIHdiNFASV-YSDYILAMRNGQLYYHGSPKEIMKAD 227
Cdd:cd03249 156 RNPKILLLDEATSALDAESEKLVQEALDRAM--KGRTTIVIAH--RLSTIrNADLIAVLQNGQVVEQGTHDELMAQK 228
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-208 |
6.78e-19 |
|
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: 85.37 E-value: 6.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 2 IEISKISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSV-NGMDVAATDS--DVLAKNLS 78
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIgETVKLAYVDQsrDALDPNKT 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 79 ILrqenqfvsrltvEELvgfgrypySKGRLTLDDKKVIDESLAFLNLTEFR----HRYLDELSGGQRQRTYVAMVLCQDT 154
Cdd:TIGR03719 403 VW------------EEI--------SGGLDIIKLGKREIPSRAYVGRFNFKgsdqQKKVGQLSGGERNRVHLAKTLKSGG 462
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1943291881 155 EYVMLDEPLNNLDmkhaVIMMKLLRKAADELGKTIIIVIHDINFASVYSDYILA 208
Cdd:TIGR03719 463 NVLLLDEPTNDLD----VETLRALEEALLNFAGCAVVISHDRWFLDRIATHILA 512
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-214 |
7.92e-19 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 82.23 E-value: 7.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 1 MIEISKISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAA-TDSDVLAKNLSI 79
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDwQTAKIMREAVAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 80 LRQENQFVSRLTVEELVGFGRYPYSKGRLTLDDKKVIDeslAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQDTEYVML 159
Cdd:PRK11614 85 VPEGRRVFSRMTVEENLAMGGFFAERDQFQERIKWVYE---LFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 160 DEPlnNLDMKHAVIM-----MKLLRkaadELGKTIIIVIHDINFASVYSDYILAMRNGQL 214
Cdd:PRK11614 162 DEP--SLGLAPIIIQqifdtIEQLR----EQGMTIFLVEQNANQALKLADRGYVLENGHV 215
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
15-197 |
2.74e-18 |
|
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: 80.10 E-value: 2.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 15 TVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATdSDVLAKNLSILRQENQFVSRLTVEE 94
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQ-RDEPHENILYLGHLPGLKPELSALE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 95 LVGFGRypyskgRLTLDDKKVIDESLAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQDTEYVMLDEPLNNLDMKHAVIM 174
Cdd:TIGR01189 93 NLHFWA------AIHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALL 166
|
170 180
....*....|....*....|...
gi 1943291881 175 MKLLRKAADELGKTIIIVIHDIN 197
Cdd:TIGR01189 167 AGLLRAHLARGGIVLLTTHQDLG 189
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
2-207 |
3.91e-18 |
|
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: 83.30 E-value: 3.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 2 IEISKISKHYQDITvLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNgMDVA------ATDSDvlak 75
Cdd:COG1245 342 VEYPDLTKSYGGFS-LEVEGGEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED-LKISykpqyiSPDYD---- 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 76 nlsilrqenqfvsrLTVEELVGFGRYPyskgrlTLDDKKVIDESLAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQDTE 155
Cdd:COG1245 416 --------------GTVEEFLRSANTD------DFGSSYYKTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDAD 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1943291881 156 YVMLDEPLNNLDMKHAVIMMKLLRKAADELGKTIIIVIHDINFASVYSDYIL 207
Cdd:COG1245 476 LYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLM 527
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-214 |
4.39e-18 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 80.88 E-value: 4.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 4 ISKISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLsvigRLLLpesgmvsvnGMDvAATDSDVLAKN--LSILR 81
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLL----RLLA---------GLE-TPSAGELLAGTapLAEAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 82 QEnqfvSRLTVEElvgfgrypyskGRLtLDDKKVID---------------ESLAFLNLTEFRHRYLDELSGGQRQRTYV 146
Cdd:PRK11247 81 ED----TRLMFQD-----------ARL-LPWKKVIDnvglglkgqwrdaalQALAAVGLADRANEWPAALSGGQKQRVAL 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1943291881 147 AMVLCQDTEYVMLDEPLNNLDMKHAVIMMKLLRKAADELGKTIIIVIHDINFASVYSDYILAMRNGQL 214
Cdd:PRK11247 145 ARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1-207 |
6.23e-18 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 82.55 E-value: 6.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 1 MIEISKISKHYQDITvLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNgMDVA------ATDSDVla 74
Cdd:PRK13409 340 LVEYPDLTKKLGDFS-LEVEGGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-LKISykpqyiKPDYDG-- 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 75 knlsilrqenqfvsrlTVEELVgfgrypySKGRLTLDDKKVIDESLAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQDT 154
Cdd:PRK13409 416 ----------------TVEDLL-------RSITDDLGSSYYKSEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDA 472
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1943291881 155 EYVMLDEPLNNLDMKHAVIMMKLLRKAADELGKTIIIVIHDINFASVYSDYIL 207
Cdd:PRK13409 473 DLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDIYMIDYISDRLM 525
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
15-197 |
6.63e-18 |
|
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: 79.07 E-value: 6.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 15 TVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATdSDVLAKNLSILRQENQFVSRLTVEE 94
Cdd:cd03231 14 ALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQ-RDSIARGLLYLGHAPGIKTTLSVLE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 95 LVGFGRypyskgrlTLDDKKVIDESLAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQDTEYVMLDEPLNNLDMKHAVIM 174
Cdd:cd03231 93 NLRFWH--------ADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARF 164
|
170 180
....*....|....*....|...
gi 1943291881 175 MKLLRKAADELGKTIIIVIHDIN 197
Cdd:cd03231 165 AEAMAGHCARGGMVVLTTHQDLG 187
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-168 |
7.66e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 82.03 E-value: 7.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 4 ISKISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVngmdvaatdsdvlAKNLSI--LR 81
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI-------------PKGLRIgyLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 82 QENQFVSRLTVEELV--GFGRY---------PYSKGRLTLDDKKVIDES-------------------LAFLNLTEFRH- 130
Cdd:COG0488 68 QEPPLDDDLTVLDTVldGDAELraleaeleeLEAKLAEPDEDLERLAELqeefealggweaearaeeiLSGLGFPEEDLd 147
|
170 180 190
....*....|....*....|....*....|....*...
gi 1943291881 131 RYLDELSGGQRQRTYVAMVLCQDTEYVMLDEPLNNLDM 168
Cdd:COG0488 148 RPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDL 185
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-236 |
8.53e-18 |
|
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: 80.87 E-value: 8.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 1 MIEISKISKHYQ----DITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLP---ESGMVSVNGMDVAATDSDVL 73
Cdd:COG0444 1 LLEVRNLKVYFPtrrgVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 74 AKnlsILRQENQFV------S---RLTVEELVG-----FGRYPYSKGRltlddKKVIdESLAFLNLT---EFRHRYLDEL 136
Cdd:COG0444 81 RK---IRGREIQMIfqdpmtSlnpVMTVGDQIAeplriHGGLSKAEAR-----ERAI-ELLERVGLPdpeRRLDRYPHEL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 137 SGGQRQRTYVAMVLCQDTEYVMLDEPLNNLDmkhAVI---MMKLLRKAADELGKTIIIVIHDINFASVYSDYILAMrngq 213
Cdd:COG0444 152 SGGMRQRVMIARALALEPKLLIADEPTTALD---VTIqaqILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVM---- 224
|
250 260
....*....|....*....|....
gi 1943291881 214 lyYHGspkEIM-KADiIEDIFDTP 236
Cdd:COG0444 225 --YAG---RIVeEGP-VEELFENP 242
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-223 |
1.19e-17 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 79.30 E-value: 1.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 1 MIEISKISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVaaTDSDV-------- 72
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDI--THLPMhkrarlgi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 73 --LAKNLSILRqenqfvsRLTVE-------ELVGFGRypysKGRltlddKKVIDESLAFLNLTEFRHRYLDELSGGQRQR 143
Cdd:COG1137 81 gyLPQEASIFR-------KLTVEdnilavlELRKLSK----KER-----EERLEELLEEFGITHLRKSKAYSLSGGERRR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 144 TYVAMVLCQDTEYVMLDEPLNNLDMKhAVI-MMKLLRKAADelgKTIIIVIHD---------INFAsvysdYIlaMRNGQ 213
Cdd:COG1137 145 VEIARALATNPKFILLDEPFAGVDPI-AVAdIQKIIRHLKE---RGIGVLITDhnvretlgiCDRA-----YI--ISEGK 213
|
250
....*....|
gi 1943291881 214 LYYHGSPKEI 223
Cdd:COG1137 214 VLAEGTPEEI 223
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
5-207 |
1.32e-17 |
|
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: 79.37 E-value: 1.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 5 SKISKHYQDITvLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVLAKNLSILRQen 84
Cdd:cd03237 4 PTMKKTLGEFT-LEVEGGSISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYIKADYEGTVRD-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 85 qfvsrLTVEELVGFGRYPYSKgrltlddkkviDESLAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQDTEYVMLDEPLN 164
Cdd:cd03237 81 -----LLSSITKDFYTHPYFK-----------TEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSA 144
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1943291881 165 NLDMKHAVIMMKLLRKAADELGKTIIIVIHDINFASVYSDYIL 207
Cdd:cd03237 145 YLDVEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLI 187
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
15-194 |
1.66e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 77.99 E-value: 1.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 15 TVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDvaATDSDVlAKNLSILRQENQFVSRLTVEE 94
Cdd:PRK13539 16 VLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGD--IDDPDV-AEACHYLGHRNAMKPALTVAE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 95 LVGFGRYPYSKGRLTlddkkvIDESLAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQDTEYVMLDEPLNNLDmKHAVIM 174
Cdd:PRK13539 93 NLEFWAAFLGGEELD------IAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALD-AAAVAL 165
|
170 180
....*....|....*....|
gi 1943291881 175 MKLLRKAADELGKTIIIVIH 194
Cdd:PRK13539 166 FAELIRAHLAQGGIVIAATH 185
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
16-224 |
1.83e-17 |
|
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: 78.81 E-value: 1.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 16 VLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVLAKNLSILRQEnqfvsrlTV--E 93
Cdd:cd03253 16 VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVVPQD-------TVlfN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 94 ELVGFG-RYpyskGRLTLDDKKVIDESLA------FLNL-----TEFRHRYLdELSGGQRQRTYVAMVLCQDTEYVMLDE 161
Cdd:cd03253 89 DTIGYNiRY----GRPDATDEEVIEAAKAaqihdkIMRFpdgydTIVGERGL-KLSGGEKQRVAIARAILKNPPILLLDE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1943291881 162 PLNNLDMKHAVIMMKLLRKAADelGKTIIIVIHdiNFASVY-SDYILAMRNGQLYYHGSPKEIM 224
Cdd:cd03253 164 ATSALDTHTEREIQAALRDVSK--GRTTIVIAH--RLSTIVnADKIIVLKDGRIVERGTHEELL 223
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
7-223 |
2.20e-17 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 80.07 E-value: 2.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 7 ISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVI--------GRLLLPESGMvsvNgmDVAATDsdvlaKNLS 78
Cdd:PRK11000 9 VTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIagleditsGDLFIGEKRM---N--DVPPAE-----RGVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 79 ILRQENQFVSRLTVEELVGFGRypyskgRLTLDDKKVIDESL----AFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQDT 154
Cdd:PRK11000 79 MVFQSYALYPHLSVAENMSFGL------KLAGAKKEEINQRVnqvaEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1943291881 155 EYVMLDEPLNNLDMKHAVIMMKLLRKAADELGKTIIIVIHDINFASVYSDYILAMRNGQLYYHGSPKEI 223
Cdd:PRK11000 153 SVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
11-227 |
2.62e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 80.66 E-value: 2.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 11 YQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVigrLL--LPESGMVSVNGMDVAATDSDVLAKNLSILRQENQFVS 88
Cdd:PRK11174 360 PDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNA---LLgfLPYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPH 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 89 RlTVEELVGFGRYPYSKGRltlddkkvIDESLAFLNLTEFRHRY---LDE--------LSGGQRQRTYVAMVLCQDTEYV 157
Cdd:PRK11174 437 G-TLRDNVLLGNPDASDEQ--------LQQALENAWVSEFLPLLpqgLDTpigdqaagLSVGQAQRLALARALLQPCQLL 507
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 158 MLDEPLNNLDMKHAVIMMKLLRKAAdeLGKTIIIVIHDINFASVYsDYILAMRNGQLYYHGSPKEIMKAD 227
Cdd:PRK11174 508 LLDEPTASLDAHSEQLVMQALNAAS--RRQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGDYAELSQAG 574
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-227 |
3.77e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 80.25 E-value: 3.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 2 IEISKISKHY--QDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVLAKNLSI 79
Cdd:PRK11160 339 LTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 80 LRQenqfvsRLtveelvgfgrYPYS---KGRLTLDDKKVIDESL-AFL------NLTEFRHRyLD--------ELSGGQR 141
Cdd:PRK11160 419 VSQ------RV----------HLFSatlRDNLLLAAPNASDEALiEVLqqvgleKLLEDDKG-LNawlgeggrQLSGGEQ 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 142 QRTYVAMVLCQDTEYVMLDEPLNNLDMKHAVIMMKLLRKAADelGKTIIIVIHDINfASVYSDYILAMRNGQLYYHGSPK 221
Cdd:PRK11160 482 RRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRLT-GLEQFDRICVMDNGQIIEQGTHQ 558
|
....*.
gi 1943291881 222 EIMKAD 227
Cdd:PRK11160 559 ELLAQQ 564
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
2-226 |
3.85e-17 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 80.17 E-value: 3.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 2 IEISKISKHYQ-DITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVLAKNLSIL 80
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 81 RQENQFVSRLTVEELVgfgrypyskgrLTLDDKKVIDESLAFLNLTEFR----------HRYLDE----LSGGQRQRTYV 146
Cdd:TIGR01193 554 PQEPYIFSGSILENLL-----------LGAKENVSQDEIWAACEIAEIKddienmplgyQTELSEegssISGGQKQRIAL 622
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 147 AMVLCQDTEYVMLDEPLNNLDMkhaVIMMKLLRKAADELGKTIIIVIHDINFASVySDYILAMRNGQLYYHGSPKEIMKA 226
Cdd:TIGR01193 623 ARALLTDSKVLILDESTSNLDT---ITEKKIVNNLLNLQDKTIIFVAHRLSVAKQ-SDKIIVLDHGKIIEQGSHDELLDR 698
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
9-226 |
4.11e-17 |
|
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: 80.11 E-value: 4.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 9 KHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTL-LSVIGrlLLPESGMVSVNGMDVAATDsdvlAKNLSILRQENQFV 87
Cdd:COG4172 294 RTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLgLALLR--LIPSEGEIRFDGQDLDGLS----RRALRPLRRRMQVV 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 88 ---------SRLTVEELVGFG----RYPYSKG-RltldDKKVIdESLAFLNLT-EFRHRYLDELSGGQRQRTYVA--MVL 150
Cdd:COG4172 368 fqdpfgslsPRMTVGQIIAEGlrvhGPGLSAAeR----RARVA-EALEEVGLDpAARHRYPHEFSGGQRQRIAIAraLIL 442
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1943291881 151 cqDTEYVMLDEPLNNLDMKHAVIMMKLLRKAADELGKTIIIVIHDINFASVYSDYILAMRNGQLYYHGSPKEIMKA 226
Cdd:COG4172 443 --EPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDA 516
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-223 |
6.13e-17 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 77.38 E-value: 6.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 2 IEISKISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRL--LLPE---SGMVSVNGMDVAATDSDVLAkn 76
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndLIPGarvEGEILLDGEDIYDPDVDVVE-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 77 lsiLRQE--------NQFvsRLTVEELVGFGryPYSKGRLtldDKKVIDE----SL--AFLnLTEFRHRyLDE----LSG 138
Cdd:COG1117 90 ---LRRRvgmvfqkpNPF--PKSIYDNVAYG--LRLHGIK---SKSELDEiveeSLrkAAL-WDEVKDR-LKKsalgLSG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 139 GQRQRTYVAMVLCQDTEYVMLDEPLNNLDMKHAVIMMKLLRkaadELGK--TIIIVIHDINFASVYSDYILAMRNGQLYY 216
Cdd:COG1117 158 GQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELIL----ELKKdyTIVIVTHNMQQAARVSDYTAFFYLGELVE 233
|
....*..
gi 1943291881 217 HGSPKEI 223
Cdd:COG1117 234 FGPTEQI 240
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
13-214 |
7.17e-17 |
|
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: 76.74 E-value: 7.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 13 DITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVLAKNLSILRQENQFVSRlTV 92
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVSLVGQEPVLFAR-SL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 93 EELVGFGRYPYSKGRLTlddkKVIDESLAFLNLTEFRHRYLDE-------LSGGQRQRTYVAMVLCQDTEYVMLDEPLNN 165
Cdd:cd03248 105 QDNIAYGLQSCSFECVK----EAAQKAHAHSFISELASGYDTEvgekgsqLSGGQKQRVAIARALIRNPQVLILDEATSA 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1943291881 166 LDMKHAVIMMKLLRKAADElgKTIIIVIHDINFASvYSDYILAMRNGQL 214
Cdd:cd03248 181 LDAESEQQVQQALYDWPER--RTVLVIAHRLSTVE-RADQILVLDGGRI 226
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
2-236 |
7.62e-17 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 78.23 E-value: 7.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 2 IEISKISKHY---------QDITV--LDNITTTIQRGGITSIIGPNGAGKSTLlsviGRLLL----PESGMVSVNGMDVA 66
Cdd:COG4608 8 LEVRDLKKHFpvrgglfgrTVGVVkaVDGVSFDIRRGETLGLVGESGCGKSTL----GRLLLrleePTSGEILFDGQDIT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 67 ATDSDVLAKnlsiLRQENQFV---------SRLTVEELVGFG-RYPYSKGRLTLDDKkvIDESLAFLNL-TEFRHRYLDE 135
Cdd:COG4608 84 GLSGRELRP----LRRRMQMVfqdpyaslnPRMTVGDIIAEPlRIHGLASKAERRER--VAELLELVGLrPEHADRYPHE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 136 LSGGQRQRTYVAMVLCQDTEYVMLDEPLNNLDMK-HAVImMKLLRKAADELGKTIIIVIHDINFASVYSDYILAMrngql 214
Cdd:COG4608 158 FSGGQRQRIGIARALALNPKLIVCDEPVSALDVSiQAQV-LNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVM----- 231
|
250 260
....*....|....*....|..
gi 1943291881 215 yYHGSPKEIMKADiieDIFDTP 236
Cdd:COG4608 232 -YLGKIVEIAPRD---ELYARP 249
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
2-225 |
7.63e-17 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 79.38 E-value: 7.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 2 IEISKISKHY---QDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVLAKNLS 78
Cdd:TIGR00958 479 IEFQDVSFSYpnrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVA 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 79 ILRQENQFVSRlTVEELVGFGRYPYSKGRLTlddkKVIDESLAFLNLTEFRHRYLDE-------LSGGQRQRTYVAMVLC 151
Cdd:TIGR00958 559 LVGQEPVLFSG-SVRENIAYGLTDTPDEEIM----AAAKAANAHDFIMEFPNGYDTEvgekgsqLSGGQKQRIAIARALV 633
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1943291881 152 QDTEYVMLDEPLNNLDmkhaVIMMKLLRKAADELGKTIIIVIHDINFASvYSDYILAMRNGQLYYHGSPKEIMK 225
Cdd:TIGR00958 634 RKPRVLILDEATSALD----AECEQLLQESRSRASRTVLLIAHRLSTVE-RADQILVLKKGSVVEMGTHKQLME 702
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-214 |
8.80e-17 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 77.42 E-value: 8.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 1 MIEISKISKHY---------QDITVLDNITTTIQRGGITSIIGPNGAGKSTLlsviGRLLL----PESGMVSVNGMDVAA 67
Cdd:PRK10419 3 LLNVSGLSHHYahgglsgkhQHQTVLNNVSLSLKSGETVALLGRSGCGKSTL----ARLLVglesPSQGNVSWRGEPLAK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 68 TD-SDVLAknlsiLRQENQFV---------SRLTVEELVgfgRYPYsKGRLTLDDKKVIDESLAFLNLTEFRHRYLD--- 134
Cdd:PRK10419 79 LNrAQRKA-----FRRDIQMVfqdsisavnPRKTVREII---REPL-RHLLSLDKAERLARASEMLRAVDLDDSVLDkrp 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 135 -ELSGGQRQRTYVAMVLCQDTEYVMLDEPLNNLDMKHAVIMMKLLRKAADELGKTIIIVIHDINFASVYSDYILAMRNGQ 213
Cdd:PRK10419 150 pQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQ 229
|
.
gi 1943291881 214 L 214
Cdd:PRK10419 230 I 230
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-223 |
9.32e-17 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 76.95 E-value: 9.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 1 MIEISKISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVLAKnLSIL 80
Cdd:PRK11300 5 LLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIAR-MGVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 81 R--QENQFVSRLTVEE--LVGFGRY---PYSKGRLTL-----DDKKVIDES---LAFLNLTEFRHRYLDELSGGQRQRTY 145
Cdd:PRK11300 84 RtfQHVRLFREMTVIEnlLVAQHQQlktGLFSGLLKTpafrrAESEALDRAatwLERVGLLEHANRQAGNLAYGQQRRLE 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1943291881 146 VAMVLCQDTEYVMLDEPLNNLDMKHAVIMMKLLRKAADELGKTIIIVIHDINFASVYSDYILAMRNGQLYYHGSPKEI 223
Cdd:PRK11300 164 IARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEI 241
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
6-233 |
1.88e-16 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 76.09 E-value: 1.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 6 KISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVLA-KNLSILRQEN 84
Cdd:PRK10895 8 NLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARArRGIGYLPQEA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 85 QFVSRLTV-EELVGFGRYpysKGRLTLDDKKV-IDESLAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQDTEYVMLDEP 162
Cdd:PRK10895 88 SIFRRLSVyDNLMAVLQI---RDDLSAEQREDrANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEP 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1943291881 163 LNNLDMKHAVIMMKLLRKAADElGKTIIIVIHDINFASVYSDYILAMRNGQLYYHGSPKEIMKADIIEDIF 233
Cdd:PRK10895 165 FAGVDPISVIDIKRIIEHLRDS-GLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRVY 234
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-206 |
3.98e-16 |
|
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: 75.48 E-value: 3.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 27 GGITSIIGPNGAGKSTLLSVIGRLLLPESG-----------MVSVNGMDVAATDSDVLAKNLSILRQEnQFVSRL----- 90
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLGkfddppdwdeiLDEFRGSELQNYFTKLLEGDVKVIVKP-QYVDLIpkavk 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 91 -TVEELVGfgrypyskgrlTLDDKKVIDESLAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQDTEYVMLDEPLNNLDMK 169
Cdd:cd03236 105 gKVGELLK-----------KKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIK 173
|
170 180 190
....*....|....*....|....*....|....*..
gi 1943291881 170 HAVIMMKLLRKAADElGKTIIIVIHDINFASVYSDYI 206
Cdd:cd03236 174 QRLNAARLIRELAED-DNYVLVVEHDLAVLDYLSDYI 209
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-213 |
4.45e-16 |
|
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: 74.78 E-value: 4.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 1 MIEISKISK----HYQD---ITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVN----GMDVA-AT 68
Cdd:COG4778 4 LLEVENLSKtftlHLQGgkrLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggWVDLAqAS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 69 DSDVLAknlsILRQENQFVS-------RLTVEELV-------GFGR-YPYSKGRltlddkkvidESLAFLNLTEfrhryl 133
Cdd:COG4778 84 PREILA----LRRRTIGYVSqflrvipRVSALDVVaepllerGVDReEARARAR----------ELLARLNLPE------ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 134 dEL--------SGGQRQRTYVAMVLCQDTEYVMLDEPLNNLDMKHAVIMMKLLRKAADElGKTIIIVIHDINFASVYSDY 205
Cdd:COG4778 144 -RLwdlppatfSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAVADR 221
|
....*...
gi 1943291881 206 ILAMRNGQ 213
Cdd:COG4778 222 VVDVTPFS 229
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-225 |
5.00e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 74.88 E-value: 5.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 2 IEISKISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLL-LPES----GMVSVNGMDVAATDSDVLA-- 74
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLeLNEEarveGEVRLFGRNIYSPDVDPIEvr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 75 KNLSILRQENQFVSRLTVEELVGFGRY--PYSKGRLTLDdkKVIDESLAFLNL-TEFRHR---YLDELSGGQRQRTYVAM 148
Cdd:PRK14267 85 REVGMVFQYPNPFPHLTIYDNVAIGVKlnGLVKSKKELD--ERVEWALKKAALwDEVKDRlndYPSNLSGGQRQRLVIAR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1943291881 149 VLCQDTEYVMLDEPLNNLDMKHAVIMMKLLRKAADELgkTIIIVIHDINFASVYSDYILAMRNGQLYYHGSPKEIMK 225
Cdd:PRK14267 163 ALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFE 237
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-197 |
8.54e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 75.12 E-value: 8.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 1 MIEISKISKHYQ---------------------DITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVS 59
Cdd:COG4586 1 IIEVENLSKTYRvyekepglkgalkglfrreyrEVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 60 VNGMDvaatdsdvlaknlsILRQENQFVSRLTVeelVgFGrypySKGRLTLD----------------DKKVIDESLAF- 122
Cdd:COG4586 81 VLGYV--------------PFKRRKEFARRIGV---V-FG----QRSQLWWDlpaidsfrllkaiyriPDAEYKKRLDEl 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 123 ---LNLTEFRHRYLDELSGGQRQRTYVAMVLCQDTEYVMLDEPLNNLD--MKHAVImmKLLRKAADELGKTIIIVIHDIN 197
Cdd:COG4586 139 velLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDvvSKEAIR--EFLKEYNRERGTTILLTSHDMD 216
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-213 |
8.88e-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: 76.02 E-value: 8.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 1 MIEISKISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRlLLPE---SGMVSVNGMDVAATD-SDVLAKN 76
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSG-VYPHgtwDGEIYWSGSPLKASNiRDTERAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 77 LSILRQENQFVSRLTVEELVGFGRYPYSKGRLTLDD------KKVIDE-SLAFLNLTefrhRYLDELSGGQRQRTYVAMV 149
Cdd:TIGR02633 80 IVIIHQELTLVPELSVAENIFLGNEITLPGGRMAYNamylraKNLLRElQLDADNVT----RPVGDYGGGQQQLVEIAKA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1943291881 150 LCQDTEYVMLDEPLNNLDMKHAVIMMKLLRKAADElGKTIIIVIHDINFASVYSDYILAMRNGQ 213
Cdd:TIGR02633 156 LNKQARLLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
23-206 |
9.97e-16 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 75.98 E-value: 9.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 23 TIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSvngmDVAATD---------------SDVLAKNLSILrQENQFV 87
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKSTALKILSGELKPNLGDYD----EEPSWDevlkrfrgtelqdyfKKLANGEIKVA-HKPQYV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 88 SRL------TVEELVGfgrypyskgrlTLDDKKVIDESLAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQDTEYVMLDE 161
Cdd:COG1245 170 DLIpkvfkgTVRELLE-----------KVDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDE 238
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1943291881 162 PLNNLDMKHAVIMMKLLRKAADElGKTIIIVIHDINFASVYSDYI 206
Cdd:COG1245 239 PSSYLDIYQRLNVARLIRELAEE-GKYVLVVEHDLAILDYLADYV 282
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
7-213 |
1.02e-15 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 74.19 E-value: 1.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 7 ISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDvaATDSDVLAKNLS----ILRQ 82
Cdd:PRK11701 12 LTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRD--GQLRDLYALSEAerrrLLRT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 83 ENQFVS-------RLTV-------EELVGFGRYPYSKGRltlddkkviDESLAFLNLTEFRHRYLDEL----SGGQRQRT 144
Cdd:PRK11701 90 EWGFVHqhprdglRMQVsaggnigERLMAVGARHYGDIR---------ATAGDWLERVEIDAARIDDLpttfSGGMQQRL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1943291881 145 YVAMVLCQDTEYVMLDEPLNNLDMKHAVIMMKLLRKAADELGKTIIIVIHDINFASVYSDYILAMRNGQ 213
Cdd:PRK11701 161 QIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGR 229
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-243 |
1.10e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 74.30 E-value: 1.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 2 IEISKISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPEsGMVSVNGmDVAATDSDVLAK--NLSI 79
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELE-SEVRVEG-RVEFFNQNIYERrvNLNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 80 LRQENQFVS------RLTVEELVGFG-RYPYSKGRLTLDDkkVIDESLAFLNL-TEFRHRYLD---ELSGGQRQRTYVAM 148
Cdd:PRK14258 86 LRRQVSMVHpkpnlfPMSVYDNVAYGvKIVGWRPKLEIDD--IVESALKDADLwDEIKHKIHKsalDLSGGQQQRLCIAR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 149 VLCQDTEYVMLDEPLNNLDMKHAVIMMKLLRKAADELGKTIIIVIHDINFASVYSDYilamrngQLYYHGSPKEI---MK 225
Cdd:PRK14258 164 ALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDF-------TAFFKGNENRIgqlVE 236
|
250
....*....|....*...
gi 1943291881 226 ADIIEDIFDTPVDVKELD 243
Cdd:PRK14258 237 FGLTKKIFNSPHDSRTRE 254
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1-214 |
2.06e-15 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 72.89 E-value: 2.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 1 MIEISKISKHY----QDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSD----V 72
Cdd:PRK10584 6 IVEVHHLKKSVgqgeHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEarakL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 73 LAKNLSILRQENQFVSRLTVEELVgfgRYP-YSKGRLTLDDKKVIDESLAFLNLTEFRHRYLDELSGGQRQRTYVAMVLC 151
Cdd:PRK10584 86 RAKHVGFVFQSFMLIPTLNALENV---ELPaLLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1943291881 152 QDTEYVMLDEPLNNLDMKHAVIMMKLLRKAADELGKTIIIVIHDINFASvYSDYILAMRNGQL 214
Cdd:PRK10584 163 GRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAA-RCDRRLRLVNGQL 224
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
4-224 |
2.86e-15 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 74.92 E-value: 2.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 4 ISKISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVI-GRLLLPE-SGMVSVNGMDVAATdsdvLAKNLSILR 81
Cdd:PLN03211 71 ISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALaGRIQGNNfTGTILANNRKPTKQ----ILKRTGFVT 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 82 QENQFVSRLTVEELVGFG---RYPYSkgrLTLDDKKVIDES-LAFLNLTE-----FRHRYLDELSGGQRQRTYVAMVLCQ 152
Cdd:PLN03211 147 QDDILYPHLTVRETLVFCsllRLPKS---LTKQEKILVAESvISELGLTKcentiIGNSFIRGISGGERKRVSIAHEMLI 223
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1943291881 153 DTEYVMLDEPLNNLDMKHAVIMMKLLRKAADElGKTIIIVIHDINfASVYS--DYILAMRNGQLYYHGSPKEIM 224
Cdd:PLN03211 224 NPSLLILDEPTSGLDATAAYRLVLTLGSLAQK-GKTIVTSMHQPS-SRVYQmfDSVLVLSEGRCLFFGKGSDAM 295
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
12-218 |
3.73e-15 |
|
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: 71.51 E-value: 3.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 12 QDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVI-GRlllPESGMVS----VNGMDVAATdsdvLAKNLSILRQENQF 86
Cdd:cd03232 18 GKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLaGR---KTAGVITgeilINGRPLDKN----FQRSTGYVEQQDVH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 87 VSRLTVEElvgfgrypyskgrltlddkkvideSLAFlnltefrHRYLDELSGGQRQRTYVAMVLCQDTEYVMLDEPLNNL 166
Cdd:cd03232 91 SPNLTVRE------------------------ALRF-------SALLRGLSVEQRKRLTIGVELAAKPSILFLDEPTSGL 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1943291881 167 DMKHAVIMMKLLRKAADElGKTIIIVIHDINfASVYS--DYILAM-RNGQLYYHG 218
Cdd:cd03232 140 DSQAAYNIVRFLKKLADS-GQAILCTIHQPS-ASIFEkfDRLLLLkRGGKTVYFG 192
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
23-206 |
5.58e-15 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 73.69 E-value: 5.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 23 TIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGM--DV----AATD-----SDVLAKNLSILrQENQFVSRL- 90
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYEEEPSwdEVlkrfRGTElqnyfKKLYNGEIKVV-HKPQYVDLIp 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 91 -----TVEELVgfgrypyskgrLTLDDKKVIDESLAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQDTEYVMLDEPLNN 165
Cdd:PRK13409 174 kvfkgKVRELL-----------KKVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSY 242
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1943291881 166 LDMKHAVIMMKLLRKAADelGKTIIIVIHDINFASVYSDYI 206
Cdd:PRK13409 243 LDIRQRLNVARLIRELAE--GKYVLVVEHDLAVLDYLADNV 281
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
15-194 |
8.18e-15 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 71.14 E-value: 8.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 15 TVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLL--PESGMVSVngmdvaatdsdvlaknlsilrQENQFVSRLTV 92
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDV---------------------PDNQFGREASL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 93 EELVGfgrypyskgrltldDKKVIDESLAFLN---LTE---FRHRYlDELSGGQRQRTYVAMVLCQDTEYVMLDEPLNNL 166
Cdd:COG2401 103 IDAIG--------------RKGDFKDAVELLNavgLSDavlWLRRF-KELSTGQKFRFRLALLLAERPKLLVIDEFCSHL 167
|
170 180
....*....|....*....|....*...
gi 1943291881 167 DMKHAVIMMKLLRKAADELGKTIIIVIH 194
Cdd:COG2401 168 DRQTAKRVARNLQKLARRAGITLVVATH 195
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-243 |
2.28e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 72.01 E-value: 2.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 1 MIEISKISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATdSDVLAKNLSI- 79
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARL-TPAKAHQLGIy 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 80 -LRQENQFVSRLTVEE--LVGFGRYPYSKGRLTlddkkvidESLAFLNLtefrHRYLDELSG----GQRQRTYVAMVLCQ 152
Cdd:PRK15439 90 lVPQEPLLFPNLSVKEniLFGLPKRQASMQKMK--------QLLAALGC----QLDLDSSAGslevADRQIVEILRGLMR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 153 DTEYVMLDEPLNNLDMKHAVIMMKLLRKAADElGKTIIIVIHDINFASVYSDYILAMRNGQLYYHGSPKEIMKADIIEDI 232
Cdd:PRK15439 158 DSRILILDEPTASLTPAETERLFSRIRELLAQ-GVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTDDIIQAI 236
|
250
....*....|.
gi 1943291881 233 fdTPVdVKELD 243
Cdd:PRK15439 237 --TPA-AREKS 244
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
16-220 |
4.23e-14 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 68.98 E-value: 4.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 16 VLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVLAKNLSILRQENQFVSRLTVEEL 95
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTIIPQDPTLFSGTIRSNL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 96 VGFGRYpyskgrltlDDKKVidesLAFLNLTEFRhrylDELSGGQRQRTYVAMVLCQDTEYVMLDEPLNNLDMKHAVIMM 175
Cdd:cd03369 103 DPFDEY---------SDEEI----YGALRVSEGG----LNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQ 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1943291881 176 KLLRKAADelGKTIIIVIHDINFASVYsDYILAMRNGQLYYHGSP 220
Cdd:cd03369 166 KTIREEFT--NSTILTIAHRLRTIIDY-DKILVMDAGEVKEYDHP 207
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
10-197 |
4.51e-14 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 68.97 E-value: 4.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 10 HYQ--DITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVLAKNLSILRQENQFV 87
Cdd:PRK10247 14 GYLagDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 88 SRLTVEELVgfgrYPYSKGRLTLDDKKVIDeSLAFLNLTE-FRHRYLDELSGGQRQRTYVAMVLCQDTEYVMLDEPLNNL 166
Cdd:PRK10247 94 GDTVYDNLI----FPWQIRNQQPDPAIFLD-DLERFALPDtILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSAL 168
|
170 180 190
....*....|....*....|....*....|.
gi 1943291881 167 DMKHAVIMMKLLRKAADELGKTIIIVIHDIN 197
Cdd:PRK10247 169 DESNKHNVNEIIHRYVREQNIAVLWVTHDKD 199
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
16-220 |
5.49e-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: 68.67 E-value: 5.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 16 VLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVLAKNLSILRQENQFVSRlTVEE- 94
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISIIPQDPVLFSG-TIRSn 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 95 LVGFGRYPYSKGRLTLDDKKVIDESLAFLNLTEFRhryLDE----LSGGQRQRTYVAMVLCQDTEYVMLDEPLNNLDMKH 170
Cdd:cd03244 98 LDPFGEYSDEELWQALERVGLKEFVESLPGGLDTV---VEEggenLSVGQRQLLCLARALLRKSKILVLDEATASVDPET 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1943291881 171 AVIMMKLLRKA-ADelgKTIIIVIHDINfASVYSDYILAMRNGQLYYHGSP 220
Cdd:cd03244 175 DALIQKTIREAfKD---CTVLTIAHRLD-TIIDSDRILVLDKGRVVEFDSP 221
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-223 |
7.59e-14 |
|
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: 70.60 E-value: 7.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 2 IEISKISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVI----------GRLLL-----PESGMV-------- 58
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgmdqyeptsGRIIYhvalcEKCGYVerpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 59 --SVNGMDVAATDSDV----------LAKNLSILRQ------ENQFVSRLTVEELVGFGrYPyskgrltldDKKVIDESL 120
Cdd:TIGR03269 81 pcPVCGGTLEPEEVDFwnlsdklrrrIRKRIAIMLQrtfalyGDDTVLDNVLEALEEIG-YE---------GKEAVGRAV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 121 AFLNLTEFRHRYLD---ELSGGQRQRTYVAMVLCQDTEYVMLDEPLNNLDMKHAVIMMKLLRKAADELGKTIIIVIHDIN 197
Cdd:TIGR03269 151 DLIEMVQLSHRITHiarDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPE 230
|
250 260
....*....|....*....|....*.
gi 1943291881 198 FASVYSDYILAMRNGQLYYHGSPKEI 223
Cdd:TIGR03269 231 VIEDLSDKAIWLENGEIKEEGTPDEV 256
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-195 |
8.02e-14 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 70.53 E-value: 8.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 2 IEISKISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVnGMDVaatdsdvlakNLSILR 81
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV----------KLAYVD 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 82 QenqfvsrltveelvgfgrypyskGRLTLDDKK----VIDESLAFLNL--TEFRHR-YL--------------DELSGGQ 140
Cdd:PRK11819 394 Q-----------------------SRDALDPNKtvweEISGGLDIIKVgnREIPSRaYVgrfnfkggdqqkkvGVLSGGE 450
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1943291881 141 RQRTYVAMVLCQDTEYVMLDEPLNNLDmkhaVIMMKLLRKAADELGKTIIIVIHD 195
Cdd:PRK11819 451 RNRLHLAKTLKQGGNVLLLDEPTNDLD----VETLRALEEALLEFPGCAVVISHD 501
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
2-227 |
1.03e-13 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 70.37 E-value: 1.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 2 IEISKISKHYQD--ITVLDNITTTIQRGGITSIIGPNGAGKSTLLsvigRLLL----PESGMVSVNGMDVAATDSDVLAK 75
Cdd:TIGR03797 452 IEVDRVTFRYRPdgPLILDDVSLQIEPGEFVAIVGPSGSGKSTLL----RLLLgfetPESGSVFYDGQDLAGLDVQAVRR 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 76 NLSILRQENQFVSRLTVEELVGfgrypysKGRLTLDDKKvidESLAFLNLTE-FR------HRYLDE----LSGGQRQRT 144
Cdd:TIGR03797 528 QLGVVLQNGRLMSGSIFENIAG-------GAPLTLDEAW---EAARMAGLAEdIRampmgmHTVISEgggtLSGGQRQRL 597
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 145 YVAMVLCQDTEYVMLDEPLNNLDMKHAVIMMKLLrkaaDELGKTIIIVIHDINfASVYSDYILAMRNGQLYYHGSPKEIM 224
Cdd:TIGR03797 598 LIARALVRKPRILLFDEATSALDNRTQAIVSESL----ERLKVTRIVIAHRLS-TIRNADRIYVLDAGRVVQQGTYDELM 672
|
...
gi 1943291881 225 KAD 227
Cdd:TIGR03797 673 ARE 675
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
13-225 |
1.52e-13 |
|
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: 67.17 E-value: 1.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 13 DITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIgrlllpesgmvsVNGMDVAATDSDVLAKNLSILRqenqfvsrLTV 92
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTI------------MGHPKYEVTEGEILFKGEDITD--------LPP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 93 EELVGFG-----RYPYSKGRLTLDDkkvideslaFLnltefrhRYLDE-LSGGQRQRTYVAMVLCQDTEYVMLDEPLNNL 166
Cdd:cd03217 72 EERARLGiflafQYPPEIPGVKNAD---------FL-------RYVNEgFSGGEKKRNEILQLLLLEPDLAILDEPDSGL 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 167 DMKHAVIMMKLLRKAADElGKTIIIVIHDIN-FASVYSDYILAMRNGQLYYHGsPKEIMK 225
Cdd:cd03217 136 DIDALRLVAEVINKLREE-GKSVLIITHYQRlLDYIKPDRVHVLYDGRIVKSG-DKELAL 193
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
4-213 |
2.02e-13 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 68.99 E-value: 2.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 4 ISKISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDS-DVLAKNLSILRQ 82
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSkEALENGISMVHQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 83 ENQFVSRLTVEELVGFGRYPySKGrLTLDDKKVIDESLAF---LNLTEFRHRYLDELSGGQRQRTYVAMVLCQDTEYVML 159
Cdd:PRK10982 81 ELNLVLQRSVMDNMWLGRYP-TKG-MFVDQDKMYRDTKAIfdeLDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIM 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1943291881 160 DEPLNNLDMKHAVIMMKLLRKAADElGKTIIIVIHDINFASVYSDYILAMRNGQ 213
Cdd:PRK10982 159 DEPTSSLTEKEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-236 |
2.09e-13 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 67.88 E-value: 2.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 2 IEISKISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRL--LLPE---SGMVSVNGMDVAATDSDVLAKN 76
Cdd:PRK14243 11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLndLIPGfrvEGKVTFHGKNLYAPDVDPVEVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 77 LSI---LRQENQFVSrlTVEELVGFG-RYPYSKGrltlDDKKVIDESLAFLNLTEFRHRYLDE----LSGGQRQRTYVAM 148
Cdd:PRK14243 91 RRIgmvFQKPNPFPK--SIYDNIAYGaRINGYKG----DMDELVERSLRQAALWDEVKDKLKQsglsLSGGQQQRLCIAR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 149 VLCQDTEYVMLDEPLNNLDMKHAVIMMKLLRkaadELGK--TIIIVIHDINFASVYSDYIlAMRNGQLYYHGSPK-EIMK 225
Cdd:PRK14243 165 AIAVQPEVILMDEPCSALDPISTLRIEELMH----ELKEqyTIIIVTHNMQQAARVSDMT-AFFNVELTEGGGRYgYLVE 239
|
250
....*....|.
gi 1943291881 226 ADIIEDIFDTP 236
Cdd:PRK14243 240 FDRTEKIFNSP 250
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
18-172 |
2.89e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 66.37 E-value: 2.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 18 DNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDsDVLAKNLSILRQENQFVSRLTVEELVG 97
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQR-DEYHQDLLYLGHQPGIKTELTALENLR 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1943291881 98 FgrypYSKGRLTLDDKKVIDeSLAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQDTEYVMLDEPLNNLDmKHAV 172
Cdd:PRK13538 97 F----YQRLHGPGDDEALWE-ALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAID-KQGV 165
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
12-226 |
3.46e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 68.73 E-value: 3.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 12 QDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGM--------------DVAATDSDVLAKNL 77
Cdd:PRK10261 27 QKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMllrrrsrqvielseQSAAQMRHVRGADM 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 78 SILRQE--NQFVSRLTVEELV--------GFGRYPYSKGRLTLDDKKVIDESLAFLNltefrhRYLDELSGGQRQRTYVA 147
Cdd:PRK10261 107 AMIFQEpmTSLNPVFTVGEQIaesirlhqGASREEAMVEAKRMLDQVRIPEAQTILS------RYPHQLSGGMRQRVMIA 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1943291881 148 MVLCQDTEYVMLDEPLNNLDMKHAVIMMKLLRKAADELGKTIIIVIHDINFASVYSDYILAMRNGQLYYHGSPKEIMKA 226
Cdd:PRK10261 181 MALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHA 259
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-223 |
3.70e-13 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 67.95 E-value: 3.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 1 MIEISKISKHYQ-DITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVaaTDSDVLAKNLSI 79
Cdd:PRK11650 3 GLKLQAVRKSYDgKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVV--NELEPADRDIAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 80 LRQENQFVSRLTVEELVGFGRypysKGRLTldDKKVIDESLA----FLNLTEFRHRYLDELSGGQRQRtyVAM--VLCQD 153
Cdd:PRK11650 81 VFQNYALYPHMSVRENMAYGL----KIRGM--PKAEIEERVAeaarILELEPLLDRKPRELSGGQRQR--VAMgrAIVRE 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 154 TEYVMLDEPLNNLDMKHAVIMMKLLRKAADELGKTIIIVIHDINFASVYSDYILAMRNGQLYYHGSPKEI 223
Cdd:PRK11650 153 PAVFLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEV 222
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-213 |
3.79e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 68.42 E-value: 3.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 1 MIEISKISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRlLLPE---SGMVSVNGMDVAATD-SDVLAKN 76
Cdd:PRK13549 5 LLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG-VYPHgtyEGEIIFEGEELQASNiRDTERAG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 77 LSILRQENQFVSRLTVEELVGFGRYPYSKGRltLDDKKVIDES---LAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQD 153
Cdd:PRK13549 84 IAIIHQELALVKELSVLENIFLGNEITPGGI--MDYDAMYLRAqklLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 154 TEYVMLDEPLNNLDMKHAVIMMKLLRKAADElGKTIIIVIHDINFASVYSDYILAMRNGQ 213
Cdd:PRK13549 162 ARLLILDEPTASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
3-214 |
3.96e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 68.44 E-value: 3.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 3 EISKISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNgmdvaatdsdvlaknlsilrq 82
Cdd:PRK11147 321 EMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCG--------------------- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 83 enqfvsrlTVEELVGFGRYpyskgRLTLD-DKKVIDeslaflNLTE----------FRH--RYLDE-------------- 135
Cdd:PRK11147 380 --------TKLEVAYFDQH-----RAELDpEKTVMD------NLAEgkqevmvngrPRHvlGYLQDflfhpkramtpvka 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 136 LSGGQRQRTYVAMVLCQDTEYVMLDEPLNNLDmkhaVIMMKLLRKAADELGKTIIIVIHDINFA--SVYSDYILAmRNGQ 213
Cdd:PRK11147 441 LSGGERNRLLLARLFLKPSNLLILDEPTNDLD----VETLELLEELLDSYQGTVLLVSHDRQFVdnTVTECWIFE-GNGK 515
|
.
gi 1943291881 214 L 214
Cdd:PRK11147 516 I 516
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-219 |
5.84e-13 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 66.59 E-value: 5.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 1 MIEISKISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIgrlllpeSGMVSVNgmdvaATDSDVLAKNLSIL 80
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVI-------AGHPAYK-----ILEGDILFKGESIL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 81 RQENQFVSRLTV-------EELVG-----FGRYPYSKGRLTLDDK--------KVIDESLAFLNLTE-FRHRYLDE-LSG 138
Cdd:CHL00131 75 DLEPEERAHLGIflafqypIEIPGvsnadFLRLAYNSKRKFQGLPeldpleflEIINEKLKLVGMDPsFLSRNVNEgFSG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 139 GQRQRTYVAMVLCQDTEYVMLDEPLNNLDMKHAVIMMKLLRKAADElGKTIIIVIHDINFAS-VYSDYILAMRNGQLYYH 217
Cdd:CHL00131 155 GEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTS-ENSIILITHYQRLLDyIKPDYVHVMQNGKIIKT 233
|
..
gi 1943291881 218 GS 219
Cdd:CHL00131 234 GD 235
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-221 |
6.61e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 66.29 E-value: 6.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 1 MIEISKISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGmvsvngmdvaatdsdvlaknlSIL 80
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEG---------------------VIK 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 81 RQENQfvsrltveelvgfgRYPYSKGRLTLD-----------------DKKVIDESLAFLNLTEFRHRYLDELSGGQRQR 143
Cdd:PRK09544 63 RNGKL--------------RIGYVPQKLYLDttlpltvnrflrlrpgtKKEDILPALKRVQAGHLIDAPMQKLSGGETQR 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1943291881 144 TYVAMVLCQDTEYVMLDEPLNNLDMKHAVIMMKLLRKAADELGKTIIIVIHDINFASVYSDYILAMrNGQLYYHGSPK 221
Cdd:PRK09544 129 VLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCL-NHHICCSGTPE 205
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-166 |
9.30e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 67.34 E-value: 9.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 1 MIEISKISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVA-ATDSDVLAKNLSI 79
Cdd:PRK10762 4 LLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfNGPKSSQEAGIGI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 80 LRQENQFVSRLTVEELVGFGRYPYSK-GRltLDDKKVIDES---LAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQDTE 155
Cdd:PRK10762 84 IHQELNLIPQLTIAENIFLGREFVNRfGR--IDWKKMYAEAdklLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESK 161
|
170
....*....|.
gi 1943291881 156 YVMLDEPLNNL 166
Cdd:PRK10762 162 VIIMDEPTDAL 172
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
13-225 |
1.22e-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: 65.36 E-value: 1.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 13 DITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVI-GRlllP----ESGMVSVNGMDVAATDSDVLAKN-LSILRQENQF 86
Cdd:TIGR01978 12 DKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIaGH---PsyevTSGTILFKGQDLLELEPDERARAgLFLAFQYPEE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 87 VSRLTVEELVGFG----RYPYSKGRLTLDD-KKVIDESLAFLNLTE-FRHRYLDE-LSGGQRQRTYVAMVLCQDTEYVML 159
Cdd:TIGR01978 89 IPGVSNLEFLRSAlnarRSARGEEPLDLLDfEKLLKEKLALLDMDEeFLNRSVNEgFSGGEKKRNEILQMALLEPKLAIL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1943291881 160 DEPLNNLDMKHAVIMMKLLRKAADElGKTIIIVIHDIN-FASVYSDYILAMRNGQLYYHGSPkEIMK 225
Cdd:TIGR01978 169 DEIDSGLDIDALKIVAEGINRLREP-DRSFLIITHYQRlLNYIKPDYVHVLLDGRIVKSGDV-ELAK 233
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
10-218 |
1.63e-12 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 66.66 E-value: 1.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 10 HY--QDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVLAKNLSILRQeNQFV 87
Cdd:PRK10789 322 TYpqTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQ-TPFL 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 88 SRLTVEELVGFGRyPYSKgrltlddKKVIDESLAFLNLTEFRHR----YLDE-------LSGGQRQRTYVAMVLCQDTEY 156
Cdd:PRK10789 401 FSDTVANNIALGR-PDAT-------QQEIEHVARLASVHDDILRlpqgYDTEvgergvmLSGGQKQRISIARALLLNAEI 472
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1943291881 157 VMLDEPLNNLDMKHAVIMMKLLRKAADelGKTIIIVIHDINfASVYSDYILAMRNGQLYYHG 218
Cdd:PRK10789 473 LILDDALSAVDGRTEHQILHNLRQWGE--GRTVIISAHRLS-ALTEASEILVMQHGHIAQRG 531
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
12-226 |
1.76e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 66.27 E-value: 1.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 12 QDITVLDNITTTIQRGGITSIIGPNGAGKS-TLLSVIGrlLLPESGMVSVNGmDVAATDSDVLAKNLSILRQ-------- 82
Cdd:PRK15134 20 TVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILR--LLPSPPVVYPSG-DIRFHGESLLHASEQTLRGvrgnkiam 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 83 ---------------ENQFVSRLTVEElvGFGRYPYSKGRLTLDDKKVIDEslAFLNLTEFRHryldELSGGQRQRTYVA 147
Cdd:PRK15134 97 ifqepmvslnplhtlEKQLYEVLSLHR--GMRREAARGEILNCLDRVGIRQ--AAKRLTDYPH----QLSGGERQRVMIA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1943291881 148 MVLCQDTEYVMLDEPLNNLDMKHAVIMMKLLRKAADELGKTIIIVIHDINFASVYSDYILAMRNGQLYYHGSPKEIMKA 226
Cdd:PRK15134 169 MALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSA 247
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
17-223 |
3.43e-12 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 64.99 E-value: 3.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 17 LDNITTTIQRGGITSIIGPNGAGKSTLlsviGRLLL----PESGMVSVNGMDVAATDSDVLAKnlsiLRQENQFVsrltv 92
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTL----ARLLTmietPTGGELYYQGQDLLKADPEAQKL----LRQKIQIV----- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 93 eelvgFgRYPYS------KGRLTLDDKKVIDESL-------------AFLNL-TEFRHRYLDELSGGQRQRTYVAMVLCQ 152
Cdd:PRK11308 98 -----F-QNPYGslnprkKVGQILEEPLLINTSLsaaerrekalammAKVGLrPEHYDRYPHMFSGGQRQRIAIARALML 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1943291881 153 DTEYVMLDEPLNNLDMKHAVIMMKLLRKAADELGKTIIIVIHDINFASVYSDYILAMRNGQLYYHGSPKEI 223
Cdd:PRK11308 172 DPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQI 242
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
4-218 |
3.68e-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: 63.44 E-value: 3.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 4 ISKISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPE---SGMVSVNGMDVAAT----DSDVLAKN 76
Cdd:cd03233 10 SFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFaekyPGEIIYVS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 77 lsilrQENQFVSRLTVEELVGFGRYpySKGrltlddkkvideslaflnltefrHRYLDELSGGQRQRTYVAMVLCQDTEY 156
Cdd:cd03233 90 -----EEDVHFPTLTVRETLDFALR--CKG-----------------------NEFVRGISGGERKRVSIAEALVSRASV 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1943291881 157 VMLDEPLNNLDMKHAVIMMKLLRKAADELGKTIIIVIH---DINFASVysDYILAMRNGQLYYHG 218
Cdd:cd03233 140 LCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSLYqasDEIYDLF--DKVLVLYEGRQIYYG 202
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-207 |
4.29e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 63.43 E-value: 4.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 1 MIEISKISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVaatDSDVLA--KNLS 78
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI---KKDLCTyqKQLC 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 79 ILRQENQFVSRLTVEELVGFGRYpYSKGRLTlddkkvIDESLAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQDTEYVM 158
Cdd:PRK13540 78 FVGHRSGINPYLTLRENCLYDIH-FSPGAVG------ITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1943291881 159 LDEPLNNLDMKHAVIMMKLLRKAADELGKTIIIVIHDINF-ASVYSDYIL 207
Cdd:PRK13540 151 LDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSHQDLPLnKADYEEYHL 200
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2-230 |
6.71e-12 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 64.61 E-value: 6.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 2 IEISKISKHYQDITV-LDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAAtdsdvlaKNLSIL 80
Cdd:PRK10522 323 LELRNVTFAYQDNGFsVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTA-------EQPEDY 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 81 RQenQFVSRLTVEELvgFGRYPYSKGrlTLDDKKVIDESLAFLN----LTEFRHRYLD-ELSGGQRQRTYVAMVLCQDTE 155
Cdd:PRK10522 396 RK--LFSAVFTDFHL--FDQLLGPEG--KPANPALVEKWLERLKmahkLELEDGRISNlKLSKGQKKRLALLLALAEERD 469
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1943291881 156 YVMLDEPLNNLDMKHAVIMMKLLRKAADELGKTIIIVIHDINFASvYSDYILAMRNGQLY-YHGSPKEIMKADIIE 230
Cdd:PRK10522 470 ILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHDDHYFI-HADRLLEMRNGQLSeLTGEERDAASRDAVA 544
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
17-219 |
8.63e-12 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 64.60 E-value: 8.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 17 LDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVLAKNLSILRQENQFVSRLTVEELv 96
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNI- 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 97 gfgrypySKGRLTLDDKKVID--ESLAFLNLTEFRHRYLD--------ELSGGQRQRTYVAMVLCQDTEYVMLDEPLNNL 166
Cdd:PRK13657 430 -------RVGRPDATDEEMRAaaERAQAHDFIERKPDGYDtvvgergrQLSGGERQRLAIARALLKDPPILILDEATSAL 502
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1943291881 167 DmkhAVIMMKlLRKAADEL--GKTIIIVIHdiNFASVYS-DYILAMRNGQLYYHGS 219
Cdd:PRK13657 503 D---VETEAK-VKAALDELmkGRTTFIIAH--RLSTVRNaDRILVFDNGRVVESGS 552
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
13-223 |
9.60e-12 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 63.59 E-value: 9.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 13 DITVLDNITTTIQRGGITSIIGPNGAGKS-TLLSVIGrlLLPESGMVS----VNGMDVAatdsDVLAKNLSILRQENqfV 87
Cdd:PRK09473 28 DVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMG--LLAANGRIGgsatFNGREIL----NLPEKELNKLRAEQ--I 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 88 SRLTVEELVGFGRYPYSKGRLT--------LDDKKVIDESLAFLN---LTEFRHR---YLDELSGGQRQRTYVAMVLCQD 153
Cdd:PRK09473 100 SMIFQDPMTSLNPYMRVGEQLMevlmlhkgMSKAEAFEESVRMLDavkMPEARKRmkmYPHEFSGGMRQRVMIAMALLCR 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 154 TEYVMLDEPLNNLDMKHAVIMMKLLRKAADELGKTIIIVIHDINFASVYSDYILAMRNGQLYYHGSPKEI 223
Cdd:PRK09473 180 PKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDV 249
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
17-227 |
1.31e-11 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 64.20 E-value: 1.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 17 LDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGmDVAATDSDVLAKNLSIlrQENqfvsrltveelV 96
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-SVAYVPQQAWIQNDSL--REN-----------I 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 97 GFGRY---PYSKGRLT----LDDKKVIDESlaflNLTEFRHRYLDeLSGGQRQRTYVAMVLCQDTEYVMLDEPLNNLDM- 168
Cdd:TIGR00957 720 LFGKAlneKYYQQVLEacalLPDLEILPSG----DRTEIGEKGVN-LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAh 794
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1943291881 169 --KHavIMMKLLRKAADELGKTIIIVIHDINFASvYSDYILAMRNGQLYYHGSPKEIMKAD 227
Cdd:TIGR00957 795 vgKH--IFEHVIGPEGVLKNKTRILVTHGISYLP-QVDVIIVMSGGKISEMGSYQELLQRD 852
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
6-218 |
1.69e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 63.97 E-value: 1.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 6 KISKhyQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVI-GRLL--LPESGMVSVNGMDVAATdsdvLAKNLSILRQ 82
Cdd:TIGR00956 770 KIKK--EKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLaERVTtgVITGGDRLVNGRPLDSS----FQRSIGYVQQ 843
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 83 ENQFVSRLTVEELVGFGRYPYSKGRLTLDDK-KVIDESLAFLNLTEfrhrYLDELSG--------GQRQRTYVAMVLCQD 153
Cdd:TIGR00956 844 QDLHLPTSTVRESLRFSAYLRQPKSVSKSEKmEYVEEVIKLLEMES----YADAVVGvpgeglnvEQRKRLTIGVELVAK 919
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1943291881 154 TE-YVMLDEPLNNLDMKHAVIMMKLLRKAADElGKTIIIVIHD---INFASvYSDYILAMRNGQLYYHG 218
Cdd:TIGR00956 920 PKlLLFLDEPTSGLDSQTAWSICKLMRKLADH-GQAILCTIHQpsaILFEE-FDRLLLLQKGGQTVYFG 986
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
18-236 |
1.80e-11 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 62.41 E-value: 1.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 18 DNITTTIQRGGITSIIGPNGAGKS-TLLSVIGrlLLPE-----SGMVSVNGMDVAAtdSDVLAKNLSILRQ--ENQFVSR 89
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSlTCAAALG--ILPAgvrqtAGRVLLDGKPVAP--CALRGRKIATIMQnpRSAFNPL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 90 LT-----VEELVGFGRypyskgrltLDDKKVIDESLAFLNLTEfRHRYLD----ELSGGQRQRTYVAMVLCQDTEYVMLD 160
Cdd:PRK10418 96 HTmhthaRETCLALGK---------PADDATLTAALEAVGLEN-AARVLKlypfEMSGGMLQRMMIALALLCEAPFIIAD 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1943291881 161 EPLNNLDMKHAVIMMKLLRKAADELGKTIIIVIHDINFASVYSDYILAMRNGQLYYHGSpkeimkadiIEDIFDTP 236
Cdd:PRK10418 166 EPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGD---------VETLFNAP 232
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2-162 |
2.11e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 63.22 E-value: 2.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 2 IEISKISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIG--RLLlpESGMVSVNGMDVAATD--SDV----- 72
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAgaRKI--QQGRVEVLGGDMADARhrRAVcpria 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 73 -----LAKNL----SIlrQEN-QFVSRLtveelvgFG-RYPYSKGRltlddkkvIDESLAFLNLTEFRHRYLDELSGGQR 141
Cdd:NF033858 80 ympqgLGKNLyptlSV--FENlDFFGRL-------FGqDAAERRRR--------IDELLRATGLAPFADRPAGKLSGGMK 142
|
170 180
....*....|....*....|....*
gi 1943291881 142 QRtyvaMVLC----QDTEYVMLDEP 162
Cdd:NF033858 143 QK----LGLCcaliHDPDLLILDEP 163
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-215 |
2.85e-11 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 61.43 E-value: 2.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 1 MIEISKISKHY-QDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSD---VLAKN 76
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNRevpFLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 77 LSILRQENQFVSRLTVEELVGFgryPYSKGRLTLDD-KKVIDESLAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQDTE 155
Cdd:PRK10908 81 IGMIFQDHHLLMDRTVYDNVAI---PLIIAGASGDDiRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 156 YVMLDEPLNNLDMKHAVIMMKLLRKaADELGKTIIIVIHDINFASVYSDYILAMRNGQLY 215
Cdd:PRK10908 158 VLLADEPTGNLDDALSEGILRLFEE-FNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
32-227 |
2.98e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 63.07 E-value: 2.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 32 IIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVLAKNLSILRQenqfvSRLTVEELVGFGRYPYSKG----- 106
Cdd:PLN03232 1267 VVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQ-----SPVLFSGTVRFNIDPFSEHndadl 1341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 107 -----RLTLDDkkVIDESLAFLNLTEFRHRylDELSGGQRQRTYVAMVLCQDTEYVMLDEPLNNLDMKHAVIMMKLLRKA 181
Cdd:PLN03232 1342 wealeRAHIKD--VIDRNPFGLDAEVSEGG--ENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREE 1417
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1943291881 182 ADELgkTIIIVIHDINfASVYSDYILAMRNGQLYYHGSPKEIMKAD 227
Cdd:PLN03232 1418 FKSC--TMLVIAHRLN-TIIDCDKILVLSSGQVLEYDSPQELLSRD 1460
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
15-226 |
3.29e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 62.80 E-value: 3.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 15 TVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLlPESGMVSVNGMDVAATDSdvlaKNLSILRQENQFV------- 87
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNR----RQLLPVRHRIQVVfqdpnss 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 88 --SRLTVEELVGFG-RYPYSKGRLTLDDKKVIdESLAFLNL-TEFRHRYLDELSGGQRQRTYVAMVLCQDTEYVMLDEPL 163
Cdd:PRK15134 375 lnPRLNVLQIIEEGlRVHQPTLSAAQREQQVI-AVMEEVGLdPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPT 453
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1943291881 164 NNLDMKHAVIMMKLLRKAADELGKTIIIVIHDINFASVYSDYILAMRNGQLYYHGSPKEIMKA 226
Cdd:PRK15134 454 SSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAA 516
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
23-214 |
3.79e-11 |
|
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: 62.51 E-value: 3.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 23 TIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATdsdvlakNLSILRQenQFVsrlTV-------EEL 95
Cdd:COG4615 354 TIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTAD-------NREAYRQ--LFS---AVfsdfhlfDRL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 96 VGFGRYPyskgrltlDDKKViDESLAFLNL---TEFRHRYLD--ELSGGQRQRtyVAMVLC--QDTEYVMLDEplnnldm 168
Cdd:COG4615 422 LGLDGEA--------DPARA-RELLERLELdhkVSVEDGRFSttDLSQGQRKR--LALLVAllEDRPILVFDE------- 483
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1943291881 169 khavimmkllrKAAD-----------EL-------GKTIIIVIHDINFASVySDYILAMRNGQL 214
Cdd:COG4615 484 -----------WAADqdpefrrvfytELlpelkarGKTVIAISHDDRYFDL-ADRVLKMDYGKL 535
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-195 |
1.04e-10 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 61.34 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 1 MIEISKISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSvngmdvaatdsdvLAK----- 75
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIG-------------LAKgiklg 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 76 -----NLSILRQEN---QFVSRLTVEE--------LVGFGrypyskgrltLDDKKVIDESLAFlnltefrhryldelSGG 139
Cdd:PRK10636 379 yfaqhQLEFLRADEsplQHLARLAPQEleqklrdyLGGFG----------FQGDKVTEETRRF--------------SGG 434
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1943291881 140 QRQRTYVAMVLCQDTEYVMLDEPLNNLDMKhaviMMKLLRKAADELGKTIIIVIHD 195
Cdd:PRK10636 435 EKARLVLALIVWQRPNLLLLDEPTNHLDLD----MRQALTEALIDFEGALVVVSHD 486
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
15-226 |
1.10e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 60.49 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 15 TVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGM-----VSVNGMDVAaTDSDVLA--KNLSILRQE-NQF 86
Cdd:PRK14271 35 TVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYrysgdVLLGGRSIF-NYRDVLEfrRRVGMLFQRpNPF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 87 VSRLTVEELVGFGRYPY---------SKGRLTldDKKVIDESLAFLNLTEFRhryldeLSGGQRQRTYVAMVLCQDTEYV 157
Cdd:PRK14271 114 PMSIMDNVLAGVRAHKLvprkefrgvAQARLT--EVGLWDAVKDRLSDSPFR------LSGGQQQLLCLARTLAVNPEVL 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1943291881 158 MLDEPLNNLDMKHAVIMMKLLRKAADELgkTIIIVIHDINFASVYSDYILAMRNGQLYYHGSPKEIMKA 226
Cdd:PRK14271 186 LLDEPTSALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSS 252
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
12-226 |
1.50e-10 |
|
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: 60.47 E-value: 1.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 12 QDITVLDNITTTIQRGGITSIIGPNGAGKS-TLLSVIGrlLLPE-----SGMVSVNGMDVAATDSDVLAKnlsiLR---- 81
Cdd:COG4172 21 GTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILR--LLPDpaahpSGSILFDGQDLLGLSERELRR----IRgnri 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 82 ----QE-----NQFvsrLTVEELVG------FGrypyskgrltLDDKKVIDESLAFLNLT-----EFR-HRYLDELSGGQ 140
Cdd:COG4172 95 amifQEpmtslNPL---HTIGKQIAevlrlhRG----------LSGAAARARALELLERVgipdpERRlDAYPHQLSGGQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 141 RQRTYVAMVLCQDTEYVMLDEPLNNLDMKHAVIMMKLLRKAADELGKTIIIVIHDINFASVYSDYILAMRNGQLYYHGSP 220
Cdd:COG4172 162 RQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPT 241
|
....*.
gi 1943291881 221 KEIMKA 226
Cdd:COG4172 242 AELFAA 247
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
34-168 |
1.69e-10 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 59.09 E-value: 1.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 34 GPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVLAKNLSILRQENQFVSRL-TVEELVGF-GRYPyskgrltld 111
Cdd:PRK13543 44 GDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAYLGHLPGLKADLSTLeNLHFLCGLhGRRA--------- 114
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1943291881 112 dKKVIDESLAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQDTEYVMLDEPLNNLDM 168
Cdd:PRK13543 115 -KQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
15-193 |
1.89e-10 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 60.21 E-value: 1.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 15 TVLDNITTTIQRGGITSIIGPNGAGKSTLLSVI--------GRLLLPEsgmvsvngmdvaatDSDVLaknlsilrqenqF 86
Cdd:COG4178 377 PLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIaglwpygsGRIARPA--------------GARVL------------F 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 87 VSRL------TVEELVgfgRYPYSKGRLTLDDkkvIDESLAFLNLTEFRHRyLDE-------LSGGQRQRTYVAMVLCQD 153
Cdd:COG4178 431 LPQRpylplgTLREAL---LYPATAEAFSDAE---LREALEAVGLGHLAER-LDEeadwdqvLSLGEQQRLAFARLLLHK 503
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1943291881 154 TEYVMLDEPLNNLDMKHAVIMMKLLRkaaDELGKTIIIVI 193
Cdd:COG4178 504 PDWLFLDEATSALDEENEAALYQLLR---EELPGTTVISV 540
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
19-214 |
1.94e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 60.18 E-value: 1.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 19 NITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVA-ATDSDVLAKNLSIL---RQENQFVSRLTVEE 94
Cdd:PRK09700 281 DISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISpRSPLDAVKKGMAYItesRRDNGFFPNFSIAQ 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 95 LVGFGRYPYS---KGRLTL----DDKKVIDESLAFLNLT-EFRHRYLDELSGGQRQRTYVAMVLCQDTEYVMLDEPLNNL 166
Cdd:PRK09700 361 NMAISRSLKDggyKGAMGLfhevDEQRTAENQRELLALKcHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGI 440
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1943291881 167 DMKHAVIMMKLLRKAADElGKTIIIVIHDINFASVYSDYILAMRNGQL 214
Cdd:PRK09700 441 DVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
16-218 |
2.04e-10 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 60.63 E-value: 2.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 16 VLDNITTTIQRGGITSIIGPNGAGKSTLLSVI-GRLLLPE-SGMVSVNGMdvaATDSDVLAKNLSILRQENQFVSRLTVE 93
Cdd:PLN03140 895 LLREVTGAFRPGVLTALMGVSGAGKTTLMDVLaGRKTGGYiEGDIRISGF---PKKQETFARISGYCEQNDIHSPQVTVR 971
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 94 ELV---GFGRYPYSKGRltlDDKKV-IDESLAFLNLTEFRHRY-----LDELSGGQRQRTYVAMVLCQDTEYVMLDEPLN 164
Cdd:PLN03140 972 ESLiysAFLRLPKEVSK---EEKMMfVDEVMELVELDNLKDAIvglpgVTGLSTEQRKRLTIAVELVANPSIIFMDEPTS 1048
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1943291881 165 NLDMKHAVIMMKLLRKAADElGKTIIIVIH--DINFASVYSDYILAMRNGQLYYHG 218
Cdd:PLN03140 1049 GLDARAAAIVMRTVRNTVDT-GRTVVCTIHqpSIDIFEAFDELLLMKRGGQVIYSG 1103
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
19-213 |
2.42e-10 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 59.89 E-value: 2.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 19 NITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVlakNLSILRQENQFV---SRL----T 91
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGI---CLPPEKRRIGYVfqdARLfphyK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 92 VEelvGFGRYPYSKGRLTLDDKKVideslAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQDTEYVMLDEPLNNLDM--K 169
Cdd:PRK11144 93 VR---GNLRYGMAKSMVAQFDKIV-----ALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLprK 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1943291881 170 HAVimMKLLRKAADELGKTIIIVIHDINFASVYSDYILAMRNGQ 213
Cdd:PRK11144 165 REL--LPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGK 206
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
18-209 |
2.77e-10 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 59.33 E-value: 2.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 18 DNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDsdvlAKNLSILRQENQFV---------S 88
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMK----DDEWRAVRSDIQMIfqdplaslnP 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 89 RLTVEELVGfgrYPYSKGRLTLDDKKVIDESLAFLN----LTEFRHRYLDELSGGQRQRTYVAMVLCQDTEYVMLDEPLN 164
Cdd:PRK15079 114 RMTIGEIIA---EPLRTYHPKLSRQEVKDRVKAMMLkvglLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVS 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1943291881 165 NLDMKHAVIMMKLLRKAADELGKTIIIVIHDINFASVYSDYILAM 209
Cdd:PRK15079 191 ALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVM 235
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-219 |
3.57e-10 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 59.52 E-value: 3.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 2 IEISKISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSvngmdvaatdsdvLAKNLSI-- 79
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVK-------------WSENANIgy 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 80 LRQ--ENQFVSRLTVEELVgfgrypySKGRLTLDDKKVIDESLAFLNLTEfrhrylDE-------LSGGQRQRTYVAMVL 150
Cdd:PRK15064 387 YAQdhAYDFENDLTLFDWM-------SQWRQEGDDEQAVRGTLGRLLFSQ------DDikksvkvLSGGEKGRMLFGKLM 453
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 151 CQDTEYVMLDEPLNNLDMKHavimMKLLRKAADELGKTIIIVIHDINFASVYSDYILAMRNGQL-YYHGS 219
Cdd:PRK15064 454 MQKPNVLVMDEPTNHMDMES----IESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVvDFSGT 519
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
10-226 |
1.78e-09 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 56.72 E-value: 1.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 10 HYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVLAKNLSILRQE--NQFV 87
Cdd:PRK15112 22 RRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDpsTSLN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 88 SRLTVEELVGFgryPYskgRLTLD-----DKKVIDESLAFLNL-TEFRHRYLDELSGGQRQRTYVAMVLCQDTEYVMLDE 161
Cdd:PRK15112 102 PRQRISQILDF---PL---RLNTDlepeqREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1943291881 162 PLNNLDMKHAVIMMKLLRKAADELGKTIIIVIHDINFASVYSDYILAMRNGQLYYHGSPKEIMKA 226
Cdd:PRK15112 176 ALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLAS 240
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
12-194 |
3.54e-09 |
|
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: 54.47 E-value: 3.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 12 QDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVngmdvaATDSDVLaknlsILRQEnQFVSRLT 91
Cdd:cd03223 12 DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM------PEGEDLL-----FLPQR-PYLPLGT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 92 VEELVgfgRYPYSkgrltlddkkvideslaflnltefrhrylDELSGGQRQRTYVAMVLCQDTEYVMLDEPLNNLDMKHA 171
Cdd:cd03223 80 LREQL---IYPWD-----------------------------DVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESE 127
|
170 180
....*....|....*....|...
gi 1943291881 172 VIMMKLLRkaadELGKTIIIVIH 194
Cdd:cd03223 128 DRLYQLLK----ELGITVISVGH 146
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
2-194 |
3.63e-09 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 56.49 E-value: 3.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 2 IEISKISKHY--QDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVLAKNLSI 79
Cdd:TIGR03796 478 VELRNITFGYspLEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAM 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 80 LRQEnQFVSRLTVEElvgfgrypyskgRLTLDDKKVIDESL-----------AFLNLTEFRHRYLDE----LSGGQRQRT 144
Cdd:TIGR03796 558 VDQD-IFLFEGTVRD------------NLTLWDPTIPDADLvrackdaaihdVITSRPGGYDAELAEgganLSGGQRQRL 624
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1943291881 145 YVAMVLCQDTEYVMLDEPLNNLDMKHAVIMMKLLRKAadelGKTIIIVIH 194
Cdd:TIGR03796 625 EIARALVRNPSILILDEATSALDPETEKIIDDNLRRR----GCTCIIVAH 670
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
26-213 |
1.21e-08 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 53.38 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 26 RGGITSIIGPNGAGKSTLLSVIGRLLLPEsgmvsvngmdvAATDSDVLAKNLSILR-QENQFVSRLTVEELVGfgrypys 104
Cdd:cd03240 21 FSPLTLIVGQNGAGKTTIIEALKYALTGE-----------LPPNSKGGAHDPKLIReGEVRAQVKLAFENANG------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 105 kgrltldDKKVIDESLAFLNLTEFRH---------RYLDELSGGQRQ------RTYVAMVLCQDTEYVMLDEPLNNLDMK 169
Cdd:cd03240 83 -------KKYTITRSLAILENVIFCHqgesnwpllDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEE 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1943291881 170 H-AVIMMKLLRKAADELGKTIIIVIHDINFASVYSDYILAMRNGQ 213
Cdd:cd03240 156 NiEESLAEIIEERKSQKNFQLIVITHDEELVDAADHIYRVEKDGR 200
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
16-214 |
1.24e-08 |
|
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: 53.20 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 16 VLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATD-SDVLAKNLSIL---RQENQFVSRLT 91
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSpRDAIRAGIAYVpedRKREGLVLDLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 92 VEELVGFGRYpyskgrltlddkkvideslaflnltefrhryldeLSGGQRQRTYVAMVLCQDTEYVMLDEPLNNLDMKHA 171
Cdd:cd03215 95 VAENIALSSL----------------------------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAK 140
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1943291881 172 VIMMKLLRKAADElGKTIIIVIHDINFASVYSDYILAMRNGQL 214
Cdd:cd03215 141 AEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
16-226 |
1.86e-08 |
|
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: 54.57 E-value: 1.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 16 VLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVLAKNLSILRQENQFVSRLTVEEL 95
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNL 1380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 96 VGFGRYPYSKGRLTLDDKKVIDESLAFLNLTEFRHRYLDE-LSGGQRQRTYVAMVLCQDTEYVMLDEPLNNLDMKHAVIM 174
Cdd:TIGR00957 1381 DPFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGEnLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLI 1460
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1943291881 175 MKLLRKAADELgkTIIIVIHDINFASVYSDyILAMRNGQLYYHGSPKEIMKA 226
Cdd:TIGR00957 1461 QSTIRTQFEDC--TVLTIAHRLNTIMDYTR-VIVLDKGEVAEFGAPSNLLQQ 1509
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
17-225 |
1.94e-08 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 53.67 E-value: 1.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 17 LDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGmdvaatDSDVLAKNLSILRQ----ENQFVSRLtv 92
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG------EVSVIAISAGLSGQltgiENIEFKML-- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 93 eeLVGFGRYpyskgrltlDDKKVIDESLAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQDTEYVMLDEPLNNLDMKHAv 172
Cdd:PRK13546 112 --CMGFKRK---------EIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFA- 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1943291881 173 imMKLLRKAAD--ELGKTIIIVIHDINFASVYSDYILAMRNGQLYYHGSPKEIMK 225
Cdd:PRK13546 180 --QKCLDKIYEfkEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLP 232
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
16-218 |
2.16e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 54.41 E-value: 2.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 16 VLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNG--------MDVAATDSDVLAKNLSILRQENQFV 87
Cdd:PRK10636 16 LLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGnwqlawvnQETPALPQPALEYVIDGDREYRQLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 88 SRLTVEELVGFGR-YPYSKGRL-TLDDKKVIDESLAFLNLTEFRHRYLDE----LSGGQRQRTYVAMVLCQDTEYVMLDE 161
Cdd:PRK10636 96 AQLHDANERNDGHaIATIHGKLdAIDAWTIRSRAASLLHGLGFSNEQLERpvsdFSGGWRMRLNLAQALICRSDLLLLDE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1943291881 162 PLNNLDMKhAVIMmklLRKAADELGKTIIIVIHDINFASVYSDYILAMRNGQLY-YHG 218
Cdd:PRK10636 176 PTNHLDLD-AVIW---LEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFeYTG 229
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
12-214 |
2.20e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 54.09 E-value: 2.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 12 QDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVaatdsDVL-AKNLSILRQENQFV--- 87
Cdd:PRK10261 335 REVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRI-----DTLsPGKLQALRRDIQFIfqd 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 88 --SRLTVEELVGFG-RYPYSKGRLTldDKKVIDESLAFLN-----LTEFRHRYLDELSGGQRQRTYVAMVLCQDTEYVML 159
Cdd:PRK10261 410 pyASLDPRQTVGDSiMEPLRVHGLL--PGKAAAARVAWLLervglLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIA 487
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1943291881 160 DEPLNNLDMKHAVIMMKLLRKAADELGKTIIIVIHDINFASVYSDYILAMRNGQL 214
Cdd:PRK10261 488 DEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQI 542
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
13-231 |
2.36e-08 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 53.15 E-value: 2.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 13 DITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVI-GR-LLLPESGMVSVNGMDVaaTDSDV---------LA------- 74
Cdd:COG0396 12 GKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmGHpKYEVTSGSILLDGEDI--LELSPderaragifLAfqypvei 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 75 ---KNLSILRQEnqfVSRLTVEELVGFgrypyskgrltlDDKKVIDESLAFLNL-TEFRHRYLDE-LSGGQRQRTYVAMV 149
Cdd:COG0396 90 pgvSVSNFLRTA---LNARRGEELSAR------------EFLKLLKEKMKELGLdEDFLDRYVNEgFSGGEKKRNEILQM 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 150 LCQDTEYVMLDEPLNNLDMKHAVIMMKLLRKAADElGKTIIIVIHD---INFasVYSDYILAMRNGQLYYHGsPKEImkA 226
Cdd:COG0396 155 LLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSP-DRGILIITHYqriLDY--IKPDFVHVLVDGRIVKSG-GKEL--A 228
|
....*
gi 1943291881 227 DIIED 231
Cdd:COG0396 229 LELEE 233
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
17-225 |
2.53e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 54.36 E-value: 2.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 17 LDNITTTIQRGGITSIIGPNGAGKSTLLS-VIGRLllpesgmvsvngmdVAATDSDVlaknlsILRQENQFVSRL----- 90
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGEL--------------PPRSDASV------VIRGTVAYVPQVswifn 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 91 -TVEELVGFGRyPYSKGRLtlddKKVID--------ESLAFLNLTEFRHRYLDeLSGGQRQRTYVAMVLCQDTEYVMLDE 161
Cdd:PLN03130 693 aTVRDNILFGS-PFDPERY----ERAIDvtalqhdlDLLPGGDLTEIGERGVN-ISGGQKQRVSMARAVYSNSDVYIFDD 766
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1943291881 162 PLNNLDMKHA-VIMMKLLRkaaDEL-GKTIIIVIHDINFASvYSDYILAMRNGQLYYHGSPKEIMK 225
Cdd:PLN03130 767 PLSALDAHVGrQVFDKCIK---DELrGKTRVLVTNQLHFLS-QVDRIILVHEGMIKEEGTYEELSN 828
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
16-223 |
3.12e-08 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 54.15 E-value: 3.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 16 VLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGmdvaatdsdvlakNLSILRQENqFVSRLTVEEL 95
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQTS-WIMPGTIKDN 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 96 VGFGrYPYSKGRLTLDDKKV-IDESLAFLnlTEFRHRYLDE----LSGGQRQRTYVAMVLCQDTEYVMLDEPLNNLD-MK 169
Cdd:TIGR01271 507 IIFG-LSYDEYRYTSVIKACqLEEDIALF--PEKDKTVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFTHLDvVT 583
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1943291881 170 HAVIMMKLLRKAAdeLGKTIIIVIHDINFASvYSDYILAMRNGQLYYHGSPKEI 223
Cdd:TIGR01271 584 EKEIFESCLCKLM--SNKTRILVTSKLEHLK-KADKILLLHEGVCYFYGTFSEL 634
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
17-229 |
3.62e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 53.83 E-value: 3.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 17 LDNITTTIQRGGITSIIGPNGAGKSTLLS-VIGRLLLPESGMVSVNGmdvaatdSDVLAKNLSilrqenqFVSRLTVEEL 95
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVIRG-------SVAYVPQVS-------WIFNATVREN 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 96 VGFGRYPYSKGRLTLDDKKVIDESLAFL---NLTEFRHRYLDeLSGGQRQRTYVAMVLCQDTEYVMLDEPLNNLDMKHAV 172
Cdd:PLN03232 699 ILFGSDFESERYWRAIDVTALQHDLDLLpgrDLTEIGERGVN-ISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAH 777
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1943291881 173 IMMKLLRKaaDEL-GKTIIIVIHDINFASVYsDYILAMRNGQLYYHGSPKEIMKADII 229
Cdd:PLN03232 778 QVFDSCMK--DELkGKTRVLVTNQLHFLPLM-DRIILVSEGMIKEEGTFAELSKSGSL 832
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
2-226 |
5.16e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 53.49 E-value: 5.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 2 IEISKISKHY---QDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRL---------------------------- 50
Cdd:PTZ00265 1166 IEIMDVNFRYisrPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFydlkndhhivfknehtndmtneqdyqgd 1245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 51 --------------------------LLPESGMVSVNGMDVAATDSDVLAKNLSILRQENQFVSrLTVEELVGFGrypys 104
Cdd:PTZ00265 1246 eeqnvgmknvnefsltkeggsgedstVFKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFN-MSIYENIKFG----- 1319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 105 KGRLTLDDKKvidESLAFLNLTEFRHR-----------YLDELSGGQRQRTYVAMVLCQDTEYVMLDEPLNNLDMKHAVI 173
Cdd:PTZ00265 1320 KEDATREDVK---RACKFAAIDEFIESlpnkydtnvgpYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKL 1396
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1943291881 174 MMKLLRKAADELGKTIIIVIHDInfASV-YSDYILAM----RNGQLYY-HGSPKEIMKA 226
Cdd:PTZ00265 1397 IEKTIVDIKDKADKTIITIAHRI--ASIkRSDKIVVFnnpdRTGSFVQaHGTHEELLSV 1453
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
16-224 |
5.41e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 53.20 E-value: 5.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 16 VLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVLAKNLSILRQENQFVSrltveEL 95
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFS-----GT 1328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 96 VGFGRYPYSKgrltlDDKKVIDESLAFLNLTEFRHRY---LD--------ELSGGQRQRTYVAMVLCQDTEYVMLDEPLN 164
Cdd:PLN03130 1329 VRFNLDPFNE-----HNDADLWESLERAHLKDVIRRNslgLDaevseageNFSVGQRQLLSLARALLRRSKILVLDEATA 1403
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1943291881 165 NLDMKHAVIMMKLLR---KAAdelgkTIIIVIHDINfASVYSDYILAMRNGQLYYHGSPKEIM 224
Cdd:PLN03130 1404 AVDVRTDALIQKTIReefKSC-----TMLIIAHRLN-TIIDCDRILVLDAGRVVEFDTPENLL 1460
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
10-223 |
7.29e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 52.59 E-value: 7.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 10 HYqditVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVLAKNLSILrqEN----Q 85
Cdd:PRK13545 37 HY----ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLNGQLTGI--ENielkG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 86 FVSRLTVEELvgfgrypyskgrltlddKKVIDESLAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQDTEYVMLDEPLNN 165
Cdd:PRK13545 111 LMMGLTKEKI-----------------KEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 166 LDMkhaVIMMKLLRKAAD--ELGKTIIIVIHDINFASVYSDYILAMRNGQLYYHGSPKEI 223
Cdd:PRK13545 174 GDQ---TFTKKCLDKMNEfkEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEV 230
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
24-250 |
7.78e-08 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 50.65 E-value: 7.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 24 IQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAatdsdvlaknlsilrqenqfvsrltveelvgfgrypy 103
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPV------------------------------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 104 skgrltlddkkvideslaflnlteFRHRYLDeLSGGQRQRTYVAMVLCQDTEYVMLDEPLNNLDMKHAVIMMKLLRKAAD 183
Cdd:cd03222 65 ------------------------YKPQYID-LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSE 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1943291881 184 ELGKTIIIVIHDINFASVYSDYILAmrngqlyYHGSPKeimkadiIEDIFDTPVDVKELDNKLIAMY 250
Cdd:cd03222 120 EGKKTALVVEHDLAVLDYLSDRIHV-------FEGEPG-------VYGIASQPKGTREGINRFLRGY 172
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
2-227 |
9.93e-08 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 52.33 E-value: 9.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 2 IEISKISKHYQ--DITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDV-----------AAT 68
Cdd:PRK11176 342 IEFRNVTFTYPgkEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLrdytlaslrnqVAL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 69 DS-------DVLAKNLSILRQEnqFVSRltvEELVGFGRYPY-----SKGRLTLDdkKVIDESLAFLnltefrhryldel 136
Cdd:PRK11176 422 VSqnvhlfnDTIANNIAYARTE--QYSR---EQIEEAARMAYamdfiNKMDNGLD--TVIGENGVLL------------- 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 137 SGGQRQRTYVAMVLCQDTEYVMLDEPLNNLDMKHAvimmKLLRKAADELGK--TIIIVIHDINFASvYSDYILAMRNGQL 214
Cdd:PRK11176 482 SGGQRQRIAIARALLRDSPILILDEATSALDTESE----RAIQAALDELQKnrTSLVIAHRLSTIE-KADEILVVEDGEI 556
|
250
....*....|...
gi 1943291881 215 YYHGSPKEIMKAD 227
Cdd:PRK11176 557 VERGTHAELLAQN 569
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
15-214 |
3.14e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 50.80 E-value: 3.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 15 TVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATD-SDVLAKNLSIL---RQENQFVSRL 90
Cdd:COG3845 272 PALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSpRERRRLGVAYIpedRLGRGLVPDM 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 91 TVEE---LVGFGRYPYSKGRLtLDDKKVIDESLAFlnLTEFRHRYLDE------LSGGQRQRTYVAMVLCQDTEYVMLDE 161
Cdd:COG3845 352 SVAEnliLGRYRRPPFSRGGF-LDRKAIRAFAEEL--IEEFDVRTPGPdtparsLSGGNQQKVILARELSRDPKLLIAAQ 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1943291881 162 PLNNLDMKHAVIMMKLLRKAADElGKTIIIVIHDIN--FAsvYSDYILAMRNGQL 214
Cdd:COG3845 429 PTRGLDVGAIEFIHQRLLELRDA-GAAVLLISEDLDeiLA--LSDRIAVMYEGRI 480
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-226 |
4.21e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 50.13 E-value: 4.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 1 MIEISKISKHYQD----ITVLDNITTTIQRGGITSIIGPNGAGKS-TLLSVIGRLLLPESGM---VSVNGMDVAATDS-- 70
Cdd:PRK11022 3 LLNVDKLSVHFGDesapFRAVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYPGRVMaekLEFNGQDLQRISEke 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 71 --DVLAKNLSILRQENqfVSRLTVEELVGFGRYPYSK-----GRLTLDDKKVidESLAFLNLTEFRHR---YLDELSGGQ 140
Cdd:PRK11022 83 rrNLVGAEVAMIFQDP--MTSLNPCYTVGFQIMEAIKvhqggNKKTRRQRAI--DLLNQVGIPDPASRldvYPHQLSGGM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 141 RQRTYVAMVLCQDTEYVMLDEPLNNLDMKHAVIMMKLLRKAADELGKTIIIVIHDINFASVYSDYILAMRNGQLYYHGSP 220
Cdd:PRK11022 159 SQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKA 238
|
....*.
gi 1943291881 221 KEIMKA 226
Cdd:PRK11022 239 HDIFRA 244
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
2-245 |
4.74e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 50.41 E-value: 4.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 2 IEISKISKHY---QDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNG---------------M 63
Cdd:PTZ00265 383 IQFKNVRFHYdtrKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDshnlkdinlkwwrskI 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 64 DVAATD----SDVLAKN-------------LSILRQENQFVSR------------------LTVEELVGFGRYPYSKGRL 108
Cdd:PTZ00265 463 GVVSQDpllfSNSIKNNikyslyslkdleaLSNYYNEDGNDSQenknkrnscrakcagdlnDMSNTTDSNELIEMRKNYQ 542
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 109 TLDDKKVIDESLAFLnLTEFRHRYLD-----------ELSGGQRQRTYVAMVLCQDTEYVMLDEPLNNLDMKHAVIMMKL 177
Cdd:PTZ00265 543 TIKDSEVVDVSKKVL-IHDFVSALPDkyetlvgsnasKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKT 621
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1943291881 178 LRKAADELGKTIIIVIHDINFASvYSDYILAMRNGQlyyHGSpkeimKADIIEDIFDTPVDVKELDNK 245
Cdd:PTZ00265 622 INNLKGNENRITIIIAHRLSTIR-YANTIFVLSNRE---RGS-----TVDVDIIGEDPTKDNKENNNK 680
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
11-47 |
5.83e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 50.01 E-value: 5.83e-07
10 20 30
....*....|....*....|....*....|....*..
gi 1943291881 11 YQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVI 47
Cdd:PRK10938 270 YNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLI 306
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1-213 |
8.25e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 49.40 E-value: 8.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 1 MIEISKISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIgrlllpeSGM---------VSVNGMDVAATD-S 70
Cdd:NF040905 1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVL-------SGVyphgsyegeILFDGEVCRFKDiR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 71 DVLAKNLSILRQENQFVSRLTVEELVGFGRYPYSKGrltlddkkVID---------ESLAFLNLTEFRHRYLDELSGGQR 141
Cdd:NF040905 74 DSEALGIVIIHQELALIPYLSIAENIFLGNERAKRG--------VIDwnetnrrarELLAKVGLDESPDTLVTDIGVGKQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1943291881 142 QRTYVAMVLCQDTEYVMLDEP---LNNLDMKHAVIMMKLLRKAadelGKTIIIVIHDINFASVYSDYILAMRNGQ 213
Cdd:NF040905 146 QLVEIAKALSKDVKLLILDEPtaaLNEEDSAALLDLLLELKAQ----GITSIIISHKLNEIRRVADSITVLRDGR 216
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
18-55 |
9.57e-07 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 44.90 E-value: 9.57e-07
10 20 30
....*....|....*....|....*....|....*...
gi 1943291881 18 DNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPES 55
Cdd:pfam13555 13 DGHTIPIDPRGNTLLTGPSGSGKSTLLDAIQTLLVPAK 50
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-226 |
1.22e-06 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 48.95 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 2 IEISKISKHYQ-DITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVLAKNLSIL 80
Cdd:PRK10790 341 IDIDNVSFAYRdDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 81 rQENQFVSRLTVEELVGFGRypyskgrlTLDDKKVIdESLAFLNLTEFR-------HRYLDE----LSGGQRQRTYVAMV 149
Cdd:PRK10790 421 -QQDPVVLADTFLANVTLGR--------DISEEQVW-QALETVQLAELArslpdglYTPLGEqgnnLSVGQKQLLALARV 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 150 LCQDTEYVMLDEPLNNLD------MKHAvimMKLLRKaadelgKTIIIVI-HDINfASVYSDYILAMRNGQLYYHGSPKE 222
Cdd:PRK10790 491 LVQTPQILILDEATANIDsgteqaIQQA---LAAVRE------HTTLVVIaHRLS-TIVEADTILVLHRGQAVEQGTHQQ 560
|
....
gi 1943291881 223 IMKA 226
Cdd:PRK10790 561 LLAA 564
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
88-225 |
1.27e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 49.06 E-value: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 88 SRLTVEELV-GFgrypysKGRLTLddkkVIDESLAFLNLtefrHRYLDELSGGQRQRTYVAMVLCQDTEYVM--LDEPLN 164
Cdd:PRK00635 442 KSLSIEEVLqGL------KSRLSI----LIDLGLPYLTP----ERALATLSGGEQERTALAKHLGAELIGITyiLDEPSI 507
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 165 NLDMKHAVIMMKLLRKAADElGKTIIIVIHD---INFAsvysDYIL------AMRNGQLYYHGSPKEIMK 225
Cdd:PRK00635 508 GLHPQDTHKLINVIKKLRDQ-GNTVLLVEHDeqmISLA----DRIIdigpgaGIFGGEVLFNGSPREFLA 572
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
16-223 |
1.78e-06 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 47.93 E-value: 1.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 16 VLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGmdvaatdsdvlakNLSILRQENqFVSRLTVEEL 95
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQFS-WIMPGTIKEN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 96 VGFGrYPYSKGRLtlddKKVIDESLAFLNLTEFRHR---YLDE----LSGGQRQRTYVAMVLCQDTEYVMLDEPLNNLDM 168
Cdd:cd03291 118 IIFG-VSYDEYRY----KSVVKACQLEEDITKFPEKdntVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1943291881 169 -KHAVIMMKLLRKAAdeLGKTIIIVIHDINFASVySDYILAMRNGQLYYHGSPKEI 223
Cdd:cd03291 193 fTEKEIFESCVCKLM--ANKTRILVTSKMEHLKK-ADKILILHEGSSYFYGTFSEL 245
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
17-199 |
1.81e-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: 46.58 E-value: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 17 LDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESgmvsvngmdvaatdsdvlaknlSILRQENQFVSRLTVeelv 96
Cdd:cd03227 11 FVPNDVTFGEGSLTIITGPNGSGKSTILDAIGLALGGAQ----------------------SATRRRSGVKAGCIV---- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 97 gfgryPYSKgrltlddkkvideslAFLNLTefrhryLDELSGGQRQRTYVAMVL----CQDTEYVMLDEPLNNLDMKHAV 172
Cdd:cd03227 65 -----AAVS---------------AELIFT------RLQLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQ 118
|
170 180
....*....|....*....|....*..
gi 1943291881 173 IMMKLLRKAADElGKTIIIVIHDINFA 199
Cdd:cd03227 119 ALAEAILEHLVK-GAQVIVITHLPELA 144
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
2-213 |
2.07e-06 |
|
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: 46.55 E-value: 2.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 2 IEISKISKHYqditvLDNITTTIQRGGITSIIGPNGAGKSTLLSVIgrllLPESGMVSVNGmdvaatDSDVLAKNLSIlr 81
Cdd:cd03238 1 LTVSGANVHN-----LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEG----LYASGKARLIS------FLPKFSRNKLI-- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 82 qenqFVSRLtveelvgfgrypyskgrltlddKKVIDESLAFLNLtefrHRYLDELSGGQRQRTYVAMVLCQDTEYVM--L 159
Cdd:cd03238 64 ----FIDQL----------------------QFLIDVGLGYLTL----GQKLSTLSGGELQRVKLASELFSEPPGTLfiL 113
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1943291881 160 DEPLNNLDMKHAVIMMKLLRKAADeLGKTIIIVIHDINFASvYSDYILAMRNGQ 213
Cdd:cd03238 114 DEPSTGLHQQDINQLLEVIKGLID-LGNTVILIEHNLDVLS-SADWIIDFGPGS 165
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-167 |
2.64e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 48.02 E-value: 2.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 1 MIEISKISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNG------------MDVAAT 68
Cdd:PRK11147 3 LISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQdlivarlqqdppRNVEGT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 69 DSDVLAKNLS----ILRQENQfVSRLTVEElvgfgrypYSKGRLT----------------LDDKkvIDESLAFLNLTEf 128
Cdd:PRK11147 83 VYDFVAEGIEeqaeYLKRYHD-ISHLVETD--------PSEKNLNelaklqeqldhhnlwqLENR--INEVLAQLGLDP- 150
|
170 180 190
....*....|....*....|....*....|....*....
gi 1943291881 129 rHRYLDELSGGQRQRTYVAMVLCQDTEYVMLDEPLNNLD 167
Cdd:PRK11147 151 -DAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLD 188
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
26-196 |
3.14e-06 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 46.54 E-value: 3.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 26 RGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSD---------VLAKNLSILRQENQFVSRLT----- 91
Cdd:COG0419 22 DDGLNLIVGPNGAGKSTILEAIRYALYGKARSRSKLRSDLINVGSEeasvelefeHGGKRYRIERRQGEFAEFLEakpse 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 92 ----VEELVGFGRYPYSKGRLTLDDKKVIDESLAFLNLTEFRHRYLDE---------LSGGQRQRTYVAMVLcqdteYVM 158
Cdd:COG0419 102 rkeaLKRLLGLEIYEELKERLKELEEALESALEELAELQKLKQEILAQlsgldpietLSGGERLRLALADLL-----SLI 176
|
170 180 190
....*....|....*....|....*....|....*...
gi 1943291881 159 LDepLNNLDMKHAVIMMKLLRKAAdelgktiiIVIHDI 196
Cdd:COG0419 177 LD--FGSLDEERLERLLDALEELA--------IITHVI 204
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
11-202 |
5.05e-06 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 46.58 E-value: 5.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 11 YQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLlpesgmvsvNGMDVAATDSDVLAKNLSILRQENQFVSRL 90
Cdd:COG1106 13 FKDELTLSMVASGLRLLRVNLIYGANASGKSNLLEALYFLR---------NLVLNSSQPGDKLVEPFLLDSESKNEPSEF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 91 TVEELVGFGRYPYskgRLTLDDKKVIDESLAFL-NLTEFRHRYLDELSGGQRQRTYVAMVLCQDTEYVMLDEPLNNLdmk 169
Cdd:COG1106 84 EILFLLDGVRYEY---GFELDKERIISEWLYFLsTAAQLNVPLLSPLYDWFDNNISLDTSSDGLTLLLKEDESLKEE--- 157
|
170 180 190
....*....|....*....|....*....|...
gi 1943291881 170 haviMMKLLRKAADELGKtIIIVIHDINFASVY 202
Cdd:COG1106 158 ----LLELLKIADPGIED-IEVEEEEIEDLVER 185
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
48-225 |
7.67e-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: 46.54 E-value: 7.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 48 GRLLLPESGMVSVNGMDVAAT------DSDVLAKNLSILRQENQfVSRLTVEELvgfgrypysKGRLTLddkkVIDESLA 121
Cdd:TIGR00630 413 GTRLKPEALAVTVGGKSIADVselsirEAHEFFNQLTLTPEEKK-IAEEVLKEI---------RERLGF----LIDVGLD 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 122 FLNLTefrhRYLDELSGGQRQRTYVAMVLCQDTEYVM--LDEPLNNLDMKHAVIMMKLLRKAADeLGKTIIIVIHD---I 196
Cdd:TIGR00630 479 YLSLS----RAAGTLSGGEAQRIRLATQIGSGLTGVLyvLDEPSIGLHQRDNRRLINTLKRLRD-LGNTLIVVEHDedtI 553
|
170 180 190
....*....|....*....|....*....|....*
gi 1943291881 197 NFAsvysDYILAM------RNGQLYYHGSPKEIMK 225
Cdd:TIGR00630 554 RAA----DYVIDIgpgageHGGEVVASGTPEEILA 584
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
17-214 |
8.34e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 46.15 E-value: 8.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 17 LDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAA-TDSDVLAKNL---SILRQENQFVSRLTV 92
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTrSPQDGLANGIvyiSEDRKRDGLVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 93 EE---LVGFGRYPYSKGRLTLDDKK--VIDESLAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQDTEYVMLDEPLNNLD 167
Cdd:PRK10762 348 KEnmsLTALRYFSRAGGSLKHADEQqaVSDFIRLFNIKTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1943291881 168 MKHAVIMMKLLRKAADElGKTIIIVIHDINFASVYSDYILAMRNGQL 214
Cdd:PRK10762 428 VGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1-196 |
9.38e-06 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 46.55 E-value: 9.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 1 MIEISKISKHYQDIT--VLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVlAKNLS 78
Cdd:TIGR01257 1937 ILRLNELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDV-HQNMG 2015
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 79 ILRQENQFVSRLTVEELVGFgrYPYSKGRLTLDDKKVIDESLAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQDTEYVM 158
Cdd:TIGR01257 2016 YCPQFDAIDDLLTGREHLYL--YARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVL 2093
|
170 180 190
....*....|....*....|....*....|....*...
gi 1943291881 159 LDEPLNNLDMKHAVIMMKLLRKAADElGKTIIIVIHDI 196
Cdd:TIGR01257 2094 LDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSM 2130
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
10-67 |
9.99e-06 |
|
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: 46.35 E-value: 9.99e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1943291881 10 HYQ-DITVLDNITTTIQRGGITSIIGPNGAGKSTllsvIGRLLL----PESGMVSVNGMDVAA 67
Cdd:COG5265 366 GYDpERPILKGVSFEVPAGKTVAIVGPSGAGKST----LARLLFrfydVTSGRILIDGQDIRD 424
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-214 |
2.31e-05 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 44.82 E-value: 2.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 1 MIEISKISKHYQD---ITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVI-GRLLLPESGMVSVNGMDVAA-TDSDVLAK 75
Cdd:TIGR02633 257 ILEARNLTCWDVInphRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALfGAYPGKFEGNVFINGKPVDIrNPAQAIRA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 76 NLSIL---RQENQFVSRLTVEELVGFGRYPYSKGRLTLDD---KKVIDESLAFLNLTEFrHRYL--DELSGGQRQRTYVA 147
Cdd:TIGR02633 337 GIAMVpedRKRHGIVPILGVGKNITLSVLKSFCFKMRIDAaaeLQIIGSAIQRLKVKTA-SPFLpiGRLSGGNQQKAVLA 415
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1943291881 148 MVLCQDTEYVMLDEPLNNLDMKHAVIMMKLLRKAADElGKTIIIVIHDINFASVYSDYILAMRNGQL 214
Cdd:TIGR02633 416 KMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
21-214 |
2.57e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.85 E-value: 2.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 21 TTTIQRGGITSIIGPNGAGKSTLLSVIG-----------RLLLPESGMVsvnGMDVAAT----DSDVLAKNLsiLRQENQ 85
Cdd:PLN03073 197 SVTLAFGRHYGLVGRNGTGKTTFLRYMAmhaidgipkncQILHVEQEVV---GDDTTALqcvlNTDIERTQL--LEEEAQ 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 86 FVS-RLTVEELVGFGRypySKGRLTLDDKK---------------VID----ES-----LAFLNLT-EFRHRYLDELSGG 139
Cdd:PLN03073 272 LVAqQRELEFETETGK---GKGANKDGVDKdavsqrleeiykrleLIDaytaEAraasiLAGLSFTpEMQVKATKTFSGG 348
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1943291881 140 QRQRTYVAMVLCQDTEYVMLDEPLNNLDMkHAVIMMK--LLRkaadeLGKTIIIVIHDINFASVYSDYILAMRNGQL 214
Cdd:PLN03073 349 WRMRIALARALFIEPDLLLLDEPTNHLDL-HAVLWLEtyLLK-----WPKTFIVVSHAREFLNTVVTDILHLHGQKL 419
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
16-232 |
3.00e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 44.77 E-value: 3.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 16 VLDNITTTIQRGGITSIIGPNGAGKSTLLsviGRLLlpesGMVSVNGMDVAAtdsdvlAKNLSILRQEnQFVSRLTVEEL 95
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLL---QSLL----SQFEISEGRVWA------ERSIAYVPQQ-AWIMNATVRGN 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 96 VGFGRyPYSKGRLTlDDKKV--IDESLAFLN---LTEFRHRYLDeLSGGQRQRTYVAMVLCQDTEYVMLDEPLNNLD--M 168
Cdd:PTZ00243 741 ILFFD-EEDAARLA-DAVRVsqLEADLAQLGgglETEIGEKGVN-LSGGQKARVSLARAVYANRDVYLLDDPLSALDahV 817
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1943291881 169 KHAVIMMKLLRKAAdelGKTIIIVIHDINFASvYSDYILAMRNGQLYYHGSPKEIMKADIIEDI 232
Cdd:PTZ00243 818 GERVVEECFLGALA---GKTRVLATHQVHVVP-RADYVVALGDGRVEFSGSSADFMRTSLYATL 877
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
16-222 |
3.34e-05 |
|
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: 44.54 E-value: 3.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 16 VLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGrlllpesgmvsvnGMDVAATDSDVLAKNLSI--LRQENQFVSRLTVE 93
Cdd:TIGR03719 20 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMA-------------GVDKDFNGEARPQPGIKVgyLPQEPQLDPTKTVR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 94 ELVGFG---------RY---------PYSKGRLTLDDKKVIDESLAFLNLTEFRHRyLD----------------ELSGG 139
Cdd:TIGR03719 87 ENVEEGvaeikdaldRFneisakyaePDADFDKLAAEQAELQEIIDAADAWDLDSQ-LEiamdalrcppwdadvtKLSGG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 140 QRQRTYVAMVLCQDTEYVMLDEPLNNLDMKHAVIMMKLLRkaadELGKTIIIVIHDINFASVYSDYILAMRNGqlyyHGS 219
Cdd:TIGR03719 166 ERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQ----EYPGTVVAVTHDRYFLDNVAGWILELDRG----RGI 237
|
...
gi 1943291881 220 PKE 222
Cdd:TIGR03719 238 PWE 240
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1-167 |
8.23e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 43.18 E-value: 8.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 1 MIEISKIskHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGrlllpesgmvsvnGMDvaaTDSD---VLAKNL 77
Cdd:PRK11819 9 MNRVSKV--VPPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMA-------------GVD---KEFEgeaRPAPGI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 78 SI--LRQENQFVSRLTVEELV--GFG-------RY---------PYSKGRLTLDDKKVIDESLAFLNLTEFRHRyLD--- 134
Cdd:PRK11819 71 KVgyLPQEPQLDPEKTVRENVeeGVAevkaaldRFneiyaayaePDADFDALAAEQGELQEIIDAADAWDLDSQ-LEiam 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1943291881 135 -------------ELSGGQRQRtyVAmvLC----QDTEYVMLDEPLNNLD 167
Cdd:PRK11819 150 dalrcppwdakvtKLSGGERRR--VA--LCrlllEKPDMLLLDEPTNHLD 195
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
19-198 |
1.36e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 42.57 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 19 NITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVngmdvaaTDSDVLAKnlsiLRQeNQFV-SRLTVEELVG 97
Cdd:PRK15064 19 NISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSL-------DPNERLGK----LRQ-DQFAfEEFTVLDTVI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 98 FGRYP-----------YSKGRLTLDD-KKVID-------------ESLA---FLNL---TEFRHRYLDELSGGQRQRTYV 146
Cdd:PRK15064 87 MGHTElwevkqerdriYALPEMSEEDgMKVADlevkfaemdgytaEARAgelLLGVgipEEQHYGLMSEVAPGWKLRVLL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1943291881 147 AMVLCQDTEYVMLDEPLNNLDmkhavimMKLLRKAADELGK---TIIIVIHDINF 198
Cdd:PRK15064 167 AQALFSNPDILLLDEPTNNLD-------INTIRWLEDVLNErnsTMIIISHDRHF 214
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
2-196 |
1.41e-04 |
|
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: 42.15 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 2 IEISKISKHYQD--ITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPEsGMVSVNGMDVAATDSDVLAKNLSI 79
Cdd:cd03289 3 MTVKDLTAKYTEggNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKAFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 80 LRQENQFVSRLTVEELVGFGRYPYSKGRLTLDD---KKVIDESLAFLNLTEFRHRYLdeLSGGQRQRTYVAMVLCQDTEY 156
Cdd:cd03289 82 IPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEvglKSVIEQFPGQLDFVLVDGGCV--LSHGHKQLMCLARSVLSKAKI 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1943291881 157 VMLDEPLNNLDMKHAVIMMKLLRKAADelGKTIIIVIHDI 196
Cdd:cd03289 160 LLLDEPSAHLDPITYQVIRKTLKQAFA--DCTVILSEHRI 197
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
14-226 |
1.58e-04 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 42.10 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 14 ITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIgrlllpeSGmVSVNGMDVAA-----TDSDVL-----------AKNL 77
Cdd:PRK15093 20 VKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAI-------CG-VTKDNWRVTAdrmrfDDIDLLrlsprerrklvGHNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 78 SILRQENQfvSRLTVEELVG------FGRYPYsKG----RLTLDDKKVID--ESLAFLNLTEFRHRYLDELSGGQRQRTY 145
Cdd:PRK15093 92 SMIFQEPQ--SCLDPSERVGrqlmqnIPGWTY-KGrwwqRFGWRKRRAIEllHRVGIKDHKDAMRSFPYELTEGECQKVM 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 146 VAMVLCQDTEYVMLDEPLNNLDMKHAVIMMKLLRKAADELGKTIIIVIHDINFASVYSDYILAMRNGQLYYHGSPKEIMK 225
Cdd:PRK15093 169 IAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVT 248
|
.
gi 1943291881 226 A 226
Cdd:PRK15093 249 T 249
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
26-102 |
1.89e-04 |
|
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: 40.82 E-value: 1.89e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1943291881 26 RGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDSDVLAKNLSILRQENQFVSRLTVEELVGFGRYP 102
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKL 77
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
15-196 |
1.90e-04 |
|
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: 42.59 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 15 TVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPEsGMVSVNGMDVAATDSDVLAKNLSILRQENQFVSRLTVEE 94
Cdd:TIGR01271 1233 AVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKN 1311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 95 LVGFGRYPYSKGRLTLDD---KKVIDESLAFLNLTEFRHRYLdeLSGGQRQRTYVAMVLCQDTEYVMLDEPLNNLDMKHA 171
Cdd:TIGR01271 1312 LDPYEQWSDEEIWKVAEEvglKSVIEQFPDKLDFVLVDGGYV--LSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTL 1389
|
170 180
....*....|....*....|....*
gi 1943291881 172 VIMMKLLRKAADELgkTIIIVIHDI 196
Cdd:TIGR01271 1390 QIIRKTLKQSFSNC--TVILSEHRV 1412
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
14-226 |
3.80e-04 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 41.04 E-value: 3.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 14 ITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVI-GrlLLPESGMVSV-----NGMDVAATDSD----VLAKNLSILRQE 83
Cdd:COG4170 20 VKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAIcG--ITKDNWHVTAdrfrwNGIDLLKLSPRerrkIIGREIAMIFQE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 84 ------------NQFVSRLTVEELVG------FGRYPYSKG---RLTLDDKKVIDESLAFlnltefrhryldELSGGQRQ 142
Cdd:COG4170 98 psscldpsakigDQLIEAIPSWTFKGkwwqrfKWRKKRAIEllhRVGIKDHKDIMNSYPH------------ELTEGECQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 143 RTYVAMVLCQDTEYVMLDEPLNNLDMKHAVIMMKLLRKAADELGKTIIIVIHDINFASVYSDYILAMRNGQLYYHGSPKE 222
Cdd:COG4170 166 KVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQ 245
|
....
gi 1943291881 223 IMKA 226
Cdd:COG4170 246 ILKS 249
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
20-214 |
4.94e-04 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 41.05 E-value: 4.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 20 ITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAAtDSDVLAKNLSIL-----RQENQFVSRLTVEE 94
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDI-RSPRDAIRAGIMlcpedRKAEGIIPVHSVAD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 95 LVGFG-RYPYSKGRLTLDDKK---VIDESLAFLNL-TEFRHRYLDELSGGQRQRTYVAMVLCQDTEYVMLDEPLNNLDM- 168
Cdd:PRK11288 351 NINISaRRHHLRAGCLINNRWeaeNADRFIRSLNIkTPSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVg 430
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1943291881 169 -KHAVimMKLLRKAADElGKTIIIVIHDINFASVYSDYILAMRNGQL 214
Cdd:PRK11288 431 aKHEI--YNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
16-214 |
4.95e-04 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 40.77 E-value: 4.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 16 VLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATD-SDVLAKNLSIL---RQENQFVSRLT 91
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSpRDAIRAGIAYVpedRKGEGLVLDLS 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 92 VEE---LVGFGRYpySKGRLtLDDKK---VIDESLAFLNL-TEFRHRYLDELSGGQRQRTYVAMVLCQDTEYVMLDEPLN 164
Cdd:COG1129 347 IREnitLASLDRL--SRGGL-LDRRReraLAEEYIKRLRIkTPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTR 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1943291881 165 NLDM--KHAVImmKLLRKAADElGKTIIIV-------IHdinfasvYSDYILAMRNGQL 214
Cdd:COG1129 424 GIDVgaKAEIY--RLIRELAAE-GKAVIVIsselpelLG-------LSDRILVMREGRI 472
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
27-51 |
6.09e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 40.30 E-value: 6.09e-04
10 20
....*....|....*....|....*
gi 1943291881 27 GGITSIIGPNGAGKSTLLSVIgRLL 51
Cdd:COG4637 21 GPLTVLIGANGSGKSNLLDAL-RFL 44
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
15-167 |
6.44e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 39.85 E-value: 6.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 15 TVLDNITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMV---SVNGMDVAATDSDVLAKNLSIlrqenqfVSRLT 91
Cdd:PRK13541 14 KNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIyykNCNINNIAKPYCTYIGHNLGL-------KLEMT 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1943291881 92 VEELVGFGRYPYskgrltlDDKKVIDESLAFLNLTEFRHRYLDELSGGQRQRTYVAMVLCQDTEYVMLDEPLNNLD 167
Cdd:PRK13541 87 VFENLKFWSEIY-------NSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLS 155
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1-194 |
1.54e-03 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 39.00 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 1 MIEISKISKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTLLSVI-GRLLLP-ESGMVSVNGMDVAATDSDVLAKN-- 76
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLaGREDYEvTGGTVEFKGKDLLELSPEDRAGEgi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 77 -------LSILRQENQFVSRLTVEELVGF-GRYPYSKgrltLDDKKVIDESLAFLNLTE-FRHRYLDE-LSGGQRQRTYV 146
Cdd:PRK09580 81 fmafqypVEIPGVSNQFFLQTALNAVRSYrGQEPLDR----FDFQDLMEEKIALLKMPEdLLTRSVNVgFSGGEKKRNDI 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1943291881 147 AMVLCQDTEYVMLDEPLNNLDMKHAVIMMKLLRKAADElGKTIIIVIH 194
Cdd:PRK09580 157 LQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDG-KRSFIIVTH 203
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
19-214 |
3.35e-03 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 38.49 E-value: 3.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 19 NITTTIQRGGITSIIGPNGAGKSTLLSVIGRLLLPESGMVSVNGMDVAATDS-DVLAKNLSILRQENQfVSRLTVEELVG 97
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTaQRLARGLVYLPEDRQ-SSGLYLDAPLA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 98 FGRYPYSKGRLTL-----DDKKVIDESLAFLNLtEFRHryLDE----LSGGQRQRTYVAMVLCQDTEYVMLDEPLNNLDM 168
Cdd:PRK15439 360 WNVCALTHNRRGFwikpaRENAVLERYRRALNI-KFNH--AEQaartLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDV 436
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1943291881 169 KHAVIMMKLLRKAADElGKTIIIVIHDINFASVYSDYILAMRNGQL 214
Cdd:PRK15439 437 SARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
158-223 |
3.53e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 38.66 E-value: 3.53e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1943291881 158 MLDEPLNNLDMKHAVIMMKLLRKAADeLGKTIIIVIHDINFaSVYSDYILAM------RNGQLYYHGSPKEI 223
Cdd:PRK00635 1725 LLDEIATSLDNQQKSALLVQLRTLVS-LGHSVIYIDHDPAL-LKQADYLIEMgpgsgkTGGKILFSGPPKDI 1794
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
2-51 |
3.81e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 37.67 E-value: 3.81e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1943291881 2 IEISKIsKHYQDITV-LDNitttiqRGGITSIIGPNGAGKSTLLSVIGRLL 51
Cdd:COG3950 6 LTIENF-RGFEDLEIdFDN------PPRLTVLVGENGSGKTTLLEAIALAL 49
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
28-44 |
4.74e-03 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 37.09 E-value: 4.74e-03
|
| RloC |
COG4694 |
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis]; |
3-43 |
4.83e-03 |
|
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 443729 [Multi-domain] Cd Length: 692 Bit Score: 37.79 E-value: 4.83e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1943291881 3 EISKIsKHYQDITVLDNITTTIQRGGITSIIGPNGAGKSTL 43
Cdd:COG4694 1 MITKI-KKLKNVGAFKDFGWLAFFKKLNLIYGENGSGKSTL 40
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
87-226 |
6.84e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 37.70 E-value: 6.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 87 VSRLTVEELVGFGRypyskgRLTLDDK-KVIDESLaflnLTEFRHR--YLDE--------------LSGGQRQRTYVAM- 148
Cdd:COG0178 430 LTALSIDEALEFFE------NLELTEReAEIAERI----LKEIRSRlgFLVDvgldyltldrsagtLSGGEAQRIRLATq 499
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943291881 149 -------VLcqdteYVmLDEPLNNL---DMKHAVIMMKLLRkaadELGKTIIIVIHD---INFAsvysDYILAM------ 209
Cdd:COG0178 500 igsglvgVL-----YV-LDEPSIGLhqrDNDRLIETLKRLR----DLGNTVIVVEHDedtIRAA----DYIIDIgpgage 565
|
170
....*....|....*..
gi 1943291881 210 RNGQLYYHGSPKEIMKA 226
Cdd:COG0178 566 HGGEVVAQGTPEEILKN 582
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
29-51 |
7.04e-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: 36.98 E-value: 7.04e-03
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
27-53 |
9.75e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 37.20 E-value: 9.75e-03
10 20
....*....|....*....|....*..
gi 1943291881 27 GGITSIIGPNGAGKSTLLSVIGRLLLP 53
Cdd:COG4913 24 GRGTLLTGDNGSGKSTLLDAIQTLLVP 50
|
|
| |
