|
Name |
Accession |
Description |
Interval |
E-value |
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-252 |
5.71e-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: 5.71e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 1 MLKIHDLNFTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEFAKICGFV 80
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 81 PQKSELNTPLKVIDVLLMSKYANLKhAFSSYSKEDILEIKEFAKDLRLENFLERSILSLSGGEFQRMLLARALLKKPKIL 160
Cdd:COG1120 81 PQEPPAPFGLTVRELVALGRYPHLG-LFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 161 FLDEPTSALDLNYAIELLSLCEKLVKEKNIAVVAILHDLNLASMFCDKILFLKEGEIKYFGTSKELFTQEILKEIYDLNC 240
Cdd:COG1120 160 LLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLTPELLEEVYGVEA 239
|
250
....*....|....
gi 919308723 241 EIIY--KNSKPYIL 252
Cdd:COG1120 240 RVIEdpVTGRPLVL 253
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
3-221 |
8.47e-76 |
|
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: 227.70 E-value: 8.47e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 3 KIHDLNFTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEFAKICGFVPQ 82
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 83 KSELntplkvidvllmskyanlkhafssyskedileikefakdLRLENFLERSILSLSGGEFQRMLLARALLKKPKILFL 162
Cdd:cd03214 81 ALEL---------------------------------------LGLAHLADRPFNELSGGERQRVLLARALAQEPPILLL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 919308723 163 DEPTSALDLNYAIELLSLCEKLVKEKNIAVVAILHDLNLASMFCDKILFLKEGEIKYFG 221
Cdd:cd03214 122 DEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-253 |
1.02e-72 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 222.68 E-value: 1.02e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 1 MLKIHDLNFTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEFAKICGFV 80
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 81 PQKSELNTPLKVIDVLLMSKYAnlkHAFSSYSKEDILEikEFAKDLRLENFLERSILSLSGGEFQRMLLARALL------ 154
Cdd:COG4559 81 PQHSSLAFPFTVEEVVALGRAP---HGSSAAQDRQIVR--EALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepv 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 155 -KKPKILFLDEPTSALDLNYAIELLSLCEKLVKEkNIAVVAILHDLNLASMFCDKILFLKEGEIKYFGTSKELFTQEILK 233
Cdd:COG4559 156 dGGPRWLFLDEPTSALDLAHQHAVLRLARQLARR-GGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLTDELLE 234
|
250 260
....*....|....*....|..
gi 919308723 234 EIYDLNCEII--YKNSKPYILA 253
Cdd:COG4559 235 RVYGADLRVLahPEGGCPQVLP 256
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-236 |
2.65e-72 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 221.12 E-value: 2.65e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 1 MLKIHDLNFTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKdfslKEFAKIcGFV 80
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPR----RARRRI-GYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 81 PQKSELN--TPLKVIDVLLMSKYANLKhAFSSYSKEDILEIKEFAKDLRLENFLERSILSLSGGEFQRMLLARALLKKPK 158
Cdd:COG1121 81 PQRAEVDwdFPITVRDVVLMGRYGRRG-LFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPD 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 919308723 159 ILFLDEPTSALDLNYAIELLSLCEKLVKEkNIAVVAILHDLNLASMFCDKILFLKEGEIkYFGTSKELFTQEILKEIY 236
Cdd:COG1121 160 LLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRGLV-AHGPPEEVLTPENLSRAY 235
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-237 |
7.07e-68 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 210.40 E-value: 7.07e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 1 MLKIHDLNFTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEFAKICGFV 80
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 81 PQKSELNTPLKVIDVLLMSKYAnlkHAFSSYSKEDILEikEFAKDLRLENFLERSILSLSGGEFQRMLLARALL------ 154
Cdd:PRK13548 82 PQHSSLSFPFTVEEVVAMGRAP---HGLSRAEDDALVA--AALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepd 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 155 KKPKILFLDEPTSALDLNYAIELLSLCEKLVKEKNIAVVAILHDLNLASMFCDKILFLKEGEIKYFGTSKELFTQEILKE 234
Cdd:PRK13548 157 GPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVLTPETLRR 236
|
...
gi 919308723 235 IYD 237
Cdd:PRK13548 237 VYG 239
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
3-221 |
4.15e-63 |
|
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: 196.60 E-value: 4.15e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 3 KIHDLNFTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFntnikDFSLKEFAKICGFVPQ 82
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVF-----GKPLEKERKRIGYVPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 83 KSELNT--PLKVIDVLLMSKYANLKHaFSSYSKEDILEIKEFAKDLRLENFLERSILSLSGGEFQRMLLARALLKKPKIL 160
Cdd:cd03235 76 RRSIDRdfPISVRDVVLMGLYGHKGL-FRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 919308723 161 FLDEPTSALDLNYAIELLSLCEKLvKEKNIAVVAILHDLNLASMFCDKILFLKeGEIKYFG 221
Cdd:cd03235 155 LLDEPFAGVDPKTQEDIYELLREL-RREGMTILVVTHDLGLVLEYFDRVLLLN-RTVVASG 213
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-234 |
3.89e-54 |
|
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: 174.44 E-value: 3.89e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 2 LKIHDLNFTYH-QKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLIlkN--LSPNKGEISLFNTNIKDFSLKEFAKICG 78
Cdd:COG1122 1 IELENLSFSYPgGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLL--NglLKPTSGEVLVDGKDITKKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 79 FVPQKSE----LNTPLKviDVllmskyanlkhAFS----SYSKEDILE-IKEFAKDLRLENFLERSILSLSGGEFQRMLL 149
Cdd:COG1122 79 LVFQNPDdqlfAPTVEE--DV-----------AFGpenlGLPREEIRErVEEALELVGLEHLADRPPHELSGGQKQRVAI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 150 ARALLKKPKILFLDEPTSALDLNYAIELLSLCEKLvKEKNIAVVAILHDLNLASMFCDKILFLKEGEIKYFGTSKELFTQ 229
Cdd:COG1122 146 AGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRL-NKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSD 224
|
....*.
gi 919308723 230 -EILKE 234
Cdd:COG1122 225 yELLEE 230
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-217 |
4.41e-49 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 160.75 E-value: 4.41e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 2 LKIHDLNFTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEFAKICGFVP 81
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 82 QKSELntplkvidvLLMSKYANLKHAFSSYSKE-DILEIKEFAKDLRL-ENFLERSILSLSGGEFQRMLLARALLKKPKI 159
Cdd:COG4619 81 QEPAL---------WGGTVRDNLPFPFQLRERKfDRERALELLERLGLpPDILDKPVERLSGGERQRLALIRALLLQPDV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 919308723 160 LFLDEPTSALDLNYAIELLSLCEKLVKEKNIAVVAILHDLNLASMFCDKILFLKEGEI 217
Cdd:COG4619 152 LLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-249 |
4.91e-49 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 161.79 E-value: 4.91e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 1 MLKIHDLNFTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEFAKICGFV 80
Cdd:COG4604 1 MIEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 81 PQKSELNTPLKVIDVLLMSKYAnlkhafssYSK-----EDILEIKEFAKDLRLENFLERSILSLSGGEFQRMLLARALLK 155
Cdd:COG4604 81 RQENHINSRLTVRELVAFGRFP--------YSKgrltaEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 156 KPKILFLDEPTSALDLNYAIELLSLCEKLVKEKNIAVVAILHDLNLASMFCDKILFLKEGEIKYFGTSKELFTQEILKEI 235
Cdd:COG4604 153 DTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEIITPEVLSDI 232
|
250
....*....|....
gi 919308723 236 YDLNCEIIYKNSKP 249
Cdd:COG4604 233 YDTDIEVEEIDGKR 246
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-243 |
6.82e-49 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 161.72 E-value: 6.82e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 1 MLKIHDLNFTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEFAKICGFV 80
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 81 PQksELNTP--LKVIDVLLM--SKYANLkhaFSSYSKEDILEIKEFAKDLRLENFLERSILSLSGGEFQRMLLARALLKK 156
Cdd:PRK11231 82 PQ--HHLTPegITVRELVAYgrSPWLSL---WGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 157 PKILFLDEPTSALDLNYAIELLSLCEKLvKEKNIAVVAILHDLNLASMFCDKILFLKEGEIKYFGTSKELFTQEILKEIY 236
Cdd:PRK11231 157 TPVVLLDEPTTYLDINHQVELMRLMREL-NTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTPGLLRTVF 235
|
....*..
gi 919308723 237 DLNCEII 243
Cdd:PRK11231 236 DVEAEIH 242
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-227 |
1.73e-48 |
|
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: 160.35 E-value: 1.73e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 1 MLKIHDLNFTY----HQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEFAKI 76
Cdd:COG1124 1 MLEVRNLSVSYgqggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 77 CGFVPQKSE--LNtPLKVIDVLLMskyANLKHAFSSYSKEdilEIKEFAKDLRL-ENFLERSILSLSGGEFQRMLLARAL 153
Cdd:COG1124 81 VQMVFQDPYasLH-PRHTVDRILA---EPLRIHGLPDREE---RIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 919308723 154 LKKPKILFLDEPTSALDLNYAIELLSLCEKLVKEKNIAVVAILHDLNLASMFCDKILFLKEGEIKYFGTSKELF 227
Cdd:COG1124 154 ILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLL 227
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-217 |
2.09e-48 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 159.44 E-value: 2.09e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 1 MLKIHDLNFTYHQKDL----LKNIHLELKNQAFIGILGPNGSGKSTLLKLI--LknLSPNKGEISLFNTNIKDFSLKEFA 74
Cdd:COG1136 4 LLELRNLTKSYGTGEGevtaLRGVSLSIEAGEFVAIVGPSGSGKSTLLNILggL--DRPTSGEVLIDGQDISSLSERELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 75 KI----CGFVPQKSELNTPLKVID-VLLMSKYANLKHafssysKEDILEIKEFAKDLRLENFLERSILSLSGGEFQRMLL 149
Cdd:COG1136 82 RLrrrhIGFVFQFFNLLPELTALEnVALPLLLAGVSR------KERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 919308723 150 ARALLKKPKILFLDEPTSALDLNYAIELLSLCEKLVKEKNIAVVAILHDLNLASMfCDKILFLKEGEI 217
Cdd:COG1136 156 ARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAAR-ADRVIRLRDGRI 222
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-236 |
2.85e-48 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 159.46 E-value: 2.85e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 2 LKIHDLNFTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEFAKIcGFVP 81
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRI-GYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 82 QKSELNTPLKVIDVLLMskYANLKHAFSSYSKEDILEIKEFakdLRLENFLERSILSLSGGEFQRMLLARALLKKPKILF 161
Cdd:COG1131 80 QEPALYPDLTVRENLRF--FARLYGLPRKEARERIDELLEL---FGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 919308723 162 LDEPTSALDLNYAIELLSLCEKLVKEKniavVAIL---HDLNLASMFCDKILFLKEGEIKYFGTSKELfTQEILKEIY 236
Cdd:COG1131 155 LDEPTSGLDPEARRELWELLRELAAEG----KTVLlstHYLEEAERLCDRVAIIDKGRIVADGTPDEL-KARLLEDVF 227
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-217 |
2.60e-46 |
|
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: 153.80 E-value: 2.60e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 2 LKIHDLNFTYHQKDL----LKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEFAKI- 76
Cdd:cd03255 1 IELKNLSKTYGGGGEkvqaLKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 77 ---CGFVPQKSELNTPLKVID-VLLMSKYANLKhafssySKEDILEIKEFAKDLRLENFLERSILSLSGGEFQRMLLARA 152
Cdd:cd03255 81 rrhIGFVFQSFNLLPDLTALEnVELPLLLAGVP------KKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 919308723 153 LLKKPKILFLDEPTSALDLNYAIELLSLCEKLVKEKNIAVVAILHDLNLASMfCDKILFLKEGEI 217
Cdd:cd03255 155 LANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEY-ADRIIELRDGKI 218
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-237 |
6.19e-46 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 158.08 E-value: 6.19e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 1 MLKIHDLNFTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEFAKICGFV 80
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 81 PQKSELNTPLKVIDVLLMSKYANLKHaFSSYSKEDILEIKEFAKDLRLENFLERSILSLSGGEFQRMLLARALLKKPKIL 160
Cdd:PRK09536 83 PQDTSLSFEFDVRQVVEMGRTPHRSR-FDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 919308723 161 FLDEPTSALDLNYAIELLSLCEKLVKEKNIAVVAIlHDLNLASMFCDKILFLKEGEIKYFGTSKELFTQEILKEIYD 237
Cdd:PRK09536 162 LLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAI-HDLDLAARYCDELVLLADGRVRAAGPPADVLTADTLRAAFD 237
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-246 |
8.79e-46 |
|
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: 153.47 E-value: 8.79e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 1 MLKIHDLNFTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEFAKIcGFV 80
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQI-GVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 81 PQKSELNTPLKVIDVLLMskYANLKHAFssySKEDILEIKEFAKDLRLENFLERSILSLSGGEFQRMLLARALLKKPKIL 160
Cdd:COG4555 80 PDERGLYDRLTVRENIRY--FAELYGLF---DEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 161 FLDEPTSALDLNYAIELLSLCEKLvKEKNIAVVAILHDLNLASMFCDKILFLKEGEIKYFGTSKELFTQEILKEIYDLNC 240
Cdd:COG4555 155 LLDEPTNGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEENLEDAFV 233
|
....*.
gi 919308723 241 EIIYKN 246
Cdd:COG4555 234 ALIGSE 239
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
3-216 |
4.57e-45 |
|
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: 150.31 E-value: 4.57e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 3 KIHDLNFTYHQKD--LLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEFAKICGFV 80
Cdd:cd03225 1 ELKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 81 PQKSE---LNTplKVIDVLlmskyanlkhAFS----SYSKEDILE-IKEFAKDLRLENFLERSILSLSGGEFQRMLLARA 152
Cdd:cd03225 81 FQNPDdqfFGP--TVEEEV----------AFGlenlGLPEEEIEErVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 919308723 153 LLKKPKILFLDEPTSALDLNYAIELLSLCEKLvKEKNIAVVAILHDLNLASMFCDKILFLKEGE 216
Cdd:cd03225 149 LAMDPDILLLDEPTAGLDPAGRRELLELLKKL-KAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-236 |
7.70e-45 |
|
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: 150.80 E-value: 7.70e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 2 LKIHDLNFTY-HQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNI---KDFSLKEFAKIC 77
Cdd:cd03256 1 IEVENLSKTYpNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDInklKGKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 78 GFVPQKSELNTPLKVIDVLLMSKYAN---LKHAFSSYSKEDILEIKEFAKDLRLENFLERSILSLSGGEFQRMLLARALL 154
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGRLGRrstWRSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 155 KKPKILFLDEPTSALDLNYAIELLSLCEKLVKEKNIAVVAILHDLNLASMFCDKILFLKEGEIKYFGTSKELfTQEILKE 234
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL-TDEVLDE 239
|
..
gi 919308723 235 IY 236
Cdd:cd03256 240 IY 241
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-217 |
8.59e-45 |
|
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: 150.35 E-value: 8.59e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 1 MLKIHDLNFTYHQKDL----LKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFS---LKEF 73
Cdd:cd03257 1 LLEVKNLSVSFPTGGGsvkaLDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 74 AKICGFVPQK--SELNTPLKVIDVLLMSkyanLKHAFSSYSKEDILEIK-EFAKDLRL-ENFLERSILSLSGGEFQRMLL 149
Cdd:cd03257 81 RKEIQMVFQDpmSSLNPRMTIGEQIAEP----LRIHGKLSKKEARKEAVlLLLVGVGLpEEVLNRYPHELSGGQRQRVAI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 919308723 150 ARALLKKPKILFLDEPTSALDLNYAIELLSLCEKLVKEKNIAVVAILHDLNLASMFCDKILFLKEGEI 217
Cdd:cd03257 157 ARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-230 |
3.64e-44 |
|
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: 158.07 E-value: 3.64e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 2 LKIHDLNFTY--HQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEFAKICGF 79
Cdd:COG2274 474 IELENVSFRYpgDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 80 VPQkselntplkviDVLLMSK--YANLKHAFSSYSKEDILEIkefAKDLRLENFLER------SILS-----LSGGEFQR 146
Cdd:COG2274 554 VLQ-----------DVFLFSGtiRENITLGDPDATDEEIIEA---ARLAGLHDFIEAlpmgydTVVGeggsnLSGGQRQR 619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 147 MLLARALLKKPKILFLDEPTSALDlnyaiellSLCEKLVKE------KNIAVVAILHDLNLASMfCDKILFLKEGEIKYF 220
Cdd:COG2274 620 LAIARALLRNPRILILDEATSALD--------AETEAIILEnlrrllKGRTVIIIAHRLSTIRL-ADRIIVLDKGRIVED 690
|
250
....*....|
gi 919308723 221 GTSKELFTQE 230
Cdd:COG2274 691 GTHEELLARK 700
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-229 |
5.66e-44 |
|
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: 155.06 E-value: 5.66e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 1 MLKIHDLNFTYHQKD-----LLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFS---LKE 72
Cdd:COG1123 260 LLEVRNLSKRYPVRGkggvrAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrsLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 73 FAKICGFVPQ--KSELNTPLKVIDVLLMSkyanLKhAFSSYSKEDILE-IKEFAKDLRL-ENFLERSILSLSGGEFQRML 148
Cdd:COG1123 340 LRRRVQMVFQdpYSSLNPRMTVGDIIAEP----LR-LHGLLSRAERRErVAELLERVGLpPDLADRYPHELSGGQRQRVA 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 149 LARALLKKPKILFLDEPTSALDLNYAIELLSLCEKLVKEKNIAVVAILHDLNLASMFCDKILFLKEGEIKYFGTSKELFT 228
Cdd:COG1123 415 IARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFA 494
|
.
gi 919308723 229 Q 229
Cdd:COG1123 495 N 495
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-216 |
6.16e-44 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 146.37 E-value: 6.16e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 2 LKIHDLNFTYHQKD--LLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEFAKICGF 79
Cdd:cd03228 1 IEFKNVSFSYPGRPkpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 80 VPQKSELntplkvidvllmskyanlkhafssyskedileikeFAKDLRlENFlersilsLSGGEFQRMLLARALLKKPKI 159
Cdd:cd03228 81 VPQDPFL-----------------------------------FSGTIR-ENI-------LSGGQRQRIAIARALLRDPPI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 919308723 160 LFLDEPTSALDLNYAIELLSLCEKLVKEKNIAVVAilHDLNLASMfCDKILFLKEGE 216
Cdd:cd03228 118 LILDEATSALDPETEALILEALRALAKGKTVIVIA--HRLSTIRD-ADRIIVLDDGR 171
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
2-243 |
4.14e-43 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 147.06 E-value: 4.14e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 2 LKIHDLNFTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEFAKICGFVP 81
Cdd:PRK10253 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 82 QKSELNTPLKVIDVLLMSKYANlKHAFSSYSKEDILEIKEFAKDLRLENFLERSILSLSGGEFQRMLLARALLKKPKILF 161
Cdd:PRK10253 88 QNATTPGDITVQELVARGRYPH-QPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIML 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 162 LDEPTSALDLNYAIELLSLCEKLVKEKNIAVVAILHDLNLASMFCDKILFLKEGEIKYFGTSKELFTQEILKEIYDLNCE 241
Cdd:PRK10253 167 LDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERIYGLRCM 246
|
..
gi 919308723 242 II 243
Cdd:PRK10253 247 II 248
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-246 |
7.58e-43 |
|
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: 146.00 E-value: 7.58e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 1 MLKIHDLNFTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKG-EISLF-----NTNIKDfsLKefA 74
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFgerrgGEDVWE--LR--K 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 75 KIcGFVpqKSEL----NTPLKVIDVLLMSKYANLkHAFSSYSKEDILEIKEFAKDLRLENFLERSILSLSGGEFQRMLLA 150
Cdd:COG1119 79 RI-GLV--SPALqlrfPRDETVLDVVLSGFFDSI-GLYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 151 RALLKKPKILFLDEPTSALDLNYAIELLSLCEKLVKEKNIAVVAILHDLN--LASMfcDKILFLKEGEIKYFGTSKELFT 228
Cdd:COG1119 155 RALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEeiPPGI--THVLLLKDGRVVAAGPKEEVLT 232
|
250
....*....|....*...
gi 919308723 229 QEILKEIYDLNCEIIYKN 246
Cdd:COG1119 233 SENLSEAFGLPVEVERRD 250
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-216 |
8.80e-42 |
|
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: 140.46 E-value: 8.80e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 3 KIHDLNFTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEFAKICGFVPQ 82
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 83 kselntplkvidvllmskyanlkhafssyskedileikefakdlrlenflersilsLSGGEFQRMLLARALLKKPKILFL 162
Cdd:cd00267 81 --------------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 919308723 163 DEPTSALDLNYAIELLSLCEKLvKEKNIAVVAILHDLNLASMFCDKILFLKEGE 216
Cdd:cd00267 105 DEPTSGLDPASRERLLELLREL-AEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
4-236 |
1.22e-41 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 143.39 E-value: 1.22e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 4 IHDLNFTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEFAKICGFVPQK 83
Cdd:PRK10575 14 LRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 84 SELNTPLKVIDVLLMSKYAnLKHAFSSYSKEDILEIKEFAKDLRLENFLERSILSLSGGEFQRMLLARALLKKPKILFLD 163
Cdd:PRK10575 94 LPAAEGMTVRELVAIGRYP-WHGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLD 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 919308723 164 EPTSALDLNYAIELLSLCEKLVKEKNIAVVAILHDLNLASMFCDKILFLKEGEIKYFGTSKELFTQEILKEIY 236
Cdd:PRK10575 173 EPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETLEQIY 245
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-229 |
1.48e-41 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 148.51 E-value: 1.48e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 1 MLKIHDLNFTYHQ--KDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPN---KGEISLFNTNIKDFSLKEFAK 75
Cdd:COG1123 4 LLEVRDLSVRYPGgdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 76 ICGFVPQ--KSELNtPLKVIDVLlmskyanlkhAFS----SYSKEDILE-IKEFAKDLRLENFLERSILSLSGGEFQRML 148
Cdd:COG1123 84 RIGMVFQdpMTQLN-PVTVGDQI----------AEAlenlGLSRAEARArVLELLEAVGLERRLDRYPHQLSGGQRQRVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 149 LARALLKKPKILFLDEPTSALDLNYAIELLSLCEKLVKEKNIAVVAILHDLNLASMFCDKILFLKEGEIKYFGTSKELFT 228
Cdd:COG1123 153 IAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILA 232
|
.
gi 919308723 229 Q 229
Cdd:COG1123 233 A 233
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-216 |
1.54e-41 |
|
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: 140.40 E-value: 1.54e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 2 LKIHDLNFTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKD--FSLKEFAKICGF 79
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDleDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 80 VPQKSELNTPLKVIDvllmskyaNLkhafssyskedileikefakdlrlenflersILSLSGGEFQRMLLARALLKKPKI 159
Cdd:cd03229 81 VFQDFALFPHLTVLE--------NI-------------------------------ALGLSGGQQQRVALARALAMDPDV 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 919308723 160 LFLDEPTSALDLNYAIELLSLCEKLVKEKNIAVVAILHDLNLASMFCDKILFLKEGE 216
Cdd:cd03229 122 LLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-226 |
2.47e-40 |
|
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: 146.06 E-value: 2.47e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 2 LKIHDLNFTY--HQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEFAKICGF 79
Cdd:COG4987 334 LELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 80 VPQKSEL-NTPLKvidvllmskyANLKHAFSSYSKEDILEIkefAKDLRLENFLER------SIL-----SLSGGEFQRM 147
Cdd:COG4987 414 VPQRPHLfDTTLR----------ENLRLARPDATDEELWAA---LERVGLGDWLAAlpdgldTWLgeggrRLSGGERRRL 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 919308723 148 LLARALLKKPKILFLDEPTSALDLNYAIELLSLCEKLVKEKniAVVAILHDLNLASMFcDKILFLKEGEIKYFGTSKEL 226
Cdd:COG4987 481 ALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGR--TVLLITHRLAGLERM-DRILVLEDGRIVEQGTHEEL 556
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-217 |
6.17e-40 |
|
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: 135.99 E-value: 6.17e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 2 LKIHDLNFTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSlKEFAKICGFVP 81
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEP-EEVKRRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 82 QKSELNTPLKVIDvllmskyanlkhafssyskedileikefakdlrlenflersILSLSGGEFQRMLLARALLKKPKILF 161
Cdd:cd03230 80 EEPSLYENLTVRE-----------------------------------------NLKLSGGMKQRLALAQALLHDPELLI 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 919308723 162 LDEPTSALDLNYAIELLSLCEKLVKEkNIAVVAILHDLNLASMFCDKILFLKEGEI 217
Cdd:cd03230 119 LDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
30-253 |
1.45e-39 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 137.28 E-value: 1.45e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 30 IGILGPNGSGKSTLLkLILKNLSPNKGEISLFNTNIKDFSLKEFAKICGFVPQKSELNTPLKVIDVLLMSKYANLKHAfs 109
Cdd:COG4138 25 IHLIGPNGAGKSTLL-ARMAGLLPGQGEILLNGRPLSDWSAAELARHRAYLSQQQSPPFAMPVFQYLALHQPAGASSE-- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 110 syskEDILEIKEFAKDLRLENFLERSILSLSGGEFQRMLLARALLK-------KPKILFLDEPTSALDLNYAIELLSLCE 182
Cdd:COG4138 102 ----AVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMNSLDVAQQAALDRLLR 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 919308723 183 KLVkEKNIAVVAILHDLNLASMFCDKILFLKEGEIKYFGTSKELFTQEILKEIYDLNCEIIYKNSKPYILA 253
Cdd:COG4138 178 ELC-QQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMTPENLSEVFGVKFRRLEVEGHRWLIP 247
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-235 |
1.88e-38 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 135.25 E-value: 1.88e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 2 LKIHDLNFTYHQKDL--LKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFS-LKEFAKICG 78
Cdd:TIGR04520 1 IEVENVSFSYPESEKpaLKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEEnLWEIRKKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 79 FVPQkselntplkvidvllmskyaNLKHAF-SSYSKEDI---LE------------IKEFAKDLRLENFLERSILSLSGG 142
Cdd:TIGR04520 81 MVFQ--------------------NPDNQFvGATVEDDVafgLEnlgvpreemrkrVDEALKLVGMEDFRDREPHLLSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 143 EFQRMLLARALLKKPKILFLDEPTSALDLNYAIELLSLCEKLVKEKNIAVVAILHDLNLASMfCDKILFLKEGEIKYFGT 222
Cdd:TIGR04520 141 QKQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGT 219
|
250
....*....|....
gi 919308723 223 SKELFTQ-EILKEI 235
Cdd:TIGR04520 220 PREIFSQvELLKEI 233
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
4-218 |
2.27e-38 |
|
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: 133.15 E-value: 2.27e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 4 IHDLNFTY-HQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLfntNIKDFSLKEFAKICGFVPQ 82
Cdd:cd03226 2 IENISFSYkKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILL---NGKPIKAKERRKSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 83 ksELNTPL---KVIDVLLMSkyanLKHAFSSYSK-EDILeikefaKDLRLENFLERSILSLSGGEFQRMLLARALLKKPK 158
Cdd:cd03226 79 --DVDYQLftdSVREELLLG----LKELDAGNEQaETVL------KDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKD 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 159 ILFLDEPTSALDLNYAIELLSLCEKLVKEKNiAVVAILHDLNLASMFCDKILFLKEGEIK 218
Cdd:cd03226 147 LLIFDEPTSGLDYKNMERVGELIRELAAQGK-AVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-221 |
2.43e-38 |
|
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: 133.03 E-value: 2.43e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 2 LKIHDLNFTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEfAKIcGFVP 81
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPER-RNI-GMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 82 QKSELNTPLKVIDVLLmskYAnLKHAFSSysKEDILE-IKEFAKDLRLENFLERSILSLSGGEFQRMLLARALLKKPKIL 160
Cdd:cd03259 79 QDYALFPHLTVAENIA---FG-LKLRGVP--KAEIRArVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 919308723 161 FLDEPTSALDLNYAIELLSLCEKLVKEKNIAVVAILHDLNLASMFCDKILFLKEGEIKYFG 221
Cdd:cd03259 153 LLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-226 |
4.68e-38 |
|
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: 139.89 E-value: 4.68e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 2 LKIHDLNFTYHQ-KDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEFAKICGFV 80
Cdd:COG4988 337 IELEDVSFSYPGgRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 81 PQKSEL--NTplkVIDVLLMSKyanlkhafSSYSKEDILEIkefAKDLRLENFLER------SILS-----LSGGEFQRM 147
Cdd:COG4988 417 PQNPYLfaGT---IRENLRLGR--------PDASDEELEAA---LEAAGLDEFVAAlpdgldTPLGeggrgLSGGQAQRL 482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 919308723 148 LLARALLKKPKILFLDEPTSALDLNYAIELLSLCEKLVKEKNIAVVAilHDLNLAsMFCDKILFLKEGEIKYFGTSKEL 226
Cdd:COG4988 483 ALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILIT--HRLALL-AQADRILVLDDGRIVEQGTHEEL 558
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-226 |
2.46e-37 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 137.99 E-value: 2.46e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 2 LKIHDLNFTYH-QKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEFAKICGFV 80
Cdd:COG1132 340 IEFENVSFSYPgDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 81 PQkselntplkviDVLLMSK--YANLKHAFSSYSKEDILEIkefAKDLRLENFLER------SIL-----SLSGGEFQRM 147
Cdd:COG1132 420 PQ-----------DTFLFSGtiRENIRYGRPDATDEEVEEA---AKAAQAHEFIEAlpdgydTVVgergvNLSGGQRQRI 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 148 LLARALLKKPKILFLDEPTSALDlnYAIELL---SLcEKLVKEKniAVVAILHDLNLAsMFCDKILFLKEGEIKYFGTSK 224
Cdd:COG1132 486 AIARALLKDPPILILDEATSALD--TETEALiqeAL-ERLMKGR--TTIVIAHRLSTI-RNADRILVLDDGRIVEQGTHE 559
|
..
gi 919308723 225 EL 226
Cdd:COG1132 560 EL 561
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
2-227 |
5.19e-37 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 130.53 E-value: 5.19e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 2 LKIHDLNFTYhqKDL-LKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEFAKicGFV 80
Cdd:cd03299 1 LKVENLSKDW--KEFkLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDI--SYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 81 PQKSELNTPLKVIDVLlmsKYAnLKHAFSSySKEDILEIKEFAKDLRLENFLERSILSLSGGEFQRMLLARALLKKPKIL 160
Cdd:cd03299 77 PQNYALFPHMTVYKNI---AYG-LKKRKVD-KKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKIL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 919308723 161 FLDEPTSALDLNYAIELLSLCEKLVKEKNIAVVAILHDLNLASMFCDKILFLKEGEIKYFGTSKELF 227
Cdd:cd03299 152 LLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVF 218
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-228 |
1.00e-36 |
|
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: 129.71 E-value: 1.00e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 1 MLKIHDLNFTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEFAKI---C 77
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELrrrI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 78 GFVPQKSELNTPLKVIDvllmskyaNLkhAF-----SSYSKEDILEIKEFA-KDLRLENFLERSILSLSGGEFQRMLLAR 151
Cdd:COG1127 85 GMLFQGGALFDSLTVFE--------NV--AFplrehTDLSEAEIRELVLEKlELVGLPGAADKMPSELSGGMRKRVALAR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 919308723 152 ALLKKPKILFLDEPTSALDLNYAIELLSLCEKLVKEKNIAVVAILHDLNLASMFCDKILFLKEGEIKYFGTSKELFT 228
Cdd:COG1127 155 ALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLA 231
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
6-226 |
1.11e-36 |
|
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: 129.66 E-value: 1.11e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 6 DLNFTYHQ-KDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEFAKICGFVPQks 84
Cdd:cd03253 5 NVTFAYDPgRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVVPQ-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 85 elNTPLKVIDVLLMSKYANLkhafsSYSKEDILEIKEFAK-DLRLENFL--------ERSiLSLSGGEFQRMLLARALLK 155
Cdd:cd03253 83 --DTVLFNDTIGYNIRYGRP-----DATDEEVIEAAKAAQiHDKIMRFPdgydtivgERG-LKLSGGEKQRVAIARAILK 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 919308723 156 KPKILFLDEPTSALDLNYAIELLSLCEKLVKEKNIAVVAilHDLNLAsMFCDKILFLKEGEIKYFGTSKEL 226
Cdd:cd03253 155 NPPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIA--HRLSTI-VNADKIIVLKDGRIVERGTHEEL 222
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
6-228 |
7.58e-36 |
|
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: 127.23 E-value: 7.58e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 6 DLNFTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEFAKI---CGFVPQ 82
Cdd:cd03261 5 GLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLrrrMGMLFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 83 KSELNTPLKVIDvllmskyaNLkhAF-----SSYSKEDILEI-KEFAKDLRLENFLERSILSLSGGEFQRMLLARALLKK 156
Cdd:cd03261 85 SGALFDSLTVFE--------NV--AFplrehTRLSEEEIREIvLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALD 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 919308723 157 PKILFLDEPTSALDLNYAIELLSLCEKLVKEKNIAVVAILHDLNLASMFCDKILFLKEGEIKYFGTSKELFT 228
Cdd:cd03261 155 PELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-217 |
8.70e-35 |
|
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: 122.71 E-value: 8.70e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 2 LKIHDLNFTY--HQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEFAKICGF 79
Cdd:cd03246 1 LEVENVSFRYpgAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 80 VPQkselntplkviDVLLmskyanlkhaFSSYSKEDILeikefakdlrlenflersilslSGGEFQRMLLARALLKKPKI 159
Cdd:cd03246 81 LPQ-----------DDEL----------FSGSIAENIL----------------------SGGQRQRLGLARALYGNPRI 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 919308723 160 LFLDEPTSALD------LNYAIELLslceklvKEKNIAVVAILHDLNLASMfCDKILFLKEGEI 217
Cdd:cd03246 118 LVLDEPNSHLDvegeraLNQAIAAL-------KAAGATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
17-167 |
1.17e-34 |
|
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: 121.60 E-value: 1.17e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 17 LKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEFAKICGFVPQKSELNTPLKVIDVL 96
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 919308723 97 LMSkyANLKHAFSSYSKEDILEIkefAKDLRLENFLERSIL----SLSGGEFQRMLLARALLKKPKILFLDEPTS 167
Cdd:pfam00005 81 RLG--LLLKGLSKREKDARAEEA---LEKLGLGDLADRPVGerpgTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
7-221 |
7.81e-33 |
|
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: 118.94 E-value: 7.81e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 7 LNFTYHQKDLLKNIHLELkNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISL-----FNTNIKDFSLKEFAKIcGFVP 81
Cdd:cd03297 4 VDIEKRLPDFTLKIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLngtvlFDSRKKINLPPQQRKI-GLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 82 QKSELNTPLKVidvllmskYANLKHAFSSYS-KEDILEIKEFAKDLRLENFLERSILSLSGGEFQRMLLARALLKKPKIL 160
Cdd:cd03297 82 QQYALFPHLNV--------RENLAFGLKRKRnREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 919308723 161 FLDEPTSALDLNYAIELLSLCEKLVKEKNIAVVAILHDLNLASMFCDKILFLKEGEIKYFG 221
Cdd:cd03297 154 LLDEPFSALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-230 |
2.92e-32 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 117.93 E-value: 2.92e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 1 MLKIHDLNFTYHqkDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSlkefakicgfv 80
Cdd:COG3840 1 MLRLDDLTYRYG--DFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALP----------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 81 PQKSelntPLKVI--DVLL---MSKYANLKHAFSS---YSKEDILEIKEFAKDLRLENFLERSILSLSGGEFQRMLLARA 152
Cdd:COG3840 68 PAER----PVSMLfqENNLfphLTVAQNIGLGLRPglkLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARC 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 919308723 153 LLKKPKILFLDEPTSALDLNYAIELLSLCEKLVKEKNIAVVAILHDLNLASMFCDKILFLKEGEIKYFGTSKELFTQE 230
Cdd:COG3840 144 LVRKRPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGE 221
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-212 |
1.10e-31 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 117.14 E-value: 1.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 1 MLKIHDLNFTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEIslfntnIKDFSLKefakiCGFV 80
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI------KRNGKLR-----IGYV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 81 PQKSELNTPLKvidvLLMSKYANLKhafSSYSKEDILEIkefAKDLRLENFLERSILSLSGGEFQRMLLARALLKKPKIL 160
Cdd:PRK09544 73 PQKLYLDTTLP----LTVNRFLRLR---PGTKKEDILPA---LKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLL 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 919308723 161 FLDEPTSALDLNYAIELLSLCEKLVKEKNIAVVAILHDLNLASMFCDKILFL 212
Cdd:PRK09544 143 VLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCL 194
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-226 |
1.67e-31 |
|
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: 115.74 E-value: 1.67e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 2 LKIHDLNFTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLI--LKNLSPNK---GEISLFNTNI--KDFSLKEFA 74
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLnrLNDLIPGApdeGEVLLDGKDIydLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 75 KICGFVPQKSelnTPLKvidvllMSKYANLkhafsSYSKEDILEIKEFAKDLRLENFLER-----------SILSLSGGE 143
Cdd:cd03260 81 RRVGMVFQKP---NPFP------GSIYDNV-----AYGLRLHGIKLKEELDERVEEALRKaalwdevkdrlHALGLSGGQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 144 FQRMLLARALLKKPKILFLDEPTSALDlnyAIELLSLcEKLVKE--KNIAVVAILHDLNLASMFCDKILFLKEGEIKYFG 221
Cdd:cd03260 147 QQRLCLARALANEPEVLLLDEPTSALD---PISTAKI-EELIAElkKEYTIVIVTHNMQQAARVADRTAFLLNGRLVEFG 222
|
....*
gi 919308723 222 TSKEL 226
Cdd:cd03260 223 PTEQI 227
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-221 |
2.52e-31 |
|
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: 114.98 E-value: 2.52e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 2 LKIHDLNFTYHQKDLLKNIHLELKNqAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDfSLKEFAKICGFVP 81
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGP-GMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 82 QKSELNTPLKVIDVLlmsKY-ANLKHAFSSYSKEDILEIKEfakDLRLENFLERSILSLSGGEFQRMLLARALLKKPKIL 160
Cdd:cd03264 79 QEFGVYPNFTVREFL---DYiAWLKGIPSKEVKARVDEVLE---LVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSIL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 919308723 161 FLDEPTSALDLNYAIELLSLCEKLVKEKniavVAIL--HDLNLASMFCDKILFLKEGEIKYFG 221
Cdd:cd03264 153 IVDEPTAGLDPEERIRFRNLLSELGEDR----IVILstHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-202 |
4.36e-31 |
|
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: 114.11 E-value: 4.36e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 1 MLKIHDLNFTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDfSLKEFAKICGFV 80
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD-AREDYRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 81 PQKSELNTPLKVIDvllmskyaNLKHAFSSY-SKEDILEIKEFAKDLRLENFLERSILSLSGGEFQRMLLARALLKKPKI 159
Cdd:COG4133 81 GHADGLKPELTVRE--------NLRFWAALYgLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 919308723 160 LFLDEPTSALDLNyAIELL-SLCEKLVKEKNIAVVAILHDLNLA 202
Cdd:COG4133 153 WLLDEPFTALDAA-GVALLaELIAAHLARGGAVLLTTHQPLELA 195
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
32-252 |
4.71e-31 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 115.42 E-value: 4.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 32 ILGPNGSGKSTLLKLIlKNLSPNKGEISLFNTNIKDFSLKEFAKICGFVPQKSelnTPLKVIDV---LLMSKYANLkhaf 108
Cdd:PRK03695 27 LVGPNGAGKSTLLARM-AGLLPGSGSIQFAGQPLEAWSAAELARHRAYLSQQQ---TPPFAMPVfqyLTLHQPDKT---- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 109 SSYSKEDILEikEFAKDLRLENFLERSILSLSGGEFQRMLLARALLK-----KP--KILFLDEPTSALDLNYAIELLSLC 181
Cdd:PRK03695 99 RTEAVASALN--EVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdiNPagQLLLLDEPMNSLDVAQQAALDRLL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 919308723 182 EKLVkEKNIAVVAILHDLNLASMFCDKILFLKEGEIKYFGTSKELFTQEILKEIYDLNCEIIYKNSKPYIL 252
Cdd:PRK03695 177 SELC-QQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPENLAQVFGVNFRRLDVEGHPMLI 246
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-217 |
8.19e-31 |
|
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: 113.78 E-value: 8.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 2 LKIHDLNFTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLIlkNL--SPNKGEISLFNTNIkDFSLKEFAKI--- 76
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCI--NLleEPDSGTIIIDGLKL-TDDKKNINELrqk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 77 CGFVPQKSEL--------NTPLKVIDVLLMSKYANLKHAfssyskEDILEikefakDLRLENFLERSILSLSGGEFQRML 148
Cdd:cd03262 78 VGMVFQQFNLfphltvleNITLAPIKVKGMSKAEAEERA------LELLE------KVGLADKADAYPAQLSGGQQQRVA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 919308723 149 LARALLKKPKILFLDEPTSALDLNYAIELLSLCEKLVKEKnIAVVAILHDLNLASMFCDKILFLKEGEI 217
Cdd:cd03262 146 IARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEG-MTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-217 |
1.07e-30 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 113.61 E-value: 1.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 1 MLKIHDLNFTYHQ-KDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEFA----K 75
Cdd:COG2884 1 MIRFENVSKRYPGgREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPylrrR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 76 IcGFVPQkselntplkviDV-LLMSK--YANLkhAF----SSYSKEDILE-IKEFAKDLRLENFLERSILSLSGGEFQRM 147
Cdd:COG2884 81 I-GVVFQ-----------DFrLLPDRtvYENV--ALplrvTGKSRKEIRRrVREVLDLVGLSDKAKALPHELSGGEQQRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 148 LLARALLKKPKILFLDEPTSALDLNYAIELLSLCEKLvKEKNIAVVAILHDLNLASMFCDKILFLKEGEI 217
Cdd:COG2884 147 AIARALVNRPELLLADEPTGNLDPETSWEIMELLEEI-NRRGTTVLIATHDLELVDRMPKRVLELEDGRL 215
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
3-229 |
1.48e-30 |
|
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: 113.47 E-value: 1.48e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 3 KIHDLNFTY-HQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEFAKICGFVP 81
Cdd:cd03254 4 EFENVNFSYdEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 82 QkselntplkviDVLLMSK--YANLKHaFSSYSKEDilEIKEFAKDLRLENFLERSI-----------LSLSGGEFQRML 148
Cdd:cd03254 84 Q-----------DTFLFSGtiMENIRL-GRPNATDE--EVIEAAKEAGAHDFIMKLPngydtvlgengGNLSQGERQLLA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 149 LARALLKKPKILFLDEPTSALDlnyaiellSLCEKLVKE------KNIAVVAILHDLNLASmFCDKILFLKEGEIKYFGT 222
Cdd:cd03254 150 IARAMLRDPKILILDEATSNID--------TETEKLIQEaleklmKGRTSIIIAHRLSTIK-NADKILVLDDGKIIEEGT 220
|
....*..
gi 919308723 223 SKELFTQ 229
Cdd:cd03254 221 HDELLAK 227
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-226 |
2.45e-30 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 112.60 E-value: 2.45e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 2 LKIHDLNFTYHQKDL--LKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEFAKIcGF 79
Cdd:cd03263 1 LQIRNLTKTYKKGTKpaVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSL-GY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 80 VPQKSELNTPLKVIDVLLMskYANLKHafssYSKEDI-LEIKEFAKDLRLENFLERSILSLSGGEfQRML-LARALLKKP 157
Cdd:cd03263 80 CPQFDALFDELTVREHLRF--YARLKG----LPKSEIkEEVELLLRVLGLTDKANKRARTLSGGM-KRKLsLAIALIGGP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 919308723 158 KILFLDEPTSALDLNYAIELLSLCEKLVKEKNIavvaIL--HDLNLASMFCDKILFLKEGEIKYFGTSKEL 226
Cdd:cd03263 153 SVLLLDEPTSGLDPASRRAIWDLILEVRKGRSI----ILttHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-227 |
2.52e-30 |
|
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: 113.06 E-value: 2.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 1 MLKIHDLNFTYHQKD----LLKNIHLELKNQAFIGILGPNGSGKSTLLKLIlkNL--SPNKGEISLFNTNIKDFS---LK 71
Cdd:cd03258 1 MIELKNVSKVFGDTGgkvtALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCI--NGleRPTSGSVLVDGTDLTLLSgkeLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 72 EFAKICGFVPQKSELNTPLKVID-VLLMSKYANLKHAfssYSKEDILEIKEFakdLRLENFLERSILSLSGGEFQRMLLA 150
Cdd:cd03258 79 KARRRIGMIFQHFNLLSSRTVFEnVALPLEIAGVPKA---EIEERVLELLEL---VGLEDKADAYPAQLSGGQKQRVGIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 919308723 151 RALLKKPKILFLDEPTSALDLNYAIELLSLCEKLVKEKNIAVVAILHDLNLASMFCDKILFLKEGEIKYFGTSKELF 227
Cdd:cd03258 153 RALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVF 229
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-229 |
5.32e-30 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 114.81 E-value: 5.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 1 MLKIHDLNFTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDfsLKEFAKICGFV 80
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTG--LPPEKRNVGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 81 PQkselntplkviDVLL---MSKYAN----LKHAfsSYSKEDILE-IKEFAKDLRLENFLERSILSLSGGEFQRMLLARA 152
Cdd:COG3842 83 FQ-----------DYALfphLTVAENvafgLRMR--GVPKAEIRArVAELLELVGLEGLADRYPHQLSGGQQQRVALARA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 919308723 153 LLKKPKILFLDEPTSALDLNYAIELLSLCEKLVKEKNIAVVAILHDLNLASMFCDKILFLKEGEIKYFGTSKELFTQ 229
Cdd:COG3842 150 LAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYER 226
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
4-230 |
5.99e-30 |
|
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: 112.25 E-value: 5.99e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 4 IHDLNFTYHQK---DLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEFAKICGFV 80
Cdd:cd03249 3 FKNVSFRYPSRpdvPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGLV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 81 PQKSELntplkvidvLLMSKYANLKhafssYSKEDI--LEIKEFAKDLRLENFL------------ERSiLSLSGGEFQR 146
Cdd:cd03249 83 SQEPVL---------FDGTIAENIR-----YGKPDAtdEEVEEAAKKANIHDFImslpdgydtlvgERG-SQLSGGQKQR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 147 MLLARALLKKPKILFLDEPTSALDlnyaiellSLCEKLVKE------KNIAVVAILHDLNlASMFCDKILFLKEGEIKYF 220
Cdd:cd03249 148 IAIARALLRNPKILLLDEATSALD--------AESEKLVQEaldramKGRTTIVIAHRLS-TIRNADLIAVLQNGQVVEQ 218
|
250
....*....|
gi 919308723 221 GTSKELFTQE 230
Cdd:cd03249 219 GTHDELMAQK 228
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-221 |
7.61e-30 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 110.10 E-value: 7.61e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 2 LKIHDLNFTYHQKD--LLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSlKEFAKICGF 79
Cdd:cd03247 1 LSINNVSFSYPEQEqqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 80 VPQKSELntplkvidvllmskyanlkhafssyskedileikeFAKDLRlENFLERsilsLSGGEFQRMLLARALLKKPKI 159
Cdd:cd03247 80 LNQRPYL-----------------------------------FDTTLR-NNLGRR----FSGGERQRLALARILLQDAPI 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 919308723 160 LFLDEPTSALDLNYAIELLSLCEKLVKEKNIavVAILHDLNLASMFcDKILFLKEGEIKYFG 221
Cdd:cd03247 120 VLLDEPTVGLDPITERQLLSLIFEVLKDKTL--IWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-220 |
7.87e-30 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 116.70 E-value: 7.87e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 4 IHDLNFTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLfNTNIKdfslkefakiCGFVPQK 83
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI-PKGLR----------IGYLPQE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 84 SELNTPLKVIDVLLMS---------KYANLKHAFSSYSKEDIL------------------EIKEFAKDLRL-ENFLERS 135
Cdd:COG0488 70 PPLDDDLTVLDTVLDGdaelraleaELEELEAKLAEPDEDLERlaelqeefealggweaeaRAEEILSGLGFpEEDLDRP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 136 ILSLSGGEFQRMLLARALLKKPKILFLDEPTSALDLNyAIELLslcEKLVKEKNIAVVAILHD---LNLAsmfCDKILFL 212
Cdd:COG0488 150 VSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLE-SIEWL---EEFLKNYPGTVLVVSHDryfLDRV---ATRILEL 222
|
....*...
gi 919308723 213 KEGEIKYF 220
Cdd:COG0488 223 DRGKLTLY 230
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
2-226 |
9.42e-30 |
|
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: 110.99 E-value: 9.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 2 LKIHDLNFTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEFAK--IcGF 79
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARagI-GY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 80 VPQKSELNTPLKVIDVLLMSKYANLKHAFssysKEDIleikEFAKDL--RLENFLERSILSLSGGEfQRML-LARALLKK 156
Cdd:cd03224 80 VPEGRRIFPELTVEENLLLGAYARRRAKR----KARL----ERVYELfpRLKERRKQLAGTLSGGE-QQMLaIARALMSR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 157 PKILFLDEPTSALDLNYAIELLSLCEKLvKEKNIAVVAILHDLNLASMFCDKILFLKEGEIKYFGTSKEL 226
Cdd:cd03224 151 PKLLLLDEPSEGLAPKIVEEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-229 |
9.78e-30 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 114.09 E-value: 9.78e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 2 LKIHDLNFTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLI--LknLSPNKGEISL----FNTNIkdfSLKEfaK 75
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIagL--ETPDSGRIVLngrdLFTNL---PPRE--R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 76 ICGFVPQkselntplkviDVLL---MSKYANLkhAF----SSYSKEDILE-IKEFAKDLRLENFLERSILSLSGGEFQRM 147
Cdd:COG1118 76 RVGFVFQ-----------HYALfphMTVAENI--AFglrvRPPSKAEIRArVEELLELVQLEGLADRYPSQLSGGQRQRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 148 LLARALLKKPKILFLDEPTSALDLNYAIELLSLCEKLVKEKNIAVVAILHDLNLASMFCDKILFLKEGEIKYFGTSKELF 227
Cdd:COG1118 143 ALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVY 222
|
..
gi 919308723 228 TQ 229
Cdd:COG1118 223 DR 224
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-229 |
1.47e-29 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 111.26 E-value: 1.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 2 LKIHDLNFTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLIlkNL--SPNKGEISL------FNTNIKDFSLKEF 73
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVL--NLleTPDSGQLNIaghqfdFSQKPSEKAIRLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 74 AKICGFVPQKSELNTPLKVID--------VLLMSKyanlkhafssysKEDILEIKEFAKDLRLENFLERSILSLSGGEFQ 145
Cdd:COG4161 81 RQKVGMVFQQYNLWPHLTVMEnlieapckVLGLSK------------EQAREKAMKLLARLRLTDKADRFPLHLSGGQQQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 146 RMLLARALLKKPKILFLDEPTSALDLNYAIELLSLCEKLvKEKNIAVVAILHDLNLASMFCDKILFLKEGEIKYFGTSkE 225
Cdd:COG4161 149 RVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIREL-SQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDA-S 226
|
....
gi 919308723 226 LFTQ 229
Cdd:COG4161 227 HFTQ 230
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
11-203 |
2.44e-29 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 109.25 E-value: 2.44e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 11 YHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISlfntnikdfslKEFAKICGFVPQKSELNT-- 88
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVR-----------RAGGARVAYVPQRSEVPDsl 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 89 PLKVIDVLLMSKYANLKhAFSSYSKEDILEIKEFAKDLRLENFLERSILSLSGGEFQRMLLARALLKKPKILFLDEPTSA 168
Cdd:NF040873 71 PLTVRDLVAMGRWARRG-LWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTG 149
|
170 180 190
....*....|....*....|....*....|....*
gi 919308723 169 LDLNYAIELLSLCEKLVKEKnIAVVAILHDLNLAS 203
Cdd:NF040873 150 LDAESRERIIALLAEEHARG-ATVVVVTHDLELVR 183
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
1-217 |
2.76e-29 |
|
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: 111.05 E-value: 2.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 1 MLKIHDLNFTY--------HQ-KDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFN---TNIKDF 68
Cdd:TIGR02769 2 LLEVRDVTHTYrtgglfgaKQrAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGqdlYQLDRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 69 SLKEFAKICGFVPQK--SELNtPLKVIDVLLMSKYANLKHAFSSYSKEDILEIKEfAKDLRLENfLERSILSLSGGEFQR 146
Cdd:TIGR02769 82 QRRAFRRDVQLVFQDspSAVN-PRMTVRQIIGEPLRHLTSLDESEQKARIAELLD-MVGLRSED-ADKLPRQLSGGQLQR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 919308723 147 MLLARALLKKPKILFLDEPTSALDLNYAIELLSLCEKLVKEKNIAVVAILHDLNLASMFCDKILFLKEGEI 217
Cdd:TIGR02769 159 INIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
17-227 |
3.93e-29 |
|
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: 110.12 E-value: 3.93e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 17 LKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEfaKICGFVPQKSELNTPLKVIDVL 96
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE--RNVGFVFQHYALFRHMTVFDNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 97 LMSkyANLKHAFSSYSKEDILE-IKEFAKDLRLENFLERSILSLSGGEFQRMLLARALLKKPKILFLDEPTSALDLNYAI 175
Cdd:cd03296 96 AFG--LRVKPRSERPPEAEIRAkVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRK 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 919308723 176 ELLSLCEKLVKEKNIAVVAILHDLNLASMFCDKILFLKEGEIKYFGTSKELF 227
Cdd:cd03296 174 ELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVY 225
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-236 |
6.80e-29 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 109.30 E-value: 6.80e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 1 MLKIHDLNFTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEFAK--IcG 78
Cdd:COG0410 3 MLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARlgI-G 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 79 FVPQKSELNTPLKVIDVLLMSkyanlkhAFSSYSKEDILEIKEFAKDL--RLENFLERSILSLSGGEfQRML-LARALLK 155
Cdd:COG0410 82 YVPEGRRIFPSLTVEENLLLG-------AYARRDRAEVRADLERVYELfpRLKERRRQRAGTLSGGE-QQMLaIGRALMS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 156 KPKILFLDEPTSALDLNYAIELLSLCEKLVKEKniavVAIL---HDLNLASMFCDKILFLKEGEIKYFGTSKELFTQEIL 232
Cdd:COG0410 154 RPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREG----VTILlveQNARFALEIADRAYVLERGRIVLEGTAAELLADPEV 229
|
....
gi 919308723 233 KEIY 236
Cdd:COG0410 230 REAY 233
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1-236 |
6.92e-29 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 110.30 E-value: 6.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 1 MLKIHDLNFTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNL----SPN----KGEISLFNTNIKDFSLKE 72
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLtgggAPRgarvTGDVTLNGEPLAAIDAPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 73 FAKICGFVPQKSELNTPLKVIDVLLMSKYANLKHAfSSYSKEDiLEIKEFAKDLR-LENFLERSILSLSGGEFQRMLLAR 151
Cdd:PRK13547 81 LARLRAVLPQAAQPAFAFSAREIVLLGRYPHARRA-GALTHRD-GEIAWQALALAgATALVGRDVTTLSGGELARVQFAR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 152 ALLK---------KPKILFLDEPTSALDLNYAIELLSLCEKLVKEKNIAVVAILHDLNLASMFCDKILFLKEGEIKYFGT 222
Cdd:PRK13547 159 VLAQlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGA 238
|
250
....*....|....
gi 919308723 223 SKELFTQEILKEIY 236
Cdd:PRK13547 239 PADVLTPAHIARCY 252
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-230 |
8.06e-29 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 108.86 E-value: 8.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 2 LKIHDLNFTY--HQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEFAKICGF 79
Cdd:cd03251 1 VEFKNVTFRYpgDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 80 VPQkselntplkviDVLLMSK--YANLKHAFSSYSKEDILEIKEFAKDL----RLENFLERSI----LSLSGGEFQRMLL 149
Cdd:cd03251 81 VSQ-----------DVFLFNDtvAENIAYGRPGATREEVEEAARAANAHefimELPEGYDTVIgergVKLSGGQRQRIAI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 150 ARALLKKPKILFLDEPTSALDLNYAIELLSLCEKLVKEKNIAVVAilHDLNlASMFCDKILFLKEGEIKYFGTSKELFTQ 229
Cdd:cd03251 150 ARALLKDPPILILDEATSALDTESERLVQAALERLMKNRTTFVIA--HRLS-TIENADRIVVLEDGKIVERGTHEELLAQ 226
|
.
gi 919308723 230 E 230
Cdd:cd03251 227 G 227
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
12-221 |
8.32e-29 |
|
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: 108.02 E-value: 8.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 12 HQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLI---LKNLSpNKGEISLfntNIKDFSLKEFAKICGFVPQKSELNT 88
Cdd:cd03213 20 SGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagrRTGLG-VSGEVLI---NGRPLDKRSFRKIIGYVPQDDILHP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 89 PLKVIDVLLMSkyANLKhafssyskedileikefakdlrlenflersilSLSGGEFQRMLLARALLKKPKILFLDEPTSA 168
Cdd:cd03213 96 TLTVRETLMFA--AKLR--------------------------------GLSGGERKRVSIALELVSNPSLLFLDEPTSG 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 919308723 169 LDLNYAIELLSLCEKLVKEkNIAVVAILHDLNlASMF--CDKILFLKEGEIKYFG 221
Cdd:cd03213 142 LDSSSALQVMSLLRRLADT-GRTIICSIHQPS-SEIFelFDKLLLLSQGRVIYFG 194
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
13-235 |
1.09e-28 |
|
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: 113.69 E-value: 1.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 13 QKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEFAKICGFVPQKSEL------ 86
Cdd:COG4618 344 KRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELfdgtia 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 87 -N-------TPLKVIDVllmSKYANLkHAFssyskedileIkefakdLRLENFLERSI----LSLSGGEFQRMLLARALL 154
Cdd:COG4618 424 eNiarfgdaDPEKVVAA---AKLAGV-HEM----------I------LRLPDGYDTRIgeggARLSGGQRQRIGLARALY 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 155 KKPKILFLDEPTSALD------LNYAIELLslceklvKEKNIAVVAILHDLNLASMfCDKILFLKEGEIKYFGTskelfT 228
Cdd:COG4618 484 GDPRLVVLDEPNSNLDdegeaaLAAAIRAL-------KARGATVVVITHRPSLLAA-VDKLLVLRDGRVQAFGP-----R 550
|
....*..
gi 919308723 229 QEILKEI 235
Cdd:COG4618 551 DEVLARL 557
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
6-217 |
1.18e-28 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 108.06 E-value: 1.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 6 DLNFTY--HQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEFAKICGFVPQK 83
Cdd:cd03245 7 NVSFSYpnQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGYVPQD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 84 SELntplkvidvLLMSKYANLKHAFSSYSKEDILEIKEFA--KDL--RLENFLERSI----LSLSGGEFQRMLLARALLK 155
Cdd:cd03245 87 VTL---------FYGTLRDNITLGAPLADDERILRAAELAgvTDFvnKHPNGLDLQIgergRGLSGGQRQAVALARALLN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 919308723 156 KPKILFLDEPTSALDLNYAIELLSLCEKLVKEKniAVVAILHDLNLASMfCDKILFLKEGEI 217
Cdd:cd03245 158 DPPILLLDEPTSAMDMNSEERLKERLRQLLGDK--TLIIITHRPSLLDL-VDRIIVMDSGRI 216
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-230 |
1.34e-28 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 113.38 E-value: 1.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 2 LKIHDLNFTYHQKDL--LKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEFAKICGF 79
Cdd:PRK11160 339 LTLNNVSFTYPDQPQpvLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 80 VPQKSelntplkvidvllmskyanlkHAFSSYSKEDILEIKEFAKDLRLENFLERSILS-------------------LS 140
Cdd:PRK11160 419 VSQRV---------------------HLFSATLRDNLLLAAPNASDEALIEVLQQVGLEklleddkglnawlgeggrqLS 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 141 GGEFQRMLLARALLKKPKILFLDEPTSALDLNYAIELLSLCEKLVKEKniAVVAILHDLN-LASMfcDKILFLKEGEIKY 219
Cdd:PRK11160 478 GGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNK--TVLMITHRLTgLEQF--DRICVMDNGQIIE 553
|
250
....*....|.
gi 919308723 220 FGTSKELFTQE 230
Cdd:PRK11160 554 QGTHQELLAQQ 564
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-248 |
1.77e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 108.92 E-value: 1.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 1 MLKIHDLNFTYH--QKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEFAKICG 78
Cdd:PRK13632 7 MIKVENVSFSYPnsENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 79 FVPQkselntplkvidvllmskyaNLKHAF-SSYSKEDI---LE------------IKEFAKDLRLENFLERSILSLSGG 142
Cdd:PRK13632 87 IIFQ--------------------NPDNQFiGATVEDDIafgLEnkkvppkkmkdiIDDLAKKVGMEDYLDKEPQNLSGG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 143 EFQRMLLARALLKKPKILFLDEPTSALDLNYAIELLSLCEKLVKEKNIAVVAILHDLNLAsMFCDKILFLKEGEIKYFGT 222
Cdd:PRK13632 147 QKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEA-ILADKVIVFSEGKLIAQGK 225
|
250 260
....*....|....*....|....*.
gi 919308723 223 SKELFTQEILKEIYDLNCEIIYKNSK 248
Cdd:PRK13632 226 PKEILNNKEILEKAKIDSPFIYKLSK 251
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-227 |
2.35e-28 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 110.55 E-value: 2.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 1 MLKIHDLNFTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLI--LknLSPNKGEISLFNTNIKDFSLKE--FAki 76
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIagL--EDPTSGEILIGGRDVTDLPPKDrnIA-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 77 cgFVPQKselntplkvidvllmskYANLKH-------AFS----SYSKEDILE-IKEFAKDLRLENFLERSILSLSGGEF 144
Cdd:COG3839 79 --MVFQS-----------------YALYPHmtvyeniAFPlklrKVPKAEIDRrVREAAELLGLEDLLDRKPKQLSGGQR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 145 QRMLLARALLKKPKILFLDEPTSALDlnyA-------IELLslceKLVKEKNIAVVAILHDLNLASMFCDKILFLKEGEI 217
Cdd:COG3839 140 QRVALGRALVREPKVFLLDEPLSNLD---AklrvemrAEIK----RLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRI 212
|
250
....*....|
gi 919308723 218 KYFGTSKELF 227
Cdd:COG3839 213 QQVGTPEELY 222
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-257 |
2.50e-28 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 108.95 E-value: 2.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 2 LKIHDLNFTYHQKD--LLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEFAKICGF 79
Cdd:PRK13635 6 IRVEHISFRYPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 80 VPQKSE---LNTPLKvIDVllmskyanlkhAFS----SYSKEDILE-IKEFAKDLRLENFLERSILSLSGGEFQRMLLAR 151
Cdd:PRK13635 86 VFQNPDnqfVGATVQ-DDV-----------AFGleniGVPREEMVErVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 152 ALLKKPKILFLDEPTSALDLNYAIELLSLCEKLVKEKNIAVVAILHDLNLASmFCDKILFLKEGEIKYFGTSKELFTQ-E 230
Cdd:PRK13635 154 VLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAA-QADRVIVMNKGEILEEGTPEEIFKSgH 232
|
250 260
....*....|....*....|....*...
gi 919308723 231 ILKEI-YDLnceiiyknskPYILALKEK 257
Cdd:PRK13635 233 MLQEIgLDV----------PFSVKLKEL 250
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1-231 |
2.54e-28 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 107.75 E-value: 2.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 1 MLKIHDLNFTYHQKDLLKNIHLELKNQafIGILGPNGSGKSTLLKLILKNLSPNKGEISLfntNIKDFSLKEFAKicgfV 80
Cdd:PRK10771 1 MLKLTDITWLYHHLPMRFDLTVERGER--VAILGPSGAGKSTLLNLIAGFLTPASGSLTL---NGQDHTTTPPSR----R 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 81 P-----QKSELNTPLKVIDVLLMSKYANLKhaFSSYSKEDILEIkefAKDLRLENFLERSILSLSGGEFQRMLLARALLK 155
Cdd:PRK10771 72 PvsmlfQENNLFSHLTVAQNIGLGLNPGLK--LNAAQREKLHAI---ARQMGIEDLLARLPGQLSGGQRQRVALARCLVR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 919308723 156 KPKILFLDEPTSALDLNYAIELLSLCEKLVKEKNIAVVAILHDLNLASMFCDKILFLKEGEIKYFGTSKELFTQEI 231
Cdd:PRK10771 147 EQPILLLDEPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLSGKA 222
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-221 |
2.78e-28 |
|
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: 106.96 E-value: 2.78e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 2 LKIHDLNFTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEfaKICGFVP 81
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD--RDIAMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 82 QKSELNTPlkvidvllMSKYANLKHAFSS--YSKEDILE-IKEFAKDLRLENFLERSILSLSGGEFQRMLLARALLKKPK 158
Cdd:cd03301 79 QNYALYPH--------MTVYDNIAFGLKLrkVPKDEIDErVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPK 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 919308723 159 ILFLDEPTSALDLNYAIELLSLCEKLVKEKNIAVVAILHDLNLASMFCDKILFLKEGEIKYFG 221
Cdd:cd03301 151 VFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-219 |
2.90e-28 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 108.25 E-value: 2.90e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 1 MLKIHDLNFTYH-----QKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKdfSLKEF-- 73
Cdd:COG1101 1 MLELKNLSKTFNpgtvnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVT--KLPEYkr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 74 AKICGFVPQKSELNT-P-LKVIDVLLMSKYANLKHAFS-SYSKEDILEIKEFAKDLR--LENFLERSILSLSGGEFQRML 148
Cdd:COG1101 79 AKYIGRVFQDPMMGTaPsMTIEENLALAYRRGKRRGLRrGLTKKRRELFRELLATLGlgLENRLDTKVGLLSGGQRQALS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 919308723 149 LARALLKKPKILFLDEPTSALDLNYAIELLSLCEKLVKEKNIAVVAILHDLNLASMFCDKILFLKEGEIKY 219
Cdd:COG1101 159 LLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRIIL 229
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-228 |
3.10e-28 |
|
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: 107.77 E-value: 3.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 2 LKIHDLNFTY-HQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEFAKICGFV 80
Cdd:cd03295 1 IEFENVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 81 PQKSELNTPLKVID-VLLMSKyanLKHafssYSKEDILE-IKEFAKDLRLE--NFLERSILSLSGGEFQRMLLARALLKK 156
Cdd:cd03295 81 IQQIGLFPHMTVEEnIALVPK---LLK----WPKEKIRErADELLALVGLDpaEFADRYPHELSGGQQQRVGVARALAAD 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 919308723 157 PKILFLDEPTSALDlnyAIELLSLCE---KLVKEKNIAVVAILHDLNLASMFCDKILFLKEGEIKYFGTSKELFT 228
Cdd:cd03295 154 PPLLLMDEPFGALD---PITRDQLQEefkRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILR 225
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-220 |
4.04e-28 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 111.70 E-value: 4.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 1 MLKIHDLNFTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLfNTNIKdfslkefakiCGFV 80
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK----------IGYF 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 81 PQKSE-LNTPLKVIDvllmskyanlkhafssyskedilEIKEFAKDLR-------LENFL------ERSILSLSGGEFQR 146
Cdd:COG0488 384 DQHQEeLDPDKTVLD-----------------------ELRDGAPGGTeqevrgyLGRFLfsgddaFKPVGVLSGGEKAR 440
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 919308723 147 MLLARALLKKPKILFLDEPTSALDLNyAIELLslcEKLVKEKNIAVVAILHDLNLASMFCDKILFLKEGEIKYF 220
Cdd:COG0488 441 LALAKLLLSPPNVLLLDEPTNHLDIE-TLEAL---EEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVREY 510
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-229 |
5.06e-28 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 107.02 E-value: 5.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 2 LKIHDLNFTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLIlkNL--SPNKGEISL------FNTNIKDFSLKEF 73
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVL--NLleMPRSGTLNIagnhfdFSKTPSDKAIREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 74 AKICGFVPQKSELNTPLKVID--------VLLMSKYANLKHAfssyskedileiKEFAKDLRLENFLERSILSLSGGEFQ 145
Cdd:PRK11124 81 RRNVGMVFQQYNLWPHLTVQQnlieapcrVLGLSKDQALARA------------EKLLERLRLKPYADRFPLHLSGGQQQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 146 RMLLARALLKKPKILFLDEPTSALDLNYAIELLSLCEKLvKEKNIAVVAILHDLNLASMFCDKILFLKEGEIKYFGTsKE 225
Cdd:PRK11124 149 RVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIREL-AETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGD-AS 226
|
....
gi 919308723 226 LFTQ 229
Cdd:PRK11124 227 CFTQ 230
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-229 |
7.71e-28 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 107.04 E-value: 7.71e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 2 LKIHDLNFTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLI--LKNLSPN---KGEISLFNTNI--KDFSLKEFA 74
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrMNDLIPGarvEGEILLDGEDIydPDVDVVELR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 75 KICGFVPQKSelnTPLKvidvllMSKYANLkhAFS-----SYSKEDILEIKEFA----------KDlRLEnfleRSILSL 139
Cdd:COG1117 92 RRVGMVFQKP---NPFP------KSIYDNV--AYGlrlhgIKSKSELDEIVEESlrkaalwdevKD-RLK----KSALGL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 140 SGGEFQRMLLARALLKKPKILFLDEPTSALDlnyAIELLSLcEKLVKE--KNIAVVAILHDLNLASMFCDKILFLKEGEI 217
Cdd:COG1117 156 SGGQQQRLCIARALAVEPEVLLMDEPTSALD---PISTAKI-EELILElkKDYTIVIVTHNMQQAARVSDYTAFFYLGEL 231
|
250
....*....|..
gi 919308723 218 KYFGTSKELFTQ 229
Cdd:COG1117 232 VEFGPTEQIFTN 243
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-253 |
7.92e-28 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 109.27 E-value: 7.92e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 2 LKIHDLNFTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSlkefakicgfvP 81
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVP-----------A 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 82 QKSELNTplkvidvlLMSKYANLKH-------AFS-SYSKEDILEIKEFAKD----LRLENFLERSILSLSGGEFQRMLL 149
Cdd:PRK09452 84 ENRHVNT--------VFQSYALFPHmtvfenvAFGlRMQKTPAAEITPRVMEalrmVQLEEFAQRKPHQLSGGQQQRVAI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 150 ARALLKKPKILFLDEPTSALDLNYAIELLSLCEKLVKEKNIAVVAILHDLNLASMFCDKILFLKEGEIKYFGTSKE---- 225
Cdd:PRK09452 156 ARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREiyee 235
|
250 260 270
....*....|....*....|....*....|.
gi 919308723 226 ---LFTQEILKEIYDLNCEIIYKNSKPYILA 253
Cdd:PRK09452 236 pknLFVARFIGEINIFDATVIERLDEQRVRA 266
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
7-226 |
8.46e-28 |
|
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: 109.05 E-value: 8.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 7 LNFTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEFAKI----CGFVPQ 82
Cdd:TIGR02142 3 ARFSKRLGDFSLDADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLPPekrrIGYVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 83 KSELNTPLKVIDVLLMSkYANLKHAFSSYSKEDILEIkefakdLRLENFLERSILSLSGGEFQRMLLARALLKKPKILFL 162
Cdd:TIGR02142 83 EARLFPHLSVRGNLRYG-MKRARPSERRISFERVIEL------LGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLM 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 919308723 163 DEPTSALDLNYAIELLSLCEKLVKEKNIAVVAILHDLNLASMFCDKILFLKEGEIKYFGTSKEL 226
Cdd:TIGR02142 156 DEPLAALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEV 219
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
11-221 |
1.47e-27 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 105.88 E-value: 1.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 11 YHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLfNTNIKDFSLKEFAKICGFV-PQKSELNTP 89
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV-AGLVPWKRRKKFLRRIGVVfGQKTQLWWD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 90 LKVIDVLLMskyanLKHAFSSYSKEDILEIKEFAKDLRLENFLERSILSLSGGEFQRMLLARALLKKPKILFLDEPTSAL 169
Cdd:cd03267 110 LPVIDSFYL-----LAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGL 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 919308723 170 DLNYAIELLSLCEKLVKEKNIAVVAILHDLNLASMFCDKILFLKEGEIKYFG 221
Cdd:cd03267 185 DVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
10-229 |
1.56e-27 |
|
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: 105.78 E-value: 1.56e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 10 TYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSlkefakicgfvPQKSELNTp 89
Cdd:cd03300 9 FYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLP-----------PHKRPVNT- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 90 lkvidvlLMSKYANLKH-------AF----SSYSKEDI-LEIKEFAKDLRLENFLERSILSLSGGEFQRMLLARALLKKP 157
Cdd:cd03300 77 -------VFQNYALFPHltvfeniAFglrlKKLPKAEIkERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEP 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 919308723 158 KILFLDEPTSALDLNYAIELLSLCEKLVKEKNIAVVAILHDLNLASMFCDKILFLKEGEIKYFGTSKELFTQ 229
Cdd:cd03300 150 KVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEE 221
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-212 |
2.58e-27 |
|
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: 104.86 E-value: 2.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 2 LKIHDLNFTYHQKDL----LKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKefakiC 77
Cdd:cd03293 1 LEVRNVSKTYGGGGGavtaLEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD-----R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 78 GFVPQKSELNTPLKVID-VLLMSKYANLkhafssySKEDILEI-KEFAKDLRLENFLERSILSLSGGEFQRMLLARALLK 155
Cdd:cd03293 76 GYVFQQDALLPWLTVLDnVALGLELQGV-------PKAEARERaEELLELVGLSGFENAYPHQLSGGMRQRVALARALAV 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 919308723 156 KPKILFLDEPTSALDLNYAIELLSLCEKLVKEKNIAVVAILHDLNLASMFCDKILFL 212
Cdd:cd03293 149 DPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-216 |
2.65e-27 |
|
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: 102.53 E-value: 2.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 2 LKIHDLNFTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTnikdfslkefAKIcGFVP 81
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST----------VKI-GYFE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 82 QkselntplkvidvllmskyanlkhafssyskedileikefakdlrlenflersilsLSGGEFQRMLLARALLKKPKILF 161
Cdd:cd03221 70 Q--------------------------------------------------------LSGGEKMRLALAKLLLENPNLLL 93
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 919308723 162 LDEPTSALDLnYAIELLslcEKLVKEKNIAVVAILHDLNLASMFCDKILFLKEGE 216
Cdd:cd03221 94 LDEPTNHLDL-ESIEAL---EEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-229 |
3.00e-27 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 105.08 E-value: 3.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 1 MLKIHDLNFTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLIlkNL--SPNKGEISLFNTNIkDFSLKEFAKIC- 77
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCI--NLleEPDSGTITVDGEDL-TDSKKDINKLRr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 78 --GFVPQKSELNTPLKVID--------VLLMSKyanlkhafssyskediLEIKEFAKDLrlenfLERSILS--------- 138
Cdd:COG1126 78 kvGMVFQQFNLFPHLTVLEnvtlapikVKKMSK----------------AEAEERAMEL-----LERVGLAdkadaypaq 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 139 LSGGEFQRMLLARALLKKPKILFLDEPTSALDLNYAIELLSLCEKLVKEKnIAVVAILHDLNLASMFCDKILFLKEGEIK 218
Cdd:COG1126 137 LSGGQQQRVAIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKEG-MTMVVVTHEMGFAREVADRVVFMDGGRIV 215
|
250
....*....|.
gi 919308723 219 YFGTSKELFTQ 229
Cdd:COG1126 216 EEGPPEEFFEN 226
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-229 |
3.01e-27 |
|
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: 106.68 E-value: 3.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 1 MLKIHDLNFTYHQKD----LLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPN---KGEISLFNTNIKDFSLKEF 73
Cdd:COG0444 1 LLEVRNLKVYFPTRRgvvkAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 74 AKICG----FVPQ--KSELNtPLK-----VIDVLLmskyanlkhAFSSYSKEdilEIKEFAKDLrlenfLER-------S 135
Cdd:COG0444 81 RKIRGreiqMIFQdpMTSLN-PVMtvgdqIAEPLR---------IHGGLSKA---EARERAIEL-----LERvglpdpeR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 136 ILS-----LSGGEFQRMLLARALLKKPKILFLDEPTSALDLNYAIELLSLCEKLVKEKNIAVVAILHDLNLASMFCDKIL 210
Cdd:COG0444 143 RLDrypheLSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVA 222
|
250
....*....|....*....
gi 919308723 211 FLKEGEIKYFGTSKELFTQ 229
Cdd:COG0444 223 VMYAGRIVEEGPVEELFEN 241
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
14-217 |
4.81e-27 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 105.15 E-value: 4.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 14 KDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFS---LKEFAKICGFVPQKS--ELNt 88
Cdd:PRK10419 25 QTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraqRKAFRRDIQMVFQDSisAVN- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 89 PLKVIDVLL---MSKYANLKHAFSSYSKEDILEikefAKDLRLEnFLERSILSLSGGEFQRMLLARALLKKPKILFLDEP 165
Cdd:PRK10419 104 PRKTVREIIrepLRHLLSLDKAERLARASEMLR----AVDLDDS-VLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 919308723 166 TSALDLNYAIELLSLCEKLVKEKNIAVVAILHDLNLASMFCDKILFLKEGEI 217
Cdd:PRK10419 179 VSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
6-226 |
7.34e-27 |
|
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: 103.60 E-value: 7.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 6 DLNFTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEFAKIcGFVPQKSE 85
Cdd:cd03265 5 NLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRI-GIVFQDLS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 86 LNTPLKVID-VLLMSKYANLKhafSSYSKEDILEIKEFakdLRLENFLERSILSLSGGEFQRMLLARALLKKPKILFLDE 164
Cdd:cd03265 84 VDDELTGWEnLYIHARLYGVP---GAERRERIDELLDF---VGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 919308723 165 PTSALDLNYAIELLSLCEKLVKEKNIAVVAILHDLNLASMFCDKILFLKEGEIKYFGTSKEL 226
Cdd:cd03265 158 PTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-218 |
8.62e-27 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 104.40 E-value: 8.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 1 MLKIHDLNFTYHQKD----LLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKefaki 76
Cdd:COG1116 7 ALELRGVSKRFPTGGggvtALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 77 CGFVPQKselntplkviDVLL--MSKYAN----LKHAfsSYSKEDILE-IKEFAKDLRLENFLERSILSLSGGEFQRMLL 149
Cdd:COG1116 82 RGVVFQE----------PALLpwLTVLDNvalgLELR--GVPKAERRErARELLELVGLAGFEDAYPHQLSGGMRQRVAI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 919308723 150 ARALLKKPKILFLDEPTSALDlnyAI---ELLSLCEKLVKEKNIAVVAILHDLNLASMFCDKILFLKE--GEIK 218
Cdd:COG1116 150 ARALANDPEVLLMDEPFGALD---ALtreRLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSArpGRIV 220
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-236 |
2.15e-26 |
|
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: 102.62 E-value: 2.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 2 LKIHDLNFTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEFAKI-CGFV 80
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLgIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 81 PQKSELNTPLKVIDVLLmskyANLKHAFSSYsKEDILEIKEFAKDLRLENFLERSILSLSGGEFQRMLLARALLKKPKIL 160
Cdd:cd03218 81 PQEASIFRKLTVEENIL----AVLEIRGLSK-KEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 919308723 161 FLDEPTSALDLNYAIELLSLCEKLvKEKNIAVVAILHDLNLASMFCDKILFLKEGEIKYFGTSKELFTQEILKEIY 236
Cdd:cd03218 156 LLDEPFAGVDPIAVQDIQKIIKIL-KDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANELVRKVY 230
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-221 |
2.73e-26 |
|
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: 101.59 E-value: 2.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 2 LKIHDLNFTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEIsLFNTNIKDFSLKEfaKIcGFVP 81
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEV-LFDGKPLDIAARN--RI-GYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 82 QKSELNTPLKVIDVLLMskYANLKhafsSYSKEDIL-EIKEFAKDLRLENFLERSILSLSGGEFQRMLLARALLKKPKIL 160
Cdd:cd03269 77 EERGLYPKMKVIDQLVY--LAQLK----GLKKEEARrRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 919308723 161 FLDEPTSALDlNYAIELLSLCEKLVKEKNIAVVAILHDLNLASMFCDKILFLKEGEIKYFG 221
Cdd:cd03269 151 ILDEPFSGLD-PVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
2-235 |
2.83e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 103.59 E-value: 2.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 2 LKIHDLNFTYHQ-----KDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNI--KDFSLKEFA 74
Cdd:PRK13637 3 IKIENLTHIYMEgtpfeKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 75 KICGFVPQKSELNTPLKVIDVLLMSKYANLkhafsSYSKEDILE-IKEFAK--DLRLENFLERSILSLSGGEFQRMLLAR 151
Cdd:PRK13637 83 KKVGLVFQYPEYQLFEETIEKDIAFGPINL-----GLSEEEIENrVKRAMNivGLDYEDYKDKSPFELSGGQKRRVAIAG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 152 ALLKKPKILFLDEPTSALDLNYAIELLSLCEKLVKEKNIAVVAILHDLNLASMFCDKILFLKEGEIKYFGTSKELFTQ-E 230
Cdd:PRK13637 158 VVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKEvE 237
|
....*
gi 919308723 231 ILKEI 235
Cdd:PRK13637 238 TLESI 242
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-222 |
2.84e-26 |
|
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: 101.80 E-value: 2.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 2 LKIHDLNFTY--HQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEFAKICGF 79
Cdd:cd03244 3 IEFKNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 80 VPQkselntplkviDVLLMSKY--ANLKhAFSSYSKEDILEI------KEFAKDL--RLENFLERSILSLSGGEFQRMLL 149
Cdd:cd03244 83 IPQ-----------DPVLFSGTirSNLD-PFGEYSDEELWQAlervglKEFVESLpgGLDTVVEEGGENLSVGQRQLLCL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 919308723 150 ARALLKKPKILFLDEPTSALDlnyaIELLSLCEKLVKE--KNIAVVAILHDLNlASMFCDKILFLKEGEIKYFGT 222
Cdd:cd03244 151 ARALLRKSKILVLDEATASVD----PETDALIQKTIREafKDCTVLTIAHRLD-TIIDSDRILVLDKGRVVEFDS 220
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-222 |
3.54e-26 |
|
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: 101.33 E-value: 3.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 2 LKIHDLNFTY--HQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEFAKICGF 79
Cdd:cd03369 7 IEVENLSVRYapDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 80 VPQKSelntplkvidVLLMSKYANLKHAFSSYSKEDI---LEIKEfakdlrlenflerSILSLSGGEFQRMLLARALLKK 156
Cdd:cd03369 87 IPQDP----------TLFSGTIRSNLDPFDEYSDEEIygaLRVSE-------------GGLNLSQGQRQLLCLARALLKR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 919308723 157 PKILFLDEPTSALDlnYAIEllSLCEKLVKE--KNIAVVAILHDLNlASMFCDKILFLKEGEIKYFGT 222
Cdd:cd03369 144 PRVLVLDEATASID--YATD--ALIQKTIREefTNSTILTIAHRLR-TIIDYDKILVMDAGEVKEYDH 206
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
6-229 |
4.03e-26 |
|
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: 104.41 E-value: 4.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 6 DLNFTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLI--LknLSPNKGEIS-----LFNTNikdfslkefAKIC- 77
Cdd:COG4148 4 EVDFRLRRGGFTLDVDFTLPGRGVTALFGPSGSGKTTLLRAIagL--ERPDSGRIRlggevLQDSA---------RGIFl 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 78 -------GFVPQKSELNTPLKVIDVLLmskYAnLKHAFSSYSKEDILEIKEFakdLRLENFLERSILSLSGGEFQRMLLA 150
Cdd:COG4148 73 pphrrriGYVFQEARLFPHLSVRGNLL---YG-RKRAPRAERRISFDEVVEL---LGIGHLLDRRPATLSGGERQRVAIG 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 919308723 151 RALLKKPKILFLDEPTSALDLNYAIELLSLCEKLVKEKNIAVVAILHDLNLASMFCDKILFLKEGEIKYFGTSKELFTQ 229
Cdd:COG4148 146 RALLSSPRLLLMDEPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSR 224
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-212 |
1.33e-25 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 100.56 E-value: 1.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 1 MLKIHDLNFTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEFAKICGFV 80
Cdd:PRK10247 7 LLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 81 PQkselnTPLKVIDvllmSKYANLKhaFSSYSKEDILEIKEFAKDLRL----ENFLERSILSLSGGEFQRMLLARALLKK 156
Cdd:PRK10247 87 AQ-----TPTLFGD----TVYDNLI--FPWQIRNQQPDPAIFLDDLERfalpDTILTKNIAELSGGEKQRISLIRNLQFM 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 919308723 157 PKILFLDEPTSALDLNYAIELLSLCEKLVKEKNIAVVAILHDLNLASMfCDKILFL 212
Cdd:PRK10247 156 PKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINH-ADKVITL 210
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
14-221 |
1.34e-25 |
|
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: 100.42 E-value: 1.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 14 KDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLI---LKNLSPNKGEISLFNtniKDFSLKEFAKICGFVPQKSELNTPL 90
Cdd:cd03234 20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAIsgrVEGGGTTSGQILFNG---QPRKPDQFQKCVAYVRQDDILLPGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 91 KVIDVLL-MSKYANLKHAFSSYSKE--DILEIKEFAkDLRLENFLERSIlslSGGEFQRMLLARALLKKPKILFLDEPTS 167
Cdd:cd03234 97 TVRETLTyTAILRLPRKSSDAIRKKrvEDVLLRDLA-LTRIGGNLVKGI---SGGERRRVSIAVQLLWDPKVLILDEPTS 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 919308723 168 ALDLNYAIELLSLCEKLVKEKNIAVVAIlHD--LNLASMFcDKILFLKEGEIKYFG 221
Cdd:cd03234 173 GLDSFTALNLVSTLSQLARRNRIVILTI-HQprSDLFRLF-DRILLLSSGEIVYSG 226
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-226 |
1.43e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 101.72 E-value: 1.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 1 MLKIHDLNFTYHQKDLLKNIHLEL-KNQAFiGILGPNGSGKSTLLKLILKNLSPNKGEISLFNtniKDFSLKEFAKIcGF 79
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVpKGEIF-GLLGPNGAGKTTTIRIILGILAPDSGEVLWDG---EPLDPEDRRRI-GY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 80 VPQKSELNTPLKVIDVLLmskY-ANLKHafssYSKEDILE-IKEFAKDLRLENFLERSILSLSGGEFQRMLLARALLKKP 157
Cdd:COG4152 76 LPEERGLYPKMKVGEQLV---YlARLKG----LSKAEAKRrADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDP 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 919308723 158 KILFLDEPTSALD-LNyaIELLslcEKLVKEKNIAVVAIL---HDLNLASMFCDKILFLKEGEIKYFGTSKEL 226
Cdd:COG4152 149 ELLILDEPFSGLDpVN--VELL---KDVIRELAAKGTTVIfssHQMELVEELCDRIVIINKGRKVLSGSVDEI 216
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
2-230 |
2.32e-25 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 104.33 E-value: 2.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 2 LKIHDLNFTYHQKDL--LKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEFAKICGF 79
Cdd:PRK11176 342 IEFRNVTFTYPGKEVpaLRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVAL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 80 VPQKSEL--NTPLKVIdvllmsKYANLKHafssYSKEDILEIKEFAKDL----RLENFLERSI----LSLSGGEFQRMLL 149
Cdd:PRK11176 422 VSQNVHLfnDTIANNI------AYARTEQ----YSREQIEEAARMAYAMdfinKMDNGLDTVIgengVLLSGGQRQRIAI 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 150 ARALLKKPKILFLDEPTSALDLNYAIELLSLCEKLVKEKNIAVVAilHDLNLASMfCDKILFLKEGEIKYFGTSKELFTQ 229
Cdd:PRK11176 492 ARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIA--HRLSTIEK-ADEILVVEDGEIVERGTHAELLAQ 568
|
.
gi 919308723 230 E 230
Cdd:PRK11176 569 N 569
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-228 |
2.65e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 100.50 E-value: 2.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 2 LKIHDLNFTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLI-----LKNLSPNKGEISLFNTNI--KDFSLKEFA 74
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLnrmneLESEVRVEGRVEFFNQNIyeRRVNLNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 75 KICGFVPQKSELntplkvidvLLMSKYANLKHAFS------SYSKEDILEIKEFAKDL--RLENFLERSILSLSGGEFQR 146
Cdd:PRK14258 88 RQVSMVHPKPNL---------FPMSVYDNVAYGVKivgwrpKLEIDDIVESALKDADLwdEIKHKIHKSALDLSGGQQQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 147 MLLARALLKKPKILFLDEPTSALDLNYAIELLSLCEKLVKEKNIAVVAILHDLNLASMFCDKILFLKE-----GEIKYFG 221
Cdd:PRK14258 159 LCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFG 238
|
....*..
gi 919308723 222 TSKELFT 228
Cdd:PRK14258 239 LTKKIFN 245
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-230 |
3.76e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 100.54 E-value: 3.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 1 MLKIHDLNFTYHQ-KDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIK--DFSLKEFAKIC 77
Cdd:PRK13639 1 ILETRDLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKydKKSLLEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 78 GFVPQKS--ELNTPLKVIDVLLMSkyANLKhafssYSKEDILE-IKEFAKDLRLENFLERSILSLSGGEFQRMLLARALL 154
Cdd:PRK13639 81 GIVFQNPddQLFAPTVEEDVAFGP--LNLG-----LSKEEVEKrVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 919308723 155 KKPKILFLDEPTSALDLNYAIELLSLCEKLVKEkNIAVVAILHDLNLASMFCDKILFLKEGEIKYFGTSKELFTQE 230
Cdd:PRK13639 154 MKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDI 228
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
2-227 |
4.40e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 100.48 E-value: 4.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 2 LKIHDLNFTYH-----QKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNI----KDFSLKE 72
Cdd:PRK13634 3 ITFQKVEHRYQyktpfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkKNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 73 FAKICGFVPQKSELN----TPLKVIdvllmskyanlkhAFS----SYSKEDILE-IKEFAKDLRL-ENFLERSILSLSGG 142
Cdd:PRK13634 83 LRKKVGIVFQFPEHQlfeeTVEKDI-------------CFGpmnfGVSEEDAKQkAREMIELVGLpEELLARSPFELSGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 143 EFQRMLLARALLKKPKILFLDEPTSALDLNYAIELLSLCEKLVKEKNIAVVAILHDLNLASMFCDKILFLKEGEIKYFGT 222
Cdd:PRK13634 150 QMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGT 229
|
....*
gi 919308723 223 SKELF 227
Cdd:PRK13634 230 PREIF 234
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-199 |
5.67e-25 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 103.21 E-value: 5.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 2 LKIHDLNFTY-HQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEFAKICGFV 80
Cdd:TIGR02868 335 LELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVC 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 81 PQKSEL-NTPLKvidvllmskyANLKHAFSSYSKEDILEIKEFAkdlRLENFLER------SIL-----SLSGGEFQRML 148
Cdd:TIGR02868 415 AQDAHLfDTTVR----------ENLRLARPDATDEELWAALERV---GLADWLRAlpdgldTVLgeggaRLSGGERQRLA 481
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 919308723 149 LARALLKKPKILFLDEPTSALDLNYAIELLSLCEKLVKEKniAVVAILHDL 199
Cdd:TIGR02868 482 LARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGR--TVVLITHHL 530
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
17-226 |
8.85e-25 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 99.77 E-value: 8.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 17 LKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIkdfsLKEFAKI---CGFVPQKSELNTPLkvi 93
Cdd:TIGR01188 9 VDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDV----VREPRKVrrsIGIVPQYASVDEDL--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 94 dvllmSKYANLK-HA-FSSYSKEDILE-IKEFAKDLRLENFLERSILSLSGGEFQRMLLARALLKKPKILFLDEPTSALD 170
Cdd:TIGR01188 82 -----TGRENLEmMGrLYGLPKDEAEErAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 919308723 171 LNYAIELLSLCEKLVKEKnIAVVAILHDLNLASMFCDKILFLKEGEIKYFGTSKEL 226
Cdd:TIGR01188 157 PRTRRAIWDYIRALKEEG-VTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEEL 211
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
17-217 |
1.32e-24 |
|
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: 97.89 E-value: 1.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 17 LKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEFAKIcG----FvpQKSELNTPLKV 92
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARL-GigrtF--QIPRLFPELTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 93 IDVLLMSKYANLKHAFSS----YSKEDILE-IKEFAKDLRLENFLERSILSLSGGEFQRMLLARALLKKPKILFLDEPTS 167
Cdd:cd03219 93 LENVMVAAQARTGSGLLLararREEREARErAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAA 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 919308723 168 ALDLNYAIELLSLCEKLvKEKNIAVVAILHDLNLASMFCDKILFLKEGEI 217
Cdd:cd03219 173 GLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQGRV 221
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1-221 |
1.80e-24 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 99.95 E-value: 1.80e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 1 MLKIhdlNFTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSlkefAKIC--- 77
Cdd:PRK11144 1 MLEL---NFKQQLGDLCLTVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAE----KGIClpp 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 78 -----GFVPQKSELNTPLKVidvllmskYANLKHAFSSYSKEDILEIKEFakdLRLENFLERSILSLSGGEFQRMLLARA 152
Cdd:PRK11144 74 ekrriGYVFQDARLFPHYKV--------RGNLRYGMAKSMVAQFDKIVAL---LGIEPLLDRYPGSLSGGEKQRVAIGRA 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 919308723 153 LLKKPKILFLDEPTSALDLNYAIELLSLCEKLVKEKNIAVVAILHDLN----LAsmfcDKILFLKEGEIKYFG 221
Cdd:PRK11144 143 LLTAPELLLMDEPLASLDLPRKRELLPYLERLAREINIPILYVSHSLDeilrLA----DRVVVLEQGKVKAFG 211
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-229 |
2.06e-24 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 99.38 E-value: 2.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 1 MLKIHDLNFTYHQKD----LLKNIHLEL-KNQAFiGILGPNGSGKSTLLKLIlkNL--SPNKGEISLFNTNIKDFSLKEF 73
Cdd:COG1135 1 MIELENLSKTFPTKGgpvtALDDVSLTIeKGEIF-GIIGYSGAGKSTLIRCI--NLleRPTSGSVLVDGVDLTALSEREL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 74 ----AKIcGFVPQKSelNtplkvidvLLMSK--YAN----LKHAfsSYSKEdilEIKEFAKDLrlenfLERSILS----- 138
Cdd:COG1135 78 raarRKI-GMIFQHF--N--------LLSSRtvAENvalpLEIA--GVPKA---EIRKRVAEL-----LELVGLSdkada 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 139 ----LSGGEFQRMLLARALLKKPKILFLDEPTSALDLNYAIELLSLCEKLVKEKNIAVVAILHDLNLASMFCDKILFLKE 214
Cdd:COG1135 137 ypsqLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLEN 216
|
250
....*....|....*
gi 919308723 215 GEIKYFGTSKELFTQ 229
Cdd:COG1135 217 GRIVEQGPVLDVFAN 231
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-212 |
2.14e-24 |
|
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: 101.21 E-value: 2.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 2 LKIHDLNFTYHQKD-LLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEFAKICGFV 80
Cdd:TIGR02857 322 LEFSGVSVAYPGRRpALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 81 PQkselnTPLKVIDVLLmskyANLKHAFSSYSKEDILE------IKEFAKDLR--LENFLERSILSLSGGEFQRMLLARA 152
Cdd:TIGR02857 402 PQ-----HPFLFAGTIA----ENIRLARPDASDAEIREaleragLDEFVAALPqgLDTPIGEGGAGLSGGQAQRLALARA 472
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 153 LLKKPKILFLDEPTSALDLNYAIELLSLCEKLVkeKNIAVVAILHDLNLASMfCDKILFL 212
Cdd:TIGR02857 473 FLRDAPLLLLDEPTAHLDAETEAEVLEALRALA--QGRTVLLVTHRLALAAL-ADRIVVL 529
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
7-229 |
2.35e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 99.01 E-value: 2.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 7 LNFTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNI-KDfsLKEFAKICGFV-PQKS 84
Cdd:COG4586 28 FRREYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPfKR--RKEFARRIGVVfGQRS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 85 ELNTPLKVIDVLLMskyanLKHAfssY--SKEDILE-IKEFAKDLRLENFLERSILSLSGGEFQRMLLARALLKKPKILF 161
Cdd:COG4586 106 QLWWDLPAIDSFRL-----LKAI---YriPDAEYKKrLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILF 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 919308723 162 LDEPTSALDLNYAIELLSLCEKLVKEKNIAVVAILHDLNLASMFCDKILFLKEGEIKYFGTSKELFTQ 229
Cdd:COG4586 178 LDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEELKER 245
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-232 |
2.67e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 97.95 E-value: 2.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 1 MLKIHDLNFTYH-QKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEFAKICGF 79
Cdd:PRK13652 3 LIETRDLCYSYSgSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 80 VPQKS--ELNTPLKVIDVLLMSKYANLKHAFSSYSKEDILEIkefakdLRLENFLERSILSLSGGEFQRMLLARALLKKP 157
Cdd:PRK13652 83 VFQNPddQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHM------LGLEELRDRVPHHLSGGEKKRVAIAGVIAMEP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 919308723 158 KILFLDEPTSALDLNYAIELLSLCEKLVKEKNIAVVAILHDLNLASMFCDKILFLKEGEIKYFGTSKELFTQEIL 232
Cdd:PRK13652 157 QVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQPDL 231
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
4-229 |
3.97e-24 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 98.64 E-value: 3.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 4 IHDLNFTYHQKDLLknihlelknqafiGILGPNGSGKS----TLLKLILKNlspnkGEIS---LFN-TNIKDFSLKEFAK 75
Cdd:PRK09473 32 VNDLNFSLRAGETL-------------GIVGESGSGKSqtafALMGLLAAN-----GRIGgsaTFNgREILNLPEKELNK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 76 ICG------FVPQKSELNTPLKV----IDVLLMSKYANLKHAFS-SYSKEDILEIKEFAKDLRL--ENFlersilslSGG 142
Cdd:PRK09473 94 LRAeqismiFQDPMTSLNPYMRVgeqlMEVLMLHKGMSKAEAFEeSVRMLDAVKMPEARKRMKMypHEF--------SGG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 143 EFQRMLLARALLKKPKILFLDEPTSALDLNYAIELLSLCEKLVKEKNIAVVAILHDLNLASMFCDKILFLKEGEIKYFGT 222
Cdd:PRK09473 166 MRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGN 245
|
....*..
gi 919308723 223 SKELFTQ 229
Cdd:PRK09473 246 ARDVFYQ 252
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-236 |
4.92e-24 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 97.01 E-value: 4.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 1 MLKIHDLNFTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLK----LILKNLSPNKGEISLFNTNIKDFSL-----K 71
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRhlsgLITGDKSAGSHIELLGRTVQREGRLardirK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 72 EFAKIcGFVPQKSELNTPLKVIDVLLMSKYANL---KHAFSSYSKEDILEIKEFAKDLRLENFLERSILSLSGGEFQRML 148
Cdd:PRK09984 84 SRANT-GYIFQQFNLVNRLSVLENVLIGALGSTpfwRTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 149 LARALLKKPKILFLDEPTSALDLNYAIELLSLCEKLVKEKNIAVVAILHDLNLASMFCDKILFLKEGEIKYFGTSKElFT 228
Cdd:PRK09984 163 IARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQ-FD 241
|
....*...
gi 919308723 229 QEILKEIY 236
Cdd:PRK09984 242 NERFDHLY 249
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
17-229 |
4.95e-24 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 97.33 E-value: 4.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 17 LKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEFAKI----CGFVPQKSELNTPLKV 92
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELrrkkISMVFQSFALLPHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 93 IDvllmskyaNLkhAFSsyskediLEIKEFAKDLR------------LENFLERSILSLSGGEFQRMLLARALLKKPKIL 160
Cdd:cd03294 120 LE--------NV--AFG-------LEVQGVPRAEReeraaealelvgLEGWEHKYPDELSGGMQQRVGLARALAVDPDIL 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 919308723 161 FLDEPTSALDLNYAIELLSLCEKLVKEKNIAVVAILHDLNLASMFCDKILFLKEGEIKYFGTSKELFTQ 229
Cdd:cd03294 183 LMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
6-226 |
6.15e-24 |
|
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: 100.28 E-value: 6.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 6 DLNFTYH-QKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEFAKICGFVPQks 84
Cdd:COG5265 362 NVSFGYDpERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQ-- 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 85 elntplkviDVLLM--SKYANLKHAFSSYSKEdilEIKEFAKDLRLENFL------------ERSiLSLSGGEFQRMLLA 150
Cdd:COG5265 440 ---------DTVLFndTIAYNIAYGRPDASEE---EVEAAARAAQIHDFIeslpdgydtrvgERG-LKLSGGEKQRVAIA 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 151 RALLKKPKILFLDEPTSALDlnyaiellSLCEKLVKE------KNIAVVAILHDLnlaS--MFCDKILFLKEGEIKYFGT 222
Cdd:COG5265 507 RTLLKNPPILIFDEATSALD--------SRTERAIQAalrevaRGRTTLVIAHRL---StiVDADEILVLEAGRIVERGT 575
|
....
gi 919308723 223 SKEL 226
Cdd:COG5265 576 HAEL 579
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
2-229 |
8.87e-24 |
|
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: 99.81 E-value: 8.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 2 LKIHDLNFTY-HQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEFAKICGFV 80
Cdd:TIGR01193 474 IVINDVSYSYgYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 81 PQKSELNTPlKVIDVLLMSKYANLkhafssySKEDILEIKEFAK-DLRLENF-------LERSILSLSGGEFQRMLLARA 152
Cdd:TIGR01193 554 PQEPYIFSG-SILENLLLGAKENV-------SQDEIWAACEIAEiKDDIENMplgyqteLSEEGSSISGGQKQRIALARA 625
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 919308723 153 LLKKPKILFLDEPTSALDLnyaIELLSLCEKLVKEKNIAVVAILHDLNLASMfCDKILFLKEGEIKYFGTSKELFTQ 229
Cdd:TIGR01193 626 LLTDSKVLILDESTSNLDT---ITEKKIVNNLLNLQDKTIIFVAHRLSVAKQ-SDKIIVLDHGKIIEQGSHDELLDR 698
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-228 |
9.22e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 96.27 E-value: 9.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 1 MLKIHDLNFTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLI--LKNLSPNK----GEISLFNTNIKDFSLKEFA 74
Cdd:PRK14246 10 VFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLnrLIEIYDSKikvdGKVLYFGKDIFQIDAIKLR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 75 KICGFVPQKSELNTPLKVidvllmskYANLKHAFSSYSKEDILEIKEFAKD-LR-------LENFLERSILSLSGGEFQR 146
Cdd:PRK14246 90 KEVGMVFQQPNPFPHLSI--------YDNIAYPLKSHGIKEKREIKKIVEEcLRkvglwkeVYDRLNSPASQLSGGQQQR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 147 MLLARALLKKPKILFLDEPTSALDLNYAIELLSLCEKLVKEknIAVVAILHDLNLASMFCDKILFLKEGEIKYFGTSKEL 226
Cdd:PRK14246 162 LTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEI 239
|
..
gi 919308723 227 FT 228
Cdd:PRK14246 240 FT 241
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
31-221 |
9.40e-24 |
|
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: 95.13 E-value: 9.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 31 GILGPNGSGKSTLLKLILKNLSPNKG--EISLFNTNIKDFSLKefAKIcGFVPQKSELNTPLKVIDVLLMskYANLkHAF 108
Cdd:cd03266 35 GLLGPNGAGKTTTLRMLAGLLEPDAGfaTVDGFDVVKEPAEAR--RRL-GFVSDSTGLYDRLTARENLEY--FAGL-YGL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 109 SSYSKEDilEIKEFAKDLRLENFLERSILSLSGGEFQRMLLARALLKKPKILFLDEPTSALDLNYAIELLSLCEKLvKEK 188
Cdd:cd03266 109 KGDELTA--RLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQL-RAL 185
|
170 180 190
....*....|....*....|....*....|...
gi 919308723 189 NIAVVAILHDLNLASMFCDKILFLKEGEIKYFG 221
Cdd:cd03266 186 GKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
2-229 |
1.70e-23 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 95.42 E-value: 1.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 2 LKIHDLNFTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNI-----KDFSLKEFAKi 76
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlvrdKDGQLKVADK- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 77 cgfvPQKSELNTPLKVI--DVLLMSKYANLKHAFSS------YSKEDILE--IKEFAKDLRLENFLERSILSLSGGEFQR 146
Cdd:PRK10619 85 ----NQLRLLRTRLTMVfqHFNLWSHMTVLENVMEApiqvlgLSKQEAREraVKYLAKVGIDERAQGKYPVHLSGGQQQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 147 MLLARALLKKPKILFLDEPTSALDLNYAIELLSLCEKLVKEKNIAVVaILHDLNLASMFCDKILFLKEGEIKYFGTSKEL 226
Cdd:PRK10619 161 VSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVV-VTHEMGFARHVSSHVIFLHQGKIEEEGAPEQL 239
|
...
gi 919308723 227 FTQ 229
Cdd:PRK10619 240 FGN 242
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
2-229 |
2.05e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 96.00 E-value: 2.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 2 LKIHDLNFTYHQ-----KDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNI----KDFSLKE 72
Cdd:PRK13646 3 IRFDNVSYTYQKgtpyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 73 FAKICGFVPQ--KSELNTPLKVIDVLLMSKYANLkhafssyskeDILEIKEFAKDLRLENFLERSILSLS-----GGEFQ 145
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFEDTVEREIIFGPKNFKM----------NLDEVKNYAHRLLMDLGFSRDVMSQSpfqmsGGQMR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 146 RMLLARALLKKPKILFLDEPTSALDLNYAIELLSLCEKLVKEKNIAVVAILHDLNLASMFCDKILFLKEGEIKYFGTSKE 225
Cdd:PRK13646 153 KIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKE 232
|
....
gi 919308723 226 LFTQ 229
Cdd:PRK13646 233 LFKD 236
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-237 |
2.42e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 94.84 E-value: 2.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 1 MLKIHDLNFTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLI--LKNLSPN---KGEISLFNTNIkdFSLK---- 71
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIVYNGHNI--YSPRtdtv 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 72 EFAKICGFVPQKSelnTPLKvidvllMSKYANLKHAFSSYSKEDILEIKE-FAKDLR-------LENFLERSILSLSGGE 143
Cdd:PRK14239 83 DLRKEIGMVFQQP---NPFP------MSIYENVVYGLRLKGIKDKQVLDEaVEKSLKgasiwdeVKDRLHDSALGLSGGQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 144 FQRMLLARALLKKPKILFLDEPTSALDLNYAIELLSLCEKLVKEKNIAVVAilHDLNLASMFCDKILFLKEGEIKYFGTS 223
Cdd:PRK14239 154 QQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVT--RSMQQASRISDRTGFFLDGDLIEYNDT 231
|
250
....*....|....
gi 919308723 224 KELFTQEILKEIYD 237
Cdd:PRK14239 232 KQMFMNPKHKETED 245
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-217 |
2.69e-23 |
|
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: 94.42 E-value: 2.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 1 MLKIHDLNFTY----HQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIkdFSLKE---- 72
Cdd:COG4181 8 IIELRGLTKTVgtgaGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDL--FALDEdara 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 73 --FAKICGFVPQKSELNTPLKVID-VLLMSKYANLKHAFSsyskedileikefakdlRLENFLERSILS---------LS 140
Cdd:COG4181 86 rlRARHVGFVFQSFQLLPTLTALEnVMLPLELAGRRDARA-----------------RARALLERVGLGhrldhypaqLS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 141 GGEFQRMLLARALLKKPKILFLDEPTSALDLNYA---IELLslcEKLVKEKNIAVVAILHDLNLASMfCDKILFLKEGEI 217
Cdd:COG4181 149 GGEQQRVALARAFATEPAILFADEPTGNLDAATGeqiIDLL---FELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRL 224
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-235 |
3.08e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 95.30 E-value: 3.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 1 MLKIHDLNFTYHQ-KDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEIsLFNTNIKDFSLK---EFAKI 76
Cdd:PRK13636 5 ILKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRI-LFDGKPIDYSRKglmKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 77 CGFVPQKSElntplkvidvllmskyanlKHAFSSYSKEDI------LEIKEFAKDLRLENFLERSILS---------LSG 141
Cdd:PRK13636 84 VGMVFQDPD-------------------NQLFSASVYQDVsfgavnLKLPEDEVRKRVDNALKRTGIEhlkdkpthcLSF 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 142 GEFQRMLLARALLKKPKILFLDEPTSALDLNYAIELLSLCEKLVKEKNIAVVAILHDLNLASMFCDKILFLKEGEIKYFG 221
Cdd:PRK13636 145 GQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQG 224
|
250
....*....|....*
gi 919308723 222 TSKELFT-QEILKEI 235
Cdd:PRK13636 225 NPKEVFAeKEMLRKV 239
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
2-236 |
3.56e-23 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 94.26 E-value: 3.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 2 LKIHDLNFTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEFAKI-CGFV 80
Cdd:TIGR04406 2 LVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARLgIGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 81 PQKSELNTPLKVIDVLLmskyANLKHAFSSYSKEDILEIKEFAKDLRLENFLERSILSLSGGEFQRMLLARALLKKPKIL 160
Cdd:TIGR04406 82 PQEASIFRKLTVEENIM----AVLEIRKDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 919308723 161 FLDEPTSALDLNYAIELLSLCEKLvKEKNIAVVAILHDLNLASMFCDKILFLKEGEIKYFGTSKELFTQEILKEIY 236
Cdd:TIGR04406 158 LLDEPFAGVDPIAVGDIKKIIKHL-KERGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVANEKVRRVY 232
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
30-222 |
3.61e-23 |
|
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: 94.40 E-value: 3.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 30 IGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIkdfSLKefakicgfvPQKSELNTPLKViDVLLMSKYANlkHAFS 109
Cdd:cd03237 28 IGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV---SYK---------PQYIKADYEGTV-RDLLSSITKD--FYTH 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 110 SYSKEDIleikefAKDLRLENFLERSILSLSGGEFQRMLLARALLKKPKILFLDEPTSALDLNYAIELLSLCEKLVKEKN 189
Cdd:cd03237 93 PYFKTEI------AKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENNE 166
|
170 180 190
....*....|....*....|....*....|...
gi 919308723 190 IAVVAILHDLNLASMFCDKILFLkEGEIKYFGT 222
Cdd:cd03237 167 KTAFVVEHDIIMIDYLADRLIVF-EGEPSVNGV 198
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
17-217 |
4.74e-23 |
|
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: 94.34 E-value: 4.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 17 LKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEFAKiCG----FvpQKSELNTPLKV 92
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIAR-LGiartF--QNPRLFPELTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 93 IDVLLMSKYANLKHAF-------SSYSKEDIlEIKEFAKDL----RLENFLERSILSLSGGEfQRML-LARALLKKPKIL 160
Cdd:COG0411 97 LENVLVAAHARLGRGLlaallrlPRARREER-EARERAEELlervGLADRADEPAGNLSYGQ-QRRLeIARALATEPKLL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 919308723 161 FLDEPTSALDLNYAIELLSLCEKLVKEKNIAVVAILHDLNLASMFCDKILFLKEGEI 217
Cdd:COG0411 175 LLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRV 231
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
1-217 |
7.18e-23 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 93.74 E-value: 7.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 1 MLKIHDLNFTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEFAKI---- 76
Cdd:TIGR02323 3 LLQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAELELYQLSEAerrr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 77 -----CGFVPQKSElntplkviDVLLM--SKYANLKHAFSSYSKEDILEIKEFAKDLRLENFLERSIL-----SLSGGEF 144
Cdd:TIGR02323 83 lmrteWGFVHQNPR--------DGLRMrvSAGANIGERLMAIGARHYGNIRATAQDWLEEVEIDPTRIddlprAFSGGMQ 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 919308723 145 QRMLLARALLKKPKILFLDEPTSALDLNYAIELLSLCEKLVKEKNIAVVAILHDLNLASMFCDKILFLKEGEI 217
Cdd:TIGR02323 155 QRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRV 227
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-242 |
7.84e-23 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 95.54 E-value: 7.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 2 LKIHDLNFTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEfaKICGFVP 81
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD--RKVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 82 QKSELNTPLKVID-------VLLMSKYANlkhafSSYSKEDILEIKEFakdLRLENFLERSILSLSGGEFQRMLLARALL 154
Cdd:PRK10851 81 QHYALFRHMTVFDniafgltVLPRRERPN-----AAAIKAKVTQLLEM---VQLAHLADRYPAQLSGGQKQRVALARALA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 155 KKPKILFLDEPTSALDLNYAIELLSLCEKLVKEKNIAVVAILHDLNLASMFCDKILFLKEGEIKYFGTSKEL-------F 227
Cdd:PRK10851 153 VEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVwrepatrF 232
|
250
....*....|....*
gi 919308723 228 TQEILKEIYDLNCEI 242
Cdd:PRK10851 233 VLEFMGEVNRLQGTI 247
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-236 |
1.21e-22 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 94.10 E-value: 1.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 2 LKIHDLNFTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEFAKIcGFVP 81
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRV-GVVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 82 QKSELNTPLKVIDVLLM-SKYANLKhafSSYSKEDILEIKEFAkdlRLENFLERSILSLSGGEFQRMLLARALLKKPKIL 160
Cdd:PRK13537 87 QFDNLDPDFTVRENLLVfGRYFGLS---AAAARALVPPLLEFA---KLENKADAKVGELSGGMKRRLTLARALVNDPDVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 161 FLDEPTSALDLNyAIELL--SLCEKLVKEKNIAVVAilHDLNLASMFCDKILFLKEGEIKYFGTSKELFTQEI---LKEI 235
Cdd:PRK13537 161 VLDEPTTGLDPQ-ARHLMweRLRSLLARGKTILLTT--HFMEEAERLCDRLCVIEEGRKIAEGAPHALIESEIgcdVIEI 237
|
.
gi 919308723 236 Y 236
Cdd:PRK13537 238 Y 238
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
2-217 |
1.41e-22 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 93.20 E-value: 1.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 2 LKIHDLNFTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNT---NIKDFSLKEFakicg 78
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAplaEAREDTRLMF----- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 79 fvpQKSELNTPLKVIDvllmskyaNLKHAFSSYSKEDILEIKEfakDLRLENFLERSILSLSGGEFQRMLLARALLKKPK 158
Cdd:PRK11247 88 ---QDARLLPWKKVID--------NVGLGLKGQWRDAALQALA---AVGLADRANEWPAALSGGQKQRVALARALIHRPG 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 919308723 159 ILFLDEPTSALDLNYAIELLSLCEKLVKEKNIAVVAILHDLNLASMFCDKILFLKEGEI 217
Cdd:PRK11247 154 LLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-200 |
1.79e-22 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 91.77 E-value: 1.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 1 MLKIHDLNFTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPN---KGEISLFNTNIKDfsLKEFAKIC 77
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTA--LPAEQRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 78 GFVPQkselntplkviDVLL---MSKYANLkhAF---SSYSKED-ILEIKEFAKDLRLENFLERSILSLSGGEFQRMLLA 150
Cdd:COG4136 79 GILFQ-----------DDLLfphLSVGENL--AFalpPTIGRAQrRARVEQALEEAGLAGFADRDPATLSGGQRARVALL 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 919308723 151 RALLKKPKILFLDEPTSALDLNYAIELLSLCEKLVKEKNIAVVAILHDLN 200
Cdd:COG4136 146 RALLAEPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEE 195
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
2-216 |
1.87e-22 |
|
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: 91.38 E-value: 1.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 2 LKIHDLNFTYHQKD-----LLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTnikdfslkefaki 76
Cdd:cd03250 1 ISVEDASFTWDSGEqetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 77 CGFVPQKSEL-NTPLKviDVLLMSKYanlkhaFSSYSKEDILEIKEFAKDLRLenfL---------ERSIlSLSGGEFQR 146
Cdd:cd03250 68 IAYVSQEPWIqNGTIR--ENILFGKP------FDEERYEKVIKACALEPDLEI---LpdgdlteigEKGI-NLSGGQKQR 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 919308723 147 MLLARALLKKPKILFLDEPTSALDLNYAIELLS--LCEKLVKEKniAVVAILHDLNLASMfCDKILFLKEGE 216
Cdd:cd03250 136 ISLARAVYSDADIYLLDDPLSAVDAHVGRHIFEncILGLLLNNK--TRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
13-226 |
3.02e-22 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 95.50 E-value: 3.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 13 QKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKlILKNLSPNKGEISLFNT-NIKDFSLKEFAKICGFVpQKSELNTP-L 90
Cdd:TIGR00955 37 RKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMN-ALAFRSPKGVKGSGSVLlNGMPIDAKEMRAISAYV-QQDDLFIPtL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 91 KVIDVLLMSkyANLKHAFSSYSKEDILEIKEFAKDLRLENF------LERSILSLSGGEFQRMLLARALLKKPKILFLDE 164
Cdd:TIGR00955 115 TVREHLMFQ--AHLRMPRRVTKKEKRERVDEVLQALGLRKCantrigVPGRVKGLSGGERKRLAFASELLTDPPLLFCDE 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 919308723 165 PTSALDLNYAIELLSLCEKLVKEKNIAVVAIlHD--LNLASMFcDKILFLKEGEIKYFGTSKEL 226
Cdd:TIGR00955 193 PTSGLDSFMAYSVVQVLKGLAQKGKTIICTI-HQpsSELFELF-DKIILMAEGRVAYLGSPDQA 254
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-235 |
3.03e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 92.51 E-value: 3.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 1 MLKIHDLNFTYhQKD---LLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEFAKIC 77
Cdd:PRK13648 7 IIVFKNVSFQY-QSDasfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 78 GFVPQKSElNTPLKVI---DVllmskyanlkhAFS----SYSKEDILEI-KEFAKDLRLENFLERSILSLSGGEFQRMLL 149
Cdd:PRK13648 86 GIVFQNPD-NQFVGSIvkyDV-----------AFGlenhAVPYDEMHRRvSEALKQVDMLERADYEPNALSGGQKQRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 150 ARALLKKPKILFLDEPTSALDLNYAIELLSLCEKLVKEKNIAVVAILHDLNLAsMFCDKILFLKEGEIKYFGTSKELFT- 228
Cdd:PRK13648 154 AGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEA-MEADHVIVMNKGTVYKEGTPTEIFDh 232
|
....*..
gi 919308723 229 QEILKEI 235
Cdd:PRK13648 233 AEELTRI 239
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
2-236 |
4.11e-22 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 91.49 E-value: 4.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 2 LKIHDLNFTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEFA-KICGFV 80
Cdd:PRK10895 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARArRGIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 81 PQKSELNTPLKVIDVLLmsKYANLKHAFSSYSKEDilEIKEFAKDLRLENFLERSILSLSGGEFQRMLLARALLKKPKIL 160
Cdd:PRK10895 84 PQEASIFRRLSVYDNLM--AVLQIRDDLSAEQRED--RANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 919308723 161 FLDEPTSALDLNYAIELLSLCEKLvKEKNIAVVAILHDLNLASMFCDKILFLKEGEIKYFGTSKELFTQEILKEIY 236
Cdd:PRK10895 160 LLDEPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRVY 234
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
19-229 |
5.06e-22 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 93.25 E-value: 5.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 19 NIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEfAKICgFVPQKSELnTPLkvidvllM 98
Cdd:PRK11432 24 NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQ-RDIC-MVFQSYAL-FPH-------M 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 99 SKYANLKHAFS--SYSKEDILE-IKEFAKDLRLENFLERSILSLSGGEFQRMLLARALLKKPKILFLDEPTSALDLNYAI 175
Cdd:PRK11432 94 SLGENVGYGLKmlGVPKEERKQrVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRR 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 919308723 176 ELLSLCEKLVKEKNIAVVAILHDLNLASMFCDKILFLKEGEIKYFGTSKELFTQ 229
Cdd:PRK11432 174 SMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQ 227
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
15-230 |
6.04e-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: 91.01 E-value: 6.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 15 DLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEFAKICGFVPQKSELntplkvid 94
Cdd:cd03252 16 VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGVVLQENVL-------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 95 vLLMSKYANLKHAFSSYSKEDILEI------KEFAKDLRL--ENFLERSILSLSGGEFQRMLLARALLKKPKILFLDEPT 166
Cdd:cd03252 88 -FNRSIRDNIALADPGMSMERVIEAaklagaHDFISELPEgyDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEAT 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 919308723 167 SALDLNYAIELLSLCEKLVKEKNIAVVAilHDLNlASMFCDKILFLKEGEIKYFGTSKELFTQE 230
Cdd:cd03252 167 SALDYESEHAIMRNMHDICAGRTVIIIA--HRLS-TVKNADRIIVMEKGRIVEQGSHDELLAEN 227
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
30-216 |
8.06e-22 |
|
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: 94.08 E-value: 8.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 30 IGILGPNGSGKSTLLKLILKNLSPNKGEIslfNTNIKdFSLKefakicgfvPQKSELNTPLKVIDVLlmskYANLKHAF- 108
Cdd:COG1245 369 LGIVGPNGIGKTTFAKILAGVLKPDEGEV---DEDLK-ISYK---------PQYISPDYDGTVEEFL----RSANTDDFg 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 109 SSYSKEDIleikefAKDLRLENFLERSILSLSGGEFQRMLLARALLKKPKILFLDEPTSALDLNYAIELLSLCEKLVKEK 188
Cdd:COG1245 432 SSYYKTEI------IKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENR 505
|
170 180
....*....|....*....|....*....
gi 919308723 189 NIAVVAILHDLNLASMFCDKIL-FlkEGE 216
Cdd:COG1245 506 GKTAMVVDHDIYLIDYISDRLMvF--EGE 532
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
31-236 |
8.50e-22 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 92.59 E-value: 8.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 31 GILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEFAKIcGFVPQKSELNTPLKVIDVLLM-SKYANLKhafS 109
Cdd:PRK13536 71 GLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARARI-GVVPQFDNLDLEFTVRENLLVfGRYFGMS---T 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 110 SYSKEDILEIKEFAkdlRLENFLERSILSLSGGEFQRMLLARALLKKPKILFLDEPTSALDlNYAIELL--SLCEKLVKE 187
Cdd:PRK13536 147 REIEAVIPSLLEFA---RLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLD-PHARHLIweRLRSLLARG 222
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 919308723 188 KNIAVVAilHDLNLASMFCDKILFLKEGEIKYFGTSKELFTQEI---LKEIY 236
Cdd:PRK13536 223 KTILLTT--HFMEEAERLCDRLCVLEAGRKIAEGRPHALIDEHIgcqVIEIY 272
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-228 |
8.56e-22 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 90.96 E-value: 8.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 1 MLKIHDLNFTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLIlkNL--SPNKGEISLFNTNI---KDFS-----L 70
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCI--NLleQPEAGTIRVGDITIdtaRSLSqqkglI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 71 KEFAKICGFVPQKSEL---NTPLK-VIDVLLMSKyanlkhafssysKEDILEIKEFAKDLrlenfLERSILS-------- 138
Cdd:PRK11264 81 RQLRQHVGFVFQNFNLfphRTVLEnIIEGPVIVK------------GEPKEEATARAREL-----LAKVGLAgketsypr 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 139 -LSGGEFQRMLLARALLKKPKILFLDEPTSALDLNYAIELLSLCEKLVKEKNIAVVaILHDLNLASMFCDKILFLKEGEI 217
Cdd:PRK11264 144 rLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVI-VTHEMSFARDVADRAIFMDQGRI 222
|
250
....*....|.
gi 919308723 218 KYFGTSKELFT 228
Cdd:PRK11264 223 VEQGPAKALFA 233
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-215 |
9.92e-22 |
|
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: 90.19 E-value: 9.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 1 MLKIHDL--NFTYHQKDL-----LKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEIsLFNTnikDFSLKEF 73
Cdd:COG4778 4 LLEVENLskTFTLHLQGGkrlpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSI-LVRH---DGGWVDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 74 AKI------------CGFV-------PQKSELNTplkVIDVLLMSkyanlkhafsSYSKEdilEIKEFAKDL--RLEnfL 132
Cdd:COG4778 80 AQAspreilalrrrtIGYVsqflrviPRVSALDV---VAEPLLER----------GVDRE---EARARARELlaRLN--L 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 133 ERSILSL-----SGGEFQRMLLARALLKKPKILFLDEPTSALDLNYAIELLSLCEKLvKEKNIAVVAILHDLNLASMFCD 207
Cdd:COG4778 142 PERLWDLppatfSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEA-KARGTAIIGIFHDEEVREAVAD 220
|
....*...
gi 919308723 208 KILFLKEG 215
Cdd:COG4778 221 RVVDVTPF 228
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-235 |
1.53e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 90.92 E-value: 1.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 1 MLKIHDLNFTYH------QKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFS-LKEF 73
Cdd:PRK13633 4 MIKCKNVSYKYEsneestEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEnLWDI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 74 AKICGFVPQKSElNTPLKVI---DVllmskyanlkhafsSYSKEDI----LEIKEfakdlRLENFLERSILS-------- 138
Cdd:PRK13633 84 RNKAGMVFQNPD-NQIVATIveeDV--------------AFGPENLgippEEIRE-----RVDESLKKVGMYeyrrhaph 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 139 -LSGGEFQRMLLARALLKKPKILFLDEPTSALDLNYAIELLSLCEKLVKEKNIAVVAILHDLNLASMfCDKILFLKEGEI 217
Cdd:PRK13633 144 lLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKV 222
|
250
....*....|....*....
gi 919308723 218 KYFGTSKELFTQ-EILKEI 235
Cdd:PRK13633 223 VMEGTPKEIFKEvEMMKKI 241
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
6-230 |
2.28e-21 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 92.86 E-value: 2.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 6 DLNFTY---HQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEFAKICGFVPQ 82
Cdd:TIGR00958 483 DVSFSYpnrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQ 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 83 KSelntplkvidvLLMSKYA--NLKHAFSSYSKEDILE----------IKEFAKDLRLENFLERSilSLSGGEFQRMLLA 150
Cdd:TIGR00958 563 EP-----------VLFSGSVreNIAYGLTDTPDEEIMAaakaanahdfIMEFPNGYDTEVGEKGS--QLSGGQKQRIAIA 629
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 151 RALLKKPKILFLDEPTSALDlnyaiellSLCEKLVKE----KNIAVVAILHDLNLASMfCDKILFLKEGEIKYFGTSKEL 226
Cdd:TIGR00958 630 RALVRKPRVLILDEATSALD--------AECEQLLQEsrsrASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQL 700
|
....
gi 919308723 227 FTQE 230
Cdd:TIGR00958 701 MEDQ 704
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-226 |
2.53e-21 |
|
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: 92.56 E-value: 2.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 2 LKIHDLNFTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLI--LKNLSPNKGEIsLFNTNIKD----FSLKEFA- 74
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRI-IYHVALCEkcgyVERPSKVg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 75 ---KICG--FVPQKSELNTPLKVIDVLLMSKYA-NLKHAFSSYSKEDILE--IKEF-------------AKDLRLENFLE 133
Cdd:TIGR03269 80 epcPVCGgtLEPEEVDFWNLSDKLRRRIRKRIAiMLQRTFALYGDDTVLDnvLEALeeigyegkeavgrAVDLIEMVQLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 134 RSIL----SLSGGEFQRMLLARALLKKPKILFLDEPTSALDLNYAIELLSLCEKLVKEKNIAVVAILHDLNLASMFCDKI 209
Cdd:TIGR03269 160 HRIThiarDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKA 239
|
250
....*....|....*..
gi 919308723 210 LFLKEGEIKYFGTSKEL 226
Cdd:TIGR03269 240 IWLENGEIKEEGTPDEV 256
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
30-209 |
2.63e-21 |
|
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: 92.54 E-value: 2.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 30 IGILGPNGSGKSTLLKLILKNLSPNKGEISlfNTNIKDFSLKEFAKicgfvpqkSELNTPLKV-----IDVLLMSKYANL 104
Cdd:COG1245 102 TGILGPNGIGKSTALKILSGELKPNLGDYD--EEPSWDEVLKRFRG--------TELQDYFKKlangeIKVAHKPQYVDL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 105 KHAFSSYSKEDILE-------IKEFAKDLRLENFLERSILSLSGGEFQRMLLARALLKKPKILFLDEPTSALDLNYAIEL 177
Cdd:COG1245 172 IPKVFKGTVRELLEkvdergkLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNV 251
|
170 180 190
....*....|....*....|....*....|..
gi 919308723 178 LSLCEKLVKEkNIAVVAILHDLNLASMFCDKI 209
Cdd:COG1245 252 ARLIRELAEE-GKYVLVVEHDLAILDYLADYV 282
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-235 |
3.63e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 89.66 E-value: 3.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 1 MLKIHDLNFTYHQ-KDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFS-LKEFAKICG 78
Cdd:PRK13644 1 MIRLENVSYSYPDgTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 79 FVPQKSELNTPLKVIDVLLMSKYANLKHAFSSYSKEDILEIKEfakdLRLENFLERSILSLSGGEFQRMLLARALLKKPK 158
Cdd:PRK13644 81 IVFQNPETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAE----IGLEKYRHRSPKTLSGGQGQCVALAGILTMEPE 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 919308723 159 ILFLDEPTSALDLNYAIELLSLCEKLvKEKNIAVVAILHDLNLASMfCDKILFLKEGEIKYFGTSKELFTQEILKEI 235
Cdd:PRK13644 157 CLIFDEVTSMLDPDSGIAVLERIKKL-HEKGKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGEPENVLSDVSLQTL 231
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-228 |
3.66e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 89.20 E-value: 3.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 2 LKIHDLNFTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLI--LKNLSPN---KGEISLFNTNIKDFSLKEFAKI 76
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFnrLIELYPEarvSGEVYLDGQDIFKMDVIELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 77 CGFVPQkseLNTPLKVIDV-------LLMSKYANLKHAFSSYSKEdILEIKEFAKDLRleNFLERSILSLSGGEFQRMLL 149
Cdd:PRK14247 84 VQMVFQ---IPNPIPNLSIfenvalgLKLNRLVKSKKELQERVRW-ALEKAQLWDEVK--DRLDAPAGKLSGGQQQRLCI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 919308723 150 ARALLKKPKILFLDEPTSALDLNYAIELLSLCEKLVKEknIAVVAILHDLNLASMFCDKILFLKEGEIKYFGTSKELFT 228
Cdd:PRK14247 158 ARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFT 234
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1-231 |
3.80e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 89.79 E-value: 3.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 1 MLKIHDLNFTYHQKD-----LLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISL----FNTNIKDFSLK 71
Cdd:PRK13643 1 MIKFEKVNYTYQPNSpfasrALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVgdivVSSTSKQKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 72 EFAKICGFVPQ--KSELNTPLKVIDVLLMSKYANLKHAFSSYSKEDILEIKEFAKDlrlenFLERSILSLSGGEFQRMLL 149
Cdd:PRK13643 81 PVRKKVGVVFQfpESQLFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADE-----FWEKSPFELSGGQMRRVAI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 150 ARALLKKPKILFLDEPTSALDLNYAIELLSLCEKlVKEKNIAVVAILHDLNLASMFCDKILFLKEGEIKYFGTSKELFtQ 229
Cdd:PRK13643 156 AGILAMEPEVLVLDEPTAGLDPKARIEMMQLFES-IHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF-Q 233
|
..
gi 919308723 230 EI 231
Cdd:PRK13643 234 EV 235
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
6-257 |
4.07e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 89.47 E-value: 4.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 6 DLNFTY--HQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSP---NKGEISLFNTNIKDFSLKEFAKICGFV 80
Cdd:PRK13640 10 HVSFTYpdSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKTVWDIREKVGIV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 81 PQKSelntplkviDVLLMSKYANLKHAFS----SYSKEDILEI-KEFAKDLRLENFLERSILSLSGGEFQRMLLARALLK 155
Cdd:PRK13640 90 FQNP---------DNQFVGATVGDDVAFGlenrAVPRPEMIKIvRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 156 KPKILFLDEPTSALDLNYAIELLSLCEKLVKEKNIAVVAILHDLNLASMfCDKILFLKEGEIKYFGTSKELFTQ-EILKE 234
Cdd:PRK13640 161 EPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANM-ADQVLVLDDGKLLAQGSPVEIFSKvEMLKE 239
|
250 260
....*....|....*....|...
gi 919308723 235 IyDLNCEIIYKnskpYILALKEK 257
Cdd:PRK13640 240 I-GLDIPFVYK----LKNKLKEK 257
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
2-251 |
4.23e-21 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 89.56 E-value: 4.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 2 LKIHDLNFTYhqkdllKNIHLELKNQAF-------IGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDfSLKEfa 74
Cdd:PRK15056 7 IVVNDVTVTW------RNGHTALRDASFtvpggsiAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ-ALQK-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 75 KICGFVPQKSELN--TPLKVIDVLLMSKYANLKhAFSSYSKEDILEIKEFAKDLRLENFLERSILSLSGGEFQRMLLARA 152
Cdd:PRK15056 78 NLVAYVPQSEEVDwsFPVLVEDVVMMGRYGHMG-WLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 153 LLKKPKILFLDEPTSALDLNYAIELLSLCEKLVKEKNIAVVAIlHDLNLASMFCDKILFLKeGEIKYFGTSKELFTQEIL 232
Cdd:PRK15056 157 IAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVST-HNLGSVTEFCDYTVMVK-GTVLASGPTETTFTAENL 234
|
250 260
....*....|....*....|....*....
gi 919308723 233 KEIYD----------LNCEIIYKNSKPYI 251
Cdd:PRK15056 235 ELAFSgvlrhvalngSEESIITDDERPFI 263
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-257 |
4.94e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 89.41 E-value: 4.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 1 MLKIHDLNFTYHQKD---LLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEFAKIC 77
Cdd:PRK13650 4 IIEVKNLTFKYKEDQekyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 78 GFVPQKSELNTPLKVI--DVLLMSKYANLKHafssysKEDILEIKEFAKDLRLENFLERSILSLSGGEFQRMLLARALLK 155
Cdd:PRK13650 84 GMVFQNPDNQFVGATVedDVAFGLENKGIPH------EEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 156 KPKILFLDEPTSALDLNYAIELLSLCEKLVKEKNIAVVAILHDLNLASMfCDKILFLKEGEIKYFGTSKELFTQEilKEI 235
Cdd:PRK13650 158 RPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVAL-SDRVLVMKNGQVESTSTPRELFSRG--NDL 234
|
250 260
....*....|....*....|..
gi 919308723 236 YDLNCEIIYKNSkpYILALKEK 257
Cdd:PRK13650 235 LQLGLDIPFTTS--LVQSLRQN 254
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
2-237 |
5.51e-21 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 88.59 E-value: 5.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 2 LKIHDLNFTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLIL--KNLSPNKGEISLFNTNIKDFSLKEFAK---- 75
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMghPKYEVTSGSILLDGEDILELSPDERARagif 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 76 --------ICGfvpqkselntpLKVIDVLLMSKYANLKHAFSsySKEDILEIKEFAKDLRL-ENFLERSI-LSLSGGEFQ 145
Cdd:COG0396 81 lafqypveIPG-----------VSVSNFLRTALNARRGEELS--AREFLKLLKEKMKELGLdEDFLDRYVnEGFSGGEKK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 146 RMLLARALLKKPKILFLDEPTSALDLNyAIELLS-LCEKLVKEKNiAVVAILHDLN-LASMFCDKILFLKEGEIKYFGTs 223
Cdd:COG0396 148 RNEILQMLLLEPKLAILDETDSGLDID-ALRIVAeGVNKLRSPDR-GILIITHYQRiLDYIKPDFVHVLVDGRIVKSGG- 224
|
250
....*....|....
gi 919308723 224 KELfTQEILKEIYD 237
Cdd:COG0396 225 KEL-ALELEEEGYD 237
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
5-226 |
6.46e-21 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 91.56 E-value: 6.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 5 HDLNFTY-HQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEFAKICGFVPQk 83
Cdd:PRK13657 338 DDVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQ- 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 84 selntplkviDVLLM--SKYANLKHAFSSYSKEDILEIKEFAKDLrleNFLERSIL-----------SLSGGEFQRMLLA 150
Cdd:PRK13657 417 ----------DAGLFnrSIEDNIRVGRPDATDEEMRAAAERAQAH---DFIERKPDgydtvvgergrQLSGGERQRLAIA 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 151 RALLKKPKILFLDEPTSALD------LNYAIELLSlceklvkeKNIAVVAILHDLNLASMfCDKILFLKEGEIKYFGTSK 224
Cdd:PRK13657 484 RALLKDPPILILDEATSALDveteakVKAALDELM--------KGRTTFIIAHRLSTVRN-ADRILVFDNGRVVESGSFD 554
|
..
gi 919308723 225 EL 226
Cdd:PRK13657 555 EL 556
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
2-221 |
7.10e-21 |
|
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: 87.55 E-value: 7.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 2 LKIHDLNFTYHQKdllkNIHLELKNQA--FIGILGPNGSGKSTLLKLILKNLSPNKGEISLfntNIKDFSLKEFA-KICG 78
Cdd:cd03298 1 VRLDKIRFSYGEQ----PMHFDLTFAQgeITAIVGPSGSGKSTLLNLIAGFETPQSGRVLI---NGVDVTAAPPAdRPVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 79 FVPQKSELNTPLKVIDVLLMSKYANLKhafssYSKEDILEIKEFAKDLRLENFLERSILSLSGGEFQRMLLARALLKKPK 158
Cdd:cd03298 74 MLFQENNLFAHLTVEQNVGLGLSPGLK-----LTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKP 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 919308723 159 ILFLDEPTSALDLNYAIELLSLCEKLVKEKNIAVVAILHDLNLASMFCDKILFLKEGEIKYFG 221
Cdd:cd03298 149 VLLLDEPFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
2-217 |
7.31e-21 |
|
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: 87.91 E-value: 7.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 2 LKIHDLNFTYHQK---DLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEFAKICG 78
Cdd:cd03248 12 VKFQNVTFAYPTRpdtLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 79 FVPQKSELNTplkvidvllMSKYANLKHAFSSYSKEDILE----------IKEFAKDLRLENFlERSILsLSGGEFQRML 148
Cdd:cd03248 92 LVGQEPVLFA---------RSLQDNIAYGLQSCSFECVKEaaqkahahsfISELASGYDTEVG-EKGSQ-LSGGQKQRVA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 919308723 149 LARALLKKPKILFLDEPTSALDLnyaiELLSLCEKLVKE--KNIAVVAILHDLNLASMfCDKILFLKEGEI 217
Cdd:cd03248 161 IARALIRNPQVLILDEATSALDA----ESEQQVQQALYDwpERRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
2-229 |
7.71e-21 |
|
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: 91.32 E-value: 7.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 2 LKIHDLNFTY--HQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEFAKICGF 79
Cdd:TIGR02203 331 VEFRNVTFRYpgRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVAL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 80 VPQkselntplkviDVLLM--SKYANLkhAFSSYSKEDILEIKEFAKDLRLENFLERSILS-----------LSGGEFQR 146
Cdd:TIGR02203 411 VSQ-----------DVVLFndTIANNI--AYGRTEQADRAEIERALAAAYAQDFVDKLPLGldtpigengvlLSGGQRQR 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 147 MLLARALLKKPKILFLDEPTSALDLNYAIELLSLCEKLVKEKNIAVVAilHDLNLASMfCDKILFLKEGEIKYFGTSKEL 226
Cdd:TIGR02203 478 LAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIA--HRLSTIEK-ADRIVVMDDGRIVERGTHNEL 554
|
...
gi 919308723 227 FTQ 229
Cdd:TIGR02203 555 LAR 557
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
30-216 |
1.60e-20 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 90.25 E-value: 1.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 30 IGILGPNGSGKSTLLKLILKNLSPNKGEISlfnTNIKdFSLKefakicgfvPQKSELNTPLKVIDVLlmskyANLKHAF- 108
Cdd:PRK13409 368 IGIVGPNGIGKTTFAKLLAGVLKPDEGEVD---PELK-ISYK---------PQYIKPDYDGTVEDLL-----RSITDDLg 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 109 SSYSKEDIleikefAKDLRLENFLERSILSLSGGEFQRMLLARALLKKPKILFLDEPTSALDLNYAIELLSLCEKLVKEK 188
Cdd:PRK13409 430 SSYYKSEI------IKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEER 503
|
170 180
....*....|....*....|....*....
gi 919308723 189 NIAVVAILHDLNLASMFCDKIL-FlkEGE 216
Cdd:PRK13409 504 EATALVVDHDIYMIDYISDRLMvF--EGE 530
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
30-209 |
2.43e-20 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 89.87 E-value: 2.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 30 IGILGPNGSGKSTLLKLILKNLSPNKGEislFNTN------IKDFSLKE----FAKIcgfvpQKSELNTPLKVIDVLLMS 99
Cdd:PRK13409 102 TGILGPNGIGKTTAVKILSGELIPNLGD---YEEEpswdevLKRFRGTElqnyFKKL-----YNGEIKVVHKPQYVDLIP 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 100 KYANLKhafssysKEDILE-------IKEFAKDLRLENFLERSILSLSGGEFQRMLLARALLKKPKILFLDEPTSALDLN 172
Cdd:PRK13409 174 KVFKGK-------VRELLKkvdergkLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIR 246
|
170 180 190
....*....|....*....|....*....|....*..
gi 919308723 173 YAIELLSLCEKLVKEKniAVVAILHDLNLASMFCDKI 209
Cdd:PRK13409 247 QRLNVARLIRELAEGK--YVLVVEHDLAVLDYLADNV 281
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-170 |
3.18e-20 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 85.39 E-value: 3.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 1 MLKIHDLNFTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDfSLKEFAKICGFV 80
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK-DLCTYQKQLCFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 81 PQKSELNTPLKVIDVLLmskyanlkhaFSSYSKEDILEIKEFAKDLRLENFLERSILSLSGGEFQRMLLARALLKKPKIL 160
Cdd:PRK13540 80 GHRSGINPYLTLRENCL----------YDIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLW 149
|
170
....*....|
gi 919308723 161 FLDEPTSALD 170
Cdd:PRK13540 150 LLDEPLVALD 159
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
17-217 |
3.31e-20 |
|
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: 85.92 E-value: 3.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 17 LKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEFAKI---CGFVPQKSELNTPLKVi 93
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLrrkIGVVFQDFRLLPDRNV- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 94 dvllmskYANLkhAFSsyskediLEI-----KEFAKdlRLENFLERSILS---------LSGGEFQRMLLARALLKKPKI 159
Cdd:cd03292 96 -------YENV--AFA-------LEVtgvppREIRK--RVPAALELVGLShkhralpaeLSGGEQQRVAIARAIVNSPTI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 919308723 160 LFLDEPTSALDLNYAIELLSLCEKLVKEKNIAVVAIlHDLNLASMFCDKILFLKEGEI 217
Cdd:cd03292 158 LIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVAT-HAKELVDTTRHRVIALERGKL 214
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-227 |
3.50e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 86.98 E-value: 3.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 1 MLKIHDLNFTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEIsLFNTNIKDFSLKefakicGFV 80
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAV-LWQGKPLDYSKR------GLL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 81 PQKSELNTPLKVIDVLLMSKYANLKHAFS----SYSKEDILE-IKEFAKDLRLENFLERSILSLSGGEFQRMLLARALLK 155
Cdd:PRK13638 74 ALRQQVATVFQDPEQQIFYTDIDSDIAFSlrnlGVPEAEITRrVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 919308723 156 KPKILFLDEPTSALDLNYAIELLSLCEKLVKEKNIAVVAIlHDLNLASMFCDKILFLKEGEIKYFGTSKELF 227
Cdd:PRK13638 154 QARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISS-HDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
30-230 |
4.10e-20 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 89.65 E-value: 4.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 30 IGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEFAKICGFVPQKSEL--NTPLKVIDVLLMSKYANLKHA 107
Cdd:PLN03232 1265 VGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLfsGTVRFNIDPFSEHNDADLWEA 1344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 108 FSSYSKEDILEIKEFAKDLRL----ENFlersilslSGGEFQRMLLARALLKKPKILFLDEPTSALDlnyaIELLSLCEK 183
Cdd:PLN03232 1345 LERAHIKDVIDRNPFGLDAEVseggENF--------SVGQRQLLSLARALLRRSKILVLDEATASVD----VRTDSLIQR 1412
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 919308723 184 LVKE--KNIAVVAILHDLNlASMFCDKILFLKEGEIKYFGTSKELFTQE 230
Cdd:PLN03232 1413 TIREefKSCTMLVIAHRLN-TIIDCDKILVLSSGQVLEYDSPQELLSRD 1460
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-227 |
9.16e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 85.28 E-value: 9.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 6 DLNFTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPN-----KGEISLFNTNI--KDFSLKEFAKICG 78
Cdd:PRK14267 9 NLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIysPDVDPIEVRREVG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 79 FVPQKSELNTPLKVID-VLLMSKYANLkhafsSYSKEDILEIKEFA-KDLRL----ENFLERSILSLSGGEFQRMLLARA 152
Cdd:PRK14267 89 MVFQYPNPFPHLTIYDnVAIGVKLNGL-----VKSKKELDERVEWAlKKAALwdevKDRLNDYPSNLSGGQRQRLVIARA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 919308723 153 LLKKPKILFLDEPTSALDLNYAIELLSLCEKLVKEKNIAVVAilHDLNLASMFCDKILFLKEGEIKYFGTSKELF 227
Cdd:PRK14267 164 LAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVT--HSPAQAARVSDYVAFLYLGKLIEVGPTRKVF 236
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
13-232 |
1.20e-19 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 87.84 E-value: 1.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 13 QKDLLKNIHLELKNQAFIGILGPNGSGKST----LLKLIlknlsPNKGEISLFNTNIKDFSLKEFAKI-----CGFVPQK 83
Cdd:PRK15134 298 HNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQPLHNLNRRQLLPVrhriqVVFQDPN 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 84 SELNTPLKVIDVL---LMSKYANLkhafSSYSKED--ILEIKEFAKDLRLENfleRSILSLSGGEFQRMLLARALLKKPK 158
Cdd:PRK15134 373 SSLNPRLNVLQIIeegLRVHQPTL----SAAQREQqvIAVMEEVGLDPETRH---RYPAEFSGGQRQRIAIARALILKPS 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 159 ILFLDEPTSALDLNYAIELLSLCEKLVKEKNIAVVAILHDLNLASMFCDKILFLKEGEI-------KYFGTSKELFTQEI 231
Cdd:PRK15134 446 LIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVveqgdceRVFAAPQQEYTRQL 525
|
.
gi 919308723 232 L 232
Cdd:PRK15134 526 L 526
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2-235 |
1.21e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 85.91 E-value: 1.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 2 LKIHDLNFTYHQK-----DLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEIslfNTNIKDFSLKEFAKI 76
Cdd:PRK13651 3 IKVKNIVKIFNKKlptelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTI---EWIFKDEKNKKKTKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 77 CGFVPQKSELNTPL--KVIDVLLMSKYANLKHAFSSYS------KEDIL-----------EIKEFAKD-LRL----ENFL 132
Cdd:PRK13651 80 KEKVLEKLVIQKTRfkKIKKIKEIRRRVGVVFQFAEYQlfeqtiEKDIIfgpvsmgvskeEAKKRAAKyIELvgldESYL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 133 ERSILSLSGGEFQRMLLARALLKKPKILFLDEPTSALDLNYAIELLSLCEKLVKEkNIAVVAILHDLNLASMFCDKILFL 212
Cdd:PRK13651 160 QRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIFF 238
|
250 260
....*....|....*....|...
gi 919308723 213 KEGEIKYFGTskelfTQEILKEI 235
Cdd:PRK13651 239 KDGKIIKDGD-----TYDILSDN 256
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1-218 |
1.28e-19 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 84.45 E-value: 1.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 1 MLKIHDLNFTY----HQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEFAKI 76
Cdd:PRK10584 6 IVEVHHLKKSVgqgeHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 77 ----CGFVPQKSELNTPLKVIDVLLMSkyANLKHAFSSYSKEDIleiKEFAKDLRLENFLERSILSLSGGEFQRMLLARA 152
Cdd:PRK10584 86 rakhVGFVFQSFMLIPTLNALENVELP--ALLRGESSRQSRNGA---KALLEQLGLGKRLDHLPAQLSGGEQQRVALARA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 919308723 153 LLKKPKILFLDEPTSALDLNYAIELLSLCEKLVKEKNIAVVAILHDLNLASMfCDKILFLKEGEIK 218
Cdd:PRK10584 161 FNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAAR-CDRRLRLVNGQLQ 225
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
13-198 |
1.45e-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: 87.30 E-value: 1.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 13 QKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEiSLFNTNIKdfslkefakiCGFVPQKSELNTPLKV 92
Cdd:TIGR03719 17 KKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGE-ARPQPGIK----------VGYLPQEPQLDPTKTV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 93 IDVL---------LMSKYANLKHAFS----SYSK--------EDILEikefAKDL-RLENFLER------------SILS 138
Cdd:TIGR03719 86 RENVeegvaeikdALDRFNEISAKYAepdaDFDKlaaeqaelQEIID----AADAwDLDSQLEIamdalrcppwdaDVTK 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 139 LSGGEFQRMLLARALLKKPKILFLDEPTSALDlnyaIELLSLCEKLVKEKNIAVVAILHD 198
Cdd:TIGR03719 162 LSGGERRRVALCRLLLSKPDMLLLDEPTNHLD----AESVAWLERHLQEYPGTVVAVTHD 217
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
17-225 |
2.29e-19 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 83.98 E-value: 2.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 17 LKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEI-------SLFNTNIkdfslkefakicGFVPQkselntp 89
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVevngrvsALLELGA------------GFHPE------- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 90 lkvidvllMSKYANLKH--AFSSYSKEDIL----EIKEFAkdlRLENFLERSILSLSGGEFQRMLLARALLKKPKILFLD 163
Cdd:COG1134 103 --------LTGRENIYLngRLLGLSRKEIDekfdEIVEFA---ELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVD 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 919308723 164 EPTSALDLNY---AIELLslcEKLvKEKNIAVVAILHDLNLASMFCDKILFLKEGEIKYFGTSKE 225
Cdd:COG1134 172 EVLAVGDAAFqkkCLARI---REL-RESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEE 232
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1-215 |
2.78e-19 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 86.78 E-value: 2.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 1 MLKIHDLN-FTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLIlKNLSPN-KGEISLfntnikdfslKEFAKICg 78
Cdd:COG4178 362 ALALEDLTlRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAI-AGLWPYgSGRIAR----------PAGARVL- 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 79 FVPQKSELntPL-KVIDVLLmskYANLKHAFSSyskEDILEIKEfakDLRLENFLERsiLS--------LSGGEFQRMLL 149
Cdd:COG4178 430 FLPQRPYL--PLgTLREALL---YPATAEAFSD---AELREALE---AVGLGHLAER--LDeeadwdqvLSLGEQQRLAF 496
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 919308723 150 ARALLKKPKILFLDEPTSALDLNYAIELLS-LCEKLvkeKNIAVVAILHDLNLASmFCDKILFLKEG 215
Cdd:COG4178 497 ARLLLHKPDWLFLDEATSALDEENEAALYQlLREEL---PGTTVISVGHRSTLAA-FHDRVLELTGD 559
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-217 |
3.17e-19 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 83.82 E-value: 3.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 1 MLKIHDLNFTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLfntNIKDFSLKEFAKIC--- 77
Cdd:PRK11701 6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHY---RMRDGQLRDLYALSeae 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 78 ---------GFVPQKSELNTPLKV-----IDVLLMS----KYANLKHAFSSYskediLEIKEFAKDlRLENfLERSilsL 139
Cdd:PRK11701 83 rrrllrtewGFVHQHPRDGLRMQVsaggnIGERLMAvgarHYGDIRATAGDW-----LERVEIDAA-RIDD-LPTT---F 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 919308723 140 SGGEFQRMLLARALLKKPKILFLDEPTSALDLNYAIELLSLCEKLVKEKNIAVVAILHDLNLASMFCDKILFLKEGEI 217
Cdd:PRK11701 153 SGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRV 230
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-170 |
3.42e-19 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 84.14 E-value: 3.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 1 MLKIHDLNFTYH----QKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEfaki 76
Cdd:COG4525 3 MLTVRHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADR---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 77 cGFVPQKSELNTPLKVID-VLLMSKYANLKHAfssyskedilEIKEFAKDL----RLENFLERSILSLSGGEFQRMLLAR 151
Cdd:COG4525 79 -GVVFQKDALLPWLNVLDnVAFGLRLRGVPKA----------ERRARAEELlalvGLADFARRRIWQLSGGMRQRVGIAR 147
|
170
....*....|....*....
gi 919308723 152 ALLKKPKILFLDEPTSALD 170
Cdd:COG4525 148 ALAADPRFLLMDEPFGALD 166
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-236 |
4.10e-19 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 83.15 E-value: 4.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 1 MLKIHDLNFTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEFAK--IcG 78
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARlgI-G 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 79 FVPQKSELNTPLKVIDVLLMskyanlkhafssyskedILEIKEFAKD---LRLENFLE-------RSIL--SLSGGEFQR 146
Cdd:COG1137 82 YLPQEASIFRKLTVEDNILA-----------------VLELRKLSKKereERLEELLEefgithlRKSKaySLSGGERRR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 147 MLLARALLKKPKILFLDEPTSALDLNYAIELLSLCEKLvKEKNIAVVAILHD----LNLasmfCDKILFLKEGEIKYFGT 222
Cdd:COG1137 145 VEIARALATNPKFILLDEPFAGVDPIAVADIQKIIRHL-KERGIGVLITDHNvretLGI----CDRAYIISEGKVLAEGT 219
|
250
....*....|....
gi 919308723 223 SKELFTQEILKEIY 236
Cdd:COG1137 220 PEEILNNPLVRKVY 233
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
17-217 |
4.19e-19 |
|
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: 81.32 E-value: 4.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 17 LKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTnikdfslkefakicgfvpqkselntplkvidvl 96
Cdd:cd03216 16 LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGK--------------------------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 97 lmskyanlKHAFSSYSKedileikefAKDLRLEnflerSILSLSGGEFQRMLLARALLKKPKILFLDEPTSALDLNYAIE 176
Cdd:cd03216 63 --------EVSFASPRD---------ARRAGIA-----MVYQLSVGERQMVEIARALARNARLLILDEPTAALTPAEVER 120
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 919308723 177 LLSLCEKLvKEKNIAVVAILHDLNLASMFCDKILFLKEGEI 217
Cdd:cd03216 121 LFKVIRRL-RAQGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
17-221 |
4.52e-19 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 82.97 E-value: 4.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 17 LKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEIslfNTNIKDFSLKEFAkiCGFVPQkselntpLKVIDvl 96
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTV---TVRGRVSSLLGLG--GGFNPE-------LTGRE-- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 97 lmskYANLKHAFSSYSKEDIL----EIKEFAKdlrLENFLERSILSLSGGEFQRMLLARALLKKPKILFLDEPTSALDLN 172
Cdd:cd03220 104 ----NIYLNGRLLGLSRKEIDekidEIIEFSE---LGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAA 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 919308723 173 YAIELLSLCEKLVKEKNIAVVAIlHDLNLASMFCDKILFLKEGEIKYFG 221
Cdd:cd03220 177 FQEKCQRRLRELLKQGKTVILVS-HDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
30-209 |
5.17e-19 |
|
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: 83.57 E-value: 5.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 30 IGILGPNGSGKSTLLKLILKNLSPNKGEISL---FNTNIKDFSLKE----FAKIcgfvpqkseLNTPLKVIdvlLMSKYA 102
Cdd:cd03236 29 LGLVGPNGIGKSTALKILAGKLKPNLGKFDDppdWDEILDEFRGSElqnyFTKL---------LEGDVKVI---VKPQYV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 103 NLKHAFSSYSKEDILEIK-------EFAKDLRLENFLERSILSLSGGEFQRMLLARALLKKPKILFLDEPTSALDLNYAI 175
Cdd:cd03236 97 DLIPKAVKGKVGELLKKKdergkldELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRL 176
|
170 180 190
....*....|....*....|....*....|....
gi 919308723 176 ELLSLCEKLVKEKNiAVVAILHDLNLASMFCDKI 209
Cdd:cd03236 177 NAARLIRELAEDDN-YVLVVEHDLAVLDYLSDYI 209
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
6-235 |
6.19e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 83.64 E-value: 6.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 6 DLNFTYH-----QKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFS----LKEFAKI 76
Cdd:PRK13649 7 NVSYTYQagtpfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSknkdIKQIRKK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 77 CGFVPQ--KSEL--NTPLKviDVllmskyanlkhAFS----SYSKEDILEIKEfaKDLRL----ENFLERSILSLSGGEF 144
Cdd:PRK13649 87 VGLVFQfpESQLfeETVLK--DV-----------AFGpqnfGVSQEEAEALAR--EKLALvgisESLFEKNPFELSGGQM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 145 QRMLLARALLKKPKILFLDEPTSALDLNYAIELLSLCEKLvKEKNIAVVAILHDLNLASMFCDKILFLKEGEIKYFGTSK 224
Cdd:PRK13649 152 RRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKL-HQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPK 230
|
250
....*....|..
gi 919308723 225 ELFTQ-EILKEI 235
Cdd:PRK13649 231 DIFQDvDFLEEK 242
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
16-229 |
6.76e-19 |
|
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: 85.77 E-value: 6.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 16 LLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEFAKICGFVPQKselntPLKVIDV 95
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQD-----PVLFSGS 1375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 96 LLMskyaNLKhAFSSYSKEDI---LEI---KEFAKDL--RLENFLERSILSLSGGEFQRMLLARALLKKPKILFLDEPTS 167
Cdd:TIGR00957 1376 LRM----NLD-PFSQYSDEEVwwaLELahlKTFVSALpdKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATA 1450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 919308723 168 ALDLnyaiELLSLCEKLVKEK--NIAVVAILHDLNlASMFCDKILFLKEGEIKYFGTSKELFTQ 229
Cdd:TIGR00957 1451 AVDL----ETDNLIQSTIRTQfeDCTVLTIAHRLN-TIMDYTRVIVLDKGEVAEFGAPSNLLQQ 1509
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-215 |
1.35e-18 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 82.44 E-value: 1.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 1 MLKIHDLNFTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEfakicGFV 80
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER-----GVV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 81 PQKSELntpLKVIDVLlmskyANLkhAF----SSYSKEDILEI-KEFAKDLRLENFLERSILSLSGGEFQRMLLARALLK 155
Cdd:PRK11248 76 FQNEGL---LPWRNVQ-----DNV--AFglqlAGVEKMQRLEIaHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 156 KPKILFLDEPTSALDLNYAIELLSLCEKLVKEKNIAVVAILHDLNLASMFCDKILFLKEG 215
Cdd:PRK11248 146 NPQLLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-229 |
1.42e-18 |
|
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: 84.35 E-value: 1.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 1 MLKIHDLNFTYHQKD----LLKNIHLELKNQAFIGILGPNGSGKS----TLLKLILKNLSPNKGEISLFNTNIKDFSLKE 72
Cdd:COG4172 6 LLSVEDLSVAFGQGGgtveAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 73 FAKICG----FVPQK--SELNtPLK-----VIDVLL----MSKYANLKHAfssyskEDILE---IKEFAKdlRLENFLER 134
Cdd:COG4172 86 LRRIRGnriaMIFQEpmTSLN-PLHtigkqIAEVLRlhrgLSGAAARARA------LELLErvgIPDPER--RLDAYPHQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 135 silsLSGGEFQRMLLARALLKKPKILFLDEPTSALDLNYAIELLSLCEKLVKEKNIAVVAILHDLNLASMFCDKILFLKE 214
Cdd:COG4172 157 ----LSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQ 232
|
250
....*....|....*
gi 919308723 215 GEIKYFGTSKELFTQ 229
Cdd:COG4172 233 GEIVEQGPTAELFAA 247
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
2-236 |
1.47e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 82.57 E-value: 1.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 2 LKIHDLNFTYH-----QKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISL----FNTNIKDFSLKE 72
Cdd:PRK13641 3 IKFENVDYIYSpgtpmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIagyhITPETGNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 73 FAKICGFVPQKSEL----NTPLKviDVllmsKYANLKHAFSsySKEDILEIKEFAKDLRL-ENFLERSILSLSGGEFQRM 147
Cdd:PRK13641 83 LRKKVSLVFQFPEAqlfeNTVLK--DV----EFGPKNFGFS--EDEAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 148 LLARALLKKPKILFLDEPTSALDLNYAIELLSLCEKLVKEKNiAVVAILHDLNLASMFCDKILFLKEGEIKYFGTSKELF 227
Cdd:PRK13641 155 AIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGH-TVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIF 233
|
250
....*....|
gi 919308723 228 T-QEILKEIY 236
Cdd:PRK13641 234 SdKEWLKKHY 243
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-228 |
1.57e-18 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 81.68 E-value: 1.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 1 MLKIHDLNFTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKE--FAKICG 78
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDErlIRQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 79 FV-------PQKSEL-NTPLKVIDVLLMSKYanlkhafssyskedilEIKEFAKDLrlenfLERSILS---------LSG 141
Cdd:PRK09493 81 MVfqqfylfPHLTALeNVMFGPLRVRGASKE----------------EAEKQAREL-----LAKVGLAerahhypseLSG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 142 GEFQRMLLARALLKKPKILFLDEPTSALDLNYAIELLSLCEKLVKEkNIAVVAILHDLNLASMFCDKILFLKEGEIKYFG 221
Cdd:PRK09493 140 GQQQRVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDG 218
|
....*..
gi 919308723 222 TSKELFT 228
Cdd:PRK09493 219 DPQVLIK 225
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
4-229 |
1.89e-18 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 84.38 E-value: 1.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 4 IHDLNFTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEFAKICGFVPQk 83
Cdd:PRK10789 318 IRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQ- 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 84 selnTPLKVIDvllmSKYANLKHAFSSYSKEDILEIKEFA---KD-LRL-ENFL----ERSILsLSGGEFQRMLLARALL 154
Cdd:PRK10789 397 ----TPFLFSD----TVANNIALGRPDATQQEIEHVARLAsvhDDiLRLpQGYDtevgERGVM-LSGGQKQRISIARALL 467
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 919308723 155 KKPKILFLDEPTSALDLNYAIELLSLCEKLVKEKNIAVVAilHDLNlASMFCDKILFLKEGEIKYFGTSKELFTQ 229
Cdd:PRK10789 468 LNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISA--HRLS-ALTEASEILVMQHGHIAQRGNHDQLAQQ 539
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
17-244 |
2.24e-18 |
|
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: 81.36 E-value: 2.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 17 LKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNI-----------KDFSLkefakicgfVPQKS- 84
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQItepgpdrmvvfQNYSL---------LPWLTv 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 85 ELNTPLKVIDVLlmskyanlkHAFSSYSKEDILEikEFAKDLRLENFLERSILSLSGGEFQRMLLARALLKKPKILFLDE 164
Cdd:TIGR01184 72 RENIALAVDRVL---------PDLSKSERRAIVE--EHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 165 PTSALDlnyAIELLSLCEKLVK---EKNIAVVAILHDLNLASMFCDKILFLKEGEIKYFGTSKEL-FTQ-----EILKE- 234
Cdd:TIGR01184 141 PFGALD---ALTRGNLQEELMQiweEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEVpFPRprdrlEVVEDp 217
|
250
....*....|.
gi 919308723 235 -IYDLNCEIIY 244
Cdd:TIGR01184 218 sYYDLRNEALY 228
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
18-227 |
3.22e-18 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 82.77 E-value: 3.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 18 KNIHLELKNQAFIGILGPNGSGKSTLLKLI--LKNLSpnKGEISLFNTNIKDFSLKEfaKICGFVPQKSELNTPLKVIDV 95
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTLLRMIagLEDIT--SGDLFIGEKRMNDVPPAE--RGVGMVFQSYALYPHLSVAEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 96 llMS---KYANLKhafssysKEDILE-IKEFAKDLRLENFLERSILSLSGGEFQRMLLARALLKKPKILFLDEPTSALDL 171
Cdd:PRK11000 96 --MSfglKLAGAK-------KEEINQrVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 919308723 172 NYAIELLSLCEKLVKEKNIAVVAILHDLNLASMFCDKILFLKEGEIKYFGTSKELF 227
Cdd:PRK11000 167 ALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELY 222
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
17-230 |
4.77e-18 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 83.25 E-value: 4.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 17 LKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEFAKICGFVPQkselnTPlkvidvL 96
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQ-----AP------V 1323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 97 LMSKYA--NLKhAFSSYSKEDILEIKEFAkdlRLENFLERSILSL-----SGGE-F---QRML--LARALLKKPKILFLD 163
Cdd:PLN03130 1324 LFSGTVrfNLD-PFNEHNDADLWESLERA---HLKDVIRRNSLGLdaevsEAGEnFsvgQRQLlsLARALLRRSKILVLD 1399
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 919308723 164 EPTSALDlnyaIELLSLCEKLVKE--KNIAVVAILHDLNlASMFCDKILFLKEGEIKYFGTSKELFTQE 230
Cdd:PLN03130 1400 EATAAVD----VRTDALIQKTIREefKSCTMLIIAHRLN-TIIDCDRILVLDAGRVVEFDTPENLLSNE 1463
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-217 |
5.12e-18 |
|
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: 79.57 E-value: 5.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 2 LKIHDLNFTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFS--LKEFAKIC-- 77
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIeaLRRIGALIea 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 78 -GFVPQKS-ELNtpLKVIDVLLMSKYANLKHAfssyskEDILEIKEFAKdlrlenfleRSILSLSGGEFQRMLLARALLK 155
Cdd:cd03268 81 pGFYPNLTaREN--LRLLARLLGIRKKRIDEV------LDVVGLKDSAK---------KKVKGFSLGMKQRLGIALALLG 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 919308723 156 KPKILFLDEPTSALDLNYAIELLSLCEKLvKEKNIAVVAILHDLNLASMFCDKILFLKEGEI 217
Cdd:cd03268 144 NPDLLILDEPTNGLDPDGIKELRELILSL-RDQGITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-227 |
9.77e-18 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 82.21 E-value: 9.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 1 MLKIHDLNFTYHQK----DLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEIS-----LFNTN-----IK 66
Cdd:PRK10261 12 VLAVENLNIAFMQEqqkiAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQcdkmlLRRRSrqvieLS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 67 DFSLKEFAKICG------FVPQKSELNTPLKVIDVLLMSkyANLKHAFSSysKEDILEIKEFAKDLRL---ENFLERSIL 137
Cdd:PRK10261 92 EQSAAQMRHVRGadmamiFQEPMTSLNPVFTVGEQIAES--IRLHQGASR--EEAMVEAKRMLDQVRIpeaQTILSRYPH 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 138 SLSGGEFQRMLLARALLKKPKILFLDEPTSALDLNYAIELLSLCEKLVKEKNIAVVAILHDLNLASMFCDKILFLKEGEI 217
Cdd:PRK10261 168 QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEA 247
|
250
....*....|
gi 919308723 218 KYFGTSKELF 227
Cdd:PRK10261 248 VETGSVEQIF 257
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
17-216 |
1.69e-17 |
|
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: 81.41 E-value: 1.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 17 LKNIHLELKNQAFIGILGPNGSGKSTLLKlILKNLSPN---KGEISLFNTNIKDFSLKEF-AKICGFVPQKSELNTPLKV 92
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMK-ILSGVYPHgtwDGEIYWSGSPLKASNIRDTeRAGIVIIHQELTLVPELSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 93 IDVLLMSKYANLKHAFSSYSkEDILEIKEFAKDLRLENF-LERSILSLSGGEFQRMLLARALLKKPKILFLDEPTSALDL 171
Cdd:TIGR02633 96 AENIFLGNEITLPGGRMAYN-AMYLRAKNLLRELQLDADnVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSLTE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 919308723 172 NYAIELLSLCEKLvKEKNIAVVAILHDLNLASMFCDKILFLKEGE 216
Cdd:TIGR02633 175 KETEILLDIIRDL-KAHGVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
13-198 |
2.48e-17 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 80.93 E-value: 2.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 13 QKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKlILKNLSpnkgeislfntniKDFS----LKEFAKIcGFVPQKSELNT 88
Cdd:PRK11819 19 KKQILKDISLSFFPGAKIGVLGLNGAGKSTLLR-IMAGVD-------------KEFEgearPAPGIKV-GYLPQEPQLDP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 89 PLKVIDVL----------------LMSKYANLKHAFSSYSKE-----DILEikefAKDL-RLENFLERS----------- 135
Cdd:PRK11819 84 EKTVRENVeegvaevkaaldrfneIYAAYAEPDADFDALAAEqgelqEIID----AADAwDLDSQLEIAmdalrcppwda 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 919308723 136 -ILSLSGGEFQRMLLARALLKKPKILFLDEPTSALDlnyaIELLSLCEKLVKEKNIAVVAILHD 198
Cdd:PRK11819 160 kVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD----AESVAWLEQFLHDYPGTVVAVTHD 219
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
19-229 |
2.86e-17 |
|
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: 80.62 E-value: 2.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 19 NIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISL------FNTNIKDFSLKEFAK-ICGFVPQKSELNTPLK 91
Cdd:TIGR03269 302 NVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdewVDMTKPGPDGRGRAKrYIGILHQEYDLYPHRT 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 92 VIDVLLMSKYANLKHAFSSYSKEDILEIKEFAKDlRLENFLERSILSLSGGEFQRMLLARALLKKPKILFLDEPTSALDL 171
Cdd:TIGR03269 382 VLDNLTEAIGLELPDELARMKAVITLKMVGFDEE-KAEEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDP 460
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 919308723 172 NYAIELLSLCEKLVKEKNIAVVAILHDLNLASMFCDKILFLKEGEIKYFGTSKELFTQ 229
Cdd:TIGR03269 461 ITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
30-227 |
7.48e-17 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 78.59 E-value: 7.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 30 IGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEFAKICG-----FVPQKSELNTPLKVIDVL---LMSKY 101
Cdd:PRK15079 50 LGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVRSdiqmiFQDPLASLNPRMTIGEIIaepLRTYH 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 102 ANLKHAfssyskedilEIKEFAKDLR-----LENFLERSILSLSGGEFQRMLLARALLKKPKILFLDEPTSALDLNYAIE 176
Cdd:PRK15079 130 PKLSRQ----------EVKDRVKAMMlkvglLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQ 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 919308723 177 LLSLCEKLVKEKNIAVVAILHDLNLASMFCDKILFLKEGEIKYFGTSKELF 227
Cdd:PRK15079 200 VVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVY 250
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
8-226 |
1.16e-16 |
|
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: 79.18 E-value: 1.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 8 NFTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEIslfntnikdfslKEFAKIcGFVPQKSELn 87
Cdd:TIGR01271 433 NFSLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI------------KHSGRI-SFSPQTSWI- 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 88 TPLKVIDVLLMSKyanlkhAFSSYSKEDILEIKEFAKDLRLENFLERSIL-----SLSGGEFQRMLLARALLKKPKILFL 162
Cdd:TIGR01271 499 MPGTIKDNIIFGL------SYDEYRYTSVIKACQLEEDIALFPEKDKTVLgeggiTLSGGQRARISLARAVYKDADLYLL 572
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 919308723 163 DEPTSALDLNYAIELLS--LCEKLVKEKNIAVVAILHDLNLAsmfcDKILFLKEGEIKYFGTSKEL 226
Cdd:TIGR01271 573 DSPFTHLDVVTEKEIFEscLCKLMSNKTRILVTSKLEHLKKA----DKILLLHEGVCYFYGTFSEL 634
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-230 |
1.37e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 78.73 E-value: 1.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 2 LKIHDLNFTYHQ-KDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLsPNKGEISLFNTNIKDFSLKEFAKICGFV 80
Cdd:PRK11174 350 IEAEDLEILSPDgKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWV 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 81 PQKSELntPLKVI-DVLLMSKyanlkhafSSYSKEDI---LE---IKEFAKdlRLENFLERSI----LSLSGGEFQRMLL 149
Cdd:PRK11174 429 GQNPQL--PHGTLrDNVLLGN--------PDASDEQLqqaLEnawVSEFLP--LLPQGLDTPIgdqaAGLSVGQAQRLAL 496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 150 ARALLKKPKILFLDEPTSALDlnyaiellSLCEKLVKE------KNIAVVAILHDLN-LASMfcDKILFLKEGEIKYFGT 222
Cdd:PRK11174 497 ARALLQPCQLLLLDEPTASLD--------AHSEQLVMQalnaasRRQTTLMVTHQLEdLAQW--DQIWVMQDGQIVQQGD 566
|
....*...
gi 919308723 223 SKELFTQE 230
Cdd:PRK11174 567 YAELSQAG 574
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-231 |
1.47e-16 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 78.78 E-value: 1.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 2 LKIHDLNFTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLfntnikdfslKEFAKIcGFVP 81
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKW----------SENANI-GYYA 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 82 QKS--ELNTPLKVIDvlLMSKYANLKHAFSS---------YSKEDIleikefakdlrlenflERSILSLSGGEFQRMLLA 150
Cdd:PRK15064 389 QDHayDFENDLTLFD--WMSQWRQEGDDEQAvrgtlgrllFSQDDI----------------KKSVKVLSGGEKGRMLFG 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 151 RALLKKPKILFLDEPTSALDLNyAIELLSLCEKLVKEKNIAVVailHDLNLASMFCDKILFLKEGEIKYF-GTSKE-LFT 228
Cdd:PRK15064 451 KLMMQKPNVLVMDEPTNHMDME-SIESLNMALEKYEGTLIFVS---HDREFVSSLATRIIEITPDGVVDFsGTYEEyLRS 526
|
...
gi 919308723 229 QEI 231
Cdd:PRK15064 527 QGI 529
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-250 |
1.85e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 76.70 E-value: 1.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 2 LKIHDLNFTYhqKD---LLKNIHLELKNQAFIGILGPNGSGKSTLLkLILKNL-SPNKGEISLFNTNIKDFSLKEFAKIC 77
Cdd:PRK13647 5 IEVEDLHFRY--KDgtkALKGLSLSIPEGSKTALLGPNGAGKSTLL-LHLNGIyLPQRGRVKVMGREVNAENEKWVRSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 78 GFVPQKSelntplkviDVLLMSKYANLKHAFS----SYSKEDILE-IKEFAKDLRLENFLERSILSLSGGEFQRMLLARA 152
Cdd:PRK13647 82 GLVFQDP---------DDQVFSSTVWDDVAFGpvnmGLDKDEVERrVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 153 LLKKPKILFLDEPTSALDLNYAIELLSLCEKLVKEKNIAVVAIlHDLNLASMFCDKILFLKEGEIKYFGtSKELFTQEIL 232
Cdd:PRK13647 153 LAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVAT-HDVDLAAEWADQVIVLKEGRVLAEG-DKSLLTDEDI 230
|
250
....*....|....*...
gi 919308723 233 KEIYDLNCEIIYKNSKPY 250
Cdd:PRK13647 231 VEQAGLRLPLVAQIFEDL 248
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
30-229 |
2.27e-16 |
|
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: 78.19 E-value: 2.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 30 IGILGPNGSGKSTLLKLILKnLSPNKGEISLFNTNIKDFSLKEFAkicgfvPQKSE-----------LN----------T 88
Cdd:COG4172 315 LGLVGESGSGKSTLGLALLR-LIPSEGEIRFDGQDLDGLSRRALR------PLRRRmqvvfqdpfgsLSprmtvgqiiaE 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 89 PLKVIDVLLmskyanlkhafssySKEDILE-IKEFAKDLRL-ENFLERSILSLSGGEFQRMLLARALLKKPKILFLDEPT 166
Cdd:COG4172 388 GLRVHGPGL--------------SAAERRArVAEALEEVGLdPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPT 453
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 919308723 167 SALDLNYAIELLSLCEKLVKEKNIAVVAILHDLNLASMFCDKILFLKEGEIKYFGTSKELFTQ 229
Cdd:COG4172 454 SALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDA 516
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
2-236 |
4.05e-16 |
|
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: 74.49 E-value: 4.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 2 LKIHDLNFTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPN--KGEISLFNTNIKDFSLKEFAKiCGf 79
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEvtEGEILFKGEDITDLPPEERAR-LG- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 80 vpqkselntplkvidVLLMSKYAnlkhafssyskEDILEIKefakdlrLENFLeRSI-LSLSGGEFQRMLLARALLKKPK 158
Cdd:cd03217 79 ---------------IFLAFQYP-----------PEIPGVK-------NADFL-RYVnEGFSGGEKKRNEILQLLLLEPD 124
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 919308723 159 ILFLDEPTSALDLNyAIELLSLCEKLVKEKNIAVVAILHDLNLAS-MFCDKILFLKEGEIKYFGTSkelftqEILKEIY 236
Cdd:cd03217 125 LAILDEPDSGLDID-ALRLVAEVINKLREEGKSVLIITHYQRLLDyIKPDRVHVLYDGRIVKSGDK------ELALEIE 196
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
19-215 |
4.55e-16 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 75.41 E-value: 4.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 19 NIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEFAKIcGFVP--QKSELNTPLKVIDVL 96
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARM-GVVRtfQHVRLFREMTVIENL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 97 LMSKYANLKH----------AFSSYSKEDILEIKEFAKDLRLENFLERSILSLSGGEFQRMLLARALLKKPKILFLDEPT 166
Cdd:PRK11300 102 LVAQHQQLKTglfsgllktpAFRRAESEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPA 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 919308723 167 SALDLNYAIELLSLCEKLVKEKNIAVVAILHDLNLASMFCDKILFLKEG 215
Cdd:PRK11300 182 AGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQG 230
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1-203 |
4.83e-16 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 74.85 E-value: 4.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 1 MLKIHDLNFTYH----QKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEFAKI 76
Cdd:PRK11629 5 LLQCDNLCKRYQegsvQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAEL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 77 ----CGFVPQKSELNTPLKVIDVLLMSKYANLKHAFSSYSKEdileiKEFAKDLRLENFLERSILSLSGGEFQRMLLARA 152
Cdd:PRK11629 85 rnqkLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRA-----LEMLAAVGLEHRANHRPSELSGGERQRVAIARA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 919308723 153 LLKKPKILFLDEPTSALDLNYAIELLSLCEKLVKEKNIAVVAILHDLNLAS 203
Cdd:PRK11629 160 LVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAK 210
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-219 |
5.55e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 75.20 E-value: 5.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 2 LKIHDLNFTYHQKDLLKNIHLEL-KNQ--AFIGilgPNGSGKSTLLKLI--LKNLSPN---KGEISLFNTNI--KDFSLK 71
Cdd:PRK14243 11 LRTENLNVYYGSFLAVKNVWLDIpKNQitAFIG---PSGCGKSTILRCFnrLNDLIPGfrvEGKVTFHGKNLyaPDVDPV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 72 EFAKICGFVPQKSelNTPLKVIdvllmskYANLKHA--FSSYsKEDILEIKEfaKDLR-------LENFLERSILSLSGG 142
Cdd:PRK14243 88 EVRRRIGMVFQKP--NPFPKSI-------YDNIAYGarINGY-KGDMDELVE--RSLRqaalwdeVKDKLKQSGLSLSGG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 143 EFQRMLLARALLKKPKILFLDEPTSALDlnyAIELLSLcEKLVKE--KNIAVVAILHDLNLASMFCDKILF----LKEGE 216
Cdd:PRK14243 156 QQQRLCIARAIAVQPEVILMDEPCSALD---PISTLRI-EELMHElkEQYTIIIVTHNMQQAARVSDMTAFfnveLTEGG 231
|
...
gi 919308723 217 IKY 219
Cdd:PRK14243 232 GRY 234
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-227 |
6.99e-16 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 76.03 E-value: 6.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 1 MLKIHDLNFTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSlkefakicgfv 80
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVP----------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 81 PQKSELNtplkvidvLLMSKYANLKH-------AFSSysKEDIL---EIK----EFAKDLRLENFLERSILSLSGGEFQR 146
Cdd:PRK11607 88 PYQRPIN--------MMFQSYALFPHmtveqniAFGL--KQDKLpkaEIAsrvnEMLGLVHMQEFAKRKPHQLSGGQRQR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 147 MLLARALLKKPKILFLDEPTSALDLN----YAIELLSLCEKLvkekNIAVVAILHDLNLASMFCDKILFLKEGEIKYFGT 222
Cdd:PRK11607 158 VALARSLAKRPKLLLLDEPMGALDKKlrdrMQLEVVDILERV----GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGE 233
|
....*
gi 919308723 223 SKELF 227
Cdd:PRK11607 234 PEEIY 238
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
12-221 |
8.48e-16 |
|
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: 73.45 E-value: 8.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 12 HQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPN---KGEISlFNTnikdFSLKEFAKICgfvpqkselnt 88
Cdd:cd03233 18 SKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIH-YNG----IPYKEFAEKY----------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 89 plkvidvllmskyanlkHAFSSYSKEDILEIK--------EFAKDLRLENFLeRSIlslSGGEFQRMLLARALLKKPKIL 160
Cdd:cd03233 82 -----------------PGEIIYVSEEDVHFPtltvretlDFALRCKGNEFV-RGI---SGGERKRVSIAEALVSRASVL 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 919308723 161 FLDEPTSALDLNYAIELLSLCEKLVKEKNIAVVAILHDLN--LASMFcDKILFLKEGEIKYFG 221
Cdd:cd03233 141 CWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSLYQASdeIYDLF-DKVLVLYEGRQIYYG 202
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
3-225 |
9.16e-16 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 76.46 E-value: 9.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 3 KIHDLNFTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKdfSLKEFAKICGFVPQ 82
Cdd:PLN03211 70 KISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNFTGTILANNRK--PTKQILKRTGFVTQ 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 83 KSELNTPLKVIDVLLMSKYANLKHAFSSYSKEDILE--IKEFAKDlRLENFL--ERSILSLSGGEFQRMLLARALLKKPK 158
Cdd:PLN03211 148 DDILYPHLTVRETLVFCSLLRLPKSLTKQEKILVAEsvISELGLT-KCENTIigNSFIRGISGGERKRVSIAHEMLINPS 226
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 919308723 159 ILFLDEPTSALDLNYAIELLSLCEKLVkEKNIAVVAILHDLN--LASMFcDKILFLKEGEIKYFGTSKE 225
Cdd:PLN03211 227 LLILDEPTSGLDATAAYRLVLTLGSLA-QKGKTIVTSMHQPSsrVYQMF-DSVLVLSEGRCLFFGKGSD 293
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
4-230 |
9.55e-16 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 76.30 E-value: 9.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 4 IHDLNFTY-HQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEFAKICGFVPQ 82
Cdd:PRK10790 343 IDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQ 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 83 KselntPLkvidVLLMSKYAN--LKHAFSSYSKEDILE---IKEFAKDLR--LENFLERSILSLSGGEFQRMLLARALLK 155
Cdd:PRK10790 423 D-----PV----VLADTFLANvtLGRDISEEQVWQALEtvqLAELARSLPdgLYTPLGEQGNNLSVGQKQLLALARVLVQ 493
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 919308723 156 KPKILFLDEPTSALD--LNYAIElLSLceKLVKEKNIAVVaILHDLNlASMFCDKILFLKEGEIKYFGTSKELFTQE 230
Cdd:PRK10790 494 TPQILILDEATANIDsgTEQAIQ-QAL--AAVREHTTLVV-IAHRLS-TIVEADTILVLHRGQAVEQGTHQQLLAAQ 565
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
16-257 |
1.33e-15 |
|
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: 74.51 E-value: 1.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 16 LLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSpNKGEISLFNTNIKDFSLKEFAKICGFVPQKselntplkvIDV 95
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAFGVIPQK---------VFI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 96 LLMSKYANLKhAFSSYSKEDILEI-KEFAKDLRLENF-------LERSILSLSGGEFQRMLLARALLKKPKILFLDEPTS 167
Cdd:cd03289 89 FSGTFRKNLD-PYGKWSDEEIWKVaEEVGLKSVIEQFpgqldfvLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 168 ALD-LNYAIellslCEKLVKEKNIAVVAILHDLNLASMF-CDKILFLKEGEIKYFGT------SKELFTQEI-----LKE 234
Cdd:cd03289 168 HLDpITYQV-----IRKTLKQAFADCTVILSEHRIEAMLeCQRFLVIEENKVRQYDSiqkllnEKSHFKQAIspsdrLKL 242
|
250 260
....*....|....*....|...
gi 919308723 235 IYDLNCEIIYKNSKPYILALKEK 257
Cdd:cd03289 243 FPRRNSSKSKRKPRPQIQALQEE 265
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
17-227 |
1.34e-15 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 75.45 E-value: 1.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 17 LKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEFAKI----CGFVPQKSELNTPLKV 92
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVrrkkIAMVFQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 93 IDVLLMSkyANLKHAFSSYSKEDILEIkefAKDLRLENFLERSILSLSGGEFQRMLLARALLKKPKILFLDEPTSALDLN 172
Cdd:PRK10070 124 LDNTAFG--MELAGINAEERREKALDA---LRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPL 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 919308723 173 YAIELLSLCEKLVKEKNIAVVAILHDLNLASMFCDKILFLKEGEIKYFGTSKELF 227
Cdd:PRK10070 199 IRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
16-197 |
2.44e-15 |
|
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: 71.42 E-value: 2.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 16 LLKNIHLELKNQAFIGILGPNGSGKSTLLKlILKNLSPN-KGEISL-FNTNIKdfslkefakicgFVPQKSELNTplkvi 93
Cdd:cd03223 16 LLKDLSFEIKPGDRLLITGPSGTGKSSLFR-ALAGLWPWgSGRIGMpEGEDLL------------FLPQRPYLPL----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 94 dvllmskyANLKHAfSSYSKEDILeikefakdlrlenflersilslSGGEFQRMLLARALLKKPKILFLDEPTSALDLNY 173
Cdd:cd03223 78 --------GTLREQ-LIYPWDDVL----------------------SGGEQQRLAFARLLLHKPKFVFLDEATSALDEES 126
|
170 180
....*....|....*....|....
gi 919308723 174 AIELLSLCeklvKEKNIAVVAILH 197
Cdd:cd03223 127 EDRLYQLL----KELGITVISVGH 146
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
14-221 |
2.79e-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: 71.89 E-value: 2.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 14 KDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLIL--KNLSPNKGEISLfNTNIKDfslKEFAKICGFVPQKSELNTPLK 91
Cdd:cd03232 20 RQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAgrKTAGVITGEILI-NGRPLD---KNFQRSTGYVEQQDVHSPNLT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 92 VIDVLLMSkyANLKhafssyskedileikefakDLRLEnflERSILSLsggefqrmllARALLKKPKILFLDEPTSALDL 171
Cdd:cd03232 96 VREALRFS--ALLR-------------------GLSVE---QRKRLTI----------GVELAAKPSILFLDEPTSGLDS 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 919308723 172 NYAIELLSLCEKLVkEKNIAVVAILHDLN--LASMFcDKILFLKE-GEIKYFG 221
Cdd:cd03232 142 QAAYNIVRFLKKLA-DSGQAILCTIHQPSasIFEKF-DRLLLLKRgGKTVYFG 192
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
2-232 |
4.61e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 74.63 E-value: 4.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 2 LKIHDLNFTYH---QKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIkdfslkefakicG 78
Cdd:PLN03232 615 ISIKNGYFSWDsktSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVVIRGSV------------A 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 79 FVPQKSELNTPLKVIDVLLMSKYAN-----------LKHAFSSYSKEDILEIKEfakdlrlenfleRSIlSLSGGEFQRM 147
Cdd:PLN03232 683 YVPQVSWIFNATVRENILFGSDFESerywraidvtaLQHDLDLLPGRDLTEIGE------------RGV-NISGGQKQRV 749
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 148 LLARALLKKPKILFLDEPTSALDLNYAIELLSLC--EKLVKEKNIAVVAILHDLNLAsmfcDKILFLKEGEIKYFGTSKE 225
Cdd:PLN03232 750 SMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCmkDELKGKTRVLVTNQLHFLPLM----DRIILVSEGMIKEEGTFAE 825
|
....*..
gi 919308723 226 LFTQEIL 232
Cdd:PLN03232 826 LSKSGSL 832
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
9-229 |
4.78e-15 |
|
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: 74.56 E-value: 4.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 9 FTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSpNKGEISLFNTNIKDFSLKEFAKICGFVPQKselnt 88
Cdd:TIGR01271 1227 YTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGVIPQK----- 1300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 89 plkvIDVLLMSKYANLKhAFSSYSKEDILEI-KEFAKDLRLENF-------LERSILSLSGGEFQRMLLARALLKKPKIL 160
Cdd:TIGR01271 1301 ----VFIFSGTFRKNLD-PYEQWSDEEIWKVaEEVGLKSVIEQFpdkldfvLVDGGYVLSNGHKQLMCLARSILSKAKIL 1375
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 919308723 161 FLDEPTSALD-LNYAIellslCEKLVKEKNIAVVAILHDLNLASMF-CDKILFLKEGEIKYFGTSKELFTQ 229
Cdd:TIGR01271 1376 LLDEPSAHLDpVTLQI-----IRKTLKQSFSNCTVILSEHRVEALLeCQQFLVIEGSSVKQYDSIQKLLNE 1441
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
2-201 |
4.97e-15 |
|
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: 72.29 E-value: 4.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 2 LKIHDLNFTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNlsPN----KGEISLFNTNIKDFSLKEFAKIC 77
Cdd:TIGR01978 1 LKIKDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGH--PSyevtSGTILFKGQDLLELEPDERARAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 78 GFVPQKSELNTPLKVIDVLLMSKYanlkHAFSSYSKEDILEIKEFAKDLRL--------ENFLERSI-LSLSGGEFQRML 148
Cdd:TIGR01978 79 LFLAFQYPEEIPGVSNLEFLRSAL----NARRSARGEEPLDLLDFEKLLKEklalldmdEEFLNRSVnEGFSGGEKKRNE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 919308723 149 LARALLKKPKILFLDEPTSALDLNyAIELLSLCEKLVKEKNIAVVAILHDLNL 201
Cdd:TIGR01978 155 ILQMALLEPKLAILDEIDSGLDID-ALKIVAEGINRLREPDRSFLIITHYQRL 206
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
4-198 |
6.87e-15 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 73.83 E-value: 6.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 4 IHDLNFTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISlfntnikdfslkefakiCG----- 78
Cdd:PRK11147 322 MENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIH-----------------CGtklev 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 79 --FVPQKSELNTPLKVIDVLLMSKY-----ANLKHAFSsYskedileikefakdlrLENFL---ERS---ILSLSGGEFQ 145
Cdd:PRK11147 385 ayFDQHRAELDPEKTVMDNLAEGKQevmvnGRPRHVLG-Y----------------LQDFLfhpKRAmtpVKALSGGERN 447
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 919308723 146 RMLLARALLKKPKILFLDEPTSALDlnyaIELLSLCEKLVKEKNIAVVAILHD 198
Cdd:PRK11147 448 RLLLARLFLKPSNLLILDEPTNDLD----VETLELLEELLDSYQGTVLLVSHD 496
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
139-229 |
9.64e-15 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 73.20 E-value: 9.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 139 LSGGEFQRMLLARALLKKPKILFLDEPTSALDLNYAIELLSLCEKLVKEKNIAVVAILHDLNLASMFCDKILFLKEGEIK 218
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCV 236
|
90
....*....|.
gi 919308723 219 YFGTSKELFTQ 229
Cdd:PRK15134 237 EQNRAATLFSA 247
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-229 |
1.36e-14 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 72.14 E-value: 1.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 1 MLKIHDLNFTYHQKDL----LKNIHLELKNQAFIGILGPNGSGKSTLLKLIlkNL--SPNKGEISLFNTNIKDFSLKEFA 74
Cdd:PRK11153 1 MIELKNISKVFPQGGRtihaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCI--NLleRPTSGRVLVDGQDLTALSEKELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 75 ----KIcGFVPQksELNtplkvidvLLMSK--YANLkhAF----SSYSKEDIleikefakDLRLENFLERSILS------ 138
Cdd:PRK11153 79 karrQI-GMIFQ--HFN--------LLSSRtvFDNV--ALplelAGTPKAEI--------KARVTELLELVGLSdkadry 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 139 ---LSGGEFQRMLLARALLKKPKILFLDEPTSALDLNYAIELLSLCEKLVKEKNIAVVAILHDLNLASMFCDKILFLKEG 215
Cdd:PRK11153 138 paqLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAG 217
|
250
....*....|....
gi 919308723 216 EIKYFGTSKELFTQ 229
Cdd:PRK11153 218 RLVEQGTVSEVFSH 231
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
17-216 |
1.68e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 72.65 E-value: 1.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 17 LKNIHLELKNQAFIGILGPNGSGKSTLLKlILKNLSPN---KGEIsLFN------TNIKDFSLKEFAKI---CGFVPQKS 84
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMK-VLSGVYPHgtyEGEI-IFEgeelqaSNIRDTERAGIAIIhqeLALVKELS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 85 ELN--------TPLKVIDVLLMskyanlkhafssyskedILEIKEFAKDLRLENFLERSILSLSGGEFQRMLLARALLKK 156
Cdd:PRK13549 99 VLEniflgneiTPGGIMDYDAM-----------------YLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 157 PKILFLDEPTSALDLNYAIELLSLCEKLvKEKNIAVVAILHDLNLASMFCDKILFLKEGE 216
Cdd:PRK13549 162 ARLLILDEPTASLTESETAVLLDIIRDL-KAHGIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1-217 |
1.84e-14 |
|
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: 69.38 E-value: 1.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 1 MLKIHDLnftyHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEFAKI-CGF 79
Cdd:cd03215 4 VLEVRGL----SVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 80 VPqkselntplkvidvllmskyanlkhafssyskEDileikefakdlRLEN--FLERSI-------LSLSGGEFQRMLLA 150
Cdd:cd03215 80 VP--------------------------------ED-----------RKREglVLDLSVaenialsSLLSGGNQQKVVLA 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 919308723 151 RALLKKPKILFLDEPTSALDLNYAIELLSLCEKLvKEKNIAVVAILHDLN-LASMfCDKILFLKEGEI 217
Cdd:cd03215 117 RWLARDPRVLILDEPTRGVDVGAKAEIYRLIREL-ADAGKAVLLISSELDeLLGL-CDRILVMYEGRI 182
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
8-229 |
1.96e-14 |
|
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: 71.04 E-value: 1.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 8 NFTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEIslfntnikdfslKEFAKIcGFVPQKSELn 87
Cdd:cd03291 44 NLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI------------KHSGRI-SFSSQFSWI- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 88 TPLKVIDVLLM----SKYANLKHAFSSYSKEDILEIKEfaKDlrlENFLERSILSLSGGEFQRMLLARALLKKPKILFLD 163
Cdd:cd03291 110 MPGTIKENIIFgvsyDEYRYKSVVKACQLEEDITKFPE--KD---NTVLGEGGITLSGGQRARISLARAVYKDADLYLLD 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 919308723 164 EPTSALDLNYAIELLS--LCEKLVKEKNIAVVAILHDLNLAsmfcDKILFLKEGEIKYFGTSKELFTQ 229
Cdd:cd03291 185 SPFGYLDVFTEKEIFEscVCKLMANKTRILVTSKMEHLKKA----DKILILHEGSSYFYGTFSELQSL 248
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
4-235 |
2.03e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 71.19 E-value: 2.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 4 IHDLNFTYHQKD-----LLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFN----TNIKDF-SLKEF 73
Cdd:PRK13645 9 LDNVSYTYAKKTpfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipANLKKIkEVKRL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 74 AKICGFVPQKSELNTPLKVIDVLLMSKYANLkhafSSYSKEDILEIKEFAKDLRL-ENFLERSILSLSGGEFQRMLLARA 152
Cdd:PRK13645 89 RKEIGLVFQFPEYQLFQETIEKDIAFGPVNL----GENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 153 LLKKPKILFLDEPTSALDLNYAIELLSLCEKLVKEKNIAVVAILHDLNLASMFCDKILFLKEGEIKYFGTSKELFT-QEI 231
Cdd:PRK13645 165 IAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSnQEL 244
|
....
gi 919308723 232 LKEI 235
Cdd:PRK13645 245 LTKI 248
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
17-217 |
2.14e-14 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 72.36 E-value: 2.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 17 LKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEfAKICG--FVPQksELNtplkvid 94
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRD-AQAAGiaIIHQ--ELN------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 95 vLL--MSKYANL-------KHAFSSYSKEdILEIKEFAKDLRLENFLERSILSLSGGEfQRML-LARALLKKPKILFLDE 164
Cdd:COG1129 90 -LVpnLSVAENIflgreprRGGLIDWRAM-RRRARELLARLGLDIDPDTPVGDLSVAQ-QQLVeIARALSRDARVLILDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 919308723 165 PTSALDLNYAIELLSLCEKLvKEKNIAVVAILHDLNLASMFCDKILFLKEGEI 217
Cdd:COG1129 167 PTASLTEREVERLFRIIRRL-KAQGVAIIYISHRLDEVFEIADRVTVLRDGRL 218
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
13-217 |
2.20e-14 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 72.45 E-value: 2.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 13 QKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKlILKNL-SPNKGEISLFNTNIKDFSLKEFAKI----CGFVPQKSELN 87
Cdd:PRK10535 20 QVEVLKGISLDIYAGEMVAIVGASGSGKSTLMN-ILGCLdKPTSGTYRVAGQDVATLDADALAQLrrehFGFIFQRYHLL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 88 TPLKVI-DVLLMSKYANLKhafssySKEDILEIKEFAKDLRLENFLERSILSLSGGEFQRMLLARALLKKPKILFLDEPT 166
Cdd:PRK10535 99 SHLTAAqNVEVPAVYAGLE------RKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 919308723 167 SALDLNYAIELLSLCEKLvKEKNIAVVAILHDLNLASMfCDKILFLKEGEI 217
Cdd:PRK10535 173 GALDSHSGEEVMAILHQL-RDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEI 221
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
32-202 |
2.67e-14 |
|
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: 69.44 E-value: 2.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 32 ILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIkDFSLKEFAKICGFVPQKSELNTPLKVIDvllmskyaNLK--HAFS 109
Cdd:cd03231 31 VTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPL-DFQRDSIARGLLYLGHAPGIKTTLSVLE--------NLRfwHADH 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 110 SYSkedilEIKEFAKDLRLENFLERSILSLSGGEFQRMLLARALLKKPKILFLDEPTSALDLNYAIELLSLCEKLVKEKN 189
Cdd:cd03231 102 SDE-----QVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGHCARGG 176
|
170
....*....|...
gi 919308723 190 IAVVAILHDLNLA 202
Cdd:cd03231 177 MVVLTTHQDLGLS 189
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
2-190 |
4.07e-14 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 71.98 E-value: 4.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 2 LKIHDLNFTYHQKD---LLKNIHLELKNQAFIGILGPNGSGKSTLLKLI-----LKN----------------------- 50
Cdd:PTZ00265 1166 IEIMDVNFRYISRPnvpIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLmrfydLKNdhhivfknehtndmtneqdyqgd 1245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 51 --------------------------LSPNKGEISLFNTNIKDFSLKEFAKICGFVPQKSELntplkvidvLLMSKYANL 104
Cdd:PTZ00265 1246 eeqnvgmknvnefsltkeggsgedstVFKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPML---------FNMSIYENI 1316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 105 KHAFSSYSKEDILEIKEFAKdlrLENFLERSI-----------LSLSGGEFQRMLLARALLKKPKILFLDEPTSALDLNy 173
Cdd:PTZ00265 1317 KFGKEDATREDVKRACKFAA---IDEFIESLPnkydtnvgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSN- 1392
|
250
....*....|....*..
gi 919308723 174 aiellslCEKLVkEKNI 190
Cdd:PTZ00265 1393 -------SEKLI-EKTI 1401
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-235 |
4.66e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 70.12 E-value: 4.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 1 MLKIHDLNFTYHQK---DLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEFAKIC 77
Cdd:PRK13642 4 ILEVENLVFKYEKEsdvNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 78 GFVPQkselNTPLKVIDVLLMSKYANLKHAFSSYSKEDILEIKEFAKDLRLENFLERSILSLSGGEFQRMLLARALLKKP 157
Cdd:PRK13642 84 GMVFQ----NPDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 919308723 158 KILFLDEPTSALDLNYAIELLSLCEKLVKEKNIAVVAILHDLNLASMfCDKILFLKEGEIKYFGTSKELF-TQEILKEI 235
Cdd:PRK13642 160 EIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFaTSEDMVEI 237
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-228 |
5.23e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 70.12 E-value: 5.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 6 DLNFTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLIlkNLSPNK-------GEISLFNTNIKDF-SLKEFAKIC 77
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTL--NRMNDKvsgyrysGDVLLGGRSIFNYrDVLEFRRRV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 78 GFVPQKSElNTPLKVIDVLLMSKYANL---KHAFSSYSKEDILEIKEFAKdlrLENFLERSILSLSGGEFQRMLLARALL 154
Cdd:PRK14271 104 GMLFQRPN-PFPMSIMDNVLAGVRAHKlvpRKEFRGVAQARLTEVGLWDA---VKDRLSDSPFRLSGGQQQLLCLARTLA 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 919308723 155 KKPKILFLDEPTSALDLNYAIELLSLCEKLVKEknIAVVAILHDLNLASMFCDKILFLKEGEIKYFGTSKELFT 228
Cdd:PRK14271 180 VNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFS 251
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
139-233 |
5.74e-14 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 70.16 E-value: 5.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 139 LSGGEFQRMLLARALLKKPKILFLDEPTSALDLNYAIELLSLCEKLVKEKNIAVVAILHDLNLASMFCDKILFLKEGEIK 218
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVV 233
|
90 100
....*....|....*....|..
gi 919308723 219 YFGTSKELF-------TQEILK 233
Cdd:PRK11022 234 ETGKAHDIFraprhpyTQALLR 255
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-170 |
1.02e-13 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 69.87 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 1 MLKIHDLNFTYHQK-DLLKNIHLELKNQAFIGILGPNGSGKSTLLKLI--LKNLSpnKGEISLFNTNIKDFSLKEfaKIC 77
Cdd:PRK11650 3 GLKLQAVRKSYDGKtQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVagLERIT--SGEIWIGGRVVNELEPAD--RDI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 78 GFVPQKSELnTPLkvidvllMSKYANLkhafsSY-------SKEDILE-IKEFAKDLRLENFLERSILSLSGGEFQRMLL 149
Cdd:PRK11650 79 AMVFQNYAL-YPH-------MSVRENM-----AYglkirgmPKAEIEErVAEAARILELEPLLDRKPRELSGGQRQRVAM 145
|
170 180
....*....|....*....|.
gi 919308723 150 ARALLKKPKILFLDEPTSALD 170
Cdd:PRK11650 146 GRAIVREPAVFLFDEPLSNLD 166
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
10-258 |
1.62e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 69.11 E-value: 1.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 10 TYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISL------------------FNTNIKDFslK 71
Cdd:PRK13631 35 QENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdkknnhelitnpYSKKIKNF--K 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 72 EFAKICGFVPQKSELNTPLKVIDVLLMSKYANLKHafssySKEDILEI-KEFAKDLRL-ENFLERSILSLSGGEFQRMLL 149
Cdd:PRK13631 113 ELRRRVSMVFQFPEYQLFKDTIEKDIMFGPVALGV-----KKSEAKKLaKFYLNKMGLdDSYLERSPFGLSGGQKRRVAI 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 150 ARALLKKPKILFLDEPTSALDLNYAIELLSLCeKLVKEKNIAVVAILHDLNLASMFCDKILFLKEGEIKYFGTSKELFTQ 229
Cdd:PRK13631 188 AGILAIQPEILIFDEPTAGLDPKGEHEMMQLI-LDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTD 266
|
250 260 270
....*....|....*....|....*....|....*..
gi 919308723 230 E--------ILKEIYDLNCEIIYKNSKPYILALKEKK 258
Cdd:PRK13631 267 QhiinstsiQVPRVIQVINDLIKKDPKYKKLYQKQPR 303
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
31-227 |
2.49e-13 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 68.60 E-value: 2.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 31 GILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEFAKICGFV------PQKSeLNTPLKVIDVL-------- 96
Cdd:COG4608 48 GLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPLRRRMqmvfqdPYAS-LNPRMTVGDIIaeplrihg 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 97 LMSKyanlkhafssyskediLEIKEFAKDLrLE------NFLERSILSLSGGEFQRMLLARALLKKPKILFLDEPTSALD 170
Cdd:COG4608 127 LASK----------------AERRERVAEL-LElvglrpEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALD 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 919308723 171 LNYAIELLSLCEKLVKEKNIAVVAILHDLNLASMFCDKILFLKEGEIKYFGTSKELF 227
Cdd:COG4608 190 VSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPRDELY 246
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-229 |
5.02e-13 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 68.27 E-value: 5.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 1 MLKIHDLNFTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLfntnIKDFSLKEFAkicgfv 80
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL----AKGIKLGYFA------ 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 81 pqKSELNtplkvidvLLMSKYANLKHAFSSYSKE------DILEIKEFAKDLRLENfLERsilsLSGGEFQRMLLARALL 154
Cdd:PRK10636 382 --QHQLE--------FLRADESPLQHLARLAPQEleqklrDYLGGFGFQGDKVTEE-TRR----FSGGEKARLVLALIVW 446
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 919308723 155 KKPKILFLDEPTSALDLNYAielLSLCEKLVKEKNiAVVAILHDLNLASMFCDKILFLKEGEIKYFGTSKELFTQ 229
Cdd:PRK10636 447 QRPNLLLLDEPTNHLDLDMR---QALTEALIDFEG-ALVVVSHDRHLLRSTTDDLYLVHDGKVEPFDGDLEDYQQ 517
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
17-233 |
6.75e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 67.89 E-value: 6.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 17 LKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEFAKI-CGFVPQKSELNTPLKVIDV 95
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLgIGIIYQELSVIDELTVLEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 96 LLMSKYANLKhaFSSYSKEDILEIKEFAKDLRLENFLERS----ILSLSGGEFQRMLLARALLKKPKILFLDEPTSALDl 171
Cdd:PRK09700 101 LYIGRHLTKK--VCGVNIIDWREMRVRAAMMLLRVGLKVDldekVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLT- 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 919308723 172 NYAIELLSLCEKLVKEKNIAVVAILHDLNLASMFCDKILFLKEGEIKYFGTSKELFTQEILK 233
Cdd:PRK09700 178 NKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSNDDIVR 239
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
19-217 |
7.82e-13 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 65.67 E-value: 7.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 19 NIHLELKNQAFIgiLGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKE---FAKICGFVPQKSELNTPLKVIDV 95
Cdd:PRK10908 22 TFHMRPGEMAFL--TGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQIGMIFQDHHLLMDRTVYDN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 96 LLMSKyanlkhAFSSYSKEDILEIKEFAKD-LRLENFLERSILSLSGGEFQRMLLARALLKKPKILFLDEPTSALDLNYA 174
Cdd:PRK10908 100 VAIPL------IIAGASGDDIRRRVSAALDkVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALS 173
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 919308723 175 IELLSLCEKLvKEKNIAVVAILHDLNLASMFCDKILFLKEGEI 217
Cdd:PRK10908 174 EGILRLFEEF-NRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-209 |
8.40e-13 |
|
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: 67.65 E-value: 8.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 2 LKIHDLNFTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTnikdfslkefAKIcGFVP 81
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGET----------VKL-AYVD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 82 QKSELNTPLKVI--------DVLLMSKYanlkhafssyskedilEIKEFAKDLRLeNFL----ERSILSLSGGEFQRMLL 149
Cdd:TIGR03719 392 QSRDALDPNKTVweeisgglDIIKLGKR----------------EIPSRAYVGRF-NFKgsdqQKKVGQLSGGERNRVHL 454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 150 ARALLKKPKILFLDEPTSALDLNyaiELLSLCEKLVKEKNIAVVaILHDlnlaSMFCDKI 209
Cdd:TIGR03719 455 AKTLKSGGNVLLLDEPTNDLDVE---TLRALEEALLNFAGCAVV-ISHD----RWFLDRI 506
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-197 |
1.18e-12 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 65.82 E-value: 1.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 1 MLKIHDLNFTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPN--KGEISLFNTNIKDFSLKEFAKICG 78
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKilEGDILFKGESILDLEPEERAHLGI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 79 FVpqksELNTPLKVIDV----LLMSKYaNLKHAFSSYSKEDILEIKEFAKD-LRL----ENFLERSI-LSLSGGEFQRML 148
Cdd:CHL00131 87 FL----AFQYPIEIPGVsnadFLRLAY-NSKRKFQGLPELDPLEFLEIINEkLKLvgmdPSFLSRNVnEGFSGGEKKRNE 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 919308723 149 LARALLKKPKILFLDEPTSALDLNyAIELLSLCEKLVKEKNIAVVAILH 197
Cdd:CHL00131 162 ILQMALLDSELAILDETDSGLDID-ALKIIAEGINKLMTSENSIILITH 209
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
4-226 |
1.20e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 67.46 E-value: 1.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 4 IHDLNFTYH---QKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKG-------------EIS-LFNTNIK 66
Cdd:PLN03130 617 IKNGYFSWDskaERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDasvvirgtvayvpQVSwIFNATVR 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 67 DFSLkeFAKicGFVPQKSElntplKVIDVllmskyANLKHAFSSYSKEDILEIKEfakdlrlenfleRSIlSLSGGEFQR 146
Cdd:PLN03130 697 DNIL--FGS--PFDPERYE-----RAIDV------TALQHDLDLLPGGDLTEIGE------------RGV-NISGGQKQR 748
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 147 MLLARALLKKPKILFLDEPTSALDLNYAIELLSLC--EKLVKEKNIAVVAILHDLNlasmFCDKILFLKEGEIKYFGTSK 224
Cdd:PLN03130 749 VSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCikDELRGKTRVLVTNQLHFLS----QVDRIILVHEGMIKEEGTYE 824
|
..
gi 919308723 225 EL 226
Cdd:PLN03130 825 EL 826
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
9-226 |
1.27e-12 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 65.97 E-value: 1.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 9 FTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIK--DFSLKEFAKICGFVPQKSEL 86
Cdd:PRK15112 21 FRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgDYSYRSQRIRMIFQDPSTSL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 87 NtPLKVIDVLLMSKYaNLKHAFSSYSKEdileiKEFAKDLRLENFLERSIL----SLSGGEFQRMLLARALLKKPKILFL 162
Cdd:PRK15112 101 N-PRQRISQILDFPL-RLNTDLEPEQRE-----KQIIETLRQVGLLPDHASyyphMLAPGQKQRLGLARALILRPKVIIA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 919308723 163 DEPTSALDLNYAIELLSLCEKLVKEKNIAVVAILHDLNLASMFCDKILFLKEGEIKYFGTSKEL 226
Cdd:PRK15112 174 DEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADV 237
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
16-202 |
1.28e-12 |
|
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: 64.69 E-value: 1.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 16 LLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSlKEFAKICGFVPQKSELNTPLKVIDv 95
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQR-DEPHENILYLGHLPGLKPELSALE- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 96 llmskyaNLK--HAFSSYSKEDILEIKEfakDLRLENFLERSILSLSGGEFQRMLLARALLKKPKILFLDEPTSALDLNy 173
Cdd:TIGR01189 93 -------NLHfwAAIHGGAQRTIEDALA---AVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA- 161
|
170 180 190
....*....|....*....|....*....|
gi 919308723 174 AIELL-SLCEKLVKEKNIAVVAILHDLNLA 202
Cdd:TIGR01189 162 GVALLaGLLRAHLARGGIVLLTTHQDLGLV 191
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-226 |
1.59e-12 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 65.56 E-value: 1.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 1 MLKIHDLNFTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFS---LKEFAKIC 77
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSrsrLYTVRKRM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 78 GFVPQKSELNTPLKVIDvllmskyaNLKHAFSSYSK--EDILE----IKEFAKDLRLENFLERSilSLSGGEFQRMLLAR 151
Cdd:PRK11831 87 SMLFQSGALFTDMNVFD--------NVAYPLREHTQlpAPLLHstvmMKLEAVGLRGAAKLMPS--ELSGGMARRAALAR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 919308723 152 ALLKKPKILFLDEPTSALDLNYAIELLSLCEKLVKEKNIAVVAILHDLNLASMFCDKILFLKEGEIKYFGTSKEL 226
Cdd:PRK11831 157 AIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQAL 231
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-236 |
1.72e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 64.90 E-value: 1.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 1 MLKIHDLNFTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFS----LKEFAKI 76
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQtakiMREAVAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 77 cgfVPQKSELNTPLKVIDVLLMSKYANLKHAFssysKEDILEIKEFAKDLrLENFLERSiLSLSGGEFQRMLLARALLKK 156
Cdd:PRK11614 85 ---VPEGRRVFSRMTVEENLAMGGFFAERDQF----QERIKWVYELFPRL-HERRIQRA-GTMSGGEQQMLAIGRALMSQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 157 PKILFLDEPTSALDLNYAIELLSLCEKLvKEKNIAVVAILHDLNLASMFCDKILFLKEGEIKYFGTSKELFTQEILKEIY 236
Cdd:PRK11614 156 PRLLLLDEPSLGLAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANEAVRSAY 234
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
17-216 |
2.16e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 66.29 E-value: 2.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 17 LKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEIsLFNTNIKDFSLKEFAKICGFVPQKSELNTPLK--VID 94
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSI-LFQGKEIDFKSSKEALENGISMVHQELNLVLQrsVMD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 95 VLLMSKYAnLKHAFSSYSKEdILEIKEFAKDLRLENFLERSILSLSGGEFQRMLLARALLKKPKILFLDEPTSALDLNYA 174
Cdd:PRK10982 93 NMWLGRYP-TKGMFVDQDKM-YRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEV 170
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 919308723 175 IELLSLCEKLvKEKNIAVVAILHDLNLASMFCDKILFLKEGE 216
Cdd:PRK10982 171 NHLFTIIRKL-KERGCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-217 |
4.59e-12 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 65.43 E-value: 4.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 2 LKIHDLNFT-YHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEF--AKIcG 78
Cdd:COG3845 258 LEVENLSVRdDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERrrLGV-A 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 79 FVP---QKSELNTPLKVIDVLLMSKYAnlKHAFSSYSKEDILEIKEFAKDLrLENF------LERSILSLSGGEFQRMLL 149
Cdd:COG3845 337 YIPedrLGRGLVPDMSVAENLILGRYR--RPPFSRGGFLDRKAIRAFAEEL-IEEFdvrtpgPDTPARSLSGGNQQKVIL 413
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 919308723 150 ARALLKKPKILFLDEPTSALDLNyAIELlsLCEKLVKEKN--IAVVAILHDLN--LAsmFCDKILFLKEGEI 217
Cdd:COG3845 414 ARELSRDPKLLIAAQPTRGLDVG-AIEF--IHQRLLELRDagAAVLLISEDLDeiLA--LSDRIAVMYEGRI 480
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
119-218 |
4.89e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 65.34 E-value: 4.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 119 IKEFAKDLRLENF-LERSILSLSGGEFQRMLLARALLKKPKILFLDEPTSALDLNYAIELLSLCEKLVKEkNIAVVAILH 197
Cdd:PRK13549 385 ILESIQRLKVKTAsPELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVISS 463
|
90 100
....*....|....*....|.
gi 919308723 198 DLNLASMFCDKILFLKEGEIK 218
Cdd:PRK13549 464 ELPEVLGLSDRVLVMHEGKLK 484
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-178 |
6.80e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 62.97 E-value: 6.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 1 MLKIHDLNFTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLfntNIKDFSLKEFAKICGFV 80
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKL---DGGDIDDPDVAEACHYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 81 PQKSELNTPLKVIDVLLMskYANLKHAfssyskeDILEIKEFAKDLRLENFLERSILSLSGGEFQRMLLARALLKKPKIL 160
Cdd:PRK13539 79 GHRNAMKPALTVAENLEF--WAAFLGG-------EELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIW 149
|
170
....*....|....*...
gi 919308723 161 FLDEPTSALDlNYAIELL 178
Cdd:PRK13539 150 ILDEPTAALD-AAAVALF 166
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
7-198 |
1.11e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 64.20 E-value: 1.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 7 LNFTYHQkdLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEIsLFNTNIK-----------------DF- 68
Cdd:PRK11147 11 LSFSDAP--LLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRI-IYEQDLIvarlqqdpprnvegtvyDFv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 69 ---------SLKEFAKICGFV---PQKSELNTPLKVIDVLlmsKYANLKHaFSSyskedilEIKEFAKDLRLENflERSI 136
Cdd:PRK11147 88 aegieeqaeYLKRYHDISHLVetdPSEKNLNELAKLQEQL---DHHNLWQ-LEN-------RINEVLAQLGLDP--DAAL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 919308723 137 LSLSGGEFQRMLLARALLKKPKILFLDEPTSALDLNyAIELLslcEKLVKEKNIAVVAILHD 198
Cdd:PRK11147 155 SSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIE-TIEWL---EGFLKTFQGSIIFISHD 212
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
139-227 |
1.64e-11 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 62.41 E-value: 1.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 139 LSGGEFQRMLLARALLKKPKILFLDEPTSALDLNYAIELLSLCEKLVKEKNIAVVAILHDLNLASMFCDKILFLKEGEIK 218
Cdd:PRK10418 141 MSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIV 220
|
....*....
gi 919308723 219 YFGTSKELF 227
Cdd:PRK10418 221 EQGDVETLF 229
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
17-241 |
2.19e-11 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 63.37 E-value: 2.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 17 LKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEIslfntNIKDFSlkefakicGFVPQKSELNTPLKVIDVL 96
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV-----DIKGSA--------ALIAISSGLNGQLTGIENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 97 lmskyaNLKHAFSSYSKEDILEIK----EFAKdlrLENFLERSILSLSGGEFQRMLLARALLKKPKILFLDEPTSALDLN 172
Cdd:PRK13545 107 ------ELKGLMMGLTKEKIKEIIpeiiEFAD---IGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQT 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 919308723 173 YAIELLSLCEKLvKEKNIAVVAILHDLNLASMFCDKILFLKEGEIKYFGTSKELFTQ--EILKEIYDLNCE 241
Cdd:PRK13545 178 FTKKCLDKMNEF-KEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDHydEFLKKYNQMSVE 247
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
23-222 |
2.42e-11 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 60.66 E-value: 2.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 23 ELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIkdfslkefakicGFVPQKselntplkvidvllmskya 102
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITP------------VYKPQY------------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 103 nlkhafssyskedileikefakdlrlenflersiLSLSGGEFQRMLLARALLKKPKILFLDEPTSALDLNYAIELLSLCE 182
Cdd:cd03222 70 ----------------------------------IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIR 115
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 919308723 183 KLVKEKNIAVVAILHDLNLASMFCDKILFLkEGEIKYFGT 222
Cdd:cd03222 116 RLSEEGKKTALVVEHDLAVLDYLSDRIHVF-EGEPGVYGI 154
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
17-216 |
2.66e-11 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 63.12 E-value: 2.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 17 LKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFN--TNIKD---------------FSLkefakicgf 79
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGkpVRIRSprdaialgigmvhqhFML--------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 80 VPqkselntPLKVIDVLLMSkYANLKHAFSSYSKEdILEIKEFAKDLRLENFLERSILSLSGGEFQRMLLARALLKKPKI 159
Cdd:COG3845 92 VP-------NLTVAENIVLG-LEPTKGGRLDRKAA-RARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARI 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 919308723 160 LFLDEPTSALDLNYAIELLSLCEKLVKEkNIAVVAILHDLN--LAsmFCDKILFLKEGE 216
Cdd:COG3845 163 LILDEPTAVLTPQEADELFEILRRLAAE-GKSIIFITHKLRevMA--IADRVTVLRRGK 218
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
29-213 |
2.68e-11 |
|
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: 60.08 E-value: 2.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 29 FIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNikdfslkefakicgfvpqkselntplkvidvllmskyanlkhaf 108
Cdd:smart00382 4 VILIVGPPGSGKTTLARALARELGPPGGGVIYIDGE-------------------------------------------- 39
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 109 ssyskedilEIKEFAKDLRLENFLERSILSLSGGEFQRMLLARALLKKPKILFLDEPTSALDLNYAIELLSLCE-----K 183
Cdd:smart00382 40 ---------DILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrlllL 110
|
170 180 190
....*....|....*....|....*....|....*.
gi 919308723 184 LVKEKNIAVVAI------LHDLNLASMFCDKILFLK 213
Cdd:smart00382 111 LKSEKNLTVILTtndekdLGPALLRRRFDRRIVLLL 146
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
140-199 |
3.48e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 62.29 E-value: 3.48e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 140 SGGEFQRMLLARALLKKPKILFLDEPTSALDLNYAIELLSLCEKLVKEKNIAVVAILHDL 199
Cdd:PRK11308 156 SGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDL 215
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
31-226 |
4.59e-11 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 62.72 E-value: 4.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 31 GILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDfSLKEFAKICGFVPQkselntpLKVIDVLLMSK-----YANLK 105
Cdd:TIGR01257 1969 GLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISDVHQNMGYCPQ-------FDAIDDLLTGRehlylYARLR 2040
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 106 hafsSYSKEDILEIKEFA-KDLRLENFLERSILSLSGGEFQRMLLARALLKKPKILFLDEPTSALDLNYAIELLSLCEKL 184
Cdd:TIGR01257 2041 ----GVPAEEIEKVANWSiQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSI 2116
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 919308723 185 VKEKNiAVVAILHDLNLASMFCDKILFLKEGEIKYFGTSKEL 226
Cdd:TIGR01257 2117 IREGR-AVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHL 2157
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
19-230 |
4.82e-11 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 62.15 E-value: 4.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 19 NIHLELKNQAFIGILGPNGSGKSTLLKLILkNLSPNKGEISLF----NTNIKDFSLKEFAKIC---------GFVPQKS- 84
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALF-GAYPGKFEGNVFingkPVDIRNPAQAIRAGIAmvpedrkrhGIVPILGv 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 85 ELNTPLKVID----VLLMSKYANLKHAFSSYSKediLEIKEFAKDLrlenflerSILSLSGGEFQRMLLARALLKKPKIL 160
Cdd:TIGR02633 357 GKNITLSVLKsfcfKMRIDAAAELQIIGSAIQR---LKVKTASPFL--------PIGRLSGGNQQKAVLAKMLLTNPRVL 425
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 161 FLDEPTSALDLNYAIELLSLCEKLVKEkNIAVVAILHDLNLASMFCDKILFLKEGEIKYFGTSKELfTQE 230
Cdd:TIGR02633 426 ILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKLKGDFVNHAL-TQE 493
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1-229 |
7.02e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 61.57 E-value: 7.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 1 MLKIHDLNFTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGE-ISLFNTnIKDFSLKEFAKICGF 79
Cdd:PRK10938 3 SLQISQGTFRLSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGErQSQFSH-ITRLSFEQLQKLVSD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 80 VPQKSelNTPLKVIDvllmskyanlKHAFSSYSKEDIL-EIK------EFAKDLRLENFLERSILSLSGGEFQRMLLARA 152
Cdd:PRK10938 82 EWQRN--NTDMLSPG----------EDDTGRTTAEIIQdEVKdparceQLAQQFGITALLDRRFKYLSTGETRKTLLCQA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 919308723 153 LLKKPKILFLDEPTSALDLNYAIELLSLCEKLVKEKnIAVVAILHDLNLASMFCDKILFLKEGEIKYFGTSKELFTQ 229
Cdd:PRK10938 150 LMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSG-ITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQQ 225
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
6-225 |
1.24e-10 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 61.41 E-value: 1.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 6 DLNFTYHQKDLL-KNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGeiSLFNTnikdfslkefAKICGFVPQKS 84
Cdd:PLN03073 513 DASFGYPGGPLLfKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSG--TVFRS----------AKVRMAVFSQH 580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 85 ELN-TPLKVIDVLLMSkyanlkHAFSSYSKEDI-LEIKEFAKDlrlENFLERSILSLSGGEFQRMLLARALLKKPKILFL 162
Cdd:PLN03073 581 HVDgLDLSSNPLLYMM------RCFPGVPEQKLrAHLGSFGVT---GNLALQPMYTLSGGQKSRVAFAKITFKKPHILLL 651
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 919308723 163 DEPTSALDLNyAIEllSLCEKLVKEKNiAVVAILHDLNLASMFCDKILFLKEGEIKYF-GTSKE 225
Cdd:PLN03073 652 DEPSNHLDLD-AVE--ALIQGLVLFQG-GVLMVSHDEHLISGSVDELWVVSEGKVTPFhGTFHD 711
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
13-220 |
1.27e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 59.59 E-value: 1.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 13 QKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLS--PNKGEISLFNTNIkdfslkefakicgfvPQKSELntpl 90
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVPDNQF---------------GREASL---- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 91 kvIDVLlmskyanlkhafssYSKEDILEIKEFAKDLRL-ENFL-ERSILSLSGGEFQRMLLARALLKKPKILFLDEPTSA 168
Cdd:COG2401 103 --IDAI--------------GRKGDFKDAVELLNAVGLsDAVLwLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSH 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 919308723 169 LDLNYAIELLSLCEKLVKEKNIAVVAILHDLNLAS-MFCDKILFLKEG---EIKYF 220
Cdd:COG2401 167 LDRQTAKRVARNLQKLARRAGITLVVATHHYDVIDdLQPDLLIFVGYGgvpEEKRR 222
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
33-222 |
1.54e-10 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 61.18 E-value: 1.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 33 LGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDfSLKEFAKICGFVPQKSELNTPLKVIDVLLMskYANLKhafSSYS 112
Cdd:TIGR01257 962 LGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNILFHHLTVAEHILF--YAQLK---GRSW 1035
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 113 KEDILEIKEFAKDLRLENFLERSILSLSGGEFQRMLLARALLKKPKILFLDEPTSALDlnyAIELLSLCEKLVKEKN-IA 191
Cdd:TIGR01257 1036 EEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVD---PYSRRSIWDLLLKYRSgRT 1112
|
170 180 190
....*....|....*....|....*....|.
gi 919308723 192 VVAILHDLNLASMFCDKILFLKEGEIKYFGT 222
Cdd:TIGR01257 1113 IIMSTHHMDEADLLGDRIAIISQGRLYCSGT 1143
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
139-245 |
2.33e-10 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 59.82 E-value: 2.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 139 LSGGEFQRMLLARALLKKPKILFLDEPTSALDLNYAIELLSLCEKLVKEKNIAVVAILHDLNLASMFCDKILFLKEGEIK 218
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTV 238
|
90 100 110
....*....|....*....|....*....|....
gi 919308723 219 YFGTSKEL-------FTQEILKEIYDLNCEIIYK 245
Cdd:PRK15093 239 ETAPSKELvttphhpYTQALIRAIPDFGSAMPHK 272
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
8-233 |
2.49e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 60.18 E-value: 2.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 8 NFTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFS-----------LKEFAKI 76
Cdd:PRK09700 270 NVTSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSpldavkkgmayITESRRD 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 77 CGFVPQKSeLNTPLKVIDVLLMSKYANLKHAFSSYSKEDILEIKEfaKDLRLE-NFLERSILSLSGGEFQRMLLARALLK 155
Cdd:PRK09700 350 NGFFPNFS-IAQNMAISRSLKDGGYKGAMGLFHEVDEQRTAENQR--ELLALKcHSVNQNITELSGGNQQKVLISKWLCC 426
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 919308723 156 KPKILFLDEPTSALDLNYAIELLSLCEKLVkEKNIAVVAILHDLNLASMFCDKILFLKEGEI-KYFGTSKELFTQEILK 233
Cdd:PRK09700 427 CPEVIIFDEPTRGIDVGAKAEIYKVMRQLA-DDGKVILMVSSELPEIITVCDRIAVFCEGRLtQILTNRDDMSEEEIMA 504
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
139-245 |
3.43e-10 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 59.15 E-value: 3.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 139 LSGGEFQRMLLARALLKKPKILFLDEPTSALDLNYAIELLSLCEKLVKEKNIAVVAILHDLNLASMFCDKILFLKEGEIK 218
Cdd:COG4170 159 LTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTV 238
|
90 100 110
....*....|....*....|....*....|....
gi 919308723 219 YFGTSKELF-------TQEILKEIYDLNCEIIYK 245
Cdd:COG4170 239 ESGPTEQILksphhpyTKALLRSMPDFRQPLPHK 272
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
30-214 |
3.65e-10 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 59.80 E-value: 3.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 30 IGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTnikdFSLkefakicGFVPQKS-ELNTPL--KVID----------VL 96
Cdd:PRK10636 30 VGLVGKNGCGKSTLLALLKNEISADGGSYTFPGN----WQL-------AWVNQETpALPQPAleYVIDgdreyrqleaQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 97 LMSKYANLKHAFSS-YSKEDILE---IKEFAKDLrLENF------LERSILSLSGGEFQRMLLARALLKKPKILFLDEPT 166
Cdd:PRK10636 99 HDANERNDGHAIATiHGKLDAIDawtIRSRAASL-LHGLgfsneqLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPT 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 919308723 167 SALDLNYAIELlslcEKLVKEKNIAVVAILHDLNLASMFCDKILFLKE 214
Cdd:PRK10636 178 NHLDLDAVIWL----EKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQ 221
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
3-170 |
3.77e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 60.04 E-value: 3.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 3 KIHDLNFTYH---QKD--LLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNT-NIKDFSLKEFAKI 76
Cdd:PTZ00265 382 KIQFKNVRFHydtRKDveIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDShNLKDINLKWWRSK 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 77 CGFVPQ---------KSELNTPLKVI-DVLLMSKYAN-----------------------------------LKHAFSSY 111
Cdd:PTZ00265 462 IGVVSQdpllfsnsiKNNIKYSLYSLkDLEALSNYYNedgndsqenknkrnscrakcagdlndmsnttdsneLIEMRKNY 541
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 112 SKEDILEIKEFAKDLRLENFLE-----------RSILSLSGGEFQRMLLARALLKKPKILFLDEPTSALD 170
Cdd:PTZ00265 542 QTIKDSEVVDVSKKVLIHDFVSalpdkyetlvgSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
4-232 |
4.31e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 59.25 E-value: 4.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 4 IHDLNFTYHQKDLLknihlelknqafiGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSlkefakicgfvPQK 83
Cdd:PRK10762 268 VNDVSFTLRKGEIL-------------GVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRS-----------PQD 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 84 SeLNTPLKVID--------VLLMSKYAN-----LKHaFSSYS-----KEDILEIKEFakdLRLENF----LERSILSLSG 141
Cdd:PRK10762 324 G-LANGIVYISedrkrdglVLGMSVKENmsltaLRY-FSRAGgslkhADEQQAVSDF---IRLFNIktpsMEQAIGLLSG 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 142 GEFQRMLLARALLKKPKILFLDEPTSALDLNYAIELLSLCEKLvKEKNIAVVAILHDLNLASMFCDKILFLKEGEIkyfg 221
Cdd:PRK10762 399 GNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQF-KAEGLSIILVSSEMPEVLGMSDRILVMHEGRI---- 473
|
250
....*....|....*
gi 919308723 222 tSKELF----TQEIL 232
Cdd:PRK10762 474 -SGEFTreqaTQEKL 487
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-235 |
7.88e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 58.52 E-value: 7.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 1 MLKIHDLNFTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEfAKICG-- 78
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAK-AHQLGiy 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 79 FVPQKSELNTPLKVIDVLL--MSKYAnlkhafSSYSKedileIKEFAKDLRLENFLERSILSLSGGEFQRMLLARALLKK 156
Cdd:PRK15439 90 LVPQEPLLFPNLSVKENILfgLPKRQ------ASMQK-----MKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 919308723 157 PKILFLDEPTSALDLNYAIELLSLCEKLvKEKNIAVVAILHDLNLASMFCDKILFLKEGEIKYFGTSKELFTQEILKEI 235
Cdd:PRK15439 159 SRILILDEPTASLTPAETERLFSRIREL-LAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTDDIIQAI 236
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1-203 |
1.00e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 56.74 E-value: 1.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 1 MLKIHDLNFTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDfSLKEFAKI---C 77
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRR-QRDEYHQDllyL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 78 GFVPQ-KSELnTPLKvidvllmskyaNLK---HAFSSYSKEDILEIkefakdLR---LENFLERSILSLSGGEFQRMLLA 150
Cdd:PRK13538 80 GHQPGiKTEL-TALE-----------NLRfyqRLHGPGDDEALWEA------LAqvgLAGFEDVPVRQLSAGQQRRVALA 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 919308723 151 RALLKKPKILFLDEPTSALDLNYAIELLSLCEKLVKEKNIAVVAILHDLNLAS 203
Cdd:PRK13538 142 RLWLTRAPLWILDEPFTAIDKQGVARLEALLAQHAEQGGMVILTTHQDLPVAS 194
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
17-215 |
1.22e-09 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 56.57 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 17 LKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEFAKI----CGFVPQKSELNTPLKV 92
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQKPWLLNATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 93 IDVLLMSKY--ANLKHAFSSYSKEDILEIKEFAKDLRLEnflERSIlSLSGGEFQRMLLARALLKKPKILFLDEPTSALD 170
Cdd:cd03290 97 ENITFGSPFnkQRYKAVTDACSLQPDIDLLPFGDQTEIG---ERGI-NLSGGQRQRICVARALYQNTNIVFLDDPFSALD 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 919308723 171 LNYAIELLSL-CEKLVKEKNIAVVAILHDLNLASmFCDKILFLKEG 215
Cdd:cd03290 173 IHLSDHLMQEgILKFLQDDKRTLVLVTHKLQYLP-HADWIIAMKDG 217
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
17-227 |
1.43e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 57.94 E-value: 1.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 17 LKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSlkefakicgfvpqKSELNTPLKVIDVL 96
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLS-------------PGKLQALRRDIQFI 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 97 LMSKYANLKHAFS-SYSKEDILEIKEF----AKDLRLENFLERSIL----------SLSGGEFQRMLLARALLKKPKILF 161
Cdd:PRK10261 407 FQDPYASLDPRQTvGDSIMEPLRVHGLlpgkAAAARVAWLLERVGLlpehawryphEFSGGQRQRICIARALALNPKVII 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 919308723 162 LDEPTSALDLNYAIELLSLCEKLVKEKNIAVVAILHDLNLASMFCDKILFLKEGEIKYFGTSKELF 227
Cdd:PRK10261 487 ADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVF 552
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
31-217 |
2.62e-09 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 56.95 E-value: 2.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 31 GILGPNGSGKSTLLKLILKNLSPNKGEISLFN-----TNIKDfSLKefAKIcGFVPQ--KSE-LNTPLKVIDVLLMSKYA 102
Cdd:COG1129 282 GIAGLVGAGRTELARALFGADPADSGEIRLDGkpvriRSPRD-AIR--AGI-AYVPEdrKGEgLVLDLSIRENITLASLD 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 103 NLKHA-FSSYSKEDILeIKEFAKDLRLE-NFLERSILSLSGGEFQRMLLARALLKKPKILFLDEPTSALDLNYAIELLSL 180
Cdd:COG1129 358 RLSRGgLLDRRRERAL-AEEYIKRLRIKtPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRL 436
|
170 180 190
....*....|....*....|....*....|....*...
gi 919308723 181 CEKLVKEkNIAVVAILHDLN-LASMfCDKILFLKEGEI 217
Cdd:COG1129 437 IRELAAE-GKAVIVISSELPeLLGL-SDRILVMREGRI 472
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
16-197 |
5.17e-09 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 56.30 E-value: 5.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 16 LLKNIHLELKNQAFIGILGPNGSGKSTLLKlILKNLSPNKGeislfNTNIKDFSLKEFakicgFVPQKSEL-NTPLKVID 94
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFR-ILGELWPVYG-----GRLTKPAKGKLF-----YVPQRPYMtLGTLRDQI 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 95 VLLMSKYANLKHAFSSYSKEDILEikefakDLRLENFLER----SILS-----LSGGEFQRMLLARALLKKPKILFLDEP 165
Cdd:TIGR00954 536 IYPDSSEDMKRRGLSDKDLEQILD------NVQLTHILEReggwSAVQdwmdvLSGGEKQRIAMARLFYHKPQFAILDEC 609
|
170 180 190
....*....|....*....|....*....|..
gi 919308723 166 TSALDLNYAIELLSLCeklvKEKNIAVVAILH 197
Cdd:TIGR00954 610 TSAVSVDVEGYMYRLC----REFGITLFSVSH 637
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
17-210 |
5.70e-09 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 55.31 E-value: 5.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 17 LKNIHLELKNQAFIGILGPNGSGKSTLL----------KLILKNLSP-NKGEISLFN----------------------T 63
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLIndtlypalarRLHLKKEQPgNHDRIEGLEhidkvividqspigrtprsnpaT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 64 NIKDFSL--KEFAKICG---FVPQKSELNTPLKVI-DVLLMSKYANLKHaFSSYSKedILEIKEFAKDLRLENF-LERSI 136
Cdd:cd03271 91 YTGVFDEirELFCEVCKgkrYNRETLEVRYKGKSIaDVLDMTVEEALEF-FENIPK--IARKLQTLCDVGLGYIkLGQPA 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 919308723 137 LSLSGGEFQRMLLARALLKK---PKILFLDEPTSALDLNYAIELLSLCEKLVKEKNiAVVAILHDLNLASMfCDKIL 210
Cdd:cd03271 168 TTLSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGN-TVVVIEHNLDVIKC-ADWII 242
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
8-221 |
9.43e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 55.89 E-value: 9.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 8 NFTYHQK------DLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPN--KGEISLFNTNIKDFSlkeFAKICGF 79
Cdd:TIGR00956 764 NLTYEVKikkekrVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTGviTGGDRLVNGRPLDSS---FQRSIGY 840
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 80 VpQKSELNTP-LKVIDVLLMSKYANLKHAFSSYSKEDILEikEFAKDLRLENFLErSILSLSGG-----EFQRMLLARAL 153
Cdd:TIGR00956 841 V-QQQDLHLPtSTVRESLRFSAYLRQPKSVSKSEKMEYVE--EVIKLLEMESYAD-AVVGVPGEglnveQRKRLTIGVEL 916
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 919308723 154 LKKPK-ILFLDEPTSALDLNYAIELLSLCEKLVKEKNiAVVAILH--DLNLASMFcDKILFLKEG-EIKYFG 221
Cdd:TIGR00956 917 VAKPKlLLFLDEPTSGLDSQTAWSICKLMRKLADHGQ-AILCTIHqpSAILFEEF-DRLLLLQKGgQTVYFG 986
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
2-230 |
1.19e-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: 55.34 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 2 LKIHDLNFTYHQKD--LLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTnikdfslkefakiCGF 79
Cdd:TIGR00957 637 ITVHNATFTWARDLppTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-------------VAY 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 80 VPQKSELNTPLKVIDVLLmskyanlKHAFSSYSKEDILEIKEFAKDLRLENFLERSIL-----SLSGGEFQRMLLARALL 154
Cdd:TIGR00957 704 VPQQAWIQNDSLRENILF-------GKALNEKYYQQVLEACALLPDLEILPSGDRTEIgekgvNLSGGQKQRVSLARAVY 776
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 155 KKPKILFLDEPTSALDLNYAIELLslcEKLVKE----KNIAVVAILHDLNLASMfCDKILFLKEGEIKYFGTSKELFTQE 230
Cdd:TIGR00957 777 SNADIYLFDDPLSAVDAHVGKHIF---EHVIGPegvlKNKTRILVTHGISYLPQ-VDVIIVMSGGKISEMGSYQELLQRD 852
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
18-231 |
1.74e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 54.67 E-value: 1.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 18 KNIHLELKNQAFIGILGPNGSGKsTLLKLILKNLSPNK-GEISLFNTNIKDFSLKE-FAKICGFVP---QKSELN--TPL 90
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGR-TELAETLYGLRPARgGRIMLNGKEINALSTAQrLARGLVYLPedrQSSGLYldAPL 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 91 KVIDVLLMSkyaNLKHAFSSYSKED-ILEIKEFAKDLRLENfLERSILSLSGGEFQRMLLARALLKKPKILFLDEPTSAL 169
Cdd:PRK15439 359 AWNVCALTH---NRRGFWIKPARENaVLERYRRALNIKFNH-AEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGV 434
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 919308723 170 DLNYAIELLSLCEKLVKEkNIAVVAILHDLNLASMFCDKILFLKEGEIkyfgtSKELFTQEI 231
Cdd:PRK15439 435 DVSARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEI-----SGALTGAAI 490
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1-172 |
3.84e-08 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 52.87 E-value: 3.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 1 MLKIHDLNFTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLIL--KNLSPNKGEISLFNTNIKDFSLKEFAKICG 78
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGTVEFKGKDLLELSPEDRAGEGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 79 FVPQKSELNTPlKVIDVLLMSKYANlkhAFSSYSKEDILE-------IKEFAKDLRL-ENFLERSI-LSLSGGEFQRMLL 149
Cdd:PRK09580 81 FMAFQYPVEIP-GVSNQFFLQTALN---AVRSYRGQEPLDrfdfqdlMEEKIALLKMpEDLLTRSVnVGFSGGEKKRNDI 156
|
170 180
....*....|....*....|...
gi 919308723 150 ARALLKKPKILFLDEPTSALDLN 172
Cdd:PRK09580 157 LQMAVLEPELCILDESDSGLDID 179
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1-170 |
3.99e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 52.18 E-value: 3.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 1 MLKIHDLNFTYHQKDLLkNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSlKEFakiCGFV 80
Cdd:PRK13541 1 MLSLHQLQFNIEQKNLF-DLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIA-KPY---CTYI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 81 PQkselNTPLKvidvLLMSKYANLKHAFSSYSKEDILE--IKEFakdlRLENFLERSILSLSGGEFQRMLLARALLKKPK 158
Cdd:PRK13541 76 GH----NLGLK----LEMTVFENLKFWSEIYNSAETLYaaIHYF----KLHDLLDEKCYSLSSGMQKIVAIARLIACQSD 143
|
170
....*....|..
gi 919308723 159 ILFLDEPTSALD 170
Cdd:PRK13541 144 LWLLDEVETNLS 155
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
14-220 |
6.09e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 52.97 E-value: 6.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 14 KDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLfNTNIK-------DFSLKEFakicgfvpqksel 86
Cdd:PRK15064 14 KPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSL-DPNERlgklrqdQFAFEEF------------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 87 ntplKVIDVLLMSK-------------YANLKHAFSSYSKEDILEIkEFAK------DLRL-ENFLERSI-LSLSGGEFQ 145
Cdd:PRK15064 80 ----TVLDTVIMGHtelwevkqerdriYALPEMSEEDGMKVADLEV-KFAEmdgytaEARAgELLLGVGIpEEQHYGLMS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 146 --------RMLLARALLKKPKILFLDEPTSALDLNyAIELLslcEKLVKEKNIAVVAILHDLNLASMFCDKILFLKEGEI 217
Cdd:PRK15064 155 evapgwklRVLLAQALFSNPDILLLDEPTNNLDIN-TIRWL---EDVLNERNSTMIIISHDRHFLNSVCTHMADLDYGEL 230
|
...
gi 919308723 218 KYF 220
Cdd:PRK15064 231 RVY 233
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
135-233 |
7.16e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 52.81 E-value: 7.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 135 SILSLSGGEFQRMLLARALLKKPKILFLDEPTSALDLNYAIELLSLCEKLVKeKNIAVVAILHDLNLASMFCDKILFLKE 214
Cdd:PRK10982 388 QIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAK-KDKGIIIISSEMPELLGITDRILVMSN 466
|
90
....*....|....*....
gi 919308723 215 GEIKYFGTSKELFTQEILK 233
Cdd:PRK10982 467 GLVAGIVDTKTTTQNEILR 485
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
132-199 |
7.88e-08 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 52.71 E-value: 7.88e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 919308723 132 LERSILSLSGGEFQRMLLARALLKK---PKILFLDEPTSALDLNYAIELLSLCEKLVKEKNiAVVAILHDL 199
Cdd:TIGR00630 823 LGQPATTLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGN-TVVVIEHNL 892
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
2-230 |
9.63e-08 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 51.45 E-value: 9.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 2 LKIHDLNFTYHQ--KDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEFakicgf 79
Cdd:cd03288 20 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTL------ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 80 vpqKSELNTPLKviDVLLMSKYANLKHAFSSYSKED-------ILEIKEFAKDLR--LENFLERSILSLSGGEFQRMLLA 150
Cdd:cd03288 94 ---RSRLSIILQ--DPILFSGSIRFNLDPECKCTDDrlwealeIAQLKNMVKSLPggLDAVVTEGGENFSVGQRQLFCLA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 151 RALLKKPKILFLDEPTSALDLnyAIEllSLCEKLVKE--KNIAVVAILHDLNlASMFCDKILFLKEGEIKYFGTSKELFT 228
Cdd:cd03288 169 RAFVRKSSILIMDEATASIDM--ATE--NILQKVVMTafADRTVVTIAHRVS-TILDADLVLVLSRGILVECDTPENLLA 243
|
..
gi 919308723 229 QE 230
Cdd:cd03288 244 QE 245
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
4-209 |
1.86e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 51.66 E-value: 1.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 4 IHDLNFTyhqkdLLKNihlelknqAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTnikdfslkefAKIcGFVPQK 83
Cdd:PRK11819 340 IDDLSFS-----LPPG--------GIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGET----------VKL-AYVDQS 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 84 SELNTPLKVI--------DVLLMSKYanlkhafssyskedilEIKEFAKDLRLeNFL----ERSILSLSGGEFQRMLLAR 151
Cdd:PRK11819 396 RDALDPNKTVweeisgglDIIKVGNR----------------EIPSRAYVGRF-NFKggdqQKKVGVLSGGERNRLHLAK 458
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 919308723 152 ALLKKPKILFLDEPTSALDLNyaiELLSLCEKLVKEKNIAVVaILHDlnlaSMFCDKI 209
Cdd:PRK11819 459 TLKQGGNVLLLDEPTNDLDVE---TLRALEEALLEFPGCAVV-ISHD----RWFLDRI 508
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
133-217 |
2.40e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 51.07 E-value: 2.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 133 ERSILSLSGGEFQRMLLARALLKKPKILFLDEPTSALDLNYAIELLSLCEKLVkEKNIAVVAILHDLNLASMFCDKILFL 212
Cdd:PRK11288 391 EQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELA-AQGVAVLFVSSDLPEVLGVADRIVVM 469
|
....*
gi 919308723 213 KEGEI 217
Cdd:PRK11288 470 REGRI 474
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
14-248 |
4.89e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 50.49 E-value: 4.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 14 KDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNK----GEISlFNTnikdFSLKEFAK-ICGFVPQKSELNT 88
Cdd:TIGR00956 74 FDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDGFHigveGVIT-YDG----ITPEEIKKhYRGDVVYNAETDV 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 89 PLKVIDV-----------------LLMSKYANLKHAFSSYSKEDILEIkefAKDLRLENFLERSIlslSGGEFQRMLLAR 151
Cdd:TIGR00956 149 HFPHLTVgetldfaarcktpqnrpDGVSREEYAKHIADVYMATYGLSH---TRNTKVGNDFVRGV---SGGERKRVSIAE 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 152 ALLKKPKILFLDEPTSALDLNYAIELLSLCEKLVKE-KNIAVVAILHDLNLASMFCDKILFLKEGEIKYFGTS---KELF 227
Cdd:TIGR00956 223 ASLGGAKIQCWDNATRGLDSATALEFIRALKTSANIlDTTPLVAIYQCSQDAYELFDKVIVLYEGYQIYFGPAdkaKQYF 302
|
250 260 270
....*....|....*....|....*....|...
gi 919308723 228 ------------TQEILKEIYDLNCEIIYKNSK 248
Cdd:TIGR00956 303 ekmgfkcpdrqtTADFLTSLTSPAERQIKPGYE 335
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2-217 |
5.32e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 49.97 E-value: 5.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 2 LKIHDLNFTYHQKDL-LKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEFAKicgfv 80
Cdd:PRK10522 323 LELRNVTFAYQDNGFsVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRK----- 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 81 pQKSELNTPLKVIDVLLMSKyanlKHAFSSYSKEDILEIKEFAKDLRLENFlERSILSLSGGEFQRMLLARALLKKPKIL 160
Cdd:PRK10522 398 -LFSAVFTDFHLFDQLLGPE----GKPANPALVEKWLERLKMAHKLELEDG-RISNLKLSKGQKKRLALLLALAEERDIL 471
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 919308723 161 FLDEPTSALDLNYAIELLSLCEKLVKEKNIAVVAILHDLNLASMfCDKILFLKEGEI 217
Cdd:PRK10522 472 LLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHDDHYFIH-ADRLLEMRNGQL 527
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
17-198 |
6.26e-07 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 48.79 E-value: 6.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 17 LKNIHLELKNQAFIGILGPNGSGKSTLL---------KLILKNLSPnkgeisLFNTNIKDFSLKEFAKICGFVP-----Q 82
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLAfdtiyaegqRRYVESLSA------YARQFLGQMDKPDVDSIEGLSPaiaidQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 83 KSELNTPLKVIDVL--LMSKYANLkhafssYSKEDILEIKEFAKDLRLENF-LERSILSLSGGEFQRMLLARALLKK-PK 158
Cdd:cd03270 85 KTTSRNPRSTVGTVteIYDYLRLL------FARVGIRERLGFLVDVGLGYLtLSRSAPTLSGGEAQRIRLATQIGSGlTG 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 919308723 159 ILF-LDEPTSAL---DLNYAIELLslceKLVKEKNIAVVAILHD 198
Cdd:cd03270 159 VLYvLDEPSIGLhprDNDRLIETL----KRLRDLGNTVLVVEHD 198
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
16-222 |
6.27e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 50.23 E-value: 6.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 16 LLKNIHLELKNQAFIGILGPNGSGKSTLLKLIL--KNLSPNKGEIslfntNIKDFSLKE--FAKICGFVPQkSELNTP-L 90
Cdd:PLN03140 895 LLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAgrKTGGYIEGDI-----RISGFPKKQetFARISGYCEQ-NDIHSPqV 968
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 91 KVIDVLLMSKYANLKHAFSSYSK----EDILEIKEfakdlrLENfLERSILSLSG------GEFQRMLLARALLKKPKIL 160
Cdd:PLN03140 969 TVRESLIYSAFLRLPKEVSKEEKmmfvDEVMELVE------LDN-LKDAIVGLPGvtglstEQRKRLTIAVELVANPSII 1041
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 919308723 161 FLDEPTSALDLNYAIELLSLCEKLVkEKNIAVVAILH--DLNLASMFcDKILFLKE-GEIKYFGT 222
Cdd:PLN03140 1042 FMDEPTSGLDARAAAIVMRTVRNTV-DTGRTVVCTIHqpSIDIFEAF-DELLLMKRgGQVIYSGP 1104
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
79-195 |
9.39e-07 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 49.83 E-value: 9.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 79 FVPQKSELNTPLKVI-DVLLMSKYANLKHAFSSYSkedILEIKEFAKDLRLENF-LERSILSLSGGEFQRMLLARALL-- 154
Cdd:PRK00635 751 FLPQVLEVRYKGKNIaDILEMTAYEAEKFFLDEPS---IHEKIHALCSLGLDYLpLGRPLSSLSGGEIQRLKLAYELLap 827
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 919308723 155 -KKPKILFLDEPTSAL---DLNYAIE-LLSLCEK----LVKEKNIAVVAI 195
Cdd:PRK00635 828 sKKPTLYVLDEPTTGLhthDIKALIYvLQSLTHQghtvVIIEHNMHVVKV 877
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
4-221 |
1.31e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 48.27 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 4 IHDLNFTYHQKDLlknihlelknqafIGILGPNGSGKSTLLKLILKNLSPNKGEISL------------FNTNIKDFSLK 71
Cdd:PRK13546 40 LDDISLKAYEGDV-------------IGLVGINGSGKSTLSNIIGGSLSPTVGKVDRngevsviaisagLSGQLTGIENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 72 EFAKIC-GFVPQKSELNTPlkvidvllmskyanlkhafssyskedilEIKEFAKdlrLENFLERSILSLSGGEFQRMLLA 150
Cdd:PRK13546 107 EFKMLCmGFKRKEIKAMTP----------------------------KIIEFSE---LGEFIYQPVKKYSSGMRAKLGFS 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 919308723 151 RALLKKPKILFLDEPTSALDLNYAIELLSLCEKLvKEKNIAVVAILHDLNLASMFCDKILFLKEGEIKYFG 221
Cdd:PRK13546 156 INITVNPDILVIDEALSVGDQTFAQKCLDKIYEF-KEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYG 225
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
31-170 |
2.21e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 48.58 E-value: 2.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 31 GILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNI--KDFSLKefaKICGFVPQKSELNTPLKVidvllmskYANLK-HA 107
Cdd:NF033858 296 GFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVdaGDIATR---RRVGYMSQAFSLYGELTV--------RQNLElHA 364
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 919308723 108 --FSsYSKEDILE-IKEFAKDLRLENFLERSILSLSGGEFQRMLLARALLKKPKILFLDEPTSALD 170
Cdd:NF033858 365 rlFH-LPAAEIAArVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
132-222 |
5.86e-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: 45.39 E-value: 5.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 132 LERSILSLSGGEFQRMLLARALLKKPK--ILFLDEPTSALDLNYAIELLSLCEKLVKEKNiAVVAILHDLNLASMfCDKI 209
Cdd:cd03238 81 LGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGN-TVILIEHNLDVLSS-ADWI 158
|
90
....*....|...
gi 919308723 210 LFLKEGEIKYFGT 222
Cdd:cd03238 159 IDFGPGSGKSGGK 171
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
17-215 |
6.14e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 46.83 E-value: 6.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 17 LKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISL------FnTNIKDfslkefAKICGFVPQKSELNT-P 89
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIdgqemrF-ASTTA------ALAAGVAIIYQELHLvP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 90 -LKVIDVLLMSKyanLKHAFSSYSKEDI-----LEIKEFAKDLRLENFLERsilsLSGGEFQRMLLARALLKKPKILFLD 163
Cdd:PRK11288 93 eMTVAENLYLGQ---LPHKGGIVNRRLLnyearEQLEHLGVDIDPDTPLKY----LSIGQRQMVEIAKALARNARVIAFD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 919308723 164 EPTSALDLNYAIELLSLCEKLvKEKNIAVVAILHDLNLASMFCDKILFLKEG 215
Cdd:PRK11288 166 EPTSSLSAREIEQLFRVIREL-RAEGRVILYVSHRMEEIFALCDAITVFKDG 216
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
1-179 |
1.64e-05 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 44.45 E-value: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 1 MLKIHDLNFTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLfntNIKDFSLKEFAKICGFV 80
Cdd:PRK13543 11 LLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQI---DGKTATRGDRSRFMAYL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 81 PQKSELNTPLKVIDVLlmsKYANLKHAF-SSYSKEDILEIkefakdLRLENFLERSILSLSGGEFQRMLLARALLKKPKI 159
Cdd:PRK13543 88 GHLPGLKADLSTLENL---HFLCGLHGRrAKQMPGSALAI------VGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPL 158
|
170 180
....*....|....*....|
gi 919308723 160 LFLDEPTSALDLNyAIELLS 179
Cdd:PRK13543 159 WLLDEPYANLDLE-GITLVN 177
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
4-172 |
1.73e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 45.39 E-value: 1.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 4 IHDLNFTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNlSPN--KGEISLFNT---------NIKdfslke 72
Cdd:PRK10938 263 LNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGD-HPQgySNDLTLFGRrrgsgetiwDIK------ 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 73 faKICGFVPQKSEL----NTplKVIDVLLmSKYANLKHAFSSYSKEDILEIKEFAKDLRLENFLERSIL-SLSGGEfQRM 147
Cdd:PRK10938 336 --KHIGYVSSSLHLdyrvST--SVRNVIL-SGFFDSIGIYQAVSDRQQKLAQQWLDILGIDKRTADAPFhSLSWGQ-QRL 409
|
170 180
....*....|....*....|....*..
gi 919308723 148 LL-ARALLKKPKILFLDEPTSALD-LN 172
Cdd:PRK10938 410 ALiVRALVKHPTLLILDEPLQGLDpLN 436
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
4-172 |
2.92e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.85 E-value: 2.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 4 IHDLNF--TYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLS---PNKGEI----------------SLFN 62
Cdd:PLN03073 178 IHMENFsiSVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAMHAIdgiPKNCQIlhveqevvgddttalqCVLN 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 63 TNIKDFSL-KEFAKIcgfVPQKSELNTPLKVIDVLLMSKYANLKHAFS--------------SYSKE----DILEIKEFA 123
Cdd:PLN03073 258 TDIERTQLlEEEAQL---VAQQRELEFETETGKGKGANKDGVDKDAVSqrleeiykrlelidAYTAEaraaSILAGLSFT 334
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 919308723 124 KDLRLenfleRSILSLSGGEFQRMLLARALLKKPKILFLDEPTSALDLN 172
Cdd:PLN03073 335 PEMQV-----KATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLH 378
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
32-201 |
2.96e-05 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 43.75 E-value: 2.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 32 ILGPNGSGKSTLLKLILKNLSPnkgeiSLFNTNIKDFSLkefAKICGFVpqkselntplkvidvllmSKYANLKHAFSSY 111
Cdd:cd03240 27 IVGQNGAGKTTIIEALKYALTG-----ELPPNSKGGAHD---PKLIREG------------------EVRAQVKLAFENA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 112 SKEDILEIKEFAKdlrLEN-----------FLERSILSLSGGefQRML--------LARALLKKPKILFLDEPTSALDL- 171
Cdd:cd03240 81 NGKKYTITRSLAI---LENvifchqgesnwPLLDMRGRCSGG--EKVLasliirlaLAETFGSNCGILALDEPTTNLDEe 155
|
170 180 190
....*....|....*....|....*....|
gi 919308723 172 NYAIELLSLCEKLVKEKNIAVVAILHDLNL 201
Cdd:cd03240 156 NIEESLAEIIEERKSQKNFQLIVITHDEEL 185
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
150-215 |
4.64e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 44.01 E-value: 4.64e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 919308723 150 ARALLKKPKILFLDEPTSALDLNYAIELLSLCEKLvKEKNIAVVAILHDLNLASMFCDKILFLKEG 215
Cdd:NF040905 151 AKALSKDVKLLILDEPTAALNEEDSAALLDLLLEL-KAQGITSIIISHKLNEIRRVADSITVLRDG 215
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
139-199 |
6.25e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 43.86 E-value: 6.25e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 919308723 139 LSGGEFQRMLLARALLKK--PKILF-LDEPTSAL---DlnyaIE-LLSLCEKLVKEKNiAVVAILHDL 199
Cdd:COG0178 827 LSGGEAQRVKLASELSKRstGKTLYiLDEPTTGLhfhD----IRkLLEVLHRLVDKGN-TVVVIEHNL 889
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
138-217 |
7.62e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 43.62 E-value: 7.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 138 SLSGGEFQRMLLARALLKKPKILFLDEPTSALDLNYAIELLSLCEKLVKE-KniAVVAILHDL-NLASMfCDKILFLKEG 215
Cdd:NF040905 404 NLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEgK--GVIVISSELpELLGM-CDRIYVMNEG 480
|
..
gi 919308723 216 EI 217
Cdd:NF040905 481 RI 482
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
17-156 |
7.90e-05 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 43.06 E-value: 7.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 17 LKNIHLELKNQAFIGIL-GPNGSGKSTLLKLILKNLSPNKGEISLFNTN---IKDFSLKEFAKICGFVPQKSELNTPLKV 92
Cdd:COG3950 14 FEDLEIDFDNPPRLTVLvGENGSGKTTLLEAIALALSGLLSRLDDVKFRkllIRNGEFGDSAKLILYYGTSRLLLDGPLK 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 919308723 93 IDVLLMSKYANLKHAFSSYSKEDIlEIKEFAKdlRLENFLERSILSLSGGEFQRMLLARALLKK 156
Cdd:COG3950 94 KLERLKEEYFSRLDGYDSLLDEDS-NLREFLE--WLREYLEDLENKLSDELDEKLEAVREALNK 154
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
2-60 |
8.17e-05 |
|
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: 43.25 E-value: 8.17e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 919308723 2 LKIHDLNFTYHQKD-----LLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISL 60
Cdd:COG4615 328 LELRGVTYRYPGEDgdegfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILL 391
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
139-199 |
8.22e-05 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 43.52 E-value: 8.22e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 919308723 139 LSGGEFQRMLLARALLKKP--KILF-LDEPTSAL---DLNyaiELLSLCEKLVKEKNiAVVAILHDL 199
Cdd:PRK00349 831 LSGGEAQRVKLAKELSKRStgKTLYiLDEPTTGLhfeDIR---KLLEVLHRLVDKGN-TVVVIEHNL 893
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
3-209 |
3.56e-04 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 40.72 E-value: 3.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 3 KIHDLNFTyhqkdllknihlELKNQAFIGILGPNGSGKSTLLKLI-------LKNLSPNKGEISLFNTNikdfslKEFAK 75
Cdd:cd03279 16 EEQVIDFT------------GLDNNGLFLICGPTGAGKSTILDAItyalygkTPRYGRQENLRSVFAPG------EDTAE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 76 IcGFVPQKSELNtpLKVIDVLLMSkyanlkhaFSSYSKEDILEIKEFAKdlrlenFLERSILSLSGGE-FQ-----RMLL 149
Cdd:cd03279 78 V-SFTFQLGGKK--YRVERSRGLD--------YDQFTRIVLLPQGEFDR------FLARPVSTLSGGEtFLaslslALAL 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 919308723 150 ARALLKKPKI----LFLDEPTSALD---LNYAIELLslceKLVKEKNIAVVAILHDLNLASMFCDKI 209
Cdd:cd03279 141 SEVLQNRGGArleaLFIDEGFGTLDpeaLEAVATAL----ELIRTENRMVGVISHVEELKERIPQRL 203
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
134-229 |
1.05e-03 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 39.72 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 134 RSILSLSGGEFQRMLLARALLKKPKILFLDEPTSALDLNYAIELLSLCEKLVKEkNIAVVAILHDLNLASMFCDKILFLK 213
Cdd:NF000106 140 RAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVID 218
|
90
....*....|....*.
gi 919308723 214 EGEIKYFGTSKELFTQ 229
Cdd:NF000106 219 RGRVIADGKVDELKTK 234
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
30-178 |
1.40e-03 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 38.84 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 30 IGILGPNGSGKSTLLKLI-----------------LKNLSPNKGEISL-FNTNIKDFSLK----EFAKICGFVPqkSELn 87
Cdd:COG0419 26 NLIVGPNGAGKSTILEAIryalygkarsrsklrsdLINVGSEEASVELeFEHGGKRYRIErrqgEFAEFLEAKP--SER- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 88 tpLKVIDVLL-MSKYANLKHAFSSYSKEDILEIKEFAKDLRLEN-FLER-----SILSLSGGEFQRMLLARALLkkpkiL 160
Cdd:COG0419 103 --KEALKRLLgLEIYEELKERLKELEEALESALEELAELQKLKQeILAQlsgldPIETLSGGERLRLALADLLS-----L 175
|
170 180
....*....|....*....|.
gi 919308723 161 FLDepTSALD---LNYAIELL 178
Cdd:COG0419 176 ILD--FGSLDeerLERLLDAL 194
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
4-170 |
1.97e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 39.34 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 4 IHDLNFTYHQKDLLKNIHLELKNQAFIGILGPNGSGKSTLLKLILKNLSPNKGEISLFNTNIKDFSLKEfaKICG---FV 80
Cdd:NF033858 4 LEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHRR--AVCPriaYM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 81 PQ---KS---ELntplkvidvllmSKYANLK-HA--FSSYSKEDILEIKEFAKDLRLENFLERSILSLSGGEFQRMLLAR 151
Cdd:NF033858 82 PQglgKNlypTL------------SVFENLDfFGrlFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCC 149
|
170
....*....|....*....
gi 919308723 152 ALLKKPKILFLDEPTSALD 170
Cdd:NF033858 150 ALIHDPDLLILDEPTTGVD 168
|
|
| ABC_RecF |
cd03242 |
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that ... |
17-157 |
2.16e-03 |
|
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that maintains replication in the presence of DNA damage. When replication is prematurely disrupted by DNA damage, several recF pathway gene products play critical roles processing the arrested replication fork, allowing it to resume and complete its task. This CD represents the nucleotide binding domain of RecF. RecF belongs to a large superfamily of ABC transporters 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 with 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: 213209 [Multi-domain] Cd Length: 270 Bit Score: 38.43 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 17 LKNIHL-------ELK---NQAFIGILGPNGSGKSTLLKLILKnLSPNKgeiSLFNTNIKDF--SLKEFAKICGFVpQKS 84
Cdd:cd03242 1 LKSLELrnfrnyaELElefEPGVTVLVGENAQGKTNLLEAISL-LATGK---SHRTSRDKELirWGAEEAKISAVL-ERQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 85 ELNTPLKVIDVLLMSKYANLKH----AFSSYSkeDILEIKEFA-KDLRL--------ENFLERSILSLSG------GEFQ 145
Cdd:cd03242 76 GGELALELTIRSGGGRKARLNGikvrRLSDLL--GVLNAVWFApEDLELvkgspadrRRFLDRLLGQLEPayahvlSEYQ 153
|
170
....*....|...
gi 919308723 146 RMLLAR-ALLKKP 157
Cdd:cd03242 154 KALRQRnALLKGP 166
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
31-216 |
4.06e-03 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 38.06 E-value: 4.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 31 GILGPNGSGKSTLLKLILKNLSPNKGEISLF--NTNIKDFSLKEFAKIcGFVPQksELNtplkVIDVLLMSKYANLKHAF 108
Cdd:PRK10762 34 ALVGENGAGKSTMMKVLTGIYTRDAGSILYLgkEVTFNGPKSSQEAGI-GIIHQ--ELN----LIPQLTIAENIFLGREF 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 109 SS----------YSKEDILeikefAKDLRLENFLERSILSLSGGEFQRMLLARALLKKPKILFLDEPTSALDLNYAIELL 178
Cdd:PRK10762 107 VNrfgridwkkmYAEADKL-----LARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLF 181
|
170 180 190
....*....|....*....|....*....|....*...
gi 919308723 179 SLCEKLvKEKNIAVVAILHDLNLASMFCDKILFLKEGE 216
Cdd:PRK10762 182 RVIREL-KSQGRGIVYISHRLKEIFEICDDVTVFRDGQ 218
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
17-43 |
6.12e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 37.69 E-value: 6.12e-03
10 20
....*....|....*....|....*..
gi 919308723 17 LKNIHLELKNQAFIGILGPNGSGKSTL 43
Cdd:TIGR00630 12 LKNIDVEIPRDKLVVITGLSGSGKSSL 38
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
32-55 |
6.35e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 34.11 E-value: 6.35e-03
|
| VirB4 |
COG3451 |
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and ... |
19-78 |
6.41e-03 |
|
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442674 [Multi-domain] Cd Length: 546 Bit Score: 37.62 E-value: 6.41e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 919308723 19 NIHLELKNQAFIgILGPNGSGKSTLLKLILKNLSPNKGEISLFNtniKDFSLKEFAKICG 78
Cdd:COG3451 197 DFHDGLDNGNTL-ILGPSGSGKSFLLKLLLLQLLRYGARIVIFD---PGGSYEILVRALG 252
|
|
| |
