|
Name |
Accession |
Description |
Interval |
E-value |
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
7-217 |
3.19e-90 |
|
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: 265.17 E-value: 3.19e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 7 AEGLAFRYGSKgpNIIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGSLKTFPSHSAgkQTHSMIGWVPQHF 86
Cdd:cd03235 2 VEDLTVSYGGH--PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLE--KERKRIGYVPQRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 87 SYDPCFPISVKDVVLSGRLSQLSWHGKYKKKDFEAVDHALDLVGLSDHHHHCFAHLSGGQIQRVLLARALASYPEILILD 166
Cdd:cd03235 78 SIDRDFPISVRDVVLMGLYGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLD 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 499185640 167 EPTTNIDPDNQQRILSILKKLNRT-CTILMVTHDLHHTTNYFNKVFYMNKTL 217
Cdd:cd03235 158 EPFAGVDPKTQEDIYELLRELRREgMTILVVTHDLGLVLEYFDRVLLLNRTV 209
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-235 |
5.40e-82 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 245.38 E-value: 5.40e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 1 MTIRILAEGLAFRYGSKgpNIIHDVSFSVYDGDFigiigpngggKSTLTMLILGLLTPTFGSLKTFPSHSAGKQTHsmIG 80
Cdd:COG1121 3 MMPAIELENLTVSYGGR--PVLEDVSLTIPPGEFvaivgpngagKSTLLKAILGLLPPTSGTVRLFGKPPRRARRR--IG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 81 WVPQHFSYDPCFPISVKDVVLSGRLSQLSWHGKYKKKDFEAVDHALDLVGLSDHHHHCFAHLSGGQIQRVLLARALASYP 160
Cdd:COG1121 79 YVPQRAEVDWDFPITVRDVVLMGRYGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499185640 161 EILILDEPTTNIDPDNQQRILSILKKLNRT-CTILMVTHDLHHTTNYFNKVFYMNKTLTSLADTST-LTDQFCCHPY 235
Cdd:COG1121 159 DLLLLDEPFAGVDAATEEALYELLRELRREgKTILVVTHDLGAVREYFDRVLLLNRGLVAHGPPEEvLTPENLSRAY 235
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-215 |
1.74e-56 |
|
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: 180.62 E-value: 1.74e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 4 RILAEGLAFRYGSKgpNIIHDVSFSVYDGDFigiigpngggKSTLTMLILGLLTPTFGS-------LKTFPSHSAGKQth 76
Cdd:COG1120 1 MLEAENLSVGYGGR--PVLDDVSLSLPPGEVtallgpngsgKSTLLRALAGLLKPSSGEvlldgrdLASLSRRELARR-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 77 smIGWVPQHFSYDpcFPISVKDVVLSGRLSQLSWHGKYKKKDFEAVDHALDLVGLSDHHHHCFAHLSGGQIQRVLLARAL 156
Cdd:COG1120 77 --IAYVPQEPPAP--FGLTVRELVALGRYPHLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARAL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499185640 157 ASYPEILILDEPTTNIDPDNQQRILSILKKLNRT--CTILMVTHDLHHTTNYFNKVFYMNK 215
Cdd:COG1120 153 AQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARErgRTVVMVLHDLNLAARYADRLVLLKD 213
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-213 |
3.07e-41 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 140.56 E-value: 3.07e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 1 MTIRILAEGLAFRYGSKGPN--IIHDVSFSVYDGDFigiigpngggKSTLTMLILGLLTPTFGSLKTfpshsAGKQTHSM 78
Cdd:COG1136 1 MSPLLELRNLTKSYGTGEGEvtALRGVSLSIEAGEFvaivgpsgsgKSTLLNILGGLDRPTSGEVLI-----DGQDISSL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 79 ------------IGWVPQHFSYDPCFpiSVKD-VVLSGRLSqlswhGKYKKKDFEAVDHALDLVGLSDHHHHCFAHLSGG 145
Cdd:COG1136 76 serelarlrrrhIGFVFQFFNLLPEL--TALEnVALPLLLA-----GVSRKERRERARELLERVGLGDRLDHRPSQLSGG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 146 QIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKLNRT--CTILMVTHDlHHTTNYFNKVFYM 213
Cdd:COG1136 149 QQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRElgTTIVMVTHD-PELAARADRVIRL 217
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
5-199 |
4.33e-40 |
|
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: 137.62 E-value: 4.33e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 5 ILAEGLAFRYGSKGPN--IIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGSLktfpsHSAGKQTHSM---- 78
Cdd:cd03255 1 IELKNLSKTYGGGGEKvqALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEV-----RVDGTDISKLseke 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 79 --------IGWVPQHFSYDPCFpiSVKDVVLSGrlsqLSWHGKYKKKDFEAVDHALDLVGLSDHHHHCFAHLSGGQIQRV 150
Cdd:cd03255 76 laafrrrhIGFVFQSFNLLPDL--TALENVELP----LLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRV 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 499185640 151 LLARALASYPEILILDEPTTNIDPDNQQRILSILKKLNRT--CTILMVTHD 199
Cdd:cd03255 150 AIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEagTTIVVVTHD 200
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
8-215 |
5.00e-40 |
|
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: 137.21 E-value: 5.00e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 8 EGLAFRYGSKGPNIIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGSLKTF---PSHSAGKQTHSMIGWVPQ 84
Cdd:cd03225 3 KNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDgkdLTKLSLKELRRKVGLVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 85 H----FSYDpcfpiSV-KDVVLSGRLSQLSwhgkyKKKDFEAVDHALDLVGLSDHHHHCFAHLSGGQIQRVLLARALASY 159
Cdd:cd03225 83 NpddqFFGP-----TVeEEVAFGLENLGLP-----EEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499185640 160 PEILILDEPTTNIDPDNQQRILSILKKLNRTC-TILMVTHDLHHTTNYFNKVFYMNK 215
Cdd:cd03225 153 PDILLLDEPTAGLDPAGRRELLELLKKLKAEGkTIIIVTHDLDLLLELADRVIVLED 209
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
5-215 |
8.21e-40 |
|
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: 137.08 E-value: 8.21e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 5 ILAEGLAFRYgSKGPNIIHDVSFSVYDGDFigiigpngggKSTLTMLILGLLTPTFGSLKTF---PSHSAGKQTHSMIGW 81
Cdd:COG1122 1 IELENLSFSY-PGGTPALDDVSLSIEKGEFvaiigpngsgKSTLLRLLNGLLKPTSGEVLVDgkdITKKNLRELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 82 VPQhfsyDP----CFPISVKDVVLSgrLSQLswhgKYKKKDFEA-VDHALDLVGLSDH-HHHCFaHLSGGQIQRVLLARA 155
Cdd:COG1122 80 VFQ----NPddqlFAPTVEEDVAFG--PENL----GLPREEIRErVEEALELVGLEHLaDRPPH-ELSGGQKQRVAIAGV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499185640 156 LASYPEILILDEPTTNIDPDNQQRILSILKKLNRT-CTILMVTHDLHHTTNYFNKVFYMNK 215
Cdd:COG1122 149 LAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEgKTVIIVTHDLDLVAELADRVIVLDD 209
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
5-200 |
5.57e-39 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 135.19 E-value: 5.57e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 5 ILAEGLAFRYGSKgpNIIHDVSFSVYDGDFigiigpngggKSTLTMLILGLLTPTFGSLKTF--PSHSAGKQTHSMIGWV 82
Cdd:COG1131 1 IEVRGLTKRYGDK--TALDGVSLTVEPGEIfgllgpngagKTTTIRMLLGLLRPTSGEVRVLgeDVARDPAEVRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 83 PQHFSYDPcfPISVKD-VVLSGRLsqlswHGKYKKKDFEAVDHALDLVGLSDHHHHCFAHLSGGQIQRVLLARALASYPE 161
Cdd:COG1131 79 PQEPALYP--DLTVREnLRFFARL-----YGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPE 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 499185640 162 ILILDEPTTNIDPDNQQRILSILKKLNRT-CTILMVTHDL 200
Cdd:COG1131 152 LLILDEPTSGLDPEARRELWELLRELAAEgKTVLLSTHYL 191
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
27-228 |
1.21e-38 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 133.82 E-value: 1.21e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 27 FSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGSLKTFPSHSAGKQTHsmIGWVPQ--HFSYDpcFPISVKDVVLSGR 104
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGASPGKGWRH--IGYVPQrhEFAWD--FPISVAHTVMSGR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 105 LSQLSWHGKYKKKDFEAVDHALDLVGLSDHHHHCFAHLSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSIL 184
Cdd:TIGR03771 77 TGHIGWLRRPCVADFAAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLTELF 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 499185640 185 KKLNRT-CTILMVTHDLHHTTNYFNKVFYMNKTLTSLADTSTLTD 228
Cdd:TIGR03771 157 IELAGAgTAILMTTHDLAQAMATCDRVVLLNGRVIADGTPQQLQD 201
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
45-202 |
1.73e-38 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 132.36 E-value: 1.73e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 45 KSTLTMLILGLLTPTFGSLKtfpshsagKQTHSMIGWVPQHFSYDPCFPISVKDVVLSGRLSQLSWHGKYKKKDFEAVDH 124
Cdd:NF040873 31 KSTLLKVLAGVLRPTSGTVR--------RAGGARVAYVPQRSEVPDSLPLTVRDLVAMGRWARRGLWRRLTRDDRAAVDD 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499185640 125 ALDLVGLSDHHHHCFAHLSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKLNRT-CTILMVTHDLHH 202
Cdd:NF040873 103 ALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAEEHARgATVVVVTHDLEL 181
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
7-214 |
5.50e-36 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 125.63 E-value: 5.50e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 7 AEGLAFRYGSKgpNIIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFG-------SLKTFPShsagKQTHSMI 79
Cdd:cd03214 2 VENLSVGYGGR--TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGeilldgkDLASLSP----KELARKI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 80 GWVPQhfsydpcfpisvkdvvlsgrlsqlswhgkykkkdfeavdhALDLVGLSDHHHHCFAHLSGGQIQRVLLARALASY 159
Cdd:cd03214 76 AYVPQ----------------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQE 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499185640 160 PEILILDEPTTNIDPDNQQRILSILKKLNRT--CTILMVTHDLHHTTNYFNKVFYMN 214
Cdd:cd03214 116 PPILLLDEPTSHLDIAHQIELLELLRRLARErgKTVVMVLHDLNLAARYADRVILLK 172
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
45-200 |
1.55e-35 |
|
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: 126.08 E-value: 1.55e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 45 KSTLTMLILGLLTPTFGSLKTFPSHSAG------KQTHSMIGWVPQH--FSYDPCFPI--SVKDVVLSgrlsqlswHGKY 114
Cdd:cd03257 44 KSTLARAILGLLKPTSGSIIFDGKDLLKlsrrlrKIRRKEIQMVFQDpmSSLNPRMTIgeQIAEPLRI--------HGKL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 115 KKKDF--EAVDHALDLVGLSDHHHHCFAH-LSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKL--NR 189
Cdd:cd03257 116 SKKEArkEAVLLLLVGVGLPEEVLNRYPHeLSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLqeEL 195
|
170
....*....|.
gi 499185640 190 TCTILMVTHDL 200
Cdd:cd03257 196 GLTLLFITHDL 206
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
5-201 |
2.14e-35 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 125.55 E-value: 2.14e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 5 ILAEGLAFRYGsKGPNIIHDVSFSVYDGDFigiigpngggKSTLTMLILGLLTPTFGSLKTFpshsaGKQTHSM------ 78
Cdd:COG2884 2 IRFENVSKRYP-GGREALSDVSLEIEKGEFvfltgpsgagKSTLLKLLYGEERPTSGQVLVN-----GQDLSRLkrreip 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 79 -----IGWVPQHFS--YDpcfpISVKD-VVLSGRLsqlswHGKYKKKDFEAVDHALDLVGLSdHHHHCFAH-LSGGQIQR 149
Cdd:COG2884 76 ylrrrIGVVFQDFRllPD----RTVYEnVALPLRV-----TGKSRKEIRRRVREVLDLVGLS-DKAKALPHeLSGGEQQR 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499185640 150 VLLARALASYPEILILDEPTTNIDPDNQQRILSILKKLNRT-CTILMVTHDLH 201
Cdd:COG2884 146 VAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRgTTVLIATHDLE 198
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
7-201 |
2.16e-35 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 131.56 E-value: 2.16e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 7 AEGLAFRYGSKGPN---IIHDVSFSVYDGDFigiigpngggKSTLTMLILGLLTPTFGSLK------TFPSHSAGKQTHS 77
Cdd:COG1123 263 VRNLSKRYPVRGKGgvrAVDDVSLTLRRGETlglvgesgsgKSTLARLLLGLLRPTSGSILfdgkdlTKLSRRSLRELRR 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 78 MIGWVPQH-F-SYDPCFpiSVKDVVLSGrlsqLSWHGKYKKKDFEA-VDHALDLVGLSDHHHHCFAH-LSGGQIQRVLLA 153
Cdd:COG1123 343 RVQMVFQDpYsSLNPRM--TVGDIIAEP----LRLHGLLSRAERRErVAELLERVGLPPDLADRYPHeLSGGQRQRVAIA 416
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 499185640 154 RALASYPEILILDEPTTNIDPDNQQRILSILKKLNRT--CTILMVTHDLH 201
Cdd:COG1123 417 RALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElgLTYLFISHDLA 466
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
18-225 |
2.51e-34 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 124.22 E-value: 2.51e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 18 GPNIIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGSLKTF--PSHSAGKQthSMIGWVPQHFSYDPCFPIS 95
Cdd:PRK15056 19 GHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILgqPTRQALQK--NLVAYVPQSEEVDWSFPVL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 96 VKDVVLSGRLSQLSWHGKYKKKDFEAVDHALDLVGLSDHHHHCFAHLSGGQIQRVLLARALASYPEILILDEPTTNIDPD 175
Cdd:PRK15056 97 VEDVVMMGRYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVK 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 499185640 176 NQQRILSILKKL-NRTCTILMVTHDLHHTTNYFNKVFYMNKTLTSLADTST 225
Cdd:PRK15056 177 TEARIISLLRELrDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGPTET 227
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
3-210 |
3.34e-34 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 123.24 E-value: 3.34e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 3 IRIlaEGLAFRYGSkGPNIIHDVSFSVYDGDFigiigpngggKSTLTMLILGLLTPTFGSLKTF---PSHSAGKQTHSM- 78
Cdd:COG3638 3 LEL--RNLSKRYPG-GTPALDDVSLEIERGEFvaligpsgagKSTLLRCLNGLVEPTSGEILVDgqdVTALRGRALRRLr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 79 --IGWVPQHFsydpcfPI----SVKDVVLSGRLSQL----SWHGKYKKKDFEAVDHALDLVGLSDHHHHCFAHLSGGQIQ 148
Cdd:COG3638 80 rrIGMIFQQF------NLvprlSVLTNVLAGRLGRTstwrSLLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQ 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499185640 149 RVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKLNRT--CTILMVTHDLHHTTNYFNKV 210
Cdd:COG3638 154 RVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREdgITVVVNLHQVDLARRYADRI 217
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
3-210 |
4.42e-34 |
|
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: 122.68 E-value: 4.42e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 3 IRIlaEGLAFRYGSkGPNIIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGSLK------TFPSHSAGKQTH 76
Cdd:cd03256 1 IEV--ENLSKTYPN-GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLidgtdiNKLKGKALRQLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 77 SMIGWVPQHFSYDPcfPISVKDVVLSGRLSQLSW----HGKYKKKDFEAVDHALDLVGLSDHHHHCFAHLSGGQIQRVLL 152
Cdd:cd03256 78 RQIGMIFQQFNLIE--RLSVLENVLSGRLGRRSTwrslFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 153 ARALASYPEILILDEPTTNIDPDNQQRILSILKKLNRT--CTILMVTHDLHHTTNYFNKV 210
Cdd:cd03256 156 ARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREegITVIVSLHQVDLAREYADRI 215
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
8-215 |
1.78e-33 |
|
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: 119.02 E-value: 1.78e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 8 EGLAFRYGSKGPNIIHDVSFSVYDGDFigiigpngggKSTLTMLILGLLTPTFGS-------LKTFPSHSAgkqtHSMIG 80
Cdd:cd03228 4 KNVSFSYPGRPKPVLKDVSLTIKPGEKvaivgpsgsgKSTLLKLLLRLYDPTSGEilidgvdLRDLDLESL----RKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 81 WVPQhfsyDPC-FPISVKDVVLSGrlsqlswhgkykkkdfeavdhaldlvglsdhhhhcfahlsgGQIQRVLLARALASY 159
Cdd:cd03228 80 YVPQ----DPFlFSGTIRENILSG-----------------------------------------GQRQRIAIARALLRD 114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499185640 160 PEILILDEPTTNIDPDNQQRILSILKKLNRTCTILMVTHDLhHTTNYFNKVFYMNK 215
Cdd:cd03228 115 PPILILDEATSALDPETEALILEALRALAKGKTVIVIAHRL-STIRDADRIIVLDD 169
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
12-201 |
1.08e-32 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 118.12 E-value: 1.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 12 FRYGSkGPNIIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGSLKTFP---SHSAGKQTHSM---IGWVPQH 85
Cdd:TIGR02673 9 KAYPG-GVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGedvNRLRGRQLPLLrrrIGVVFQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 86 FSYDPcfPISVKDVVlsgrlsQLSWHGKYKKKDF--EAVDHALDLVGLSDHHHHCFAHLSGGQIQRVLLARALASYPEIL 163
Cdd:TIGR02673 88 FRLLP--DRTVYENV------ALPLEVRGKKEREiqRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLL 159
|
170 180 190
....*....|....*....|....*....|....*....
gi 499185640 164 ILDEPTTNIDPDNQQRILSILKKLN-RTCTILMVTHDLH 201
Cdd:TIGR02673 160 LADEPTGNLDPDLSERILDLLKRLNkRGTTVIVATHDLS 198
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-215 |
1.23e-32 |
|
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: 123.86 E-value: 1.23e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 1 MTIRILAEGLAFRYGSKGPNIIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPT---FGS-------LKTFPSHS 70
Cdd:COG1123 1 MTPLLEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEvlldgrdLLELSEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 71 AGKQthsmIGWVPQhfsyDPC---FPISV-KDVVLSGRLSQLSwhgkyKKKDFEAVDHALDLVGLSDHHHHCFAHLSGGQ 146
Cdd:COG1123 81 RGRR----IGMVFQ----DPMtqlNPVTVgDQIAEALENLGLS-----RAEARARVLELLEAVGLERRLDRYPHQLSGGQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499185640 147 IQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKLNRT--CTILMVTHDLHHTTNYFNKVFYMNK 215
Cdd:COG1123 148 RQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRErgTTVLLITHDLGVVAEIADRVVVMDD 218
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
3-215 |
3.07e-32 |
|
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: 123.33 E-value: 3.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 3 IRILAEGLAFRYGSkGPNIIHDVSFSVYDGDFigiigpngggKSTLTMLILGLLTPTFGS-------LKTFPSHSAGKQt 75
Cdd:COG4988 335 PSIELEDVSFSYPG-GRPALDGLSLTIPPGERvalvgpsgagKSTLLNLLLGFLPPYSGSilingvdLSDLDPASWRRQ- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 76 hsmIGWVPQHfsydPC-FPISVKDVVLSGRlSQLSWhgkykkkdfEAVDHALDLVGLSDhhhhcFAH------------- 141
Cdd:COG4988 413 ---IAWVPQN----PYlFAGTIRENLRLGR-PDASD---------EELEAALEAAGLDE-----FVAalpdgldtplgeg 470
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499185640 142 ---LSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKLNRTCTILMVTHDLHHTTNYfNKVFYMNK 215
Cdd:COG4988 471 grgLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQA-DRILVLDD 546
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
7-200 |
5.26e-32 |
|
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: 117.21 E-value: 5.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 7 AEGLAFRYGSKGPN--IIHDVSFSVYDGDfigiigpngggKSTLTMLILGLLTPTFGSLkTF----PSHSAGKQTHSMIG 80
Cdd:COG1124 4 VRNLSVSYGQGGRRvpVLKDVSLEVAPGEsfglvgesgsgKSTLLRALAGLERPWSGEV-TFdgrpVTRRRRKAFRRRVQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 81 WVPQHF--SYDPCFpiSVKDVVLSGrlsqLSWHGKYKKKdfEAVDHALDLVGLSDHHHHCFAH-LSGGQIQRVLLARALA 157
Cdd:COG1124 83 MVFQDPyaSLHPRH--TVDRILAEP----LRIHGLPDRE--ERIAELLEQVGLPPSFLDRYPHqLSGGQRQRVAIARALI 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 499185640 158 SYPEILILDEPTTNIDPDNQQRILSILKKLN--RTCTILMVTHDL 200
Cdd:COG1124 155 LEPELLLLDEPTSALDVSVQAEILNLLKDLReeRGLTYLFVSHDL 199
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-200 |
1.00e-31 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 116.73 E-value: 1.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 1 MTIRILAEGLAFRYGSKGPN--IIHDVSFSVYDGDFigiigpngggKSTLTMLILGLLTPTFGSLKTFPSHSAGKQTHsm 78
Cdd:COG1116 4 AAPALELRGVSKRFPTGGGGvtALDDVSLTVAAGEFvalvgpsgcgKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 79 IGWVPQHFSydpCFP-ISVKDVVLSGrlsqLSWHGKYKKKDFEAVDHALDLVGLSDHHHHcFAH-LSGGQIQRVLLARAL 156
Cdd:COG1116 82 RGVVFQEPA---LLPwLTVLDNVALG----LELRGVPKAERRERARELLELVGLAGFEDA-YPHqLSGGMRQRVAIARAL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 499185640 157 ASYPEILILDEPTTNIDPDN----QQRILSILKKLNRtcTILMVTHDL 200
Cdd:COG1116 154 ANDPEVLLMDEPFGALDALTrerlQDELLRLWQETGK--TVLFVTHDV 199
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
8-201 |
2.05e-31 |
|
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: 115.95 E-value: 2.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 8 EGLAFRYGSKgpNIIHDVSFSVYDGDFigiigpngggKSTLTMLILGLLTPTFG-SLKTFpshsaGKQT--------HSM 78
Cdd:COG1119 7 RNVTVRRGGK--TILDDISWTVKPGEHwailgpngagKSTLLSLITGDLPPTYGnDVRLF-----GERRggedvwelRKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 79 IGWVPQHFSYDPCFPISVKDVVLSGRLSQLSWHGKYKKKDFEAVDHALDLVGLSDHHHHCFAHLSGGQIQRVLLARALAS 158
Cdd:COG1119 80 IGLVSPALQLRFPRDETVLDVVLSGFFDSIGLYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 499185640 159 YPEILILDEPTTNIDPDNQQRILSILKKL--NRTCTILMVTHDLH 201
Cdd:COG1119 160 DPELLILDEPTAGLDLGARELLLALLDKLaaEGAPTLVLVTHHVE 204
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
5-215 |
2.36e-31 |
|
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: 113.65 E-value: 2.36e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 5 ILAEGLAFRYGSKgpNIIHDVSFSVYDGDFigiigpngggKSTLTMLILGLLTPTFGSLKTF--PSHSAGKQTHSMIGWV 82
Cdd:cd03230 1 IEVRNLSKRYGKK--TALDDISLTVEKGEIygllgpngagKTTLIKIILGLLKPDSGEIKVLgkDIKKEPEEVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 83 PQHFSYDPCFpiSVKDVVlsgrlsqlswhgkykkkdfeavdhaldlvglsdhhhhcfaHLSGGQIQRVLLARALASYPEI 162
Cdd:cd03230 79 PEEPSLYENL--TVRENL----------------------------------------KLSGGMKQRLALAQALLHDPEL 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499185640 163 LILDEPTTNIDPDNQQRILSILKKLNRT-CTILMVTHDLHHTTNYFNKVFYMNK 215
Cdd:cd03230 117 LILDEPTSGLDPESRREFWELLRELKKEgKTILLSSHILEEAERLCDRVAILNN 170
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
5-201 |
5.44e-31 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 114.11 E-value: 5.44e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 5 ILAEGLAFRYGSKGPN--IIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGSLkTFpshsAGK---QTHSMI 79
Cdd:cd03293 1 LEVRNVSKTYGGGGGAvtALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEV-LV----DGEpvtGPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 80 GWVPQHFSYdpcFP-ISVKDVVLSGrlsqLSWHGKYKKKDFEAVDHALDLVGLSDHHHHCFAHLSGGQIQRVLLARALAS 158
Cdd:cd03293 76 GYVFQQDAL---LPwLTVLDNVALG----LELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAV 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 499185640 159 YPEILILDEPTTNIDP----DNQQRILSILKKLNRtcTILMVTHDLH 201
Cdd:cd03293 149 DPDVLLLDEPFSALDAltreQLQEELLDIWRETGK--TVLLVTHDID 193
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
12-201 |
8.94e-31 |
|
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: 113.83 E-value: 8.94e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 12 FRYGSKGPNIIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGSLK------TFPSHSAGKQTHSMIGWVPQH 85
Cdd:cd03258 11 FGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLvdgtdlTLLSGKELRKARRRIGMIFQH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 86 FSydpcfpisvkdvVLSGRLSQ------LSWHGKYKKKDFEAVDHALDLVGLSDHHHHCFAHLSGGQIQRVLLARALASY 159
Cdd:cd03258 91 FN------------LLSSRTVFenvalpLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANN 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 499185640 160 PEILILDEPTTNIDPDNQQRILSILKKLNRT--CTILMVTHDLH 201
Cdd:cd03258 159 PKVLLCDEATSALDPETTQSILALLRDINRElgLTIVLITHEME 202
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
5-200 |
2.20e-30 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 113.29 E-value: 2.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 5 ILAEGLAFRYGSKgpNIIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGSLktfpsHSAGKQTHSMIGW--- 81
Cdd:COG4559 2 LEAENLSVRLGGR--TLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEV-----RLNGRPLAAWSPWela 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 82 -----VPQHFSYDpcFPISVKDVVLSGRLSqlswHGKYKKKDFEAVDHALDLVGLSDHHHHCFAHLSGGQIQRVLLARAL 156
Cdd:COG4559 75 rrravLPQHSSLA--FPFTVEEVVALGRAP----HGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 499185640 157 A-------SYPEILILDEPTTNIDPDNQQRILSILKKL-NRTCTILMVTHDL 200
Cdd:COG4559 149 AqlwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLaRRGGGVVAVLHDL 200
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
4-215 |
2.59e-30 |
|
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: 118.40 E-value: 2.59e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 4 RILAEGLAFRYGSKGPNIIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGS-------LKTFPSHSagkqTH 76
Cdd:COG2274 473 DIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRilidgidLRQIDPAS----LR 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 77 SMIGWVPQHfsyDPCFPISVKDVVLSGRLSQlswhgkykkkDFEAVDHALDLVGLSDhhhhcF----------------A 140
Cdd:COG2274 549 RQIGVVLQD---VFLFSGTIRENITLGDPDA----------TDEEIIEAARLAGLHD-----FiealpmgydtvvgeggS 610
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499185640 141 HLSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKLNRTCTILMVTHDLhHTTNYFNKVFYMNK 215
Cdd:COG2274 611 NLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRL-STIRLADRIIVLDK 684
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
5-215 |
5.02e-29 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 110.23 E-value: 5.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 5 ILAEGLAFRYGSKGPN---IIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGS-----LKTFPSHS-AGKQT 75
Cdd:TIGR04521 1 IKLKNVSYIYQPGTPFekkALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTvtidgRDITAKKKkKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 76 HSMIGWVPQhFSYDPCFPISV-KDVVLsGRLSQlswhGKYKKKDFEAVDHALDLVGLSDH--HHHCFaHLSGGQIQRVLL 152
Cdd:TIGR04521 81 RKKVGLVFQ-FPEHQLFEETVyKDIAF-GPKNL----GLSEEEAEERVKEALELVGLDEEylERSPF-ELSGGQMRRVAI 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499185640 153 ARALASYPEILILDEPTTNIDPDNQQRILSILKKLNRTC--TILMVTHDLHHTTNYFNKVFYMNK 215
Cdd:TIGR04521 154 AGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKglTVILVTHSMEDVAEYADRVIVMHK 218
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
8-214 |
5.12e-29 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 109.31 E-value: 5.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 8 EGLAFRYGSkGPNIIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGSlKTFPSHSAGK-------QTHSMIG 80
Cdd:TIGR02315 5 ENLSKVYPN-GKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGS-ILLEGTDITKlrgkklrKLRRRIG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 81 WVPQHFSYDPcfPISVKDVVLSGRLSQL----SWHGKYKKKDFEAVDHALDLVGLSDHHHHCFAHLSGGQIQRVLLARAL 156
Cdd:TIGR02315 83 MIFQHYNLIE--RLTVLENVLHGRLGYKptwrSLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 157 ASYPEILILDEPTTNIDPDNQQRILSILKKLNRT--CTILMVTHDLHHTTNYFNKVFYMN 214
Cdd:TIGR02315 161 AQQPDLILADEPIASLDPKTSKQVMDYLKRINKEdgITVIINLHQVDLAKKYADRIVGLK 220
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-199 |
1.46e-28 |
|
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: 107.18 E-value: 1.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 4 RILAEGLAFRYGskGPNIIHDVSFSVYDGDfigiigpngggKSTLTMLILGLLTPTFGS--LKTFPSHSAGKQTHSMIGW 81
Cdd:COG4133 2 MLEAENLSCRRG--ERLLFSGLSFTLAAGEalaltgpngsgKTTLLRILAGLLPPSAGEvlWNGEPIRDAREDYRRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 82 VPQhfsYDPCFPisvkdvVLSGRlSQLSWHGKYKKKDF--EAVDHALDLVGLSDHHHHCFAHLSGGQIQRVLLARALASY 159
Cdd:COG4133 80 LGH---ADGLKP------ELTVR-ENLRFWAALYGLRAdrEAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSP 149
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 499185640 160 PEILILDEPTTNIDPDNQQRILSILKK-LNRTCTILMVTHD 199
Cdd:COG4133 150 APLWLLDEPFTALDAAGVALLAELIAAhLARGGAVLLTTHQ 190
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
5-200 |
4.93e-28 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 107.52 E-value: 4.93e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 5 ILAEGLAFRYGSKGPNIIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGSLKTFPSHSAGKQT----HSMIG 80
Cdd:TIGR04520 1 IEVENVSFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEENlweiRKKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 81 WVPQHfsydpcfP------ISVKDVVLSG----RLSqlswHGKYKKKdfeaVDHALDLVGLSDHHHHCFAHLSGGQIQRV 150
Cdd:TIGR04520 81 MVFQN-------PdnqfvgATVEDDVAFGlenlGVP----REEMRKR----VDEALKLVGMEDFRDREPHLLSGGQKQRV 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 499185640 151 LLARALASYPEILILDEPTTNIDPDNQQRILSILKKLNRTC--TILMVTHDL 200
Cdd:TIGR04520 146 AIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEgiTVISITHDM 197
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
3-200 |
5.19e-28 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 107.16 E-value: 5.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 3 IRILAEGLAFRYGSKgpNIIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGSLKTFpshsaGKQTHSMIGW- 81
Cdd:PRK13548 1 AMLEARNLSVRLGGR--TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLN-----GRPLADWSPAe 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 82 -------VPQHFSYDpcFPISVKDVVLSGRLSqlswHGKYKKKDFEAVDHALDLVGLSDHHHHCFAHLSGGQIQRVLLAR 154
Cdd:PRK13548 74 larrravLPQHSSLS--FPFTVEEVVAMGRAP----HGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLAR 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499185640 155 ALA------SYPEILILDEPTTNIDPDNQQRILSILKKLNRT--CTILMVTHDL 200
Cdd:PRK13548 148 VLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHErgLAVIVVLHDL 201
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
3-201 |
7.39e-28 |
|
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: 106.05 E-value: 7.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 3 IRIlaEGLAFRYGSKgpNIIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGSLKTFpshsaGKQTHSM---- 78
Cdd:cd03261 1 IEL--RGLTKSFGGR--TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLID-----GEDISGLseae 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 79 -------IGWVPQH---FSydpcfPISVKDVVlSGRLSQlswHGKYKKKD-FEAVDHALDLVGLSDHHHHCFAHLSGGQI 147
Cdd:cd03261 72 lyrlrrrMGMLFQSgalFD-----SLTVFENV-AFPLRE---HTRLSEEEiREIVLEKLEAVGLRGAEDLYPAELSGGMK 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499185640 148 QRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKLNRT--CTILMVTHDLH 201
Cdd:cd03261 143 KRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKElgLTSIMVTHDLD 198
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
22-199 |
8.81e-28 |
|
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: 105.57 E-value: 8.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 22 IHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGSLK---TFPSHSAGKQTHSM---IGWVPQHFSYDPCFPIs 95
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRvngQDVSDLRGRAIPYLrrkIGVVFQDFRLLPDRNV- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 96 VKDVVLSGRLSQLSwHGKYKKKdfeaVDHALDLVGLSDHHHHCFAHLSGGQIQRVLLARALASYPEILILDEPTTNIDPD 175
Cdd:cd03292 96 YENVAFALEVTGVP-PREIRKR----VPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPD 170
|
170 180
....*....|....*....|....*
gi 499185640 176 NQQRILSILKKLN-RTCTILMVTHD 199
Cdd:cd03292 171 TTWEIMNLLKKINkAGTTVVVATHA 195
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
7-214 |
1.50e-27 |
|
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: 104.65 E-value: 1.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 7 AEGLAFRYGsKGPNIIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGSLKTFPSHSAGKQTHSMIGWVPQHf 86
Cdd:cd03226 2 IENISFSYK-KGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERRKSIGYVMQD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 87 SYDPCFPISVKDVVLSGRlsqlswhgKYKKKDFEAVDHALDLVGLSD-HHHHCFAhLSGGQIQRVLLARALASYPEILIL 165
Cdd:cd03226 80 VDYQLFTDSVREELLLGL--------KELDAGNEQAETVLKDLDLYAlKERHPLS-LSGGQKQRLAIAAALLSGKDLLIF 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 499185640 166 DEPTTNIDPDNQQRILSILKKL-NRTCTILMVTHDLHHTTNYFNKVFYMN 214
Cdd:cd03226 151 DEPTSGLDYKNMERVGELIRELaAQGKAVIVITHDYEFLAKVCDRVLLLA 200
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-199 |
2.28e-27 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 107.49 E-value: 2.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 1 MTIRILAEGLAFRYGSKgpNIIHDVSFSVYDGDFigiigpngggKSTLTMLILGLLTPTFGSLktfpsHSAGKQTHSM-- 78
Cdd:COG3842 2 AMPALELENVSKRYGDV--TALDDVSLSIEPGEFvallgpsgcgKTTLLRMIAGFETPDSGRI-----LLDGRDVTGLpp 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 79 ----IGWVPQHFsydPCFP-ISVKDVV---LSGRlsqlswhgKYKKKDFEA-VDHALDLVGLSDHHHHcFAH-LSGGQIQ 148
Cdd:COG3842 75 ekrnVGMVFQDY---ALFPhLTVAENVafgLRMR--------GVPKAEIRArVAELLELVGLEGLADR-YPHqLSGGQQQ 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499185640 149 RVLLARALASYPEILILDEPTTNIDPDN----QQRILSILKKLNRTCtiLMVTHD 199
Cdd:COG3842 143 RVALARALAPEPRVLLLDEPLSALDAKLreemREELRRLQRELGITF--IYVTHD 195
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
7-215 |
3.43e-27 |
|
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: 102.32 E-value: 3.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 7 AEGLAFRYGSKgpNIIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGSL---KTFPSHSAGKQTHSMIGWVP 83
Cdd:cd00267 2 IENLSFRYGGR--TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEIlidGKDIAKLPLEELRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 84 QhfsydpcfpisvkdvvlsgrlsqlswhgkykkkdfeavdhaldlvglsdhhhhcfahLSGGQIQRVLLARALASYPEIL 163
Cdd:cd00267 80 Q---------------------------------------------------------LSGGQRQRVALARALLLNPDLL 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499185640 164 ILDEPTTNIDPDNQQRILSILKKLNRT-CTILMVTHDLHHTTNYFNKVFYMNK 215
Cdd:cd00267 103 LLDEPTSGLDPASRERLLELLRELAEEgRTVIIVTHDPELAELAADRVIVLKD 155
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-201 |
4.98e-27 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 104.43 E-value: 4.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 1 MTIRILAEGLAFRYGSKgpNIIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGSLKtfpshsagKQTHSMIG 80
Cdd:PRK09544 1 MTSLVSLENVSVSFGQR--RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK--------RNGKLRIG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 81 WVPQHFSYDPCFPISVKdvvlsgRLSQLswHGKYKKKDfeaVDHALDLVGLSDHHHHCFAHLSGGQIQRVLLARALASYP 160
Cdd:PRK09544 71 YVPQKLYLDTTLPLTVN------RFLRL--RPGTKKED---ILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRP 139
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 499185640 161 EILILDEPTTNIDPDNQQRILSILKKLNRT--CTILMVTHDLH 201
Cdd:PRK09544 140 QLLVLDEPTQGVDVNGQVALYDLIDQLRREldCAVLMVSHDLH 182
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
3-206 |
1.09e-26 |
|
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: 107.37 E-value: 1.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 3 IRILAEGLAFRYGSKGPnIIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGS-------LKTFPSHSAGKQt 75
Cdd:TIGR02857 320 SSLEFSGVSVAYPGRRP-ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSiavngvpLADADADSWRDQ- 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 76 hsmIGWVPQHfsydP-CFPISVKDVVLSGRLSQlswhgkykkkDFEAVDHALDLVGLSD------HHHHCF-----AHLS 143
Cdd:TIGR02857 398 ---IAWVPQH----PfLFAGTIAENIRLARPDA----------SDAEIREALERAGLDEfvaalpQGLDTPigeggAGLS 460
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499185640 144 GGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKLNRTCTILMVTHDLHHTTNY 206
Cdd:TIGR02857 461 GGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALA 523
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
5-215 |
1.62e-26 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 103.56 E-value: 1.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 5 ILAEGLAFRYGSKGPNIIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGSLKTFP---SHSAGKQTHSMIGW 81
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGmvlSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 82 VPQHfsYDPCF-PISVKDVVLSGrlsqLSWHGKYKKKDFEAVDHALDLVGLSDHHHHCFAHLSGGQIQRVLLARALASYP 160
Cdd:PRK13635 86 VFQN--PDNQFvGATVQDDVAFG----LENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499185640 161 EILILDEPTTNIDPDNQQRILSILKKLNR--TCTILMVTHDLHHTTNYfNKVFYMNK 215
Cdd:PRK13635 160 DIIILDEATSMLDPRGRREVLETVRQLKEqkGITVLSITHDLDEAAQA-DRVIVMNK 215
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
45-200 |
3.38e-26 |
|
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: 103.59 E-value: 3.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 45 KSTLTMLILGLLTP---TFGSLkTFpshsAGKQTHSM------------IGWVPQH-FSY-DPCFPI--SVKDVVLSgrl 105
Cdd:COG0444 44 KSTLARAILGLLPPpgiTSGEI-LF----DGEDLLKLsekelrkirgreIQMIFQDpMTSlNPVMTVgdQIAEPLRI--- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 106 sqlswHGKYKKKDFEA-VDHALDLVGLSD--HHHHCFAH-LSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRIL 181
Cdd:COG0444 116 -----HGGLSKAEARErAIELLERVGLPDpeRRLDRYPHeLSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQIL 190
|
170 180
....*....|....*....|.
gi 499185640 182 SILKKLNRT--CTILMVTHDL 200
Cdd:COG0444 191 NLLKDLQRElgLAILFITHDL 211
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
8-200 |
4.98e-26 |
|
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: 100.67 E-value: 4.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 8 EGLAFRYGSKGpnIIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGSLktfpsHSAGKQTHSM------IGW 81
Cdd:cd03259 4 KGLSKTYGSVR--ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEI-----LIDGRDVTGVpperrnIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 82 VPQHFSYdpcFP-ISVKDVVLSGrlsqLSWHGKYKKKDFEAVDHALDLVGLSDHHHHCFAHLSGGQIQRVLLARALASYP 160
Cdd:cd03259 77 VFQDYAL---FPhLTVAENIAFG----LKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREP 149
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 499185640 161 EILILDEPTTNIDPDNQQRILSILKKLNRT--CTILMVTHDL 200
Cdd:cd03259 150 SLLLLDEPLSALDAKLREELREELKELQRElgITTIYVTHDQ 191
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
3-201 |
5.64e-26 |
|
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: 101.21 E-value: 5.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 3 IRIlaEGLAFRYGSKgpNIIHDVSFSVYDGDFIgiigpngggKSTLTMLILGLLTPTFGSLKTFpshsaGKQTHSM---- 78
Cdd:COG1127 6 IEV--RNLTKSFGDR--VVLDGVSLDVPRGEILaiiggsgsgKSVLLKLIIGLLRPDSGEILVD-----GQDITGLseke 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 79 -------IGWVPQH---FSYdpcfpISVKD-VVLsgRLSQlswHGKYKKKD-FEAVDHALDLVGLSDHHHHCFAHLSGGQ 146
Cdd:COG1127 77 lyelrrrIGMLFQGgalFDS-----LTVFEnVAF--PLRE---HTDLSEAEiRELVLEKLELVGLPGAADKMPSELSGGM 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499185640 147 IQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKLNRT--CTILMVTHDLH 201
Cdd:COG1127 147 RKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDElgLTSVVVTHDLD 203
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
92-201 |
6.99e-26 |
|
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: 100.72 E-value: 6.99e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 92 FPISVKD-VVLSGRLsqlswHGKYKKKDFEA-VDHALDLVGLSD--HHHHCFAHLSGGQIQRVLLARALASYPEILILDE 167
Cdd:cd03260 93 FPGSIYDnVAYGLRL-----HGIKLKEELDErVEEALRKAALWDevKDRLHALGLSGGQQQRLCLARALANEPEVLLLDE 167
|
90 100 110
....*....|....*....|....*....|....
gi 499185640 168 PTTNIDPDNQQRILSILKKLNRTCTILMVTHDLH 201
Cdd:cd03260 168 PTSALDPISTAKIEELIAELKKEYTIVIVTHNMQ 201
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
7-215 |
1.16e-25 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 99.51 E-value: 1.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 7 AEGLAFRYGSKgpNIIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGS-------LKTFPSHSAGKQthsmI 79
Cdd:COG4619 3 LEGLSFRVGGK--PILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEiyldgkpLSAMPPPEWRRQ----V 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 80 GWVPQhfsyDPC-FPISVKDVVlsgrlsQLSWHGKYKKKDFEAVDHALDLVGLSDH--HHHCfAHLSGGQIQRVLLARAL 156
Cdd:COG4619 77 AYVPQ----EPAlWGGTVRDNL------PFPFQLRERKFDRERALELLERLGLPPDilDKPV-ERLSGGERQRLALIRAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499185640 157 ASYPEILILDEPTTNIDPDNQQRILSILKKLNRTC--TILMVTHDLHHTTNYFNKVFYMNK 215
Cdd:COG4619 146 LLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEgrAVLWVSHDPEQIERVADRVLTLEA 206
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
45-215 |
1.24e-25 |
|
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: 99.57 E-value: 1.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 45 KSTLTMLILGLLTPTFGSLkTFPSHSAGKQT---HSMIGWVPQHFSYDPCFpiSVKDVV-LSGRLSQLSwhgkyKKKDFE 120
Cdd:cd03264 38 KTTLMRILATLTPPSSGTI-RIDGQDVLKQPqklRRRIGYLPQEFGVYPNF--TVREFLdYIAWLKGIP-----SKEVKA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 121 AVDHALDLVGLSDHHHHCFAHLSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKLNRTCTILMVTHDL 200
Cdd:cd03264 110 RVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIV 189
|
170
....*....|....*
gi 499185640 201 HHTTNYFNKVFYMNK 215
Cdd:cd03264 190 EDVESLCNQVAVLNK 204
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
8-214 |
1.51e-25 |
|
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: 98.41 E-value: 1.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 8 EGLAFRYGSKgpNIIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGSL----KTFPSHSAGKQTH-SMIGWV 82
Cdd:cd03229 4 KNVSKRYGQK--TVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSIlidgEDLTDLEDELPPLrRRIGMV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 83 PQHFSYdpcFPisvkdvvlsgRLSqlswhgkykkkdfeavdhALDLVGLSdhhhhcfahLSGGQIQRVLLARALASYPEI 162
Cdd:cd03229 82 FQDFAL---FP----------HLT------------------VLENIALG---------LSGGQQQRVALARALAMDPDV 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499185640 163 LILDEPTTNIDPDNQQRILSILKKLNRT--CTILMVTHDLHHTTNYFNKVFYMN 214
Cdd:cd03229 122 LLLDEPTSALDPITRREVRALLKSLQAQlgITVVLVTHDLDEAARLADRVVVLR 175
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
5-201 |
1.52e-25 |
|
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: 99.50 E-value: 1.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 5 ILAEGLAFRYGSKGPNIIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGSLkTFPSHSAG---KQTHSMIGW 81
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTA-YINGYSIRtdrKAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 82 VPQHfsyDPCFP-ISVKD-VVLSGRLsqlswHGKYKKKDFEAVDHALDLVGLSDHHHhCFAH-LSGGQIQRVLLARALAS 158
Cdd:cd03263 80 CPQF---DALFDeLTVREhLRFYARL-----KGLPKSEIKEEVELLLRVLGLTDKAN-KRARtLSGGMKRKLSLAIALIG 150
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 499185640 159 YPEILILDEPTTNIDPDNQQRILSILKKLNRTCTILMVTHDLH 201
Cdd:cd03263 151 GPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMD 193
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
5-198 |
1.93e-25 |
|
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: 98.06 E-value: 1.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 5 ILAEGLAFRYGSKGPNIIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGS--LKTFPSHSAGKQTH-SMIGW 81
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRvrLDGADISQWDPNELgDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 82 VPQhfsydpcfpisvKDVVLSGRLSQlswhgkykkkdfeavdhaldlvglsdhhhhcfAHLSGGQIQRVLLARALASYPE 161
Cdd:cd03246 81 LPQ------------DDELFSGSIAE--------------------------------NILSGGQRQRLGLARALYGNPR 116
|
170 180 190
....*....|....*....|....*....|....*...
gi 499185640 162 ILILDEPTTNIDPDNQQRILSILKKLN-RTCTILMVTH 198
Cdd:cd03246 117 ILVLDEPNSHLDVEGERALNQAIAALKaAGATRIVIAH 154
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
4-200 |
2.23e-25 |
|
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: 104.08 E-value: 2.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 4 RILAEGLAFRYGSKGPNIIHDVSFSVYDGDfigiigpngggKSTLTMLILGLLTPTFGS-------LKTFPshsaGKQTH 76
Cdd:COG4987 333 SLELEDVSFRYPGAGRPVLDGLSLTLPPGErvaivgpsgsgKSTLLALLLRFLDPQSGSitlggvdLRDLD----EDDLR 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 77 SMIGWVPQHFsydPCFPISVKDVVLSGRlsqlswhgkyKKKDFEAVDHALDLVGLSDhhhhcF----------------A 140
Cdd:COG4987 409 RRIAVVPQRP---HLFDTTLRENLRLAR----------PDATDEELWAALERVGLGD-----WlaalpdgldtwlgeggR 470
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 141 HLSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKLNRTCTILMVTHDL 200
Cdd:COG4987 471 RLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRL 530
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
22-200 |
3.25e-25 |
|
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: 100.03 E-value: 3.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 22 IHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGSLKTfpshsAGKQTHSM------------IGWVPQHFSYd 89
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLI-----DGQDIAAMsrkelrelrrkkISMVFQSFAL- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 90 pcFP-ISVKDVVLSGrlsqLSWHGKYKKKDFEAVDHALDLVGLSDHHHHCFAHLSGGQIQRVLLARALASYPEILILDEP 168
Cdd:cd03294 114 --LPhRTVLENVAFG----LEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEA 187
|
170 180 190
....*....|....*....|....*....|....*.
gi 499185640 169 TTNIDP----DNQQRILSILKKLNRtcTILMVTHDL 200
Cdd:cd03294 188 FSALDPlirrEMQDELLRLQAELQK--TIVFITHDL 221
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
3-201 |
6.16e-25 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 100.54 E-value: 6.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 3 IRIlaEGLAFRYGSKGPNII--HDVSFSVYDGDfigiigpngggKSTLTMLILGLLTPTFGS-------LKTFPSHSAGK 73
Cdd:COG1135 2 IEL--ENLSKTFPTKGGPVTalDDVSLTIEKGEifgiigysgagKSTLIRCINLLERPTSGSvlvdgvdLTALSERELRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 74 QTHSmIGWVPQHFS-------YDP-CFPIsvkdvvlsgRLSqlswhgKYKKKDFEA-VDHALDLVGLSDHHHHCFAHLSG 144
Cdd:COG1135 80 ARRK-IGMIFQHFNllssrtvAENvALPL---------EIA------GVPKAEIRKrVAELLELVGLSDKADAYPSQLSG 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499185640 145 GQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKLNRT--CTILMVTHDLH 201
Cdd:COG1135 144 GQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRElgLTIVLITHEMD 202
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
5-201 |
1.27e-24 |
|
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: 97.50 E-value: 1.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 5 ILAEGLAFRYGS-KGP-NIIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGSLktfpsHSAGKQTHSM---- 78
Cdd:COG4181 9 IELRGLTKTVGTgAGElTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTV-----RLAGQDLFALdeda 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 79 --------IGWVPQHFsydPCFP-ISVKDVV-----LSGRlsqlswhgkykKKDFEAVDHALDLVGLSDHHHHCFAHLSG 144
Cdd:COG4181 84 rarlrarhVGFVFQSF---QLLPtLTALENVmlpleLAGR-----------RDARARARALLERVGLGHRLDHYPAQLSG 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499185640 145 GQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKLNRT--CTILMVTHDLH 201
Cdd:COG4181 150 GEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRErgTTLVLVTHDPA 208
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-206 |
3.53e-24 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 97.01 E-value: 3.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 1 MTIRIlaEGLAFRYGSKgpNIIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGSLKTFP---SHSAGKQTHS 77
Cdd:PRK11231 1 MTLRT--ENLTVGYGTK--RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDkpiSMLSSRQLAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 78 MIGWVPQHfsydPCFP--ISVKDVVLSGRLSQLSWHGKYKKKDFEAVDHALDLVGLSDHHHHCFAHLSGGQIQRVLLARA 155
Cdd:PRK11231 77 RLALLPQH----HLTPegITVRELVAYGRSPWLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMV 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 499185640 156 LASYPEILILDEPTTNIDPDNQQRILSILKKLNRTC-TILMVTHDLHHTTNY 206
Cdd:PRK11231 153 LAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGkTVVTVLHDLNQASRY 204
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
5-200 |
4.61e-24 |
|
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: 95.90 E-value: 4.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 5 ILAEGLAFRYGskGPNIIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGSLKTFpSHSAGKQTHSM---IGW 81
Cdd:cd03265 1 IEVENLVKKYG--DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVA-GHDVVREPREVrrrIGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 82 VPQHFSYDPcfpisvkdvVLSGRlSQLSWHGK---YKKKDF-EAVDHALDLVGLSDHHHHCFAHLSGGQIQRVLLARALA 157
Cdd:cd03265 78 VFQDLSVDD---------ELTGW-ENLYIHARlygVPGAERrERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLV 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 499185640 158 SYPEILILDEPTTNIDPDNQQRILSILKKLNRT--CTILMVTHDL 200
Cdd:cd03265 148 HRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEfgMTILLTTHYM 192
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
5-198 |
8.15e-24 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 97.56 E-value: 8.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 5 ILAEGLAFRYGSKGPNII--HDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGSLK------TFPSHSAGKQTH 76
Cdd:PRK11153 2 IELKNISKVFPQGGRTIHalNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLvdgqdlTALSEKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 77 SMIGWVPQHFS-------YDpcfpisvkDVVLSGRLSQLSwhgkykKKDFEA-VDHALDLVGLSDHHHHCFAHLSGGQIQ 148
Cdd:PRK11153 82 RQIGMIFQHFNllssrtvFD--------NVALPLELAGTP------KAEIKArVTELLELVGLSDKADRYPAQLSGGQKQ 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 499185640 149 RVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKLNRT--CTILMVTH 198
Cdd:PRK11153 148 RVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRElgLTIVLITH 199
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
5-201 |
9.67e-24 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 95.31 E-value: 9.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 5 ILAEGLAFRYGSKgpNIIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGS--LKTFPSHSAGKQTHSMIGWV 82
Cdd:COG4555 2 IEVENLSKKYGKV--PALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSilIDGEDVRKEPREARRQIGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 83 PQ-HFSYDPcfpISVKDVV-LSGRLsqlswHGKYKKKDFEAVDHALDLVGLSDHHHHCFAHLSGGQIQRVLLARALASYP 160
Cdd:COG4555 80 PDeRGLYDR---LTVRENIrYFAEL-----YGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDP 151
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 499185640 161 EILILDEPTTNIDPDNQQRILSILKKL-NRTCTILMVTHDLH 201
Cdd:COG4555 152 KVLLLDEPTNGLDVMARRLLREILRALkKEGKTVLFSSHIMQ 193
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
8-201 |
1.84e-23 |
|
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: 93.82 E-value: 1.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 8 EGLAFRYGSKgpNIIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGSLKTFPS-----HSAGKQTHSMI--- 79
Cdd:cd03268 4 NDLTKTYGKK--RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKsyqknIEALRRIGALIeap 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 80 GWVPQhfsydpcfpisvkdvvLSGRlSQLSWHGKYKKKDFEAVDHALDLVGLSDHHHHCFAHLSGGQIQRVLLARALASY 159
Cdd:cd03268 82 GFYPN----------------LTAR-ENLRLLARLLGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGN 144
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 499185640 160 PEILILDEPTTNIDPDNQQRILSILKKLNRT-CTILMVTHDLH 201
Cdd:cd03268 145 PDLLILDEPTNGLDPDGIKELRELILSLRDQgITVLISSHLLS 187
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
45-200 |
2.18e-23 |
|
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: 93.75 E-value: 2.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 45 KSTLTMLILGLLTPTFGSL-----KTFPSHSAGKQTHSMIGWVPQHFSYdpcFP-ISVKDVVLsgrLSQLSWHGKYKKkd 118
Cdd:cd03262 39 KSTLLRCINLLEEPDSGTIiidglKLTDDKKNINELRQKVGMVFQQFNL---FPhLTVLENIT---LAPIKVKGMSKA-- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 119 fEAVDHALDL---VGLSDHHHHCFAHLSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKLNRT-CTIL 194
Cdd:cd03262 111 -EAEERALELlekVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEgMTMV 189
|
....*.
gi 499185640 195 MVTHDL 200
Cdd:cd03262 190 VVTHEM 195
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
4-206 |
2.28e-23 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 95.05 E-value: 2.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 4 RILAEGLAFRYGSKgpNIIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGSL---KTFPSHSAGKQTHSMIG 80
Cdd:PRK10253 7 RLRGEQLTLGYGKY--TVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVwldGEHIQHYASKEVARRIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 81 WVPQHFSYDPcfPISVKDVVLSGRLSQLSWHGKYKKKDFEAVDHALDLVGLSDHHHHCFAHLSGGQIQRVLLARALASYP 160
Cdd:PRK10253 85 LLAQNATTPG--DITVQELVARGRYPHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQET 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 499185640 161 EILILDEPTTNIDPDNQQRILSILKKLNRT--CTILMVTHDLHHTTNY 206
Cdd:PRK10253 163 AIMLLDEPTTWLDISHQIDLLELLSELNREkgYTLAAVLHDLNQACRY 210
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
21-206 |
5.86e-23 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 96.06 E-value: 5.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 21 IIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGS--LKTFPSHSAGKQTHS-MIGWVPQHFSYdpCFPISVK 97
Cdd:PRK09536 18 VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTvlVAGDDVEALSARAASrRVASVPQDTSL--SFEFDVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 98 DVVLSGRLSQLSWHGKYKKKDFEAVDHALDLVGLSDHHHHCFAHLSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQ 177
Cdd:PRK09536 96 QVVEMGRTPHRSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDINHQ 175
|
170 180 190
....*....|....*....|....*....|
gi 499185640 178 QRILSILKKLNRTC-TILMVTHDLHHTTNY 206
Cdd:PRK09536 176 VRTLELVRRLVDDGkTAVAAIHDLDLAARY 205
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
44-170 |
7.54e-23 |
|
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: 90.78 E-value: 7.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 44 GKSTLTMLILGLLTPTFGSLK---TFPSHSAGKQTHSMIGWVPQHFSYDPcfPISVKDVVLSGRLSQlSWHGKYKKKDFE 120
Cdd:pfam00005 23 GKSTLLKLIAGLLSPTEGTILldgQDLTDDERKSLRKEIGYVFQDPQLFP--RLTVRENLRLGLLLK-GLSKREKDARAE 99
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 499185640 121 AVDHALDLVGLSDHH-HHCFAHLSGGQIQRVLLARALASYPEILILDEPTT 170
Cdd:pfam00005 100 EALEKLGLGDLADRPvGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
8-215 |
1.93e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 92.75 E-value: 1.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 8 EGLAFRYGSKGPNIIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGSLKTFP---SHSAGKQTHSMIGWVPQ 84
Cdd:PRK13632 11 ENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGitiSKENLKEIRKKIGIIFQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 85 hfSYDPCF-PISVKDVVLSGRLSQLSWHGKYKKKdfeaVDHALDLVGLSDHHHHCFAHLSGGQIQRVLLARALASYPEIL 163
Cdd:PRK13632 91 --NPDNQFiGATVEDDIAFGLENKKVPPKKMKDI----IDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEII 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499185640 164 ILDEPTTNIDPDNQQRILSILKKL--NRTCTILMVTHDLHHTTNYfNKVFYMNK 215
Cdd:PRK13632 165 IFDESTSMLDPKGKREIKKIMVDLrkTRKKTLISITHDMDEAILA-DKVIVFSE 217
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
10-201 |
3.86e-22 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 91.03 E-value: 3.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 10 LAFRY--GSKGPNIIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFG-------SLKTFPSHSAGKQTHSMIG 80
Cdd:PRK11629 11 LCKRYqeGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGdvifngqPMSKLSSAAKAELRNQKLG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 81 WVPQHFSYDPCFPiSVKDV---VLSGrlsqlswhgkyKKKDFEAVDHALDL---VGLSDHHHHCFAHLSGGQIQRVLLAR 154
Cdd:PRK11629 91 FIYQFHHLLPDFT-ALENVampLLIG-----------KKKPAEINSRALEMlaaVGLEHRANHRPSELSGGERQRVAIAR 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 499185640 155 ALASYPEILILDEPTTNIDPDNQQRILSILKKLNRT--CTILMVTHDLH 201
Cdd:PRK11629 159 ALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLqgTAFLVVTHDLQ 207
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
8-200 |
1.01e-21 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 90.05 E-value: 1.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 8 EGLAFRYGSkGPNIIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGSLKTfpshsAGKQTHSM--------I 79
Cdd:cd03295 4 ENVTKRYGG-GKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFI-----DGEDIREQdpvelrrkI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 80 GWVPQHFSYDPCFPISvKDVVLSGRLSqlswhgKYKKKDFEA-VDHALDLVGLSDHHhhcFAH-----LSGGQIQRVLLA 153
Cdd:cd03295 78 GYVIQQIGLFPHMTVE-ENIALVPKLL------KWPKEKIRErADELLALVGLDPAE---FADrypheLSGGQQQRVGVA 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 499185640 154 RALASYPEILILDEPTTNIDP---DN-QQRILSILKKLNRtcTILMVTHDL 200
Cdd:cd03295 148 RALAADPPLLLMDEPFGALDPitrDQlQEEFKRLQQELGK--TIVFVTHDI 196
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
13-215 |
1.40e-21 |
|
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: 89.60 E-value: 1.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 13 RYGSKgpNIIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGSLkTFpshsAGKQTHSM------IGWVPQHF 86
Cdd:cd03300 9 FYGGF--VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEI-LL----DGKDITNLpphkrpVNTVFQNY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 87 SYdpcFP-ISVKDVVLSG-RLSQLSwhgkyKKKDFEAVDHALDLVGLSDHHHHCFAHLSGGQIQRVLLARALASYPEILI 164
Cdd:cd03300 82 AL---FPhLTVFENIAFGlRLKKLP-----KAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499185640 165 LDEPTTNIDPDNQQRILSILKKLNRTC--TILMVTHDLHHTTNYFNKVFYMNK 215
Cdd:cd03300 154 LDEPLGALDLKLRKDMQLELKRLQKELgiTFVFVTHDQEEALTMSDRIAVMNK 206
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
24-215 |
4.31e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 89.03 E-value: 4.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 24 DVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGSLKTF----PSHSAGKQTHSM---IGWVPQhFSYDPCFPISV 96
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDdtliTSTSKNKDIKQIrkkVGLVFQ-FPESQLFEETV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 97 -KDVVLSGRLSQLSwhgkykKKDFEAV-DHALDLVGLSDH--HHHCFaHLSGGQIQRVLLARALASYPEILILDEPTTNI 172
Cdd:PRK13649 104 lKDVAFGPQNFGVS------QEEAEALaREKLALVGISESlfEKNPF-ELSGGQMRRVAIAGILAMEPKILVLDEPTAGL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 499185640 173 DPDNQQRILSILKKLNRT-CTILMVTHDLHHTTNYFNKVFYMNK 215
Cdd:PRK13649 177 DPKGRKELMTLFKKLHQSgMTIVLVTHLMDDVANYADFVYVLEK 220
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
7-216 |
1.22e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 87.83 E-value: 1.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 7 AEGLAFRYgSKGPNIIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGS--LKTFP---SHSAGKQTHSMIGW 81
Cdd:PRK13639 4 TRDLKYSY-PDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEvlIKGEPikyDKKSLLEVRKTVGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 82 VPQHfSYDPCFPISVKDVVLSGRLSQlswhgKYKKKDFEA-VDHALDLVGLSDHHHHCFAHLSGGQIQRVLLARALASYP 160
Cdd:PRK13639 83 VFQN-PDDQLFAPTVEEDVAFGPLNL-----GLSKEEVEKrVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499185640 161 EILILDEPTTNIDPDNQQRILSILKKLNRT-CTILMVTHDLHHTTNYFNKVFYMNKT 216
Cdd:PRK13639 157 EIIVLDEPTSGLDPMGASQIMKLLYDLNKEgITIIISTHDVDLVPVYADKVYVMSDG 213
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
8-198 |
2.21e-20 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 89.45 E-value: 2.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 8 EGLAFRYGsKGPNIIHDVSFSVYDGDFigiigpngggKSTLTMLILGLLTPTFGS-------LKTFPSHSAgkqtHSMIG 80
Cdd:COG1132 343 ENVSFSYP-GDRPVLKDISLTIPPGETvalvgpsgsgKSTLVNLLLRFYDPTSGRilidgvdIRDLTLESL----RRQIG 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 81 WVPQHFSydpCFPISVKDVVLSGRLSQlswhgkykkkDFEAVDHALDLVGLSDhhhhcF----------------AHLSG 144
Cdd:COG1132 418 VVPQDTF---LFSGTIRENIRYGRPDA----------TDEEVEEAAKAAQAHE-----FiealpdgydtvvgergVNLSG 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499185640 145 GQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKLNRTCTILMVTH 198
Cdd:COG1132 480 GQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAH 533
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
7-199 |
2.51e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 89.35 E-value: 2.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 7 AEGLAFRYGSKgpNIIHDVSFSVYDGDfigiigpnggGKSTLTMLILGLLTPTFGSLktfpSHSAGKQthsmIGWVPQHF 86
Cdd:COG0488 1 LENLSKSFGGR--PLLDDVSLSINPGDriglvgrngaGKSTLLKILAGELEPDSGEV----SIPKGLR----IGYLPQEP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 87 SYDPCFpiSVKDVVLSG--------------------------RLSQLswHGKYKKKD---FEA-VDHALDLVGLSDHHH 136
Cdd:COG0488 71 PLDDDL--TVLDTVLDGdaelraleaeleeleaklaepdedleRLAEL--QEEFEALGgweAEArAEEILSGLGFPEEDL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 137 HC-FAHLSGGQIQRVLLARALASYPEILILDEPTTNIDpdnqqrILSI------LKklNRTCTILMVTHD 199
Cdd:COG0488 147 DRpVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLD------LESIewleefLK--NYPGTVLVVSHD 208
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1-215 |
3.94e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 86.64 E-value: 3.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 1 MTIRIlaEGLAFRYGSKGP---NIIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGSLKTFPSHSAGKQTH- 76
Cdd:PRK13637 1 MSIKI--ENLTHIYMEGTPfekKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 77 ----SMIGWVPQHFSYDpCFPISV-KDVVLSGRLSQLSWHGKYKKkdfeaVDHALDLVGLS--DHHHHCFAHLSGGQIQR 149
Cdd:PRK13637 79 sdirKKVGLVFQYPEYQ-LFEETIeKDIAFGPINLGLSEEEIENR-----VKRAMNIVGLDyeDYKDKSPFELSGGQKRR 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499185640 150 VLLARALASYPEILILDEPTTNIDPDNQQRILSILKKLNR--TCTILMVTHDLHHTTNYFNKVFYMNK 215
Cdd:PRK13637 153 VAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKeyNMTIILVSHSMEDVAKLADRIIVMNK 220
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-198 |
7.54e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 86.81 E-value: 7.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 2 TIRILAEGLAFRYGSKGpnIIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGSLKTF--PSHSAGKQTHSMI 79
Cdd:PRK13536 39 TVAIDLAGVSKSYGDKA--VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLgvPVPARARLARARI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 80 GWVPQHFSYDPCFPISvKDVVLSGRLSQLSwhgkykKKDFEAV-DHALDLVGLSDHHHHCFAHLSGGQIQRVLLARALAS 158
Cdd:PRK13536 117 GVVPQFDNLDLEFTVR-ENLLVFGRYFGMS------TREIEAViPSLLEFARLESKADARVSDLSGGMKRRLTLARALIN 189
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 499185640 159 YPEILILDEPTTNIDPDNQQRILSILKK-LNRTCTILMVTH 198
Cdd:PRK13536 190 DPQLLILDEPTTGLDPHARHLIWERLRSlLARGKTILLTTH 230
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1-200 |
1.02e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 85.17 E-value: 1.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 1 MTIRILAEGLAFRYgSKGPNIIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGSLKTFP---SHSAGKQTHS 77
Cdd:PRK13647 1 MDNIIEVEDLHFRY-KDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGrevNAENEKWVRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 78 MIGWVPQhfsyDP---CFPISVKDVVLSGRLSQlswhGKYKKKDFEAVDHALDLVGLSDHHHHCFAHLSGGQIQRVLLAR 154
Cdd:PRK13647 80 KVGLVFQ----DPddqVFSSTVWDDVAFGPVNM----GLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAG 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 499185640 155 ALASYPEILILDEPTTNIDPDNQQRILSILKKLNRT-CTILMVTHDL 200
Cdd:PRK13647 152 VLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQgKTVIVATHDV 198
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
79-202 |
1.11e-19 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 84.70 E-value: 1.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 79 IGWVPQHfsydPC-FPISVKDVVLSG-RLsqlswHGKYKKKDF-EAVDHALDLVGL----SDHHHHCFAHLSGGQIQRVL 151
Cdd:COG1117 94 VGMVFQK----PNpFPKSIYDNVAYGlRL-----HGIKSKSELdEIVEESLRKAALwdevKDRLKKSALGLSGGQQQRLC 164
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 499185640 152 LARALASYPEILILDEPTTNIDPDNQQRILSILKKLNRTCTILMVTHDLHH 202
Cdd:COG1117 165 IARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHNMQQ 215
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
120-215 |
1.25e-19 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 84.85 E-value: 1.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 120 EAVDHA---LDLVGLSDHHHHCFAHLSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKL---NRtcTI 193
Cdd:COG4598 130 EAIERAealLAKVGLADKRDAYPAHLSGGQQQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLaeeGR--TM 207
|
90 100
....*....|....*....|..
gi 499185640 194 LMVTHDLHHTTNYFNKVFYMNK 215
Cdd:COG4598 208 LVVTHEMGFARDVSSHVVFLHQ 229
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
79-200 |
1.29e-19 |
|
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters. [Transport and binding proteins, Anions]
Pssm-ID: 273372 [Multi-domain] Cd Length: 247 Bit Score: 84.65 E-value: 1.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 79 IGWVPQHFsyDPcFPISVKDVVLSGrlsqLSWHG-KYKKKDFEAVDHALDLVGL----SDHHHHCFAHLSGGQIQRVLLA 153
Cdd:TIGR00972 84 VGMVFQKP--NP-FPMSIYDNIAYG----PRLHGiKDKKELDEIVEESLKKAALwdevKDRLHDSALGLSGGQQQRLCIA 156
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 499185640 154 RALASYPEILILDEPTTNIDPDNQQRILSILKKLNRTCTILMVTHDL 200
Cdd:TIGR00972 157 RALAVEPEVLLLDEPTSALDPIATGKIEELIQELKKKYTIVIVTHNM 203
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
7-215 |
1.33e-19 |
|
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: 83.87 E-value: 1.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 7 AEGLAFRYGSKgpNIIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGSLKtFPSHSAGKQTHSMIGWVPQHF 86
Cdd:cd03269 3 VENVTKRFGRV--TALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVL-FDGKPLDIAARNRIGYLPEER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 87 SYDPcfPISVKDVVLsgRLSQLswHGkYKKKDFEA-VDHALDLVGLSDHHHHCFAHLSGGQIQRVLLARALASYPEILIL 165
Cdd:cd03269 80 GLYP--KMKVIDQLV--YLAQL--KG-LKKEEARRrIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLIL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 499185640 166 DEPTTNIDPDNQQRILSILKKLNRT-CTILMVTHDLHHTTNYFNKVFYMNK 215
Cdd:cd03269 153 DEPFSGLDPVNVELLKDVIRELARAgKTVILSTHQMELVEELCDRVLLLNK 203
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
3-200 |
2.27e-19 |
|
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: 86.65 E-value: 2.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 3 IRILAEGLAFRYGSkGPNIIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFG--SLKTFPSHSA-GKQTHSMI 79
Cdd:TIGR02868 333 PTLELRDLSAGYPG-APPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGevTLDGVPVSSLdQDEVRRRV 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 80 GWVPQhfsyDP-CFPISVKDVVLSGRlsqlswhgkyKKKDFEAVDHALDLVGLSDH------------HHHCfAHLSGGQ 146
Cdd:TIGR02868 412 SVCAQ----DAhLFDTTVRENLRLAR----------PDATDEELWAALERVGLADWlralpdgldtvlGEGG-ARLSGGE 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499185640 147 IQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKLNRTCTILMVTHDL 200
Cdd:TIGR02868 477 RQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
45-201 |
2.74e-19 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 83.50 E-value: 2.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 45 KSTLTMLILGLLTPTFGSLK------TFPSHSAGKQtHSMIGWVPQHFSYdpcFP-ISVKDVVLSGrlsqLSWHGKYKKK 117
Cdd:COG1126 40 KSTLLRCINLLEEPDSGTITvdgedlTDSKKDINKL-RRKVGMVFQQFNL---FPhLTVLENVTLA----PIKVKKMSKA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 118 dfEAVDHALDL---VGLSDHHHHCFAHLSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKLNRT-CTI 193
Cdd:COG1126 112 --EAEERAMELlerVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKEgMTM 189
|
....*...
gi 499185640 194 LMVTHDLH 201
Cdd:COG1126 190 VVVTHEMG 197
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1-215 |
2.91e-19 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 83.53 E-value: 2.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 1 MTIRIlaEGLAFRYGSKgpNIIHDVSFSVYDGDFIGIIGPNGGGKSTLtMLILGLL-TPTFGSL---------KTFPSHS 70
Cdd:PRK11124 1 MSIQL--NGINCFYGAH--QALFDITLDCPQGETLVLLGPSGAGKSSL-LRVLNLLeMPRSGTLniagnhfdfSKTPSDK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 71 AGKQTHSMIGWVPQHFSYDPCFPISVKDVVLSGRLSQLSwhgkyKKKDFEAVDHALDLVGLSDHHHHCFAHLSGGQIQRV 150
Cdd:PRK11124 76 AIRELRRNVGMVFQQYNLWPHLTVQQNLIEAPCRVLGLS-----KDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRV 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499185640 151 LLARALASYPEILILDEPTTNIDPDNQQRILSILKKLNRT-CTILMVTHDLHHTTNYFNKVFYMNK 215
Cdd:PRK11124 151 AIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETgITQVIVTHEVEVARKTASRVVYMEN 216
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
7-199 |
3.66e-19 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 83.76 E-value: 3.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 7 AEGLAFRYGSKGPN--IIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGSLK------TFPSHSAGK--QTH 76
Cdd:COG4525 6 VRHVSVRYPGGGQPqpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITldgvpvTGPGADRGVvfQKD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 77 SMIGWvpqhfsydpcfpISVKD-VVLSGRLSQLSwhgkyKKKDFEAVDHALDLVGLSDHHHHCFAHLSGGQIQRVLLARA 155
Cdd:COG4525 86 ALLPW------------LNVLDnVAFGLRLRGVP-----KAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARA 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 499185640 156 LASYPEILILDEPTTNIDPDN----QQRILSILKKLNRtcTILMVTHD 199
Cdd:COG4525 149 LAADPRFLLMDEPFGALDALTreqmQELLLDVWQRTGK--GVFLITHS 194
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
4-198 |
3.92e-19 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 86.07 E-value: 3.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 4 RILAEGLAFRYGSKGPNIIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGSLkTFPSHSAgKQTHSM----- 78
Cdd:TIGR03375 463 EIEFRNVSFAYPGQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSV-LLDGVDI-RQIDPAdlrrn 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 79 IGWVPQhfsyDP-CFPISVKDVVLSGRLSqlswhgkykkKDFEAVDHALDLVGLSD---HHHHCFAH--------LSGGQ 146
Cdd:TIGR03375 541 IGYVPQ----DPrLFYGTLRDNIALGAPY----------ADDEEILRAAELAGVTEfvrRHPDGLDMqigergrsLSGGQ 606
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 499185640 147 IQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKLNRTCTILMVTH 198
Cdd:TIGR03375 607 RQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLAGKTLVLVTH 658
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
45-198 |
4.08e-19 |
|
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: 82.64 E-value: 4.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 45 KSTLTMLILGLLTPTFGSLKtFPSHSAgKQTH-----SMIGWVPQHFSYdpcFPISVKDVVLSGRLSQlswhgkykkkDF 119
Cdd:cd03245 43 KSTLLKLLAGLYKPTSGSVL-LDGTDI-RQLDpadlrRNIGYVPQDVTL---FYGTLRDNITLGAPLA----------DD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 120 EAVDHALDLVGLSD---HHHHCFA--------HLSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKLN 188
Cdd:cd03245 108 ERILRAAELAGVTDfvnKHPNGLDlqigergrGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLL 187
|
170
....*....|
gi 499185640 189 RTCTILMVTH 198
Cdd:cd03245 188 GDKTLIIITH 197
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
22-200 |
5.76e-19 |
|
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: 82.51 E-value: 5.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 22 IHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGSL--------KTFPSHSAGKQTHSMIGW--VPQHFSydpc 91
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVilegkqitEPGPDRMVVFQNYSLLPWltVRENIA---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 92 fpISVKDVvlsgrLSQLSwhgkyKKKDFEAVDHALDLVGLSDHHHHCFAHLSGGQIQRVLLARALASYPEILILDEPTTN 171
Cdd:TIGR01184 77 --LAVDRV-----LPDLS-----KSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGA 144
|
170 180 190
....*....|....*....|....*....|...
gi 499185640 172 IDP----DNQQRILSILKKlnRTCTILMVTHDL 200
Cdd:TIGR01184 145 LDAltrgNLQEELMQIWEE--HRVTVLMVTHDV 175
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
14-200 |
6.22e-19 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 81.89 E-value: 6.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 14 YGSKgpNIIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGSLKTFPSHSA---GKQTHSM----IGWVPQHF 86
Cdd:TIGR03608 8 FGDK--VILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPplnSKKASKFrrekLGYLFQNF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 87 SYdpcfpI---SVKDVVLSGrlsqLSWHGKYKKKDFEAVDHALDLVGLSDHHHHCFAHLSGGQIQRVLLARALASYPEIL 163
Cdd:TIGR03608 86 AL-----IeneTVEENLDLG----LKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLI 156
|
170 180 190
....*....|....*....|....*....|....*...
gi 499185640 164 ILDEPTTNIDPDNQQRILSILKKLN-RTCTILMVTHDL 200
Cdd:TIGR03608 157 LADEPTGSLDPKNRDEVLDLLLELNdEGKTIIIVTHDP 194
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-200 |
6.92e-19 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 84.04 E-value: 6.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 1 MTIRIlaEGLAFRYGSKgpNIIHDVSFSVYD------------GdfigiigpngggKSTLTMLILGLLTPTFGSL----K 64
Cdd:COG1118 1 MSIEV--RNISKRFGSF--TLLDDVSLEIASgelvallgpsgsG------------KTTLLRIIAGLETPDSGRIvlngR 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 65 TFPSHSAGKQTHsmIGWVPQHFSYdpcFP-ISVKDVVLSGrlsqLSwHGKYKKKDFEA-VDHALDLVGLSDHHHHCFAHL 142
Cdd:COG1118 65 DLFTNLPPRERR--VGFVFQHYAL---FPhMTVAENIAFG----LR-VRPPSKAEIRArVEELLELVQLEGLADRYPSQL 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499185640 143 SGGQIQRVLLARALASYPEILILDEPTTNIDPD--NQQRIL--SILKKLNRTCtiLMVTHDL 200
Cdd:COG1118 135 SGGQRQRVALARALAVEPEVLLLDEPFGALDAKvrKELRRWlrRLHDELGGTT--VFVTHDQ 194
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
4-200 |
1.08e-18 |
|
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: 81.50 E-value: 1.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 4 RILAEGLAFRYGSKGPnIIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGSLKT--FPSHSAGKQT-HSMIG 80
Cdd:cd03254 2 EIEFENVNFSYDEKKP-VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIdgIDIRDISRKSlRSMIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 81 WVPQhfsyDP-CFPISVKDVVLSGRLSQlswhgkyKKKDFEAVD---HALDLV-----GLSDHHHHCFAHLSGGQIQRVL 151
Cdd:cd03254 81 VVLQ----DTfLFSGTIMENIRLGRPNA-------TDEEVIEAAkeaGAHDFImklpnGYDTVLGENGGNLSQGERQLLA 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 499185640 152 LARALASYPEILILDEPTTNIDPDNQQRILSILKKLNRTCTILMVTHDL 200
Cdd:cd03254 150 IARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRL 198
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1-215 |
2.13e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 81.99 E-value: 2.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 1 MTIRIlaEGLAFRYGSKGP---NIIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGSLK----TFPSHSAGK 73
Cdd:PRK13634 1 MDITF--QKVEHRYQYKTPferRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTigerVITAGKKNK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 74 QTHSM---IGWV---PQHFSY------DPCF-PISVkdvvlsgrlsqlswhGKYKKKDFEAVDHALDLVGLSDH--HHHC 138
Cdd:PRK13634 79 KLKPLrkkVGIVfqfPEHQLFeetvekDICFgPMNF---------------GVSEEDAKQKAREMIELVGLPEEllARSP 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499185640 139 FAhLSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKLNR--TCTILMVTHDLHHTTNYFNKVFYMNK 215
Cdd:PRK13634 144 FE-LSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKekGLTTVLVTHSMEDAARYADQIVVMHK 221
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
24-215 |
2.54e-18 |
|
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: 80.84 E-value: 2.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 24 DVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGS-------LKTFPSHSAGkqthsmIGWVPQHFSYdpcFP-IS 95
Cdd:cd03299 17 NVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKillngkdITNLPPEKRD------ISYVPQNYAL---FPhMT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 96 VKDVVLSGrlsqLSWHGKYKKKDFEAVDHALDLVGLSDHHHHCFAHLSGGQIQRVLLARALASYPEILILDEPTTNIDPD 175
Cdd:cd03299 88 VYKNIAYG----LKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVR 163
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 499185640 176 NQQRILSILKKLNR--TCTILMVTHDLHHTTNYFNKVFYMNK 215
Cdd:cd03299 164 TKEKLREELKKIRKefGVTVLHVTHDFEEAWALADKVAIMLN 205
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
120-200 |
4.54e-18 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 80.14 E-value: 4.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 120 EAVDHALDL---VGLSDHHHHCFAHLSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKL-NRTCTILM 195
Cdd:PRK09493 112 EAEKQARELlakVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLaEEGMTMVI 191
|
....*
gi 499185640 196 VTHDL 200
Cdd:PRK09493 192 VTHEI 196
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
21-234 |
6.65e-18 |
|
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: 80.23 E-value: 6.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 21 IIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGSLKTfpshsAGKQTHSMIGWVPQHF----------SYDP 90
Cdd:TIGR02769 26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSF-----RGQDLYQLDRKQRRAFrrdvqlvfqdSPSA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 91 CFPISVKDVVLSGRLSQLSWHGKYKKKdfEAVDHALDLVGL-SDHHHHCFAHLSGGQIQRVLLARALASYPEILILDEPT 169
Cdd:TIGR02769 101 VNPRMTVRQIIGEPLRHLTSLDESEQK--ARIAELLDMVGLrSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAV 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499185640 170 TNIDPDNQQRILSILKKLNRTCTI--LMVTHDLHHTTNYFNKVFYMNKtlTSLADTSTLTDQFC-CHP 234
Cdd:TIGR02769 179 SNLDMVLQAVILELLRKLQQAFGTayLFITHDLRLVQSFCQRVAVMDK--GQIVEECDVAQLLSfKHP 244
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-226 |
6.92e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 79.82 E-value: 6.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 1 MTIRILA-EGLAFRYGSKgpNIIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLI--LGLLTP---TFGSLKtFPSHSA-GK 73
Cdd:PRK14239 1 MTEPILQvSDLSVYYNKK--KALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPevtITGSIV-YNGHNIySP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 74 QTHSM-----IGWVPQHfsYDPcFPISVKDVVLSG-RLSQLswhgkykkKDFEAVDHALD--LVGLS------DHHHHCF 139
Cdd:PRK14239 78 RTDTVdlrkeIGMVFQQ--PNP-FPMSIYENVVYGlRLKGI--------KDKQVLDEAVEksLKGASiwdevkDRLHDSA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 140 AHLSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKLNRTCTILMVTHDLHHTTNYFNKV-FYMNKTLT 218
Cdd:PRK14239 147 LGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRISDRTgFFLDGDLI 226
|
....*...
gi 499185640 219 SLADTSTL 226
Cdd:PRK14239 227 EYNDTKQM 234
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
45-201 |
7.57e-18 |
|
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: 79.40 E-value: 7.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 45 KSTLTMLILGLLTPTFGS-------LKTFPSH---SAGkqthsmIGWVPQHFSydpCFP-ISVKDVVLSGRLSQ------ 107
Cdd:cd03219 39 KTTLFNLISGFLRPTSGSvlfdgedITGLPPHeiaRLG------IGRTFQIPR---LFPeLTVLENVMVAAQARtgsgll 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 108 LSWHGKYKKKDFEAVDHALDLVGLSDHHHHCFAHLSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKL 187
Cdd:cd03219 110 LARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIREL 189
|
170
....*....|....*
gi 499185640 188 N-RTCTILMVTHDLH 201
Cdd:cd03219 190 ReRGITVLLVEHDMD 204
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1-215 |
8.10e-18 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 79.67 E-value: 8.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 1 MTIRIlaEGLAFRYGSKgpNIIHDVSFSVYDGDFIGIIGPNGGGKSTLtMLILGLL-TPTFGSL---------KTFPSHS 70
Cdd:COG4161 1 MSIQL--KNINCFYGSH--QALFDINLECPSGETLVLLGPSGAGKSSL-LRVLNLLeTPDSGQLniaghqfdfSQKPSEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 71 AGKQTHSMIGWVPQHFSYDPCFpiSVKDVVLSGRLSQLswhGKYKKKDFEAVDHALDLVGLSDHHHHCFAHLSGGQIQRV 150
Cdd:COG4161 76 AIRLLRQKVGMVFQQYNLWPHL--TVMENLIEAPCKVL---GLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRV 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499185640 151 LLARALASYPEILILDEPTTNIDPDNQQRILSILKKLNRT-CTILMVTHDLHHTTNYFNKVFYMNK 215
Cdd:COG4161 151 AIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTgITQVIVTHEVEFARKVASQVVYMEK 216
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-200 |
1.48e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 79.39 E-value: 1.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 1 MTIRILAEGLAFRYGSKGPN-IIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGSL-----KTFPSHSAGKQ 74
Cdd:PRK13650 1 MSNIIEVKNLTFKYKEDQEKyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIiidgdLLTEENVWDIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 75 THsmIGWVPQhfSYDPCF-PISVKDVVLSGrlsqLSWHGKYKKKDFEAVDHALDLVGLSDHHHHCFAHLSGGQIQRVLLA 153
Cdd:PRK13650 81 HK--IGMVFQ--NPDNQFvGATVEDDVAFG----LENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 499185640 154 RALASYPEILILDEPTTNIDPDNQQRILSILKKLNRT--CTILMVTHDL 200
Cdd:PRK13650 153 GAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDyqMTVISITHDL 201
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
5-200 |
1.58e-17 |
|
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: 78.68 E-value: 1.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 5 ILAEGLAFRYGSKGPNIIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFG-------SLKTFPSHSAGKQths 77
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGrvlvdghDLALADPAWLRRQ--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 78 mIGWVPQHfsyDPCFPISVKDVVLSGRlsqlswhgkyKKKDFEAVDHALDLVGLsdhhhHCF----------------AH 141
Cdd:cd03252 78 -VGVVLQE---NVLFNRSIRDNIALAD----------PGMSMERVIEAAKLAGA-----HDFiselpegydtivgeqgAG 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499185640 142 LSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKLNRTCTILMVTHDL 200
Cdd:cd03252 139 LSGGQRQRIAIARALIHNPRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRL 197
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
8-198 |
2.25e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 79.46 E-value: 2.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 8 EGLAFRYGSKgpNIIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGSLK----TFPSHSagKQTHSMIGWVP 83
Cdd:PRK13537 11 RNVEKRYGDK--LVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISlcgePVPSRA--RHARQRVGVVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 84 QHFSYDPCFPISvKDVVLSGRLSQLSWHGKYkkkdfEAVDHALDLVGLSDHHHHCFAHLSGGQIQRVLLARALASYPEIL 163
Cdd:PRK13537 87 QFDNLDPDFTVR-ENLLVFGRYFGLSAAAAR-----ALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVL 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 499185640 164 ILDEPTTNIDPDNQQRILSILKKL-NRTCTILMVTH 198
Cdd:PRK13537 161 VLDEPTTGLDPQARHLMWERLRSLlARGKTILLTTH 196
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
102-201 |
2.59e-17 |
|
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: 78.54 E-value: 2.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 102 SGRLSQLSWHGKYKKKDFEAVDHA---LDLVGLSDHHHHCFAHLSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQ 178
Cdd:COG0411 110 RGLLAALLRLPRARREEREARERAeelLERVGLADRADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETE 189
|
90 100
....*....|....*....|....*
gi 499185640 179 RILSILKKLNRT--CTILMVTHDLH 201
Cdd:COG0411 190 ELAELIRRLRDErgITILLIEHDMD 214
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
97-198 |
4.42e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 77.65 E-value: 4.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 97 KDVVLSGRLSQLSwhgKYKKKDFEAVDHALDLVGLSDHHHHCF----AHLSGGQIQRVLLARALASYPEILILDEPTTNI 172
Cdd:PRK14247 101 ENVALGLKLNRLV---KSKKELQERVRWALEKAQLWDEVKDRLdapaGKLSGGQQQRLCIARALAFQPEVLLADEPTANL 177
|
90 100
....*....|....*....|....*.
gi 499185640 173 DPDNQQRILSILKKLNRTCTILMVTH 198
Cdd:PRK14247 178 DPENTAKIESLFLELKKDMTIVLVTH 203
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
45-199 |
6.04e-17 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 77.13 E-value: 6.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 45 KSTLTMLILGLLTPTFGSLktfpsHSAGKQTHSM------------IGWVPQHFSYDPCFPiSVKDVVLSGRLsqlswHG 112
Cdd:PRK10584 49 KSTLLAILAGLDDGSSGEV-----SLVGQPLHQMdeearaklrakhVGFVFQSFMLIPTLN-ALENVELPALL-----RG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 113 KYKKKDFEAVDHALDLVGLSDHHHHCFAHLSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKLNR--T 190
Cdd:PRK10584 118 ESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNRehG 197
|
....*....
gi 499185640 191 CTILMVTHD 199
Cdd:PRK10584 198 TTLILVTHD 206
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
3-228 |
8.41e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 77.82 E-value: 8.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 3 IRILAEGLAFRYGSKGP---NIIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGSLKTFPSHSAGKQTHSMI 79
Cdd:PRK13651 1 MQIKVKNIVKIFNKKLPtelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 80 GWVPQHFSYDPCFPISVKDVV-LSGRLSQLSWHGKYK------KKDF------------EAVDHA---LDLVGLSDHH-- 135
Cdd:PRK13651 81 EKVLEKLVIQKTRFKKIKKIKeIRRRVGVVFQFAEYQlfeqtiEKDIifgpvsmgvskeEAKKRAakyIELVGLDESYlq 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 136 HHCFAhLSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKLNRTC-TILMVTHDLHHTTNYFNKVFYMN 214
Cdd:PRK13651 161 RSPFE-LSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGkTIILVTHDLDNVLEWTKRTIFFK 239
|
250 260
....*....|....*....|..
gi 499185640 215 --------KTLTSLADTSTLTD 228
Cdd:PRK13651 240 dgkiikdgDTYDILSDNKFLIE 261
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
3-199 |
8.47e-17 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 77.03 E-value: 8.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 3 IRILAEGLAFRYGSKgpNIIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGSL--KTFPSHSAGKQTHSMig 80
Cdd:PRK11247 11 TPLLLNAVSKRYGER--TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELlaGTAPLAEAREDTRLM-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 81 wvpqhFSYDPCFPI-SVKDVVlsgrlsQLSWHGKYKKKDFEAvdhaLDLVGLSDHHHHCFAHLSGGQIQRVLLARALASY 159
Cdd:PRK11247 87 -----FQDARLLPWkKVIDNV------GLGLKGQWRDAALQA----LAAVGLADRANEWPAALSGGQKQRVALARALIHR 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 499185640 160 PEILILDEPTTNIDP----DNQQRILSILKKLNrtCTILMVTHD 199
Cdd:PRK11247 152 PGLLLLDEPLGALDAltriEMQDLIESLWQQHG--FTVLLVTHD 193
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
45-200 |
9.88e-17 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 76.33 E-value: 9.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 45 KSTLTMLILGLLTPTFGSL----KTFPSHSAGKQTHSMIgwvpqhFSYDPCFP-ISVKDVVLSGrlsqLSWHGKYKKKDF 119
Cdd:COG3840 38 KSTLLNLIAGFLPPDSGRIlwngQDLTALPPAERPVSML------FQENNLFPhLTVAQNIGLG----LRPGLKLTAEQR 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 120 EAVDHALDLVGLSDHHHHCFAHLSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKLNRT--CTILMVT 197
Cdd:COG3840 108 AQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRErgLTVLMVT 187
|
...
gi 499185640 198 HDL 200
Cdd:COG3840 188 HDP 190
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
8-199 |
1.17e-16 |
|
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: 75.75 E-value: 1.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 8 EGLAFRYGSKgpNIIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGSL--------KTFPSHSAgkqthsmI 79
Cdd:cd03301 4 ENVTKRFGNV--TALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIyiggrdvtDLPPKDRD-------I 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 80 GWVPQHFSYDPcfPISVKDVVLSGrlsqLSWHGKYKKKDFEAVDHALDLVGLSDHHHHCFAHLSGGQIQRVLLARALASY 159
Cdd:cd03301 75 AMVFQNYALYP--HMTVYDNIAFG----LKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVRE 148
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 499185640 160 PEILILDEPTTNIDPDNQQRILSILKKLNRT--CTILMVTHD 199
Cdd:cd03301 149 PKVFLMDEPLSNLDAKLRVQMRAELKRLQQRlgTTTIYVTHD 190
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
108-201 |
1.23e-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: 78.57 E-value: 1.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 108 LSWHGKYKKKDFEA-VDHALDLVGLSDHHH--HCFAH-LSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSI 183
Cdd:COG4172 119 LRLHRGLSGAAARArALELLERVGIPDPERrlDAYPHqLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDL 198
|
90 100
....*....|....*....|
gi 499185640 184 LKKLNRT--CTILMVTHDLH 201
Cdd:COG4172 199 LKDLQRElgMALLLITHDLG 218
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
8-215 |
1.26e-16 |
|
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: 75.99 E-value: 1.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 8 EGLAFRYGSKGPNIIHDVSFSVY------------DGdfigiigpngggKSTLTMLILGLLTPTFGS-------LKTFPS 68
Cdd:cd03244 6 KNVSLRYRPNLPPVLKNISFSIKpgekvgivgrtgSG------------KSSLLLALFRLVELSSGSilidgvdISKIGL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 69 HsagkQTHSMIGWVPQhfsyDPcfpisvkdVVLSGRL-SQLSWHGKYkkkDFEAVDHALDLVGLSDH-----------HH 136
Cdd:cd03244 74 H----DLRSRISIIPQ----DP--------VLFSGTIrSNLDPFGEY---SDEELWQALERVGLKEFveslpggldtvVE 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499185640 137 HCFAHLSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKLNRTCTILMVTHDLHHTTNYfNKVFYMNK 215
Cdd:cd03244 135 EGGENLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDS-DRILVLDK 212
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
12-215 |
1.79e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 76.33 E-value: 1.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 12 FRYGSKGPNIIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGSLkTFPSHSAGKQTHS----MIGWVPQhfS 87
Cdd:PRK13648 15 FQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEI-FYNNQAITDDNFEklrkHIGIVFQ--N 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 88 YDPCFPIS-VKDVVLSGRLSQLSWHGKYKKKdfeaVDHALDLVGLSDHHHHCFAHLSGGQIQRVLLARALASYPEILILD 166
Cdd:PRK13648 92 PDNQFVGSiVKYDVAFGLENHAVPYDEMHRR----VSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILD 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 499185640 167 EPTTNIDPDNQQRILSILKKLNRT--CTILMVTHDLHHTTNYfNKVFYMNK 215
Cdd:PRK13648 168 EATSMLDPDARQNLLDLVRKVKSEhnITIISITHDLSEAMEA-DHVIVMNK 217
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
7-200 |
1.81e-16 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 76.26 E-value: 1.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 7 AEGLAFRYGSKG-------PNIIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGS----------LKTfPSH 69
Cdd:PRK10419 6 VSGLSHHYAHGGlsgkhqhQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNvswrgeplakLNR-AQR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 70 SAGKQTHSM-----IGWV-PQHfsydpcfpiSVKDVvLSGRLSQLSwhgKYKKKDFEA-VDHALDLVGLSDHH-HHCFAH 141
Cdd:PRK10419 85 KAFRRDIQMvfqdsISAVnPRK---------TVREI-IREPLRHLL---SLDKAERLArASEMLRAVDLDDSVlDKRPPQ 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499185640 142 LSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKLNRTCTI--LMVTHDL 200
Cdd:PRK10419 152 LSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTacLFITHDL 212
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1-215 |
1.84e-16 |
|
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: 75.84 E-value: 1.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 1 MTIRIlaEGLAFRYGSKgpNIIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGSLkTFPSHSAGKQT--HSM 78
Cdd:cd03296 1 MSIEV--RNVSKRFGDF--VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTI-LFGGEDATDVPvqERN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 79 IGWVPQHFSYdpcFP-ISVKDVVLSGRLSQLSWHGKYKKKDFEAVDHALDLVGLSDHHHHCFAHLSGGQIQRVLLARALA 157
Cdd:cd03296 76 VGFVFQHYAL---FRhMTVFDNVAFGLRVKPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 158 SYPEILILDEPTTNIDPDNQQRILSILKKLNRTC--TILMVTHDLHHTTNYFNKVFYMNK 215
Cdd:cd03296 153 VEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELhvTTVFVTHDQEEALEVADRVVVMNK 212
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
45-206 |
3.40e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 77.19 E-value: 3.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 45 KSTLTMLILGLLtPTFGSLK---TFPSHSAGKQTHSMIGWVPQhfsyDP-CFPISVKDVVLSGRlSQLSwhgkykkkDfE 120
Cdd:PRK11174 389 KTSLLNALLGFL-PYQGSLKingIELRELDPESWRKHLSWVGQ----NPqLPHGTLRDNVLLGN-PDAS--------D-E 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 121 AVDHALDLVGLSD---HHHHCFAH--------LSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKLNR 189
Cdd:PRK11174 454 QLQQALENAWVSEflpLLPQGLDTpigdqaagLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASR 533
|
170
....*....|....*..
gi 499185640 190 TCTILMVTHDLHHTTNY 206
Cdd:PRK11174 534 RQTTLMVTHQLEDLAQW 550
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
2-199 |
4.96e-16 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 75.88 E-value: 4.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 2 TIRIlaEGLAFRYGSKgpNIIHDVSFSVYDGDFigiigpngggKSTLTMLILGLLTPTFGSLktfpsHSAGKQTHSM--- 78
Cdd:COG3839 3 SLEL--ENVSKSYGGV--EALKDIDLDIEDGEFlvllgpsgcgKSTLLRMIAGLEDPTSGEI-----LIGGRDVTDLppk 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 79 ---IGWVPQhfSYDpCFP-ISVKDVVLSG-RLSqlswhgKYKKKDFEA-VDHALDLVGLSDHHHHCFAHLSGGQIQRVLL 152
Cdd:COG3839 74 drnIAMVFQ--SYA-LYPhMTVYENIAFPlKLR------KVPKAEIDRrVREAAELLGLEDLLDRKPKQLSGGQRQRVAL 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 499185640 153 ARALASYPEILILDEPTTNIDPD--NQQRILsiLKKLNRT--CTILMVTHD 199
Cdd:COG3839 145 GRALVREPKVFLLDEPLSNLDAKlrVEMRAE--IKRLHRRlgTTTIYVTHD 193
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
10-213 |
6.76e-16 |
|
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: 73.12 E-value: 6.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 10 LAFRYGSKGPNIIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGS--LKTFPSHSAGKQTHSMIGWVPQhfs 87
Cdd:cd03247 6 VSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEitLDGVPVSDLEKALSSLISVLNQ--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 88 ydpcfpisvKDVVLSGRLsqlswhgkykkkdfeavdhaLDLVGlsdhhhhcfAHLSGGQIQRVLLARALASYPEILILDE 167
Cdd:cd03247 83 ---------RPYLFDTTL--------------------RNNLG---------RRFSGGERQRLALARILLQDAPIVLLDE 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 499185640 168 PTTNIDPDNQQRILSILKKLNRTCTILMVTHDLhHTTNYFNKVFYM 213
Cdd:cd03247 125 PTVGLDPITERQLLSLIFEVLKDKTLIWITHHL-TGIEHMDKILFL 169
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
10-200 |
8.04e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 74.84 E-value: 8.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 10 LAFRYGSKGPNIIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTP--TFGSLKTFPSHSAGKQT----HSMIGWVP 83
Cdd:PRK13640 11 VSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddNPNSKITVDGITLTAKTvwdiREKVGIVF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 84 QHfsYDPCF-PISVKDVVLSGrlsqLSWHGKYKKKDFEAVDHALDLVGLSDHHHHCFAHLSGGQIQRVLLARALASYPEI 162
Cdd:PRK13640 91 QN--PDNQFvGATVGDDVAFG----LENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKI 164
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 499185640 163 LILDEPTTNIDPDNQQRILSILKKL--NRTCTILMVTHDL 200
Cdd:PRK13640 165 IILDESTSMLDPAGKEQILKLIRKLkkKNNLTVISITHDI 204
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
45-200 |
8.64e-16 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 75.15 E-value: 8.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 45 KSTLTMLILGLLTPTFGSLK------TFPSHSAGKQTHSMIGWVPQ--HFSYDPCFpiSVKDVVLSGrlsqLSWHGKYKK 116
Cdd:COG4608 57 KSTLGRLLLRLEEPTSGEILfdgqdiTGLSGRELRPLRRRMQMVFQdpYASLNPRM--TVGDIIAEP----LRIHGLASK 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 117 KDFEA-VDHALDLVGLSDHHHHCFAH-LSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKLNRT--CT 192
Cdd:COG4608 131 AERRErVAELLELVGLRPEHADRYPHeFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDElgLT 210
|
....*...
gi 499185640 193 ILMVTHDL 200
Cdd:COG4608 211 YLFISHDL 218
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
92-216 |
8.80e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 74.30 E-value: 8.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 92 FPISVKDVVLSGrLSQLSWHGKYKKKDF-EAVDHALDLVGLSDHHHHCFA-HLSGGQIQRVLLARALASYPEILILDEPT 169
Cdd:PRK14258 100 FPMSVYDNVAYG-VKIVGWRPKLEIDDIvESALKDADLWDEIKHKIHKSAlDLSGGQQQRLCIARALAVKPKVLLMDEPC 178
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 499185640 170 TNIDPDNQQRILSILK--KLNRTCTILMVTHDLHHTTNY--FNKVFYMNKT 216
Cdd:PRK14258 179 FGLDPIASMKVESLIQslRLRSELTMVIVSHNLHQVSRLsdFTAFFKGNEN 229
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
5-206 |
9.53e-16 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 73.96 E-value: 9.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 5 ILAEGLAFRYGSKgpNIIHDVSFSVYD------------GdfigiigpngggKSTLTMLILGLLTPTFGS-------LKT 65
Cdd:COG4604 2 IEIKNVSKRYGGK--VVLDDVSLTIPKggitaligpngaG------------KSTLLSMISRLLPPDSGEvlvdgldVAT 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 66 FPSH------SAGKQTHsmigwvpqHFSydpcFPISVKDVVLSGRL--SQlswhGKYKKKDFEAVDHALDLVGLSDhhhh 137
Cdd:COG4604 68 TPSRelakrlAILRQEN--------HIN----SRLTVRELVAFGRFpySK----GRLTAEDREIIDEAIAYLDLED---- 127
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499185640 138 cFAH-----LSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKL----NRtcTILMVTHDLHHTTNY 206
Cdd:COG4604 128 -LADryldeLSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLadelGK--TVVIVLHDINFASCY 202
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
100-202 |
1.16e-15 |
|
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: 72.08 E-value: 1.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 100 VLSGRLS----QLSWHGKykKKDFEAVDHALDLvGLSdhhhhCFAHLSGGQIQRVLLARALASYPEILILDEPTTNIDPD 175
Cdd:cd03216 45 ILSGLYKpdsgEILVDGK--EVSFASPRDARRA-GIA-----MVYQLSVGERQMVEIARALARNARLLILDEPTAALTPA 116
|
90 100
....*....|....*....|....*...
gi 499185640 176 NQQRILSILKKL-NRTCTILMVTHDLHH 202
Cdd:cd03216 117 EVERLFKVIRRLrAQGVAVIFISHRLDE 144
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
22-215 |
1.18e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 74.43 E-value: 1.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 22 IHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGSL---------KTFPSHSagKQTHSMIGWVPQhFSYDPCF 92
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVtvdditithKTKDKYI--RPVRKRIGMVFQ-FPESQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 93 PISVKDVVLSGRlsqlswhgKYKKKDFEAV-DHALDLV---GLS-DHHHHCFAHLSGGQIQRVLLARALASYPEILILDE 167
Cdd:PRK13646 100 EDTVEREIIFGP--------KNFKMNLDEVkNYAHRLLmdlGFSrDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 499185640 168 PTTNIDPDNQQRILSILKKL--NRTCTILMVTHDLHHTTNYFNKVFYMNK 215
Cdd:PRK13646 172 PTAGLDPQSKRQVMRLLKSLqtDENKTIILVSHDMNEVARYADEVIVMKE 221
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
139-215 |
1.42e-15 |
|
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: 71.33 E-value: 1.42e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499185640 139 FAHLSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKLNRtcTILMVTHDLHHTTNYFNKVFYMNK 215
Cdd:cd03221 68 FEQLSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPG--TVILVSHDRYFLDQVATKIIELED 142
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
24-215 |
2.03e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 73.71 E-value: 2.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 24 DVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGSLKTFPSH-------SAGKQTHSMIGWVPQhFSYDPCFPISV 96
Cdd:PRK13641 25 NISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHitpetgnKNLKKLRKKVSLVFQ-FPEAQLFENTV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 97 KDVVLSGRLSqlswHGKYKKKDFEAVDHALDLVGLSDH--HHHCFaHLSGGQIQRVLLARALASYPEILILDEPTTNIDP 174
Cdd:PRK13641 104 LKDVEFGPKN----FGFSEDEAKEKALKWLKKVGLSEDliSKSPF-ELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDP 178
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 499185640 175 DNQQRILSILKKLNRTC-TILMVTHDLHHTTNYFNKVFYMNK 215
Cdd:PRK13641 179 EGRKEMMQLFKDYQKAGhTVILVTHNMDDVAEYADDVLVLEH 220
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
45-198 |
2.11e-15 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 72.53 E-value: 2.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 45 KSTLTMLILGLLTPTFGSLK------TFPSHSAgkQTHSMIgwvpqhFSYDPCFP-ISVKDVVLSGRLSQLswhgKYKKK 117
Cdd:cd03298 37 KSTLLNLIAGFETPQSGRVLingvdvTAAPPAD--RPVSML------FQENNLFAhLTVEQNVGLGLSPGL----KLTAE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 118 DFEAVDHALDLVGLSDHHHHCFAHLSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKL--NRTCTILM 195
Cdd:cd03298 105 DRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLhaETKMTVLM 184
|
...
gi 499185640 196 VTH 198
Cdd:cd03298 185 VTH 187
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
8-215 |
2.26e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 73.61 E-value: 2.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 8 EGLAFRYGSKGP---NIIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGSLKT----FPSHSAGKQTHSM-- 78
Cdd:PRK13643 5 EKVNYTYQPNSPfasRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVgdivVSSTSKQKEIKPVrk 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 79 -IGWVPQhFSYDPCFPISV-KDVVLSGRLSQLSwhgkyKKKDFEAVDHALDLVGLSDHH-HHCFAHLSGGQIQRVLLARA 155
Cdd:PRK13643 85 kVGVVFQ-FPESQLFEETVlKDVAFGPQNFGIP-----KEKAEKIAAEKLEMVGLADEFwEKSPFELSGGQMRRVAIAGI 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499185640 156 LASYPEILILDEPTTNIDPDNQQRILSILKKLNRTC-TILMVTHDLHHTTNYFNKVFYMNK 215
Cdd:PRK13643 159 LAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGqTVVLVTHLMDDVADYADYVYLLEK 219
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
4-215 |
2.61e-15 |
|
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: 72.06 E-value: 2.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 4 RILAEGLAFRYGSKGPNIIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGSLK-------TFPSHsagkQTH 76
Cdd:cd03369 6 EIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEidgidisTIPLE----DLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 77 SMIGWVPQhfsyDPcfpisvkdVVLSGRL-SQLSWHGKYKKKDFEAvdhALDLVGLSDhhhhcfaHLSGGQIQRVLLARA 155
Cdd:cd03369 82 SSLTIIPQ----DP--------TLFSGTIrSNLDPFDEYSDEEIYG---ALRVSEGGL-------NLSQGQRQLLCLARA 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 156 LASYPEILILDEPTTNIDPDNQQRILSILKKLNRTCTILMVTHDLHHTTNYfNKVFYMNK 215
Cdd:cd03369 140 LLKRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDY-DKILVMDA 198
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
4-199 |
2.77e-15 |
|
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: 74.40 E-value: 2.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 4 RILAEGLAFRY-GSKGPnIIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGS-------LKTFPSHSAGKqt 75
Cdd:COG4618 330 RLSVENLTVVPpGSKRP-ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSvrldgadLSQWDREELGR-- 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 76 hsMIGWVPQhfsyDP-CFPISVKDVVlsGRLSQLswhgkykkkDFEAVDHALDLVGlsdhhhhcfAH------------- 141
Cdd:COG4618 407 --HIGYLPQ----DVeLFDGTIAENI--ARFGDA---------DPEKVVAAAKLAG---------VHemilrlpdgydtr 460
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499185640 142 -------LSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQ---RILSILKKlnRTCTILMVTHD 199
Cdd:COG4618 461 igeggarLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAalaAAIRALKA--RGATVVVITHR 526
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
7-202 |
4.30e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 72.83 E-value: 4.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 7 AEGLAFRYGSKgpNIIHDVSFSVYD------------GdfigiigpngggKSTlTM-LILGLLTPTFGSLkTFPSHSAGK 73
Cdd:COG4152 4 LKGLTKRFGDK--TAVDDVSFTVPKgeifgllgpngaG------------KTT-TIrIILGILAPDSGEV-LWDGEPLDP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 74 QTHSMIGWVPQHFSYDPcfPISVKDVVLsgRLSQLswHGKYKKKDFEAVDHALDLVGLSDHHHHCFAHLSGGQIQRVLLA 153
Cdd:COG4152 68 EDRRRIGYLPEERGLYP--KMKVGEQLV--YLARL--KGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLI 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 499185640 154 RALASYPEILILDEPTTNIDPDNQQRILSILKKLNRT-CTILMVTHDLHH 202
Cdd:COG4152 142 AALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKgTTVIFSSHQMEL 191
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
8-202 |
4.87e-15 |
|
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: 71.70 E-value: 4.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 8 EGLAFRYGskGPNIIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGSLKTFPSHSAGKQTHSM----IGWVP 83
Cdd:cd03224 4 ENLNAGYG--KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERaragIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 84 QHfsyDPCFP-ISVKDVVLSGrlsqlsWHGKYKKKDFEAVDHALDLV-GLSDHHHHCFAHLSGGQIQRVLLARALASYPE 161
Cdd:cd03224 82 EG---RRIFPeLTVEENLLLG------AYARRRAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPK 152
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 499185640 162 ILILDEPTTNIDPDNQQRILSILKKLNRT-CTILMVTHDLHH 202
Cdd:cd03224 153 LLLLDEPSEGLAPKIVEEIFEAIRELRDEgVTILLVEQNARF 194
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
126-215 |
5.25e-15 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 72.31 E-value: 5.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 126 LDLVGLSDHHHHCF-AHLSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKL-NRTCTILMVTHDLHHT 203
Cdd:PRK10619 136 LAKVGIDERAQGKYpVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLaEEGKTMVVVTHEMGFA 215
|
90
....*....|..
gi 499185640 204 TNYFNKVFYMNK 215
Cdd:PRK10619 216 RHVSSHVIFLHQ 227
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
120-198 |
5.34e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 72.43 E-value: 5.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 120 EAVDHALDLVGLSDHHHHCFAHLSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKLNRT--CTILMVT 197
Cdd:PRK13633 123 ERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKygITIILIT 202
|
.
gi 499185640 198 H 198
Cdd:PRK13633 203 H 203
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
140-198 |
6.20e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 71.80 E-value: 6.20e-15
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 499185640 140 AHLSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKLNRTCTILMVTH 198
Cdd:PRK14267 148 SNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTH 206
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
45-200 |
6.22e-15 |
|
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: 72.83 E-value: 6.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 45 KSTLTMLILGLLTPTFGSL------------KTF-PSHsagkQTHsmIGWVPQhfsyDPC-FP-ISVKDVVLSGRlsqls 109
Cdd:COG4148 38 KTTLLRAIAGLERPDSGRIrlggevlqdsarGIFlPPH----RRR--IGYVFQ----EARlFPhLSVRGNLLYGR----- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 110 WHGKyKKKDFEAVDHALDLVGLSDHHHHCFAHLSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKLNR 189
Cdd:COG4148 103 KRAP-RAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILPYLERLRD 181
|
170
....*....|...
gi 499185640 190 TCTI--LMVTHDL 200
Cdd:COG4148 182 ELDIpiLYVSHSL 194
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
45-200 |
6.71e-15 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 71.54 E-value: 6.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 45 KSTLTMLILGLLTPTFGSL--------KTFPShsagKQTHSMIgwvpqhFSYDPCFP-ISVKDVVLSGRLSQLSWHGKYK 115
Cdd:PRK10771 38 KSTLLNLIAGFLTPASGSLtlngqdhtTTPPS----RRPVSML------FQENNLFShLTVAQNIGLGLNPGLKLNAAQR 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 116 KKdfeaVDHALDLVGLSDHHHHCFAHLSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKL--NRTCTI 193
Cdd:PRK10771 108 EK----LHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVcqERQLTL 183
|
....*..
gi 499185640 194 LMVTHDL 200
Cdd:PRK10771 184 LMVSHSL 190
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
45-200 |
6.75e-15 |
|
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: 71.17 E-value: 6.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 45 KSTLTMLILGLLTPTFGSLK-------------TFPSHSAGkqthsmIGWVPQHFSYdpcFP-ISVKDVVLSGrlsqLSW 110
Cdd:cd03297 36 KSTLLRCIAGLEKPDGGTIVlngtvlfdsrkkiNLPPQQRK------IGLVFQQYAL---FPhLNVRENLAFG----LKR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 111 HGKYKKKDFeaVDHALDLVGLSDHHHHCFAHLSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRIL----SILKK 186
Cdd:cd03297 103 KRNREDRIS--VDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLpelkQIKKN 180
|
170
....*....|....
gi 499185640 187 LNRTCtiLMVTHDL 200
Cdd:cd03297 181 LNIPV--IFVTHDL 192
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
7-203 |
6.78e-15 |
|
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: 71.42 E-value: 6.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 7 AEGLAFRYGSKgpNIIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGS-------LKTFPSHsagKQTHSMI 79
Cdd:cd03218 3 AENLSKRYGKR--KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKilldgqdITKLPMH---KRARLGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 80 GWVPQHFSydpcfpISVKDVVLSGRLSQLSWHGKYKKKDFEAVDHALDLVGLSDHHHHCFAHLSGGQIQRVLLARALASY 159
Cdd:cd03218 78 GYLPQEAS------IFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATN 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 499185640 160 PEILILDEPTTNIDPDNQQRILSILKKL-NRTCTILMVTHDLHHT 203
Cdd:cd03218 152 PKFLLLDEPFAGVDPIAVQDIQKIIKILkDRGIGVLITDHNVRET 196
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
120-201 |
7.16e-15 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 73.20 E-value: 7.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 120 EAVDHALDLVGLSDHHHHCF-AHLSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKLNRTCTI--LMV 196
Cdd:PRK15134 403 QQVIAVMEEVGLDPETRHRYpAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLayLFI 482
|
....*
gi 499185640 197 THDLH 201
Cdd:PRK15134 483 SHDLH 487
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
92-200 |
7.26e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 72.05 E-value: 7.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 92 FPISVKDVVLSGrlsqLSWHGKYKKKDFEAVDHA-LDLVGLSDHHHHCFA----HLSGGQIQRVLLARALASYPEILILD 166
Cdd:PRK14271 113 FPMSIMDNVLAG----VRAHKLVPRKEFRGVAQArLTEVGLWDAVKDRLSdspfRLSGGQQQLLCLARTLAVNPEVLLLD 188
|
90 100 110
....*....|....*....|....*....|....
gi 499185640 167 EPTTNIDPDNQQRILSILKKLNRTCTILMVTHDL 200
Cdd:PRK14271 189 EPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNL 222
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
7-198 |
7.60e-15 |
|
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: 70.47 E-value: 7.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 7 AEGLAFRYGskGPNIIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGSLKTFPSHSAGKQTHSmigwvPQHF 86
Cdd:TIGR01189 3 ARNLACSRG--ERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEP-----HENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 87 SYdpcfpISVKDVvLSGRLS---QLSWHGKYKKKDFEAVDHALDLVGLSDHHHHCFAHLSGGQIQRVLLARALASYPEIL 163
Cdd:TIGR01189 76 LY-----LGHLPG-LKPELSaleNLHFWAAIHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLW 149
|
170 180 190
....*....|....*....|....*....|....*.
gi 499185640 164 ILDEPTTNIDPDNQQRILSILKK-LNRTCTILMVTH 198
Cdd:TIGR01189 150 ILDEPTTALDKAGVALLAGLLRAhLARGGIVLLTTH 185
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
45-198 |
8.46e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 70.67 E-value: 8.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 45 KSTLTMLILGLLTPTFGSLK------TFPSHSAgkQTHsMIGwvpqHfsYDPCFP-ISVKDvvlsgrlsQLSWHGKYKKK 117
Cdd:PRK13539 41 KTTLLRLIAGLLPPAAGTIKldggdiDDPDVAE--ACH-YLG----H--RNAMKPaLTVAE--------NLEFWAAFLGG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 118 DFEAVDHALDLVGLSDHHHHCFAHLSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILS-ILKKLNRTCTILMV 196
Cdd:PRK13539 104 EELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAElIRAHLAQGGIVIAA 183
|
..
gi 499185640 197 TH 198
Cdd:PRK13539 184 TH 185
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
8-200 |
9.24e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 71.66 E-value: 9.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 8 EGLAFRYGSKGP-NIIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGSLKTFPSHSAGKQTHSM---IGWVP 83
Cdd:PRK13642 8 ENLVFKYEKESDvNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLrrkIGMVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 84 QHFSyDPCFPISVKDVVLSGRLSQlswhGKYKKKDFEAVDHALDLVGLSDHHHHCFAHLSGGQIQRVLLARALASYPEIL 163
Cdd:PRK13642 88 QNPD-NQFVGATVEDDVAFGMENQ----GIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEII 162
|
170 180 190
....*....|....*....|....*....|....*....
gi 499185640 164 ILDEPTTNIDPDNQQRILSILKKLNRT--CTILMVTHDL 200
Cdd:PRK13642 163 ILDESTSMLDPTGRQEIMRVIHEIKEKyqLTVLSITHDL 201
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
45-199 |
9.62e-15 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 72.14 E-value: 9.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 45 KSTLTMLILGLLTPTFGSLK-------TFPSHSAGkqthsmIGWVPQHFSYdpcFP-ISVKDVVLSGrlsqLSWHGKYKK 116
Cdd:TIGR01187 9 KTTLLRLLAGFEQPDSGSIMldgedvtNVPPHLRH------INMVFQSYAL---FPhMTVEENVAFG----LKMRKVPRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 117 KDFEAVDHALDLVGLSDHHHHCFAHLSGGQIQRVLLARALASYPEILILDEPTTNIDPD----NQQRILSILKKLNRTCt 192
Cdd:TIGR01187 76 EIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKlrdqMQLELKTIQEQLGITF- 154
|
....*..
gi 499185640 193 iLMVTHD 199
Cdd:TIGR01187 155 -VFVTHD 160
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
94-206 |
1.49e-14 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 70.97 E-value: 1.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 94 ISVKDVVLSGRLSqlsWHG---KYKKKDFEAVDHALDLVGLSDHHHHCFAHLSGGQIQRVLLARALASYPEILILDEPTT 170
Cdd:PRK10575 100 MTVRELVAIGRYP---WHGalgRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTS 176
|
90 100 110
....*....|....*....|....*....|....*...
gi 499185640 171 NIDPDNQQRILSILKKLN--RTCTILMVTHDLHHTTNY 206
Cdd:PRK10575 177 ALDIAHQVDVLALVHRLSqeRGLTVIAVLHDINMAARY 214
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
8-200 |
1.56e-14 |
|
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: 70.34 E-value: 1.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 8 EGLAFRYGSKGPNIIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGS-------LKTFPSHSAGKQthsmIG 80
Cdd:cd03251 4 KNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRilidghdVRDYTLASLRRQ----IG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 81 WVPQhfsyDP-CFPISVKDVVLSGRLSQlswhgkykkkDFEAVDHALDLVglsdhHHHCF----------------AHLS 143
Cdd:cd03251 80 LVSQ----DVfLFNDTVAENIAYGRPGA----------TREEVEEAARAA-----NAHEFimelpegydtvigergVKLS 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499185640 144 GGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKLNRTCTILMVTHDL 200
Cdd:cd03251 141 GGQRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRL 197
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
122-200 |
2.05e-14 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 69.90 E-value: 2.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 122 VDHALDLVGLSDHHHHCFAHLSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKLNRT-CTILMVTHDL 200
Cdd:PRK10908 118 VSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRVgVTVLMATHDI 197
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
120-201 |
2.08e-14 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 72.02 E-value: 2.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 120 EAVDHALDLVGLSDHHHHCFAH-LSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKLNRT--CTILMV 196
Cdd:COG4172 403 ARVAEALEEVGLDPAARHRYPHeFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREhgLAYLFI 482
|
....*
gi 499185640 197 THDLH 201
Cdd:COG4172 483 SHDLA 487
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
129-235 |
2.41e-14 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 71.09 E-value: 2.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 129 VGLSDHHH--HCFAH-LSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKLNRT--CTILMVTHDLHHT 203
Cdd:COG4170 143 VGIKDHKDimNSYPHeLTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLqgTSILLISHDLESI 222
|
90 100 110
....*....|....*....|....*....|....
gi 499185640 204 TNYFNK--VFYMNKTLTSLADTSTLTDQFccHPY 235
Cdd:COG4170 223 SQWADTitVLYCGQTVESGPTEQILKSPH--HPY 254
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
126-235 |
2.41e-14 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 70.99 E-value: 2.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 126 LDLVGLSDHHH--HCFAH-LSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKLNR--TCTILMVTHDL 200
Cdd:PRK15093 140 LHRVGIKDHKDamRSFPYeLTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnnNTTILLISHDL 219
|
90 100 110
....*....|....*....|....*....|....*..
gi 499185640 201 HHTTNYFNK--VFYMNKTLTSLADTSTLTDQFccHPY 235
Cdd:PRK15093 220 QMLSQWADKinVLYCGQTVETAPSKELVTTPH--HPY 254
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
26-200 |
7.37e-14 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 68.35 E-value: 7.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 26 SFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGSLK--------TFPShsagKQTHSMIgwvpqhFSYDPCFP-ISV 96
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKvndqshtgLAPY----QRPVSML------FQENNLFAhLTV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 97 KDVVLSGRLSQLSWHGKYKKKdfeaVDHALDLVGLSDHHHHCFAHLSGGQIQRVLLARALASYPEILILDEPTTNIDPDN 176
Cdd:TIGR01277 88 RQNIGLGLHPGLKLNAEQQEK----VVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLL 163
|
170 180
....*....|....*....|....*.
gi 499185640 177 QQRILSILKKL--NRTCTILMVTHDL 200
Cdd:TIGR01277 164 REEMLALVKQLcsERQRTLLMVTHHL 189
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
142-218 |
9.49e-14 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 68.66 E-value: 9.49e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499185640 142 LSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKLNRTCTILMVTHDLHHTTNYFNKVFYMNKTLT 218
Cdd:PRK14243 152 LSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTAFFNVELT 228
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
22-201 |
9.83e-14 |
|
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: 68.13 E-value: 9.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 22 IHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGSLktfpshsagkqthSMIGWVPqhFSYDPCFpisVKDV-V 100
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEV-------------RVAGLVP--WKRRKKF---LRRIgV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 101 LSGRLSQLSW-----------HGKYKKKDFEA---VDHALDLVGLSDHHHHCFAHLSGGQIQRVLLARALASYPEILILD 166
Cdd:cd03267 99 VFGQKTQLWWdlpvidsfyllAAIYDLPPARFkkrLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLD 178
|
170 180 190
....*....|....*....|....*....|....*..
gi 499185640 167 EPTTNIDPDNQQRILSILKKLN--RTCTILMVTHDLH 201
Cdd:cd03267 179 EPTIGLDVVAQENIRNFLKEYNreRGTTVLLTSHYMK 215
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
18-215 |
1.27e-13 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 69.48 E-value: 1.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 18 GPNIIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGS-------LKTFPSHsagKQTHSMIgwvpqhFSYDP 90
Cdd:PRK11607 31 GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQimldgvdLSHVPPY---QRPINMM------FQSYA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 91 CFP-ISVKDVVLSGrLSQlswhGKYKKKDFEA-VDHALDLVGLSDHHHHCFAHLSGGQIQRVLLARALASYPEILILDEP 168
Cdd:PRK11607 102 LFPhMTVEQNIAFG-LKQ----DKLPKAEIASrVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEP 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 499185640 169 TTNIDPDNQQR----ILSILKKLNRTCtiLMVTHDLHHTTNYFNKVFYMNK 215
Cdd:PRK11607 177 MGALDKKLRDRmqleVVDILERVGVTC--VMVTHDQEEAMTMAGRIAIMNR 225
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
7-200 |
1.49e-13 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 68.19 E-value: 1.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 7 AEGLAFRYGskGPNIIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGSLK------TFPSHSAGK--QTHSM 78
Cdd:PRK11248 4 ISHLYADYG--GKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITldgkpvEGPGAERGVvfQNEGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 79 IGWVpqhfsydpcfpiSVKDVVLSGrlsqLSWHGKYKKKDFEAVDHALDLVGLSDHHHHCFAHLSGGQIQRVLLARALAS 158
Cdd:PRK11248 82 LPWR------------NVQDNVAFG----LQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAA 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 499185640 159 YPEILILDEPTTNIDPDNQQRILSILKKL-NRTCT-ILMVTHDL 200
Cdd:PRK11248 146 NPQLLLLDEPFGALDAFTREQMQTLLLKLwQETGKqVLLITHDI 189
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
120-203 |
1.53e-13 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 69.45 E-value: 1.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 120 EAVDHALDLVGLSDHHHHCFAH------LSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKLNRTCTI 193
Cdd:COG4178 458 AELREALEAVGLGHLAERLDEEadwdqvLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTV 537
|
90
....*....|....
gi 499185640 194 LMVTH----DLHHT 203
Cdd:COG4178 538 ISVGHrstlAAFHD 551
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
90-199 |
1.88e-13 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 67.93 E-value: 1.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 90 PCFPISVKDVVLSGRLSQLSWHGKYKKKDFEAVDHALDLVGLSDHHHHCFAHLSGGQIQRVLLARALA---------SYP 160
Cdd:PRK13547 94 PAFAFSAREIVLLGRYPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAqlwpphdaaQPP 173
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 499185640 161 EILILDEPTTNIDPDNQQRILSILKKLNRTCTI--LMVTHD 199
Cdd:PRK13547 174 RYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLgvLAIVHD 214
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
8-215 |
1.94e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 67.95 E-value: 1.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 8 EGLAFRYgSKGPNIIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGSL----KTFPSHSAG----KQTHSMI 79
Cdd:PRK13636 9 EELNYNY-SDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRIlfdgKPIDYSRKGlmklRESVGMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 80 GWVPQHfsydPCFPISVKDVVLSGRLSQlswhGKYKKKDFEAVDHALDLVGLSDHHH---HCfahLSGGQIQRVLLARAL 156
Cdd:PRK13636 88 FQDPDN----QLFSASVYQDVSFGAVNL----KLPEDEVRKRVDNALKRTGIEHLKDkptHC---LSFGQKKRVAIAGVL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499185640 157 ASYPEILILDEPTTNIDPDNQQRILSILKKLNRT--CTILMVTHDLHHTTNYFNKVFYMNK 215
Cdd:PRK13636 157 VMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElgLTIIIATHDIDIVPLYCDNVFVMKE 217
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
122-200 |
2.62e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 67.70 E-value: 2.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 122 VDHALDLVGLSDHHHHCFAHLSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKLNRTC-TILMVTHDL 200
Cdd:PRK13644 117 VDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGkTIVYITHNL 196
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
126-200 |
3.50e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 68.19 E-value: 3.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 126 LDLVG-------LSDHHHHcfahLSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKLNR--TCTILMV 196
Cdd:PRK15134 138 LDRVGirqaakrLTDYPHQ----LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFI 213
|
....
gi 499185640 197 THDL 200
Cdd:PRK15134 214 THNL 217
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
8-199 |
3.73e-13 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 66.66 E-value: 3.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 8 EGLAFRYGSKgpNIIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGSL-------KTFPSHSAGKQThsmig 80
Cdd:PRK10247 11 QNVGYLAGDA--KILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLlfegediSTLKPEIYRQQV----- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 81 wvpqhfSYdpCF--PISVKDVVLSGRLsqLSWHGKYKKKDFEAVDHALDLVGLSDHH-HHCFAHLSGGQIQRVLLARALA 157
Cdd:PRK10247 84 ------SY--CAqtPTLFGDTVYDNLI--FPWQIRNQQPDPAIFLDDLERFALPDTIlTKNIAELSGGEKQRISLIRNLQ 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 499185640 158 SYPEILILDEPTTNIDPDNQQRILSILKKLNR--TCTILMVTHD 199
Cdd:PRK10247 154 FMPKVLLLDEITSALDESNKHNVNEIIHRYVReqNIAVLWVTHD 197
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
17-215 |
4.11e-13 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 66.70 E-value: 4.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 17 KGPNIIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGSLKTF-----PSHSAGKQT------HSMIGWVPQH 85
Cdd:PRK11264 14 HGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGditidTARSLSQQKglirqlRQHVGFVFQN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 86 FSYdpcFP-ISVKDVVLSGRLSQlswhgKYKKKDfEAVDHALDL---VGLSDHHHHCFAHLSGGQIQRVLLARALASYPE 161
Cdd:PRK11264 94 FNL---FPhRTVLENIIEGPVIV-----KGEPKE-EATARARELlakVGLAGKETSYPRRLSGGQQQRVAIARALAMRPE 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499185640 162 ILILDEPTTNIDPDNQQRILSILKKL---NRTCTIlmVTHDLHHTTNYFNKVFYMNK 215
Cdd:PRK11264 165 VILFDEPTSALDPELVGEVLNTIRQLaqeKRTMVI--VTHEMSFARDVADRAIFMDQ 219
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
8-202 |
4.12e-13 |
|
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: 66.54 E-value: 4.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 8 EGLAFRYGSKgpNIIHDVSFSVYD------------GdfigiigpngggKSTLTMLILGLLTPTFGSLkTFpshsAGKQT 75
Cdd:COG0410 7 ENLHAGYGGI--HVLHGVSLEVEEgeivallgrngaG------------KTTLLKAISGLLPPRSGSI-RF----DGEDI 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 76 HSM---------IGWVPQHfsyDPCFP-ISVKDVVLSGRlsqlswhgkYKKKDFEAVDHALDLVG-----LSDHHHHCFA 140
Cdd:COG0410 68 TGLpphriarlgIGYVPEG---RRIFPsLTVEENLLLGA---------YARRDRAEVRADLERVYelfprLKERRRQRAG 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499185640 141 HLSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKLNRT-CTILMVTHDLHH 202
Cdd:COG0410 136 TLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREgVTILLVEQNARF 198
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
14-201 |
4.40e-13 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 66.39 E-value: 4.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 14 YGskGPNIIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGSL----KTFPSHSAGKQTHSMIGWVPQH---F 86
Cdd:TIGR03410 10 YG--QSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIrldgEDITKLPPHERARAGIAYVPQGreiF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 87 SYdpcfpISVKDVVLSGrlsqLSWHGKYKKKdfeAVDHALDL--VgLSDHHHHCFAHLSGGQIQRVLLARALASYPEILI 164
Cdd:TIGR03410 88 PR-----LTVEENLLTG----LAALPRRSRK---IPDEIYELfpV-LKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLL 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 499185640 165 LDEPTTNIDPDNQQRILSILKKLN--RTCTILMVTHDLH 201
Cdd:TIGR03410 155 LDEPTEGIQPSIIKDIGRVIRRLRaeGGMAILLVEQYLD 193
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
5-201 |
5.23e-13 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 65.85 E-value: 5.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 5 ILAEGLAFRYGSKGPNI--IHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGS--LKTFPSHSAGKQTHSMIG 80
Cdd:cd03266 2 ITADALTKRFRDVKKTVqaVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFatVDGFDVVKEPAEARRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 81 WVPQHFS-YDpcfPISVKDVVLS-GRLsqlswHGKYKKKDFEAVDHALDLVGLSDHHHHCFAHLSGGQIQRVLLARALAS 158
Cdd:cd03266 82 FVSDSTGlYD---RLTARENLEYfAGL-----YGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVH 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 499185640 159 YPEILILDEPTTNIDPDNQQRILSILKKLNRT-CTILMVTHDLH 201
Cdd:cd03266 154 DPPVLLLDEPTTGLDVMATRALREFIRQLRALgKCILFSTHIMQ 197
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
108-213 |
5.68e-13 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 67.06 E-value: 5.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 108 LSWHGKYKKKD-FEAVDHALDLVGLSDHHHHC--FAH-LSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSI 183
Cdd:PRK09473 124 LMLHKGMSKAEaFEESVRMLDAVKMPEARKRMkmYPHeFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTL 203
|
90 100 110
....*....|....*....|....*....|..
gi 499185640 184 LKKLNR--TCTILMVTHDLHHTTNYFNKVFYM 213
Cdd:PRK09473 204 LNELKRefNTAIIMITHDLGVVAGICDKVLVM 235
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
21-215 |
5.99e-13 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 67.42 E-value: 5.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 21 IIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGSLK---TFPSHSAGKQTHsmIGWVPQHFSYdpcFP-ISV 96
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRfhgTDVSRLHARDRK--VGFVFQHYAL---FRhMTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 97 KDVVLSGrLSQLSWHGK-----YKKKdfeaVDHALDLVGLSDHHHHCFAHLSGGQIQRVLLARALASYPEILILDEPTTN 171
Cdd:PRK10851 92 FDNIAFG-LTVLPRRERpnaaaIKAK----VTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 499185640 172 IDPDNQQRILSILKKLNRTC--TILMVTHDLHHTTNYFNKVFYMNK 215
Cdd:PRK10851 167 LDAQVRKELRRWLRQLHEELkfTSVFVTHDQEEAMEVADRVVVMSQ 212
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
124-200 |
6.11e-13 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 66.26 E-value: 6.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 124 HALDLVGLSDHHH----HCFaHLSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKL--NRTCTILMVT 197
Cdd:PRK10418 120 AALEAVGLENAARvlklYPF-EMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIvqKRALGMLLVT 198
|
...
gi 499185640 198 HDL 200
Cdd:PRK10418 199 HDM 201
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
25-198 |
6.96e-13 |
|
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: 65.21 E-value: 6.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 25 VSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFG--SLKTFPSHSAGKQTHSMIGWVPQHFSydpcfpisvkdvvLS 102
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGrvLLNGGPLDFQRDSIARGLLYLGHAPG-------------IK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 103 GRLSQLS----WHGKYkkkDFEAVDHALDLVGLSDHHHHCFAHLSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQ 178
Cdd:cd03231 86 TTLSVLEnlrfWHADH---SDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVA 162
|
170 180
....*....|....*....|.
gi 499185640 179 RILSILKK-LNRTCTILMVTH 198
Cdd:cd03231 163 RFAEAMAGhCARGGMVVLTTH 183
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
4-200 |
8.06e-13 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 67.44 E-value: 8.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 4 RILAEGLAFRYGsKGPNIIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFG-------SLKTFpSHSAGKQTH 76
Cdd:PRK10790 340 RIDIDNVSFAYR-DDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGeirldgrPLSSL-SHSVLRQGV 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 77 SMigwVPQhfsyDPC-FPISVKDVVLSGR-LSQlswhgkykkkdfEAVDHALDLV-------GLSDHHHHCFAH----LS 143
Cdd:PRK10790 418 AM---VQQ----DPVvLADTFLANVTLGRdISE------------EQVWQALETVqlaelarSLPDGLYTPLGEqgnnLS 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499185640 144 GGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKLNRTCTILMVTHDL 200
Cdd:PRK10790 479 VGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRL 535
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
22-210 |
8.67e-13 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 66.19 E-value: 8.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 22 IHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTfgslKTFPSH---------SAGK------QTHSMIGWVPQHF 86
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGD----KSAGSHiellgrtvqREGRlardirKSRANTGYIFQQF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 87 SYdpCFPISVKDVVLSGRLSQ-------LSWHGKYKKKdfEAVdHALDLVGLSDHHHHCFAHLSGGQIQRVLLARALASY 159
Cdd:PRK09984 96 NL--VNRLSVLENVLIGALGStpfwrtcFSWFTREQKQ--RAL-QALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQ 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499185640 160 PEILILDEPTTNIDPDNQQRILSILKKLNRT--CTILMVTHDLHHTTNYFNKV 210
Cdd:PRK09984 171 AKVILADEPIASLDPESARIVMDTLRDINQNdgITVVVTLHQVDYALRYCERI 223
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
21-198 |
1.21e-12 |
|
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: 64.49 E-value: 1.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 21 IIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTP--TFGSLKT--FPSHSagKQTHSMIGWVPQHFSYDPCFPIsv 96
Cdd:cd03213 24 LLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLIngRPLDK--RSFRKIIGYVPQDDILHPTLTV-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 97 kdvvlsgrlsqlswhgkykkkdFEAVDHALDLVGlsdhhhhcfahLSGGQIQRVLLARALASYPEILILDEPTTNIDPDN 176
Cdd:cd03213 100 ----------------------RETLMFAAKLRG-----------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSS 146
|
170 180
....*....|....*....|...
gi 499185640 177 QQRILSILKKLNRT-CTILMVTH 198
Cdd:cd03213 147 ALQVMSLLRRLADTgRTIICSIH 169
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
21-215 |
1.31e-12 |
|
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: 64.98 E-value: 1.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 21 IIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTP---TFGSLKTFPSHSAGKQTHSMIGWVPQHFSYDPCFpiSVK 97
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQPRKPDQFQKCVAYVRQDDILLPGL--TVR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 98 DVVLSGRLSQLSWHGKYKKKDFEAVDHALDLVGLSDHHHHCFAHLSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQ 177
Cdd:cd03234 100 ETLTYTAILRLPRKSSDAIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTA 179
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 499185640 178 QRILSILKKLNRT-CTILMVTH----DLHHTtnyFNKVFYMNK 215
Cdd:cd03234 180 LNLVSTLSQLARRnRIVILTIHqprsDLFRL---FDRILLLSS 219
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
120-199 |
1.66e-12 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 64.43 E-value: 1.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 120 EAVDHALDLVGLSDHHHHCFAHLSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKLNRTCTI--LMVT 197
Cdd:COG4136 112 ARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIpaLLVT 191
|
..
gi 499185640 198 HD 199
Cdd:COG4136 192 HD 193
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
8-214 |
2.12e-12 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 64.03 E-value: 2.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 8 EGLAFRYGSK---GPNIIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGSLktfpshsagkQTHSMIGWVPQ 84
Cdd:cd03250 4 EDASFTWDSGeqeTSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSV----------SVPGSIAYVSQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 85 hFSYdpCFPISVKDVVLSGrlSQLSwHGKYKK--------KDFEAVDHAlDLV-----GLSdhhhhcfahLSGGQIQRVL 151
Cdd:cd03250 74 -EPW--IQNGTIRENILFG--KPFD-EERYEKvikacalePDLEILPDG-DLTeigekGIN---------LSGGQKQRIS 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499185640 152 LARALASYPEILILDEPTTNIDPDNQQRILS--ILKKLNRTCTILMVTHDLHHTTnYFNKVFYMN 214
Cdd:cd03250 138 LARAVYSDADIYLLDDPLSAVDAHVGRHIFEncILGLLLNNKTRILVTHQLQLLP-HADQIVVLD 201
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
5-200 |
2.21e-12 |
|
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: 66.30 E-value: 2.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 5 ILAEGLAFRYGSkGPNIIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFG-------SLKTFPSHsagkQTHS 77
Cdd:TIGR01193 474 IVINDVSYSYGY-GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGeillngfSLKDIDRH----TLRQ 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 78 MIGWVPQhfsyDP-CFPISVKDVVLSGRLSQLSWHGKYK-------KKDFEAVDHALDlVGLSDHHhhcfAHLSGGQIQR 149
Cdd:TIGR01193 549 FINYLPQ----EPyIFSGSILENLLLGAKENVSQDEIWAaceiaeiKDDIENMPLGYQ-TELSEEG----SSISGGQKQR 619
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 499185640 150 VLLARALASYPEILILDEPTTNIDPDNQQRILSILKKLNRTcTILMVTHDL 200
Cdd:TIGR01193 620 IALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDK-TIIFVAHRL 669
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
140-200 |
2.77e-12 |
|
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: 63.22 E-value: 2.77e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499185640 140 AHLSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKLNRT-CTILMVTHDL 200
Cdd:cd03215 103 SLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADAgKAVLLISSEL 164
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
45-200 |
3.09e-12 |
|
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: 65.13 E-value: 3.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 45 KSTLTMLILGLLTPTFGSL----KTFPSHSAGKQT---HSMIGWVPQHFSYdpcFP-ISVKDVVLSGRLSQlswHGKYKK 116
Cdd:TIGR02142 36 KTTLIRLIAGLTRPDEGEIvlngRTLFDSRKGIFLppeKRRIGYVFQEARL---FPhLSVRGNLRYGMKRA---RPSERR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 117 KDFEAVdhaLDLVGLSDHHHHCFAHLSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKLNRTCTI--L 194
Cdd:TIGR02142 110 ISFERV---IELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLERLHAEFGIpiL 186
|
....*.
gi 499185640 195 MVTHDL 200
Cdd:TIGR02142 187 YVSHSL 192
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
44-215 |
4.69e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 64.05 E-value: 4.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 44 GKSTLTMLILGLLTPTFGS--LKTFPSHSAG-KQTHSMIGWVPQHfSYDPCFPISVKDVVLSGRLSQlswhgkykKKDFE 120
Cdd:PRK13652 42 GKSTLFRHFNGILKPTSGSvlIRGEPITKENiREVRKFVGLVFQN-PDDQIFSPTVEQDIAFGPINL--------GLDEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 121 AVDH----ALDLVGLSDHHHHCFAHLSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKLNRT--CTIL 194
Cdd:PRK13652 113 TVAHrvssALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETygMTVI 192
|
170 180
....*....|....*....|.
gi 499185640 195 MVTHDLHHTTNYFNKVFYMNK 215
Cdd:PRK13652 193 FSTHQLDLVPEMADYIYVMDK 213
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
108-199 |
7.50e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 63.53 E-value: 7.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 108 LSWHGKYKKKDFEA-VDHALDLVGL----SDHHHHCFAHLSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILS 182
Cdd:PRK14246 115 LKSHGIKEKREIKKiVEECLRKVGLwkevYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEK 194
|
90
....*....|....*..
gi 499185640 183 ILKKLNRTCTILMVTHD 199
Cdd:PRK14246 195 LITELKNEIAIVIVSHN 211
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
142-201 |
8.46e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 64.46 E-value: 8.46e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 142 LSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKLNRTCTILMVTHDLH 201
Cdd:PRK11160 476 LSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLT 535
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
9-199 |
9.99e-12 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 63.81 E-value: 9.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 9 GLAFRYGSKgpNIIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGSL---KTFPSHSAGKQTHsmIGWVPQH 85
Cdd:PRK09452 19 GISKSFDGK--EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRImldGQDITHVPAENRH--VNTVFQS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 86 FSYdpcFP-ISVKDVVLSGRLSQlswhgKYKKKDFEA-VDHALDLVGLSDHHHHCFAHLSGGQIQRVLLARALASYPEIL 163
Cdd:PRK09452 95 YAL---FPhMTVFENVAFGLRMQ-----KTPAAEITPrVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVL 166
|
170 180 190
....*....|....*....|....*....|....*...
gi 499185640 164 ILDEPTTNIDPDNQQRILSILKKLNRT--CTILMVTHD 199
Cdd:PRK09452 167 LLDESLSALDYKLRKQMQNELKALQRKlgITFVFVTHD 204
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
142-215 |
1.16e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 63.33 E-value: 1.16e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499185640 142 LSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSIL---KKLNRtcTILMVTHDLHHTTNYFNKVFYMNK 215
Cdd:PRK13631 177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLIldaKANNK--TVFVITHTMEHVLEVADEVIVMDK 251
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
45-215 |
1.21e-11 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 63.59 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 45 KSTLTMLILGLLTPTFGslKTF-----PSHSAGKQTHsmIGWVPQhfSYdPCFP-ISVKDVVLSGrlsqLSWHGKYKKKD 118
Cdd:PRK11432 45 KTTVLRLVAGLEKPTEG--QIFidgedVTHRSIQQRD--ICMVFQ--SY-ALFPhMSLGENVGYG----LKMLGVPKEER 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 119 FEAVDHALDLVGLSDHHHHCFAHLSGGQIQRVLLARALASYPEILILDEPTTNIDPdNQQR-----ILSILKKLNrtCTI 193
Cdd:PRK11432 114 KQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDA-NLRRsmrekIRELQQQFN--ITS 190
|
170 180
....*....|....*....|..
gi 499185640 194 LMVTHDLHHTTNYFNKVFYMNK 215
Cdd:PRK11432 191 LYVTHDQSEAFAVSDTVIVMNK 212
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
45-201 |
1.38e-11 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 63.51 E-value: 1.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 45 KSTLtMLIL-GLLTPTFGSLK------TFPS----HSAGkqthsmIGWVPQHFSYDPCFpiSVKD-VVLSgrlSQLSWHG 112
Cdd:COG3845 44 KSTL-MKILyGLYQPDSGEILidgkpvRIRSprdaIALG------IGMVHQHFMLVPNL--TVAEnIVLG---LEPTKGG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 113 KYKKKDFEAvdhalDLVGLSDHHHhcF--------AHLSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSIL 184
Cdd:COG3845 112 RLDRKAARA-----RIRELSERYG--LdvdpdakvEDLSVGEQQRVEILKALYRGARILILDEPTAVLTPQEADELFEIL 184
|
170
....*....|....*...
gi 499185640 185 KKLNRT-CTILMVTHDLH 201
Cdd:COG3845 185 RRLAAEgKSIIFITHKLR 202
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
143-200 |
1.53e-11 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 62.07 E-value: 1.53e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 499185640 143 SGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILS-ILKKLNRTCTILMVTHDL 200
Cdd:COG4778 154 SGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVElIEEAKARGTAIIGIFHDE 212
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
15-198 |
1.59e-11 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 63.52 E-value: 1.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 15 GSKGPnIIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGS-------LKTFPSHSAGKQthsmIGWVPQHFS 87
Cdd:TIGR01842 328 GGKKP-TLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSvrldgadLKQWDRETFGKH----IGYLPQDVE 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 88 YdpcFPISVKD-------------VVLSGRLSQ-----LSWHGKYkkkdfeavDHALDLVGlsdhhhhcfAHLSGGQIQR 149
Cdd:TIGR01842 403 L---FPGTVAEniarfgenadpekIIEAAKLAGvheliLRLPDGY--------DTVIGPGG---------ATLSGGQRQR 462
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 499185640 150 VLLARALASYPEILILDEPTTNIDPDNQQRILSILKKLN-RTCTILMVTH 198
Cdd:TIGR01842 463 IALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKaRGITVVVITH 512
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
142-215 |
1.70e-11 |
|
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: 61.86 E-value: 1.70e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499185640 142 LSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKLNRTCTILMVTHDLHHTTNYfNKVFYMNK 215
Cdd:cd03253 138 LSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNA-DKIIVLKD 210
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
21-199 |
2.10e-11 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 63.20 E-value: 2.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 21 IIHDVSFSVYDGDFIGIIGPNGGGKSTLtMLILGLL-TPTFGSLKTFPSHSAGKQTHSMIGWVPQHFSYdpcfpisvkdv 99
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTL-MNILGCLdKPTSGTYRVAGQDVATLDADALAQLRREHFGF----------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 100 vLSGR---LSQLS----------WHGKYKKKDFEAVDHALDLVGLSDHHHHCFAHLSGGQIQRVLLARALASYPEILILD 166
Cdd:PRK10535 91 -IFQRyhlLSHLTaaqnvevpavYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILAD 169
|
170 180 190
....*....|....*....|....*....|....
gi 499185640 167 EPTTNIDPDNQQRILSILKKLN-RTCTILMVTHD 199
Cdd:PRK10535 170 EPTGALDSHSGEEVMAILHQLRdRGHTVIIVTHD 203
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
7-199 |
3.23e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 62.39 E-value: 3.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 7 AEGLAFRYGSKgpNIIHDVSFSVYDGDfigiigpngggKSTLTMLILGLLTPTFGSLKTfpshsaGKQTHsmIGWVPQHF 86
Cdd:COG0488 318 LEGLSKSYGDK--TLLDDLSLRIDRGDrigligpngagKSTLLKLLAGELEPDSGTVKL------GETVK--IGYFDQHQ 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 87 SY-DPcfPISVKDVVlsgrlsqlsWHGKYKKKDFEAV----------DHALDLVGlsdhhhhcfaHLSGGQIQRVLLARA 155
Cdd:COG0488 388 EElDP--DKTVLDEL---------RDGAPGGTEQEVRgylgrflfsgDDAFKPVG----------VLSGGEKARLALAKL 446
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 499185640 156 LASYPEILILDEPTTNIDPDNQQRILSILKklNRTCTILMVTHD 199
Cdd:COG0488 447 LLSPPNVLLLDEPTNHLDIETLEALEEALD--DFPGTVLLVSHD 488
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
142-216 |
4.04e-11 |
|
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: 59.86 E-value: 4.04e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499185640 142 LSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKlnRTCTILMVTHDlHHTTNYFNKVFYMNKT 216
Cdd:cd03223 92 LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKE--LGITVISVGHR-PSLWKFHDRVLDLDGE 163
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
20-200 |
4.54e-11 |
|
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: 60.56 E-value: 4.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 20 NIIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGSL----KTFPSHSAgKQTHSMIGWVPQhfsyDPC-FPI 94
Cdd:cd03248 28 LVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVlldgKPISQYEH-KYLHSKVSLVGQ----EPVlFAR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 95 SVKDVVLSGrLSQLSwhgkykkkdFEAVDHALDlvglsDHHHHCF----------------AHLSGGQIQRVLLARALAS 158
Cdd:cd03248 103 SLQDNIAYG-LQSCS---------FECVKEAAQ-----KAHAHSFiselasgydtevgekgSQLSGGQKQRVAIARALIR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 499185640 159 YPEILILDEPTTNIDPDNQQRILSILKKLNRTCTILMVTHDL 200
Cdd:cd03248 168 NPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRL 209
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
8-215 |
5.37e-11 |
|
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: 60.63 E-value: 5.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 8 EGLAFRYGSKgPN--IIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGS-------LKTFPSHSAGKQthsm 78
Cdd:cd03249 4 KNVSFRYPSR-PDvpILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEilldgvdIRDLNLRWLRSQ---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 79 IGWVPQhfsyDPC-FPISVKDVVLsgrlsqlswHGKYKKKDFEAVDHALD------LVGLSDHHH-HCFAH---LSGGQI 147
Cdd:cd03249 79 IGLVSQ----EPVlFDGTIAENIR---------YGKPDATDEEVEEAAKKanihdfIMSLPDGYDtLVGERgsqLSGGQK 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499185640 148 QRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKLNRTCTILMVTHDLhHTTNYFNKVFYMNK 215
Cdd:cd03249 146 QRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRL-STIRNADLIAVLQN 212
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
87-213 |
6.71e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 61.80 E-value: 6.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 87 SYDPCFPISvKDVVLSGRLSQlswhGKYKKKDFEAVDHALDLVGLSDHHHHC--FAH-LSGGQIQRVLLARALASYPEIL 163
Cdd:PRK10261 116 SLNPVFTVG-EQIAESIRLHQ----GASREEAMVEAKRMLDQVRIPEAQTILsrYPHqLSGGMRQRVMIAMALSCRPAVL 190
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 499185640 164 ILDEPTTNIDPDNQQRILSILKKLNRTCT--ILMVTHDLHHTTNYFNKVFYM 213
Cdd:PRK10261 191 IADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEIADRVLVM 242
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
112-215 |
1.25e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 60.02 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 112 GKYKKKDFEAVDHALDLVGL-SDHHHHCFAHLSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKLNRT 190
Cdd:PRK13645 120 GENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKE 199
|
90 100
....*....|....*....|....*..
gi 499185640 191 CT--ILMVTHDLHHTTNYFNKVFYMNK 215
Cdd:PRK13645 200 YKkrIIMVTHNMDQVLRIADEVIVMHE 226
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
105-196 |
1.32e-10 |
|
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: 60.59 E-value: 1.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 105 LSQLSWHGKykkkdfEAVDHALDL---VGLSDHHHHCFAHLSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRIL 181
Cdd:TIGR03269 135 LEEIGYEGK------EAVGRAVDLiemVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVH 208
|
90
....*....|....*
gi 499185640 182 SILKKLNRTCTILMV 196
Cdd:TIGR03269 209 NALEEAVKASGISMV 223
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
121-203 |
1.56e-10 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 59.47 E-value: 1.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 121 AVDHALDLVGLSDHHHHCFAHLSGGQIQRVLLARA-LASYPEI------LILDEPTTNIDPdNQQRILsiLKKLNRTC-- 191
Cdd:COG4138 106 LLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVlLQVWPTInpegqlLLLDEPMNSLDV-AQQAAL--DRLLRELCqq 182
|
90
....*....|....
gi 499185640 192 --TILMVTHDLHHT 203
Cdd:COG4138 183 giTVVMSSHDLNHT 196
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
112-200 |
2.21e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 59.76 E-value: 2.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 112 GKYKKKDFEAVDhALDLVGLSDHHHH--CFAH-LSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKLN 188
Cdd:PRK11022 122 GNKKTRRQRAID-LLNQVGIPDPASRldVYPHqLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQ 200
|
90
....*....|....
gi 499185640 189 R--TCTILMVTHDL 200
Cdd:PRK11022 201 QkeNMALVLITHDL 214
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
121-214 |
2.31e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 58.79 E-value: 2.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 121 AVDHALDLVGLSDHHHHCFAHLSGGQIQRVLLA-------RALASYPEILILDEPTTNIDPdNQQRILSILkkLNRTC-- 191
Cdd:PRK03695 106 ALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAavvlqvwPDINPAGQLLLLDEPMNSLDV-AQQAALDRL--LSELCqq 182
|
90 100
....*....|....*....|....*
gi 499185640 192 --TILMVTHDLHHTTNYFNKVFYMN 214
Cdd:PRK03695 183 giAVVMSSHDLNHTLRHADRVWLLK 207
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
22-213 |
4.26e-10 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 58.89 E-value: 4.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 22 IHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGS-------LKTFPSHSAGKQTHSMIGWVPQHFSYDPCFPI 94
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQvlidgvdIAKISDAELREVRRKKIAMVFQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 95 sVKDVVLSGRLSQLSWHGKYKKkdfeAVDhALDLVGLSDHHHHCFAHLSGGQIQRVLLARALASYPEILILDEPTTNIDP 174
Cdd:PRK10070 124 -LDNTAFGMELAGINAEERREK----ALD-ALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDP 197
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 499185640 175 ----DNQQRILSILKKLNRtcTILMVTHDLHHTTNYFNKVFYM 213
Cdd:PRK10070 198 lirtEMQDELVKLQAKHQR--TIVFISHDLDEAMRIGDRIAIM 238
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
149-222 |
4.80e-10 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 59.14 E-value: 4.80e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499185640 149 RVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKlnRTCTILMVTHDLHhttnyfnkvfYMNKTLTSLAD 222
Cdd:PRK15064 163 RVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNE--RNSTMIIISHDRH----------FLNSVCTHMAD 224
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
22-201 |
5.52e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 58.56 E-value: 5.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 22 IHDVSFSVYDGDFigiigpngggKSTLTMLILGLLTPTFGSLKTFpshsagkqthsmiGWVPQ----HFSYDpcfpISVk 97
Cdd:COG4586 38 VDDISFTIEPGEIvgfigpngagKSTTIKMLTGILVPTSGEVRVL-------------GYVPFkrrkEFARR----IGV- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 98 dvVLsGRLSQLSW----------HGK-YK--KKDFEA-VDHALDLVGLSDhhhhcFAH-----LSGGQIQRVLLARALAS 158
Cdd:COG4586 100 --VF-GQRSQLWWdlpaidsfrlLKAiYRipDAEYKKrLDELVELLDLGE-----LLDtpvrqLSLGQRMRCELAAALLH 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 499185640 159 YPEILILDEPTTNIDPDNQQRILSILKKLNRT--CTILMVTHDLH 201
Cdd:COG4586 172 RPKILFLDEPTIGLDVVSKEAIREFLKEYNRErgTTILLTSHDMD 216
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
142-199 |
6.15e-10 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 58.50 E-value: 6.15e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499185640 142 LSGGQIQRVLLARALASYPEILILDEPTTNIDP--DNQQRI-LSIL-KKLNrtCTILMVTHD 199
Cdd:PRK11000 134 LSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAalRVQMRIeISRLhKRLG--RTMIYVTHD 193
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
114-198 |
1.27e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 56.51 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 114 YKKKDFEAVDHALDLVGLSDH--HHHCFAHLSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKLNRTC 191
Cdd:COG2401 107 GRKGDFKDAVELLNAVGLSDAvlWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLARRA 186
|
....*....
gi 499185640 192 --TILMVTH 198
Cdd:COG2401 187 giTLVVATH 195
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
79-198 |
1.45e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 57.72 E-value: 1.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 79 IGWVPQHFSYDPCFPISVKDVVLSGRLSQLSWHGKYKKKDFEAVDHALDLVGLSDHHHHC-FAHLSGGQIQRVLLARALA 157
Cdd:PRK10938 338 IGYVSSSLHLDYRVSTSVRNVILSGFFDSIGIYQAVSDRQQKLAQQWLDILGIDKRTADApFHSLSWGQQRLALIVRALV 417
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 499185640 158 SYPEILILDEPTTNIDPDNQQRILSILKKL--NRTCTILMVTH 198
Cdd:PRK10938 418 KHPTLLILDEPLQGLDPLNRQLVRRFVDVLisEGETQLLFVSH 460
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
126-215 |
1.49e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 56.63 E-value: 1.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 126 LDLvGLSDHHHHCFAHLSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILS----ILKKLNRTCtiLMVTHDLH 201
Cdd:COG1101 134 LGL-GLENRLDTKVGLLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLEltekIVEENNLTT--LMVTHNME 210
|
90
....*....|....
gi 499185640 202 HTTNYFNKVFYMNK 215
Cdd:COG1101 211 QALDYGNRLIMMHE 224
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
120-200 |
1.59e-09 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 56.77 E-value: 1.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 120 EAVDHALDLVGLSDHHHHCFAH-LSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKLNRTCTI--LMV 196
Cdd:COG4167 127 ERIFATLRLVGLLPEHANFYPHmLSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGIsyIYV 206
|
....
gi 499185640 197 THDL 200
Cdd:COG4167 207 SQHL 210
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
4-203 |
1.73e-09 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 56.44 E-value: 1.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 4 RILAEGLAFRYgsKGPNIIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGS-------LKTFPSHSAGKQTh 76
Cdd:PRK10895 3 TLTAKNLAKAY--KGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNiiiddedISLLPLHARARRG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 77 smIGWVPQHFSydpCF-PISVKD---VVLSGRLSQLSWHGKYKKKDFEA---VDHALDLVGLSdhhhhcfahLSGGQIQR 149
Cdd:PRK10895 80 --IGYLPQEAS---IFrRLSVYDnlmAVLQIRDDLSAEQREDRANELMEefhIEHLRDSMGQS---------LSGGERRR 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499185640 150 VLLARALASYPEILILDEPTTNIDPDNQQRILSILKKL-NRTCTILMVTHDLHHT 203
Cdd:PRK10895 146 VEIARALAANPKFILLDEPFAGVDPISVIDIKRIIEHLrDSGLGVLITDHNVRET 200
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
140-201 |
2.49e-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: 2.49e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499185640 140 AHLSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKL-NRTCTILMVTHDLH 201
Cdd:COG1129 139 GDLSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLkAQGVAIIYISHRLD 201
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
95-200 |
3.23e-09 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 56.57 E-value: 3.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 95 SVKDVVLSGRLSQLSWHGKY-KKKDFEAVDHALDLVGL--SDHHHHCfAHLSGG-QiQRVLLARALASYPEILILDEPTT 170
Cdd:COG1129 346 SIRENITLASLDRLSRGGLLdRRRERALAEEYIKRLRIktPSPEQPV-GNLSGGnQ-QKVVLAKWLATDPKVLILDEPTR 423
|
90 100 110
....*....|....*....|....*....|.
gi 499185640 171 NIDPDNQQRILSILKKLNRT-CTILMVTHDL 200
Cdd:COG1129 424 GIDVGAKAEIYRLIRELAAEgKAVIVISSEL 454
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
111-200 |
3.94e-09 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 56.18 E-value: 3.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 111 HGKYKKKDFEA---VDHALDLVGLSDHHHHCF-----AHLSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILS 182
Cdd:PRK11176 442 TEQYSREQIEEaarMAYAMDFINKMDNGLDTVigengVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQA 521
|
90
....*....|....*...
gi 499185640 183 ILKKLNRTCTILMVTHDL 200
Cdd:PRK11176 522 ALDELQKNRTSLVIAHRL 539
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
142-200 |
6.77e-09 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 55.27 E-value: 6.77e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499185640 142 LSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKLNRTCT--ILMVTHDL 200
Cdd:PRK11144 129 LSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREINipILYVSHSL 189
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
45-200 |
1.09e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 54.59 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 45 KSTLTMLILGLLTPTFGSLK------TFPSHSAGKQTHSMIGWVPQ--HFSYDPcfpisVKDV--VLSGRL---SQLSwh 111
Cdd:PRK11308 54 KSTLARLLTMIETPTGGELYyqgqdlLKADPEAQKLLRQKIQIVFQnpYGSLNP-----RKKVgqILEEPLlinTSLS-- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 112 gkyKKKDFEAVDHALDLVGLSDHHHHCFAHL-SGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKLNRT 190
Cdd:PRK11308 127 ---AAERREKALAMMAKVGLRPEHYDRYPHMfSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQE 203
|
170
....*....|..
gi 499185640 191 --CTILMVTHDL 200
Cdd:PRK11308 204 lgLSYVFISHDL 215
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
142-200 |
1.10e-08 |
|
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: 54.83 E-value: 1.10e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 499185640 142 LSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKLNRTCTILMVTHDL 200
Cdd:COG5265 495 LSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRL 553
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
11-215 |
1.44e-08 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 54.73 E-value: 1.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 11 AFRYGSKgPN--IIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGS-------LKTFPSHSAGKQThSMIGW 81
Cdd:TIGR00958 485 SFSYPNR-PDvpVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQvlldgvpLVQYDHHYLHRQV-ALVGQ 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 82 VPQHFSYdpcfpiSVKDVVLSGRlsqlswhGKYKKKDFEAV---DHALDLVG--LSDHHHHCFAH---LSGGQIQRVLLA 153
Cdd:TIGR00958 563 EPVLFSG------SVRENIAYGL-------TDTPDEEIMAAakaANAHDFIMefPNGYDTEVGEKgsqLSGGQKQRIAIA 629
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499185640 154 RALASYPEILILDEPTTNIDPDNQQRILSILKKLNRtcTILMVTHDLhHTTNYFNKVFYMNK 215
Cdd:TIGR00958 630 RALVRKPRVLILDEATSALDAECEQLLQESRSRASR--TVLLIAHRL-STVERADQILVLKK 688
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
21-202 |
2.80e-08 |
|
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: 53.32 E-value: 2.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 21 IIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGSLKtfpsHSAGKQTHSMIGWVpqhfsydpcFPISVKDVV 100
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIK----HSGRISFSSQFSWI---------MPGTIKENI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 101 LSGrlsqLSWHGKYKKKDFEAVDHALDLVGLSDHHHHCFAH----LSGGQIQRVLLARALASYPEILILDEPTTNIDPDN 176
Cdd:cd03291 119 IFG----VSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFT 194
|
170 180
....*....|....*....|....*..
gi 499185640 177 QQRIL-SILKKLNRTCTILMVTHDLHH 202
Cdd:cd03291 195 EKEIFeSCVCKLMANKTRILVTSKMEH 221
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
142-200 |
3.65e-08 |
|
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: 51.55 E-value: 3.65e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499185640 142 LSGGQIQRVLLARALASYPE--ILILDEPTTNIDPDNQQRILSILKKL-NRTCTILMVTHDL 200
Cdd:cd03238 88 LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLiDLGNTVILIEHNL 149
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
21-215 |
4.00e-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: 53.80 E-value: 4.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 21 IIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGSLKTFPSHSAGKQTHSM---IGWVPQhfsyDPcfpisvk 97
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLrfkITIIPQ----DP------- 1369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 98 dVVLSGRLS-QLSWHGKYKKKDfeaVDHALDLVGLSDH--------HHHCFA---HLSGGQIQRVLLARALASYPEILIL 165
Cdd:TIGR00957 1370 -VLFSGSLRmNLDPFSQYSDEE---VWWALELAHLKTFvsalpdklDHECAEggeNLSVGQRQLVCLARALLRKTKILVL 1445
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 499185640 166 DEPTTNIDPDNQQRILSILKKLNRTCTILMVTHDLHHTTNYfNKVFYMNK 215
Cdd:TIGR00957 1446 DEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDY-TRVIVLDK 1494
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
4-200 |
4.43e-08 |
|
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: 53.18 E-value: 4.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 4 RILAEGLAFRYGSKGPNIIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGSLkTFPSHSAGKQT----HSMI 79
Cdd:TIGR02203 330 DVEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQI-LLDGHDLADYTlaslRRQV 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 80 GWVPQHFSYdpcFPISVKDVVLSGRLSQlswhgkYKKKDFEAV---DHALDLVGLSDHHHHCF-----AHLSGGQIQRVL 151
Cdd:TIGR02203 409 ALVSQDVVL---FNDTIANNIAYGRTEQ------ADRAEIERAlaaAYAQDFVDKLPLGLDTPigengVLLSGGQRQRLA 479
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 499185640 152 LARALASYPEILILDEPTTNIDPDNQQRILSILKKLNRTCTILMVTHDL 200
Cdd:TIGR02203 480 IARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRL 528
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
142-200 |
4.57e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 53.25 E-value: 4.57e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 142 LSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKL-NRTCTILMVTHDL 200
Cdd:PRK09700 410 LSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLaDDGKVILMVSSEL 469
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
126-200 |
4.93e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 52.94 E-value: 4.93e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499185640 126 LDLVGLSDHHHHCFAH-LSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKLNRTCTI--LMVTHDL 200
Cdd:PRK10261 447 LERVGLLPEHAWRYPHeFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIayLFISHDM 524
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
45-198 |
5.39e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 53.20 E-value: 5.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 45 KSTlTMLIL-GLLTPTFGSLKTFpshsaGK-------QTHSMIGWVPQHFS-YDPcfpISVK-DVVLSGRLSQLSwhgky 114
Cdd:NF033858 305 KST-TMKMLtGLLPASEGEAWLF-----GQpvdagdiATRRRVGYMSQAFSlYGE---LTVRqNLELHARLFHLP----- 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 115 KKKDFEAVDHALDLVGLSDHHHHCFAHLSGGQIQRVLLARALASYPEILILDEPTTNIDP---DNQQRILSILKKlNRTC 191
Cdd:NF033858 371 AAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPvarDMFWRLLIELSR-EDGV 449
|
....*..
gi 499185640 192 TILMVTH 198
Cdd:NF033858 450 TIFISTH 456
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
143-200 |
5.74e-08 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 52.24 E-value: 5.74e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 143 SGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKLNRT--CTILMVTHDL 200
Cdd:PRK11701 153 SGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRElgLAVVIVTHDL 212
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
122-200 |
7.36e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 51.93 E-value: 7.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 122 VDHALDLVGLSDHHHHCFAHLSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKL-NRTCTILMVTHDL 200
Cdd:PRK13638 117 VDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIvAQGNHVIISSHDI 196
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
142-201 |
8.22e-08 |
|
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: 51.46 E-value: 8.22e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499185640 142 LSGGQIQRVLLARAL---ASYPEILILDEPTTNIDPDNQQRILSILKKL-NRTCTILMVTHDLH 201
Cdd:cd03271 170 LSGGEAQRIKLAKELskrSTGKTLYILDEPTTGLHFHDVKKLLEVLQRLvDKGNTVVVIEHNLD 233
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
142-213 |
8.54e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 52.36 E-value: 8.54e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499185640 142 LSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKL-NRTCTILMVTHDLHHTTNYFNKVFYM 213
Cdd:PRK15439 404 LSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIaAQNVAVLFISSDLEEIEQMADRVLVM 476
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
140-214 |
9.93e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 52.34 E-value: 9.93e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499185640 140 AHLSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQ---QRILSILKKLNRTCTILmVTHDLhHTTNYFNKVFYMN 214
Cdd:PTZ00265 578 SKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEylvQKTINNLKGNENRITII-IAHRL-STIRYANTIFVLS 653
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
140-199 |
1.02e-07 |
|
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: 52.24 E-value: 1.02e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 140 AHLSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKLnrTCTILMVTHD 199
Cdd:TIGR03719 160 TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEY--PGTVVAVTHD 217
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
8-198 |
1.07e-07 |
|
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: 52.22 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 8 EGLAFRYGSKGPNIIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTpTFG--SLKTFPSHSAGKQT-HSMIGWVPQ 84
Cdd:TIGR01271 1221 QGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGeiQIDGVSWNSVTLQTwRKAFGVIPQ 1299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 85 hfsydpcfpisvKDVVLSGRLSQ-LSWHGKYKKKDF-------------EAVDHALDLVgLSDHHHHcfahLSGGQIQRV 150
Cdd:TIGR01271 1300 ------------KVFIFSGTFRKnLDPYEQWSDEEIwkvaeevglksviEQFPDKLDFV-LVDGGYV----LSNGHKQLM 1362
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 499185640 151 LLARALASYPEILILDEPTTNIDPDNQQRILSILKKLNRTCTILMVTH 198
Cdd:TIGR01271 1363 CLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEH 1410
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
114-200 |
1.38e-07 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 50.76 E-value: 1.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 114 YKKKDFEAVDHA---LDLVGLSDHHHHCFAHLSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKLNRT 190
Cdd:PRK11300 123 FRRAESEALDRAatwLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNE 202
|
90
....*....|..
gi 499185640 191 --CTILMVTHDL 200
Cdd:PRK11300 203 hnVTVLLIEHDM 214
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
21-202 |
1.40e-07 |
|
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: 51.83 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 21 IIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGSLKtfpsHSAGKQTHSMIGWVpqhfsydpcFPISVKDVV 100
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIK----HSGRISFSPQTSWI---------MPGTIKDNI 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 101 LSGrlsqLSWHGKYKKKDFEAVDHALDLVGLSDHHHHCFAH----LSGGQIQRVLLARALASYPEILILDEPTTNIDPDN 176
Cdd:TIGR01271 508 IFG----LSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVT 583
|
170 180
....*....|....*....|....*..
gi 499185640 177 QQRIL-SILKKLNRTCTILMVTHDLHH 202
Cdd:TIGR01271 584 EKEIFeSCLCKLMSNKTRILVTSKLEH 610
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
142-199 |
1.44e-07 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 50.30 E-value: 1.44e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499185640 142 LSGGQ------IQRVLLARALASYPEILILDEPTTNIDPDN-QQRILSILKKLNRTCT--ILMVTHD 199
Cdd:cd03240 116 CSGGEkvlaslIIRLALAETFGSNCGILALDEPTTNLDEENiEESLAEIIEERKSQKNfqLIVITHD 182
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
143-200 |
1.58e-07 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 51.25 E-value: 1.58e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 143 SGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKLNRT--CTILMVTHDL 200
Cdd:PRK15079 163 SGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREmgLSLIFIAHDL 222
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-188 |
1.64e-07 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 50.41 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 1 MTIRilAEGLAFRYGSKgpNIIHDVSFSVYD------------GdfigiigpngggKSTLTMLILGLLTPTFGSLK---- 64
Cdd:COG1137 2 MTLE--AENLVKSYGKR--TVVKDVSLEVNQgeivgllgpngaG------------KTTTFYMIVGLVKPDSGRIFldge 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 65 ---TFPSH---SAGkqthsmIGWVPQHFSydpcfpI----SVKDVVLSgrlsQLSWHGKYKKKDFEAVDHALDLVGLSdH 134
Cdd:COG1137 66 ditHLPMHkraRLG------IGYLPQEAS------IfrklTVEDNILA----VLELRKLSKKEREERLEELLEEFGIT-H 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499185640 135 HHHCFAH-LSGGQIQRVLLARALASYPEILILDEPTTNIDP---DNQQRILSILKKLN 188
Cdd:COG1137 129 LRKSKAYsLSGGERRRVEIARALATNPKFILLDEPFAGVDPiavADIQKIIRHLKERG 186
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
140-173 |
1.92e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 51.08 E-value: 1.92e-07
10 20 30
....*....|....*....|....*....|....
gi 499185640 140 AHLSGGQIQRVLLARALASYPEILILDEPTTNID 173
Cdd:PRK13549 404 ARLSGGNQQKAVLAKCLLLNPKILILDEPTRGID 437
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
45-200 |
2.46e-07 |
|
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: 51.17 E-value: 2.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 45 KSTLTMLILGLLTPTFGSLKTfpshsAGKQTHSMIGWVPQHFSYDPCFPISVKDVVLSgrlSQLSWHGKYKKKDFEA--- 121
Cdd:TIGR01257 969 KTTTLSILTGLLPPTSGTVLV-----GGKDIETNLDAVRQSLGMCPQHNILFHHLTVA---EHILFYAQLKGRSWEEaql 1040
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 122 -VDHALDLVGLSDHHHHCFAHLSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKLNRTCTILMVTHDL 200
Cdd:TIGR01257 1041 eMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHM 1120
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
142-198 |
2.82e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 51.18 E-value: 2.82e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499185640 142 LSGGQIQRVLLARALASYPEILILDEPTTNIDPDN----QQRILSILKKLNRtcTILMVTH 198
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSekliEKTIVDIKDKADK--TIITIAH 1417
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
25-200 |
3.63e-07 |
|
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: 50.57 E-value: 3.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 25 VSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGSLK----------TFPSHSAGKQTHSMIGWVPQHFSYDPcfpi 94
Cdd:TIGR03269 303 VSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvrvgdewvdmTKPGPDGRGRAKRYIGILHQEYDLYP---- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 95 svKDVVLSGRLSQLSWHGKYKKKDFEAVdHALDLVGLSDHHHHCF-----AHLSGGQIQRVLLARALASYPEILILDEPT 169
Cdd:TIGR03269 379 --HRTVLDNLTEAIGLELPDELARMKAV-ITLKMVGFDEEKAEEIldkypDELSEGERHRVALAQVLIKEPRIVILDEPT 455
|
170 180 190
....*....|....*....|....*....|....*
gi 499185640 170 TNIDP----DNQQRILSILKKLNRtcTILMVTHDL 200
Cdd:TIGR03269 456 GTMDPitkvDVTHSILKAREEMEQ--TFIIVSHDM 488
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
142-200 |
3.94e-07 |
|
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: 49.85 E-value: 3.94e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 499185640 142 LSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKLNRTCTILMVTHDL 200
Cdd:cd03289 139 LSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRI 197
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
142-200 |
5.06e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 49.91 E-value: 5.06e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 142 LSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKL-NRTCTILMVTHDL 200
Cdd:PRK11288 397 LSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELaAQGVAVLFVSSDL 456
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
120-173 |
5.89e-07 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 48.65 E-value: 5.89e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 499185640 120 EAVDHALDLVGLSDHHHHCFAHLSGGQIQRVLLARALASYPEILILDEPTTNID 173
Cdd:PRK13538 108 EALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAID 161
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
142-199 |
5.90e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 49.95 E-value: 5.90e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 499185640 142 LSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKLNRtcTILMVTHD 199
Cdd:PRK11147 157 LSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQG--SIIFISHD 212
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
14-199 |
6.23e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 49.95 E-value: 6.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 14 YGSKGPNIIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGSLKT--------FPSHSA-------------- 71
Cdd:PRK11147 327 YQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCgtklevayFDQHRAeldpektvmdnlae 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 72 GKQThSMIGWVPQHfsydpcfpisvkdvVLsGRLSQLSWHGKYKKKDFEAvdhaldlvglsdhhhhcfahLSGGQIQRVL 151
Cdd:PRK11147 407 GKQE-VMVNGRPRH--------------VL-GYLQDFLFHPKRAMTPVKA--------------------LSGGERNRLL 450
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 499185640 152 LARALASYPEILILDEPTTNIDPDNqqriLSILKKL--NRTCTILMVTHD 199
Cdd:PRK11147 451 LARLFLKPSNLLILDEPTNDLDVET----LELLEELldSYQGTVLLVSHD 496
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
142-201 |
6.62e-07 |
|
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: 49.63 E-value: 6.62e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499185640 142 LSGGQIQRVLLARAL---ASYPEILILDEPTTNIDPDNQQRILSILKKL-NRTCTILMVTHDLH 201
Cdd:TIGR00630 830 LSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLvDKGNTVVVIEHNLD 893
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
114-198 |
7.20e-07 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 49.66 E-value: 7.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 114 YKKKDFEAVDHALDLVGLSDhhhhCfAH-----------LSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILS 182
Cdd:TIGR00955 133 TKKEKRERVDEVLQALGLRK----C-ANtrigvpgrvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQ 207
|
90
....*....|....*..
gi 499185640 183 ILKKL-NRTCTILMVTH 198
Cdd:TIGR00955 208 VLKGLaQKGKTIICTIH 224
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
142-200 |
7.56e-07 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 47.74 E-value: 7.56e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499185640 142 LSGGQIQRVLLAR--ALASYPE--ILILDEPTTNIDPDNQQRIL-SILKKLNRTCTILMVTHDL 200
Cdd:cd03227 78 LSGGEKELSALALilALASLKPrpLYILDEIDRGLDPRDGQALAeAILEHLVKGAQVIVITHLP 141
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
140-199 |
8.12e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 49.35 E-value: 8.12e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499185640 140 AHLSGGQIQRVLLARALASYPEILILDEPTTNIDPDnqqrilSIL---KKLNR-TCTILMVTHD 199
Cdd:PRK11819 162 TKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAE------SVAwleQFLHDyPGTVVAVTHD 219
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
139-196 |
8.79e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 49.24 E-value: 8.79e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 499185640 139 FAHLSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKLNRT-CTILMV 196
Cdd:PRK10938 133 FKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSgITLVLV 191
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
142-200 |
1.01e-06 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 48.94 E-value: 1.01e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 499185640 142 LSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKLNRTCTILMVTHDL 200
Cdd:PRK10789 452 LSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRL 510
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
142-173 |
1.11e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 49.02 E-value: 1.11e-06
10 20 30
....*....|....*....|....*....|..
gi 499185640 142 LSGGQIQRVLLARALASYPEILILDEPTTNID 173
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEPTRGID 436
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
125-175 |
1.39e-06 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 47.54 E-value: 1.39e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 499185640 125 ALDLVGLSDHHHHCFAHLSGGQIQRVLLARALASYPEILILDEPTTNIDPD 175
Cdd:PRK13543 121 ALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLE 171
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
4-215 |
1.47e-06 |
|
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: 47.53 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 4 RILAEGLAFRYGSKGPN-IIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGSLKTfpshsaGKQTHSMI--- 79
Cdd:cd03220 19 SLKKLGILGRKGEVGEFwALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTV------RGRVSSLLglg 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 80 -GWVPQhfsydpcfpISVKD-VVLSGRLsqlswHGKYKKKDFEAVDHALDLVGLSDHHHHCFAHLSGGQIQRVLLARALA 157
Cdd:cd03220 93 gGFNPE---------LTGREnIYLNGRL-----LGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499185640 158 SYPEILILDEPTTNIDPDNQQRILSILKKLNRTC-TILMVTHDLHHTTNYFNKVFYMNK 215
Cdd:cd03220 159 LEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGkTVILVSHDPSSIKRLCDRALVLEK 217
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
142-199 |
1.88e-06 |
|
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: 47.25 E-value: 1.88e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499185640 142 LSGGQIQRVLLARALAS--YPEILILDEPTTNIDPDNQQRILSILKKL-NRTCTILMVTHD 199
Cdd:cd03270 138 LSGGEAQRIRLATQIGSglTGVLYVLDEPSIGLHPRDNDRLIETLKRLrDLGNTVLVVEHD 198
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
126-200 |
1.88e-06 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 47.84 E-value: 1.88e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499185640 126 LDLVGLSDHHHHCFAHLSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKLNRT--CTILMVTHDL 200
Cdd:PRK11831 128 LEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSAlgVTCVVVSHDV 204
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
21-215 |
2.02e-06 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 47.38 E-value: 2.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 21 IIHDVSFSVYDGDFigiigpngggKSTLTMLILGLLTPTFGSLKTfpshsAGKqTHSMI----GWVPQHfsydpcfpiSV 96
Cdd:COG1134 41 ALKDVSFEVERGESvgiigrngagKSTLLKLIAGILEPTSGRVEV-----NGR-VSALLelgaGFHPEL---------TG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 97 KD-VVLSGRLsqlswHGkYKKKDFEA-VDHALDLVGLSDHHHHCFAHLSGGQIQRVLLARALASYPEILILDEPTTNIDP 174
Cdd:COG1134 106 REnIYLNGRL-----LG-LSRKEIDEkFDEIVEFAELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDA 179
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 499185640 175 DNQQRILSILKKL-NRTCTILMVTHDLHHTTNYFNKVFYMNK 215
Cdd:COG1134 180 AFQKKCLARIRELrESGRTVIFVSHSMGAVRRLCDRAIWLEK 221
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
43-222 |
2.11e-06 |
|
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: 47.40 E-value: 2.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 43 GGKSTLTMLILGLLTPTFGSLKTFPSHSAGKqthsmigwvPQHFSYDpcFPISVKDvVLSGRLSQLSWHGKYKKKdfeaV 122
Cdd:cd03237 36 IGKTTFIKMLAGVLKPDEGDIEIELDTVSYK---------PQYIKAD--YEGTVRD-LLSSITKDFYTHPYFKTE----I 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 123 DHALDLVGLSDHHhhcFAHLSGGQIQRVLLARALASYPEILILDEPTTNIdpDNQQRIL--SILKK--LNRTCTILMVTH 198
Cdd:cd03237 100 AKPLQIEQILDRE---VPELSGGELQRVAIAACLSKDADIYLLDEPSAYL--DVEQRLMasKVIRRfaENNEKTAFVVEH 174
|
170 180
....*....|....*....|....
gi 499185640 199 DlhhttnyfnkvFYMnktLTSLAD 222
Cdd:cd03237 175 D-----------IIM---IDYLAD 184
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
140-215 |
2.92e-06 |
|
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: 47.51 E-value: 2.92e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499185640 140 AHLSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKL-NRTCTILMVTHDLHHTTNYFNKVFYMNK 215
Cdd:TIGR02633 402 GRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLaQEGVAIIVVSSELAEVLGLSDRVLVIGE 478
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
141-200 |
3.04e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 47.50 E-value: 3.04e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 141 HLSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKLNRTCTILMVTHDL 200
Cdd:PRK13409 212 ELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAEGKYVLVVEHDL 271
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
141-205 |
3.09e-06 |
|
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: 46.56 E-value: 3.09e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 141 HLSGGQIQRVLLARALASYPEILILDEPTTNID---PDN--QQRILSILKKLNRtcTILMVTHDLHHTTN 205
Cdd:cd03290 140 NLSGGQRQRICVARALYQNTNIVFLDDPFSALDihlSDHlmQEGILKFLQDDKR--TLVLVTHKLQYLPH 207
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
142-199 |
3.10e-06 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 47.15 E-value: 3.10e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499185640 142 LSGGQIQRVLLARALASYPEILILDEPTTNIDPD--NQQRILsiLKKLNRT--CTILMVTHD 199
Cdd:PRK11650 135 LSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKlrVQMRLE--IQRLHRRlkTTSLYVTHD 194
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
55-201 |
3.43e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 47.66 E-value: 3.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 55 LLTPTFGSLKtfPSHSAGKQTHSMIGWVPQhFSYdpCFPISVKDVVLSGrlSQLSWHGKYKKKDFEAVDHALDLVGLSDH 134
Cdd:PLN03232 659 LISAMLGELS--HAETSSVVIRGSVAYVPQ-VSW--IFNATVRENILFG--SDFESERYWRAIDVTALQHDLDLLPGRDL 731
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 135 HH--HCFAHLSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRIL-SILKKLNRTCTILMVTHDLH 201
Cdd:PLN03232 732 TEigERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFdSCMKDELKGKTRVLVTNQLH 801
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
135-173 |
3.92e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 47.42 E-value: 3.92e-06
10 20 30
....*....|....*....|....*....|....*....
gi 499185640 135 HHHCFAHLSGGQIQRVLLARALASYPEILILDEPTTNID 173
Cdd:PRK10982 385 HRTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGID 423
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
115-200 |
4.03e-06 |
|
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: 46.59 E-value: 4.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 115 KKKD----FEAVDHALDLVGLSDHHhhcFAHLSGGQIQRVLLARALASYPEILILDEPTTNIDPdnQQRILS--ILKKLN 188
Cdd:cd03236 112 KKKDergkLDELVDQLELRHVLDRN---IDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDI--KQRLNAarLIRELA 186
|
90
....*....|...
gi 499185640 189 R-TCTILMVTHDL 200
Cdd:cd03236 187 EdDNYVLVVEHDL 199
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
142-198 |
5.68e-06 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 45.60 E-value: 5.68e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 499185640 142 LSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKL-NRTCTILMVTH 198
Cdd:cd03217 105 FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLrEEGKSVLIITH 162
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
45-198 |
7.07e-06 |
|
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: 46.67 E-value: 7.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 45 KSTLtMLILGLLTPTFGSLKTFPSHSAgkqthsmIGWVPQH-------FSYDPCFPISVKDVVLSGrlsqlswhgkYKKK 117
Cdd:TIGR00954 491 KSSL-FRILGELWPVYGGRLTKPAKGK-------LFYVPQRpymtlgtLRDQIIYPDSSEDMKRRG----------LSDK 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 118 DFEAVdhaLDLVGLsdhhHHCFAH-------------LSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSIL 184
Cdd:TIGR00954 553 DLEQI---LDNVQL----THILEReggwsavqdwmdvLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLC 625
|
170
....*....|....
gi 499185640 185 KKLNrtCTILMVTH 198
Cdd:TIGR00954 626 REFG--ITLFSVSH 637
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
142-200 |
7.71e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 46.17 E-value: 7.71e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 142 LSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKL-NRTCTILMVTHDL 200
Cdd:COG3845 403 LSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELrDAGAAVLLISEDL 462
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
22-213 |
8.79e-06 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 45.55 E-value: 8.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 22 IHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGSLK------TFPSHSAGKQTHSMIGWVPQHfSYDPCFPIS 95
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLiddhplHFGDYSYRSQRIRMIFQDPST-SLNPRQRIS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 96 -VKDVVLsgRL-SQLSWHGKYKkkdfeAVDHALDLVGLSDHHHHCFAH-LSGGQIQRVLLARALASYPEILILDEPTTNI 172
Cdd:PRK15112 108 qILDFPL--RLnTDLEPEQREK-----QIIETLRQVGLLPDHASYYPHmLAPGQKQRLGLARALILRPKVIIADEALASL 180
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 499185640 173 DPDNQQRILSILKKLNRTCTI--LMVTHDLHHTTNYFNKVFYM 213
Cdd:PRK15112 181 DMSMRSQLINLMLELQEKQGIsyIYVTQHLGMMKHISDQVLVM 223
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
142-200 |
1.02e-05 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 46.11 E-value: 1.02e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 499185640 142 LSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKLNRTCTILMVTHDL 200
Cdd:PRK13657 472 LSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRL 530
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
97-198 |
1.14e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 45.50 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 97 KDVVLSGRLSQLSwhgkykKKDFEA-VDHALDLVGLSDHHHHCFAHLSGGQIQRVLLARALASYPEILILDEPTTNIDPD 175
Cdd:NF000106 105 ENLYMIGR*LDLS------RKDARArADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPR 178
|
90 100
....*....|....*....|....
gi 499185640 176 NQQRILSILKKLNRT-CTILMVTH 198
Cdd:NF000106 179 TRNEVWDEVRSMVRDgATVLLTTQ 202
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
142-199 |
1.21e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 45.79 E-value: 1.21e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499185640 142 LSGGQIQRVLLARALAS------YpeilILDEPTTNIDP-DNqQRILSILKKL----NrtcTILMVTHD 199
Cdd:COG0178 486 LSGGEAQRIRLATQIGSglvgvlY----VLDEPSIGLHQrDN-DRLIETLKRLrdlgN---TVIVVEHD 546
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
142-173 |
1.30e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 45.76 E-value: 1.30e-05
10 20 30
....*....|....*....|....*....|..
gi 499185640 142 LSGGQIQRVLLARALASYPEILILDEPTTNID 173
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
142-203 |
1.71e-05 |
|
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: 43.52 E-value: 1.71e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499185640 142 LSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSIL-------KKLNRTCTILMVTHDLHHT 203
Cdd:smart00382 61 GSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEelrllllLKSEKNLTVILTTNDEKDL 129
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
24-200 |
1.89e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 45.16 E-value: 1.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 24 DVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGSLkTFPSHSAGKQTHSM-----IGWVPQHFSYdpCFPISVKD 98
Cdd:PRK09700 23 SVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTI-TINNINYNKLDHKLaaqlgIGIIYQELSV--IDELTVLE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 99 VVLSGRLSQLSWHG----KYKKKDFEAvDHALDLVGLSDHHHHCFAHLSGGQIQRVLLARALASYPEILILDEPTTNIDP 174
Cdd:PRK09700 100 NLYIGRHLTKKVCGvniiDWREMRVRA-AMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTN 178
|
170 180
....*....|....*....|....*..
gi 499185640 175 DNQQRILSILKKLNRTCT-ILMVTHDL 200
Cdd:PRK09700 179 KEVDYLFLIMNQLRKEGTaIVYISHKL 205
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
105-201 |
2.01e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 2.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 105 LSQLSwHGKYKKKDfeaVDHALDL-VGLSDHHHHCFAHLSGG---QI---QRVLLARALASYPEILILDEPTTNIDPDNQ 177
Cdd:COG4717 525 FSRLT-DGRYRLIR---IDEDLSLkVDTEDGRTRPVEELSRGtreQLylaLRLALAELLAGEPLPLILDDAFVNFDDERL 600
|
90 100
....*....|....*....|....
gi 499185640 178 QRILSILKKLNRTCTILMVTHDLH 201
Cdd:COG4717 601 RAALELLAELAKGRQVIYFTCHEE 624
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
142-200 |
2.11e-05 |
|
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: 45.16 E-value: 2.11e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499185640 142 LSGGQIQRVLLARALASYPEILILDEPTTNIDPDnqQRIL--SILKKL--NRTCTILMVTHDL 200
Cdd:COG1245 456 LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVE--QRLAvaKAIRRFaeNRGKTAMVVDHDI 516
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
45-186 |
2.78e-05 |
|
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: 45.00 E-value: 2.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 45 KSTLTMLILGLLTPTFGSLKTfpshsAGKQTHSMIGWVPQHFSYDPCFpiSVKDVVLSGRlSQLSWHGKYK---KKDFEA 121
Cdd:TIGR01257 1978 KTTTFKMLTGDTTVTSGDATV-----AGKSILTNISDVHQNMGYCPQF--DAIDDLLTGR-EHLYLYARLRgvpAEEIEK 2049
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 122 VDH-ALDLVGLSDHHHHCFAHLSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQR----ILSILKK 186
Cdd:TIGR01257 2050 VANwSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMlwntIVSIIRE 2119
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
142-201 |
2.83e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.85 E-value: 2.83e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 142 LSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKLNRtcTILMVTHDLH 201
Cdd:PLN03073 628 LSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQG--GVLMVSHDEH 685
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
142-201 |
2.86e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 44.97 E-value: 2.86e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 142 LSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKLNRTCTILMVTHDLH 201
Cdd:PLN03232 1372 FSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLN 1431
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
142-200 |
3.10e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 44.41 E-value: 3.10e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499185640 142 LSGGQIQRVLLARALASYPEILILDEPTTNIDPdnQQRIL--SILKKL--NRTCTILMVTHDL 200
Cdd:PRK13409 454 LSGGELQRVAIAACLSRDADLYLLDEPSAHLDV--EQRLAvaKAIRRIaeEREATALVVDHDI 514
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
79-201 |
4.34e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 44.34 E-value: 4.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 79 IGWVPQhFSYdpCFPISVKDVVLSGRLSQLSwhgKYKKK-DFEAVDHALDLVGLSDHHH--HCFAHLSGGQIQRVLLARA 155
Cdd:PLN03130 681 VAYVPQ-VSW--IFNATVRDNILFGSPFDPE---RYERAiDVTALQHDLDLLPGGDLTEigERGVNISGGQKQRVSMARA 754
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 499185640 156 LASYPEILILDEPTTNIDPD-NQQRILSILKKLNRTCTILMVTHDLH 201
Cdd:PLN03130 755 VYSNSDVYIFDDPLSALDAHvGRQVFDKCIKDELRGKTRVLVTNQLH 801
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
45-200 |
5.79e-05 |
|
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: 43.62 E-value: 5.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 45 KSTlTMLIL-GLLTPTFGSLKTFPS------HSAGKQTHsmigwvpQHFS--YDPCFPISVK----DV---VLSGRLSQL 108
Cdd:COG1245 112 KST-ALKILsGELKPNLGDYDEEPSwdevlkRFRGTELQ-------DYFKklANGEIKVAHKpqyvDLipkVFKGTVREL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 109 swhgkYKKKD-FEAVDHALDLVGLSDHHHHCFAHLSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKL 187
Cdd:COG1245 184 -----LEKVDeRGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIREL 258
|
170
....*....|....
gi 499185640 188 NRTC-TILMVTHDL 200
Cdd:COG1245 259 AEEGkYVLVVEHDL 272
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
45-207 |
6.64e-05 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 43.42 E-value: 6.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 45 KSTLTMLILGLLTPTFGS--LKTFPSHSAGKQTHSmigwvpQHFSydpcfpiSV-KDVVLSGRLSQlswhGKYKKKDFEA 121
Cdd:PRK10522 362 KSTLAMLLTGLYQPQSGEilLDGKPVTAEQPEDYR------KLFS-------AVfTDFHLFDQLLG----PEGKPANPAL 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 122 VDHALDLVGLSD---HHHHCFAH--LSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQ----QRILSILKKLNRtcT 192
Cdd:PRK10522 425 VEKWLERLKMAHkleLEDGRISNlkLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRrefyQVLLPLLQEMGK--T 502
|
170
....*....|....*
gi 499185640 193 ILMVTHDLHhttnYF 207
Cdd:PRK10522 503 IFAISHDDH----YF 513
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
142-200 |
8.61e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 43.48 E-value: 8.61e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499185640 142 LSGGQIQRVLLARALA---SYPEILILDEPTTNIDPDNQQRILSILKKL----NrtcTILMVTHDL 200
Cdd:COG0178 827 LSGGEAQRVKLASELSkrsTGKTLYILDEPTTGLHFHDIRKLLEVLHRLvdkgN---TVVVIEHNL 889
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
110-198 |
9.47e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 43.18 E-value: 9.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 110 WHGKYKKKDFeAVDHA---------LDLVGLSDHHHHCFAHLSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRI 180
Cdd:PRK10982 95 WLGRYPTKGM-FVDQDkmyrdtkaiFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNHL 173
|
90
....*....|....*....
gi 499185640 181 LSILKKL-NRTCTILMVTH 198
Cdd:PRK10982 174 FTIIRKLkERGCGIVYISH 192
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
142-193 |
9.71e-05 |
|
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: 41.85 E-value: 9.71e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 499185640 142 LSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKLNRT-----CTI 193
Cdd:cd03232 109 LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADSgqailCTI 165
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
142-174 |
1.11e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 42.80 E-value: 1.11e-04
10 20 30
....*....|....*....|....*....|...
gi 499185640 142 LSGGQIQRVLLARALASYPEILILDEPTTNIDP 174
Cdd:NF033858 137 LSGGMKQKLGLCCALIHDPDLLILDEPTTGVDP 169
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
97-173 |
1.43e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.54 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 97 KDVVlSGRLSQLswhgkYKKkdFEAVDH-------ALDLVGLS---DHHHHCFAHLSGGQIQRVLLARALASYPEILILD 166
Cdd:PLN03073 298 KDAV-SQRLEEI-----YKR--LELIDAytaearaASILAGLSftpEMQVKATKTFSGGWRMRIALARALFIEPDLLLLD 369
|
....*..
gi 499185640 167 EPTTNID 173
Cdd:PLN03073 370 EPTNHLD 376
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
142-196 |
1.49e-04 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 41.79 E-value: 1.49e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 499185640 142 LSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKLNRT-CTILMV 196
Cdd:PRK11614 138 MSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQgMTIFLV 193
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
142-201 |
1.51e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.89 E-value: 1.51e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499185640 142 LSGGQIQRVLLARALAS---YPEILILDEPTTNIDPDNQQRILSILKKL-NRTCTILMVTHDLH 201
Cdd:PRK00635 810 LSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLtHQGHTVVIIEHNMH 873
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
12-200 |
2.41e-04 |
|
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: 42.24 E-value: 2.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 12 FRYGSKGPNIIHDVSFSVYDGDFIGIIGPNGGGKSTLtmlilglLTPTFGSLKTFPSHSAGKQThsmIGWVPQHFSYDPC 91
Cdd:TIGR00957 644 FTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSL-------LSALLAEMDKVEGHVHMKGS---VAYVPQQAWIQND 713
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 92 fpiSVKDVVLSGRLSQlswhGKYKKKDFEAVDHALDLVGLSDHHHHCFA----HLSGGQIQRVLLARALASYPEILILDE 167
Cdd:TIGR00957 714 ---SLRENILFGKALN----EKYYQQVLEACALLPDLEILPSGDRTEIGekgvNLSGGQKQRVSLARAVYSNADIYLFDD 786
|
170 180 190
....*....|....*....|....*....|....*.
gi 499185640 168 PTTNIDPDNQQRILSIL---KKLNRTCTILMVTHDL 200
Cdd:TIGR00957 787 PLSAVDAHVGKHIFEHVigpEGVLKNKTRILVTHGI 822
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
91-198 |
2.92e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 41.45 E-value: 2.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 91 CFPiSVKDVVLS----GRLsQLSWHGKYKKKDFEAvdhaldlvglsdhhhhcfAHLSGGQIqRVL-LARALASY--PEIL 163
Cdd:COG4637 224 AFP-GFEDIEVEpdedGRV-LLEFREKGLDRPFPA------------------RELSDGTL-RFLaLLAALLSPrpPPLL 282
|
90 100 110
....*....|....*....|....*....|....*
gi 499185640 164 ILDEPTTNIDPDNQQRILSILKKLNRTCTILMVTH 198
Cdd:COG4637 283 CIEEPENGLHPDLLPALAELLREASERTQVIVTTH 317
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
120-225 |
3.03e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 41.31 E-value: 3.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 120 EAVDHALDL---VGLSDHHHHCFAHLSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKLNR---TCTI 193
Cdd:NF040905 115 ETNRRARELlakVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAqgiTSII 194
|
90 100 110
....*....|....*....|....*....|..
gi 499185640 194 lmVTHDLhhttnyfNKVFYMNKTLTSLADTST 225
Cdd:NF040905 195 --ISHKL-------NEIRRVADSITVLRDGRT 217
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
18-201 |
3.05e-04 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 41.58 E-value: 3.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 18 GPNIIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGSLK---TFPSHSAGKQTHSM-IGWVPQhfsyDP-CF 92
Cdd:PRK15439 23 GVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEiggNPCARLTPAKAHQLgIYLVPQ----EPlLF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 93 P-ISVKDVVLSGrlsqLSWHGKYKKKdfeaVDHALDLVGLSDHHHHCFAHLSGGQIQRVLLARALASYPEILILDEPTTN 171
Cdd:PRK15439 99 PnLSVKENILFG----LPKRQASMQK----MKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTAS 170
|
170 180 190
....*....|....*....|....*....|.
gi 499185640 172 IDPDNQQRILSILKKL-NRTCTILMVTHDLH 201
Cdd:PRK15439 171 LTPAETERLFSRIRELlAQGVGIVFISHKLP 201
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
142-200 |
3.39e-04 |
|
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: 40.25 E-value: 3.39e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499185640 142 LSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKLNRTC--TILMVTHDL 200
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGkkTALVVEHDL 132
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
141-222 |
3.79e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 41.07 E-value: 3.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 141 HLSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKL-NRTCTILMVTHDLhhttnyfNKVFYMNKTLTS 219
Cdd:PRK13549 143 NLGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLkAHGIACIYISHKL-------NEVKAISDTICV 215
|
...
gi 499185640 220 LAD 222
Cdd:PRK13549 216 IRD 218
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
143-200 |
4.20e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 41.26 E-value: 4.20e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 499185640 143 SGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKLNRTCTILMVTHDL 200
Cdd:PLN03130 1376 SVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRL 1433
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
140-199 |
4.23e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.35 E-value: 4.23e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499185640 140 AHLSGGQIQRVLLARALASypEIL----ILDEPTTNIDPDNQQRILSILKKL-NRTCTILMVTHD 199
Cdd:PRK00635 475 ATLSGGEQERTALAKHLGA--ELIgityILDEPSIGLHPQDTHKLINVIKKLrDQGNTVLLVEHD 537
|
|
| ABC_RecN |
cd03241 |
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ... |
142-198 |
5.59e-04 |
|
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to 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 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: 213208 [Multi-domain] Cd Length: 276 Bit Score: 40.26 E-value: 5.59e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499185640 142 LSGGQIQRVLLA--RALASYPEI--LILDEPTTNIDPDNQQRILSILKKLNRTCTILMVTH 198
Cdd:cd03241 171 ASGGELSRLMLAlkAILARKDAVptLIFDEIDTGISGEVAQAVGKKLKELSRSHQVLCITH 231
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
142-198 |
5.80e-04 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 40.63 E-value: 5.80e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 499185640 142 LSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKL-NRTCTILMVTH 198
Cdd:PLN03211 207 ISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLaQKGKTIVTSMH 264
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-173 |
6.55e-04 |
|
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: 40.30 E-value: 6.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 5 ILAEGLAFRYGSKgpNIIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGSLKTfpshsaGKQTHsmIGWVPQ 84
Cdd:TIGR03719 323 IEAENLTKAFGDK--LLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI------GETVK--LAYVDQ 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 85 -HFSYDPcfpisVKDV--VLSGRLSQLSWhGKYKKK--------DFEAVDHAlDLVGLsdhhhhcfahLSGGQIQRVLLA 153
Cdd:TIGR03719 393 sRDALDP-----NKTVweEISGGLDIIKL-GKREIPsrayvgrfNFKGSDQQ-KKVGQ----------LSGGERNRVHLA 455
|
170 180
....*....|....*....|
gi 499185640 154 RALASYPEILILDEPTTNID 173
Cdd:TIGR03719 456 KTLKSGGNVLLLDEPTNDLD 475
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
142-200 |
6.69e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 40.44 E-value: 6.69e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 142 LSGGQIQRVLLARALAS-------YpeilILDEPTTNIDPDNQQRILSILKKL----NrtcTILMVTHDL 200
Cdd:PRK00349 831 LSGGEAQRVKLAKELSKrstgktlY----ILDEPTTGLHFEDIRKLLEVLHRLvdkgN---TVVVIEHNL 893
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
142-201 |
8.19e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 40.53 E-value: 8.19e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499185640 142 LSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILS--ILKKLnRTCTILMVTHDLH 201
Cdd:PTZ00243 783 LSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEecFLGAL-AGKTRVLATHQVH 843
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
142-199 |
8.64e-04 |
|
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: 40.38 E-value: 8.64e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499185640 142 LSGGQIQRVLLARALAS------YpeilILDEPTTNIDPDNQQRILSILKKL-NRTCTILMVTHD 199
Cdd:TIGR00630 489 LSGGEAQRIRLATQIGSgltgvlY----VLDEPSIGLHQRDNRRLINTLKRLrDLGNTLIVVEHD 549
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
140-201 |
1.02e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 40.15 E-value: 1.02e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499185640 140 AHLSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILkkLNRTCTILMVTHDLH 201
Cdd:PRK10636 429 RRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEAL--IDFEGALVVVSHDRH 488
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
45-199 |
1.82e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 39.00 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 45 KSTLTMLILGLLTPTFGSLkTFPSHSAgkqthsmIGWVPQHfsyDPCFPISVKDVVLSG----RLSQLSWHGKYKKKDFE 120
Cdd:PRK10636 40 KSTLLALLKNEISADGGSY-TFPGNWQ-------LAWVNQE---TPALPQPALEYVIDGdreyRQLEAQLHDANERNDGH 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 121 AVDHA---LD--------------LVGL---SDHHHHCFAHLSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRI 180
Cdd:PRK10636 109 AIATIhgkLDaidawtirsraaslLHGLgfsNEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWL 188
|
170
....*....|....*....
gi 499185640 181 LSILKklNRTCTILMVTHD 199
Cdd:PRK10636 189 EKWLK--SYQGTLILISHD 205
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
142-189 |
3.01e-03 |
|
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: 38.27 E-value: 3.01e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 499185640 142 LSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKLNR 189
Cdd:TIGR02633 142 YGGGQQQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKA 189
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
125-214 |
3.05e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 38.61 E-value: 3.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499185640 125 ALDLVGLSDHhhhcFAHLSGGQIQRVL---------------LARALASYPEILIL-DEPTTNIDPDNQQRILSILKKLN 188
Cdd:PTZ00243 1418 ALELVGLRER----VASESEGIDSRVLeggsnysvgqrqlmcMARALLKKGSGFILmDEATANIDPALDRQIQATVMSAF 1493
|
90 100
....*....|....*....|....*.
gi 499185640 189 RTCTILMVTHDLHHTTNYfNKVFYMN 214
Cdd:PTZ00243 1494 SAYTVITIAHRLHTVAQY-DKIIVMD 1518
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
142-186 |
4.07e-03 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 35.67 E-value: 4.07e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 499185640 142 LSGGQIQR---VLLARALASY----------PEILILDEPTTNIDPDNQQRILSILKK 186
Cdd:pfam13558 33 LSGGEKQLlayLPLAAALAAQygsaegrppaPRLVFLDEAFAKLDEENIRTALELLRA 90
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
142-199 |
4.62e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 38.12 E-value: 4.62e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499185640 142 LSGGQIQRVLLA-R-ALASYP----EILILDEPTTNIDPDNQQRILSILKK-LNRTCTILMVTHD 199
Cdd:PRK03918 789 LSGGERIALGLAfRlALSLYLagniPLLILDEPTPFLDEERRRKLVDIMERyLRKIPQVIIVSHD 853
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
141-202 |
9.52e-03 |
|
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: 36.43 E-value: 9.52e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499185640 141 HLSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQqrilSILKKLNRTC----TILMVTHDLHH 202
Cdd:cd03288 156 NFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATE----NILQKVVMTAfadrTVVTIAHRVST 217
|
|
| |
