|
Name |
Accession |
Description |
Interval |
E-value |
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
17-268 |
2.68e-115 |
|
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: 331.23 E-value: 2.68e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 17 TEPALEVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQLPERRARSG 96
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 97 VRRTFQRAQLYSRLSVEDNVLTAMEWRGGGGGLLAdLFAAPGRRRREAERREYALSVLAACGLADLRHKPAGALPIGQAR 176
Cdd:COG0411 81 IARTFQNPRLFPELTVLENVLVAAHARLGRGLLAA-LLRLPRARREEREARERAEELLERVGLADRADEPAGNLSYGQQR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 177 LVELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLR-TTGVAVVLVEHDVGFVMGQSDRVVVLNLGSVLAEGTPDE 255
Cdd:COG0411 160 RLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRdERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAE 239
|
250
....*....|...
gi 521297957 256 IQAHPAVRAAYLG 268
Cdd:COG0411 240 VRADPRVIEAYLG 252
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
21-262 |
1.29e-102 |
|
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: 298.20 E-value: 1.29e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 21 LEVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQLPERRARSGVRRT 100
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 101 FQRAQLYSRLSVEDNVLTAMEWRGGGGglladlFAAPGRRRREAERREYALSVLAACGLADLRHKPAGALPIGQARLVEL 180
Cdd:cd03219 81 FQIPRLFPELTVLENVMVAAQARTGSG------LLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 181 ARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLRTTGVAVVLVEHDVGFVMGQSDRVVVLNLGSVLAEGTPDEIQAHP 260
Cdd:cd03219 155 ARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNP 234
|
..
gi 521297957 261 AV 262
Cdd:cd03219 235 RV 236
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
15-268 |
3.82e-74 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 226.54 E-value: 3.82e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 15 VTTEPALEVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRqLPE-RRA 93
Cdd:COG4674 5 TMHGPILYVEDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTG-LDEhEIA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 94 RSGVRRTFQRAQLYSRLSVEDNVLTAMewrGGGGGLLADLFAAPGRRRREAERreyalSVLAACGLADLRHKPAGALPIG 173
Cdd:COG4674 84 RLGIGRKFQKPTVFEELTVFENLELAL---KGDRGVFASLFARLTAEERDRIE-----EVLETIGLTDKADRLAGLLSHG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 174 QARLVELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLRTTGvAVVLVEHDVGFVMGQSDRVVVLNLGSVLAEGTP 253
Cdd:COG4674 156 QKQWLEIGMLLAQDPKLLLLDEPVAGMTDAETERTAELLKSLAGKH-SVVVVEHDMEFVRQIARKVTVLHQGSVLAEGSL 234
|
250
....*....|....*
gi 521297957 254 DEIQAHPAVRAAYLG 268
Cdd:COG4674 235 DEVQADPRVIEVYLG 249
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
17-268 |
4.63e-72 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 221.40 E-value: 4.63e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 17 TEPALEVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQLPERRARSG 96
Cdd:PRK11300 2 SQPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 97 VRRTFQRAQLYSRLSVEDNVLTAmEWRGGGGGLLADLFAAPGRRRREAERREYALSVLAACGLADLRHKPAGALPIGQAR 176
Cdd:PRK11300 82 VVRTFQHVRLFREMTVIENLLVA-QHQQLKTGLFSGLLKTPAFRRAESEALDRAATWLERVGLLEHANRQAGNLAYGQQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 177 LVELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLRTT-GVAVVLVEHDVGFVMGQSDRVVVLNLGSVLAEGTPDE 255
Cdd:PRK11300 161 RLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEE 240
|
250
....*....|...
gi 521297957 256 IQAHPAVRAAYLG 268
Cdd:PRK11300 241 IRNNPDVIKAYLG 253
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
21-258 |
3.52e-65 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 202.99 E-value: 3.52e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 21 LEVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQLPERRARSGVrrT 100
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGY--V 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 101 FQRAQLYSRLSVEDNVLTAmewrgggggllADLFAAPGrrrreAERREYALSVLAACGLADLRHKPAGALPIGQARLVEL 180
Cdd:COG1131 79 PQEPALYPDLTVRENLRFF-----------ARLYGLPR-----KEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGL 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521297957 181 ARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLRTTGVAVVLVEHDVGFVMGQSDRVVVLNLGSVLAEGTPDEIQA 258
Cdd:COG1131 143 ALALLHDPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKA 220
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
18-268 |
4.04e-62 |
|
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: 195.20 E-value: 4.04e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 18 EPALEVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQLPERRARSGV 97
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 98 ------RRTFqraqlySRLSVEDNVLTAMEWRGGGGGLLAD------LFAApgrrrreaerreyalsvlaacgLADLRHK 165
Cdd:COG0410 81 gyvpegRRIF------PSLTVEENLLLGAYARRDRAEVRADlervyeLFPR----------------------LKERRRQ 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 166 PAGALPIGQARLVELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLRTTGVAVVLVEHDVGFVMGQSDRVVVLNLG 245
Cdd:COG0410 133 RAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERG 212
|
250 260
....*....|....*....|...
gi 521297957 246 SVLAEGTPDEIQAHPAVRAAYLG 268
Cdd:COG0410 213 RIVLEGTAAELLADPEVREAYLG 235
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
21-268 |
2.86e-60 |
|
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: 190.45 E-value: 2.86e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 21 LEVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQLPERRARSGVRRT 100
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 101 FQRAQLYSRLSVEDNVLTAMEWRGGGGGLLADLfaapgrrrreaerreyALSVLAACGLADLRHKPAGALPIGQARLVEL 180
Cdd:cd03218 81 PQEASIFRKLTVEENILAVLEIRGLSKKEREEK----------------LEELLEEFHITHLRKSKASSLSGGERRRVEI 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 181 ARAIADRPRLLLLDEPTSG---LSAHETElfgEQIQRLRTTGVAVVLVEHDVGFVMGQSDRVVVLNLGSVLAEGTPDEIQ 257
Cdd:cd03218 145 ARALATNPKFLLLDEPFAGvdpIAVQDIQ---KIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIA 221
|
250
....*....|.
gi 521297957 258 AHPAVRAAYLG 268
Cdd:cd03218 222 ANELVRKVYLG 232
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
21-258 |
2.48e-58 |
|
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: 185.33 E-value: 2.48e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 21 LEVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQLPERRARSGVRRT 100
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 101 FQRAQLYSRLSVEDNVLTAMEWRGGGGGLLA-----DLFAApgrrrreaerreyalsvlaacgLADLRHKPAGALPIGQA 175
Cdd:cd03224 81 PEGRRIFPELTVEENLLLGAYARRRAKRKARlervyELFPR----------------------LKERRKQLAGTLSGGEQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 176 RLVELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLRTTGVAVVLVEHDVGFVMGQSDRVVVLNLGSVLAEGTPDE 255
Cdd:cd03224 139 QMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAE 218
|
...
gi 521297957 256 IQA 258
Cdd:cd03224 219 LLA 221
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
18-268 |
3.46e-58 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 185.23 E-value: 3.46e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 18 EPALEVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRqLP-ERRARSG 96
Cdd:COG1137 1 MMTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITH-LPmHKRARLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 97 VRRTFQRAQLYSRLSVEDNVLTAMEWRGGGGGLLADLFAapgrrrreaerreyalSVLAACGLADLRHKPAGALPIGQAR 176
Cdd:COG1137 80 IGYLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLE----------------ELLEEFGITHLRKSKAYSLSGGERR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 177 LVELARAIADRPRLLLLDEPTSG---LSAHEtelFGEQIQRLRTTGVAVVLVEHDVGFVMGQSDRVVVLNLGSVLAEGTP 253
Cdd:COG1137 144 RVEIARALATNPKFILLDEPFAGvdpIAVAD---IQKIIRHLKERGIGVLITDHNVRETLGICDRAYIISEGKVLAEGTP 220
|
250
....*....|....*
gi 521297957 254 DEIQAHPAVRAAYLG 268
Cdd:COG1137 221 EEILNNPLVRKVYLG 235
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
16-264 |
2.50e-55 |
|
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: 178.25 E-value: 2.50e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 16 TTEPALEVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVT----RQLPER 91
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITglseKELYEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 92 RARSGVrrTFQRAQLYSRLSVEDNVLTAM-EWRGGGGGLLADLfaapgrrrreaerreyALSVLAACGLADLRHKPAGAL 170
Cdd:COG1127 81 RRRIGM--LFQGGALFDSLTVFENVAFPLrEHTDLSEAEIREL----------------VLEKLELVGLPGAADKMPSEL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 171 PIGQARLVELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLRTT-GVAVVLVEHDVGFVMGQSDRVVVLNLGSVLA 249
Cdd:COG1127 143 SGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIA 222
|
250
....*....|....*..
gi 521297957 250 EGTPDEIQA--HPAVRA 264
Cdd:COG1127 223 EGTPEELLAsdDPWVRQ 239
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
21-258 |
9.60e-55 |
|
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: 176.59 E-value: 9.60e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 21 LEVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQLPERRARSGVrrT 100
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGV--L 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 101 FQRAQLYSRLSVEDNVltamewrggggglladLFAAPGRRRREAERREYALSVLAACGLADLRHKPAGALPIGQARLVEL 180
Cdd:COG4555 80 PDERGLYDRLTVRENI----------------RYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVAL 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521297957 181 ARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLRTTGVAVVLVEHDVGFVMGQSDRVVVLNLGSVLAEGTPDEIQA 258
Cdd:COG4555 144 ARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELRE 221
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
21-268 |
7.83e-54 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 174.38 E-value: 7.83e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 21 LEVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQLPERRARSGVRRT 100
Cdd:TIGR04406 2 LVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARLGIGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 101 FQRAQLYSRLSVEDNVLTAMEWRGggggllaDLFAApgrrrreaERREYALSVLAACGLADLRHKPAGALPIGQARLVEL 180
Cdd:TIGR04406 82 PQEASIFRKLTVEENIMAVLEIRK-------DLDRA--------EREERLEALLEEFQISHLRDNKAMSLSGGERRRVEI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 181 ARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLRTTGVAVVLVEHDVGFVMGQSDRVVVLNLGSVLAEGTPDEIQAHP 260
Cdd:TIGR04406 147 ARALATNPKFILLDEPFAGVDPIAVGDIKKIIKHLKERGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVANE 226
|
....*...
gi 521297957 261 AVRAAYLG 268
Cdd:TIGR04406 227 KVRRVYLG 234
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
16-266 |
2.93e-53 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 172.97 E-value: 2.93e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 16 TTEPALEVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQ------LP 89
Cdd:COG1121 2 MMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRArrrigyVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 90 ERRArsgVRRTFQraqlysrLSVEDNVLTAMeWRGGGgglladLFAAPGRRRREAerreyALSVLAACGLADLRHKPAGA 169
Cdd:COG1121 82 QRAE---VDWDFP-------ITVRDVVLMGR-YGRRG------LFRRPSRADREA-----VDEALERVGLEDLADRPIGE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 170 LPIGQARLVELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLRTTGVAVVLVEHDVGFVMGQSDRVVVLNlGSVLA 249
Cdd:COG1121 140 LSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLN-RGLVA 218
|
250
....*....|....*..
gi 521297957 250 EGTPDEIQAHPAVRAAY 266
Cdd:COG1121 219 HGPPEEVLTPENLSRAY 235
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
21-256 |
4.48e-53 |
|
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: 172.13 E-value: 4.48e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 21 LEVRHVTKRY-GGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTR-QLPERRARSGVr 98
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKkNLRELRRKVGL- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 99 rTFQ--RAQLYSRlSVEDNV---LTAMEWRGGGGGLLADlfaapgrrrreaerreyalSVLAACGLADLRHKPAGALPIG 173
Cdd:COG1122 80 -VFQnpDDQLFAP-TVEEDVafgPENLGLPREEIRERVE-------------------EALELVGLEHLADRPPHELSGG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 174 QARLVELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLRTTGVAVVLVEHDVGFVMGQSDRVVVLNLGSVLAEGTP 253
Cdd:COG1122 139 QKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTP 218
|
...
gi 521297957 254 DEI 256
Cdd:COG1122 219 REV 221
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
20-266 |
4.09e-52 |
|
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: 170.22 E-value: 4.09e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 20 ALEVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQLPERRARsgvRR 99
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELAR---RI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 100 TF--QRAQLYSRLSVEDNVLTA-MEWRGGGGGLLADLFAApgrrrreaerreyALSVLAACGLADLRHKPAGALPIGQAR 176
Cdd:COG1120 78 AYvpQEPPAPFGLTVRELVALGrYPHLGLFGRPSAEDREA-------------VEEALERTGLEHLADRPVDELSGGERQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 177 LVELARAIADRPRLLLLDEPTSGLS-AHETELFgEQIQRL-RTTGVAVVLVEHDVGFVMGQSDRVVVLNLGSVLAEGTPD 254
Cdd:COG1120 145 RVLIARALAQEPPLLLLDEPTSHLDlAHQLEVL-ELLRRLaRERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPE 223
|
250
....*....|..
gi 521297957 255 EIQAHPAVRAAY 266
Cdd:COG1120 224 EVLTPELLEEVY 235
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
17-261 |
3.63e-51 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 170.66 E-value: 3.63e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 17 TEPALEVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQLPERRarsG 96
Cdd:COG3842 2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKR---N 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 97 VRRTFQRAQLYSRLSVEDNV---LTAMEWRGGGGGLLADlfaapgrrrreaerreyalSVLAACGLADLRHKPAGALPIG 173
Cdd:COG3842 79 VGMVFQDYALFPHLTVAENVafgLRMRGVPKAEIRARVA-------------------ELLELVGLEGLADRYPHQLSGG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 174 QARLVELARAIADRPRLLLLDEPTSGLSAH-----ETELFgeQIQrlRTTGVAVVLVEHDVG--FVMgqSDRVVVLNLGS 246
Cdd:COG3842 140 QQQRVALARALAPEPRVLLLDEPLSALDAKlreemREELR--RLQ--RELGITFIYVTHDQEeaLAL--ADRIAVMNDGR 213
|
250
....*....|....*
gi 521297957 247 VLAEGTPDEIQAHPA 261
Cdd:COG3842 214 IEQVGTPEEIYERPA 228
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
21-263 |
1.30e-50 |
|
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: 165.75 E-value: 1.30e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 21 LEVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTR----QLPERRARSG 96
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGlseaELYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 97 VrrTFQRAQLYSRLSVEDNVltAMEWRGGGGGLLADLFAApgrrrreaerreyALSVLAACGLADLRHKPAGALPIGQAR 176
Cdd:cd03261 81 M--LFQSGALFDSLTVFENV--AFPLREHTRLSEEEIREI-------------VLEKLEAVGLRGAEDLYPAELSGGMKK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 177 LVELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRL-RTTGVAVVLVEHDVGFVMGQSDRVVVLNLGSVLAEGTPDE 255
Cdd:cd03261 144 RVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLkKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEE 223
|
250
....*....|
gi 521297957 256 IQA--HPAVR 263
Cdd:cd03261 224 LRAsdDPLVR 233
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
21-251 |
8.17e-48 |
|
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: 158.07 E-value: 8.17e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 21 LEVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQLPERRarsGVRRT 100
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERR---NIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 101 FQRAQLYSRLSVEDNVLTAMEWRGGGGGLLADLfaapgrrrreaerreyALSVLAACGLADLRHKPAGALPIGQARLVEL 180
Cdd:cd03259 78 FQDYALFPHLTVAENIAFGLKLRGVPKAEIRAR----------------VRELLELVGLEGLLNRYPHELSGGQQQRVAL 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 521297957 181 ARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRL-RTTGVAVVLVEHDVGFVMGQSDRVVVLNLGSVLAEG 251
Cdd:cd03259 142 ARALAREPSLLLLDEPLSALDAKLREELREELKELqRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
21-247 |
4.26e-47 |
|
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: 154.86 E-value: 4.26e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 21 LEVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQLPERRARSGVrrT 100
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGY--L 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 101 FQRAQLYSRLSVEDNVLtamewrggggglladlfaapgrrrreaerreyalsvlaacgladlrhkpagaLPIGQARLVEL 180
Cdd:cd03230 79 PEEPSLYENLTVRENLK----------------------------------------------------LSGGMKQRLAL 106
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 521297957 181 ARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLRTTGVAVVLVEHDVGFVMGQSDRVVVLNLGSV 247
Cdd:cd03230 107 AQALLHDPELLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
17-256 |
1.09e-46 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 162.50 E-value: 1.09e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 17 TEPALEVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQLPERRARSG 96
Cdd:COG1129 1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 97 VRRTFQRAQLYSRLSVEDNVLTAMEWRGGGGGLLADLFAApgrrrreaerreyALSVLAACGLA-DLRhKPAGALPIGQA 175
Cdd:COG1129 81 IAIIHQELNLVPNLSVAENIFLGREPRRGGLIDWRAMRRR-------------ARELLARLGLDiDPD-TPVGDLSVAQQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 176 RLVELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLRTTGVAVVLVEHDVGFVMGQSDRVVVLNLGSVLAEG---- 251
Cdd:COG1129 147 QLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGpvae 226
|
....*.
gi 521297957 252 -TPDEI 256
Cdd:COG1129 227 lTEDEL 232
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
22-245 |
2.52e-46 |
|
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: 154.16 E-value: 2.52e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 22 EVRHVTKRYGGLT--AISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVT-RQLPERRARSGVr 98
Cdd:cd03225 1 ELKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTkLSLKELRRKVGL- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 99 rTFQ--RAQLySRLSVEDNVLtamewrggggglladlFAAPGRRRREAERREYALSVLAACGLADLRHKPAGALPIGQAR 176
Cdd:cd03225 80 -VFQnpDDQF-FGPTVEEEVA----------------FGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQ 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521297957 177 LVELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLRTTGVAVVLVEHDVGFVMGQSDRVVVLNLG 245
Cdd:cd03225 142 RVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
18-250 |
3.77e-46 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 154.05 E-value: 3.77e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 18 EPALEVRHVTKRYG----GLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRqLPERrA 93
Cdd:COG1136 2 SPLLELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISS-LSER-E 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 94 RSGVRRT-----FQRAQLYSRLSVEDNVLTAMEWRGGGGGLLADLfaapgrrrreaerreyALSVLAACGLADLRHKPAG 168
Cdd:COG1136 80 LARLRRRhigfvFQFFNLLPELTALENVALPLLLAGVSRKERRER----------------ARELLERVGLGDRLDHRPS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 169 ALPIGQARLVELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRL-RTTGVAVVLVEHDVgFVMGQSDRVVVLNLGSV 247
Cdd:COG1136 144 QLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELnRELGTTIVMVTHDP-ELAARADRVIRLRDGRI 222
|
...
gi 521297957 248 LAE 250
Cdd:COG1136 223 VSD 225
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
21-268 |
1.53e-45 |
|
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: 152.78 E-value: 1.53e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 21 LEVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQLPERRarsGVRRT 100
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKR---PVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 101 FQRAQLYSRLSVEDNVLTAMEWRGGGGGLLADLFAApgrrrreaerreyalsVLAACGLADLRHKPAGALPIGQARLVEL 180
Cdd:cd03300 78 FQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAE----------------ALDLVQLEGYANRKPSQLSGGQQQRVAI 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 181 ARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRL-RTTGVAVVLVEHDVGFVMGQSDRVVVLNLGSVLAEGTPDEIQAH 259
Cdd:cd03300 142 ARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLqKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEE 221
|
250
....*....|.
gi 521297957 260 PAVR--AAYLG 268
Cdd:cd03300 222 PANRfvADFIG 232
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
21-250 |
3.25e-45 |
|
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: 149.50 E-value: 3.25e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 21 LEVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQLPERRARSGVRRT 100
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 101 FQraqlysrlsvednvltamewrggggglladlfaapgrrrreaerreyalsvlaacgladlrhkpagaLPIGQARLVEL 180
Cdd:cd03216 81 YQ-------------------------------------------------------------------LSVGERQMVEI 93
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 181 ARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLRTTGVAVVLVEHDVGFVMGQSDRVVVLNLGSVLAE 250
Cdd:cd03216 94 ARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
22-251 |
3.40e-45 |
|
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: 150.28 E-value: 3.40e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 22 EVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQLPERRARsgvrrtf 101
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELAR------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 102 qraqlysRLSVednVLTAMEwrggggglladlfaapgrrrreaerreyalsvlaACGLADLRHKPAGALPIGQARLVELA 181
Cdd:cd03214 74 -------KIAY---VPQALE----------------------------------LLGLAHLADRPFNELSGGERQRVLLA 109
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 521297957 182 RAIADRPRLLLLDEPTSGLS-AHETELFgEQIQRL-RTTGVAVVLVEHDVGFVMGQSDRVVVLNLGSVLAEG 251
Cdd:cd03214 110 RALAQEPPILLLDEPTSHLDiAHQIELL-ELLRRLaRERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
21-257 |
8.70e-45 |
|
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: 150.60 E-value: 8.70e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 21 LEVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQLPERRARSGVrrT 100
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGI--V 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 101 FQRAQLysrlsveDNVLTAMEwrggGGGLLADLFAAPGRRRREAerreyALSVLAACGLADLRHKPAGALPIGQARLVEL 180
Cdd:cd03265 79 FQDLSV-------DDELTGWE----NLYIHARLYGVPGAERRER-----IDELLDFVGLLEAADRLVKTYSGGMRRRLEI 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521297957 181 ARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRL-RTTGVAVVLVEHDVGFVMGQSDRVVVLNLGSVLAEGTPDEIQ 257
Cdd:cd03265 143 ARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLkEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
21-242 |
9.46e-45 |
|
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: 150.33 E-value: 9.46e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 21 LEVRHVTKRYGG----LTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQLPERRARsg 96
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAA-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 97 VRRT-----FQRAQLYSRLSVEDNVLTAMEWRGGGGGLLADlfaapgrrrreaerreYALSVLAACGLADLRHKPAGALP 171
Cdd:cd03255 79 FRRRhigfvFQSFNLLPDLTALENVELPLLLAGVPKKERRE----------------RAEELLERVGLGDRLNHYPSELS 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 521297957 172 IGQARLVELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRL-RTTGVAVVLVEHDVGFVmGQSDRVVVL 242
Cdd:cd03255 143 GGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELnKEAGTTIVVVTHDPELA-EYADRIIEL 213
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
21-245 |
1.17e-44 |
|
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: 148.87 E-value: 1.17e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 21 LEVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTR---QLPERRARSGV 97
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDledELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 98 rrTFQRAQLYSRLSVEDNVltamewrggggglladlfaapgrrrreaerrEYALSvlaacGladlrhkpagalpiGQARL 177
Cdd:cd03229 81 --VFQDFALFPHLTVLENI-------------------------------ALGLS-----G--------------GQQQR 108
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521297957 178 VELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLRTT-GVAVVLVEHDVGFVMGQSDRVVVLNLG 245
Cdd:cd03229 109 VALARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
20-258 |
2.53e-44 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 151.41 E-value: 2.53e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 20 ALEVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQ-------LPERR 92
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEdrrrigyLPEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 93 ArsgvrrtfqraqLYSRLSVEDNVL-----------TAMEWrggggglladlfaapgrrrreaerreyALSVLAACGLAD 161
Cdd:COG4152 81 G------------LYPKMKVGEQLVylarlkglskaEAKRR---------------------------ADEWLERLGLGD 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 162 LRHKPAGALPIGQARLVELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLRTTGVAVVLVEHDVGFVMGQSDRVVV 241
Cdd:COG4152 122 RANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVI 201
|
250
....*....|....*..
gi 521297957 242 LNLGSVLAEGTPDEIQA 258
Cdd:COG4152 202 INKGRKVLSGSVDEIRR 218
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
16-242 |
5.77e-44 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 149.47 E-value: 5.77e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 16 TTEPALEVRHVTKRY----GGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQLPER 91
Cdd:COG1116 3 AAAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 92 rarsGVrrTFQRAQLYSRLSVEDNVLTAMEWRGGGGGLLADLfaapgrrrreaerreyALSVLAACGLADLRHKPAGALP 171
Cdd:COG1116 83 ----GV--VFQEPALLPWLTVLDNVALGLELRGVPKAERRER----------------ARELLELVGLAGFEDAYPHQLS 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 521297957 172 IGQARLVELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRL-RTTGVAVVLVEHDVG---FVmgqSDRVVVL 242
Cdd:COG1116 141 GGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLwQETGKTVLFVTHDVDeavFL---ADRVVVL 212
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
21-243 |
1.30e-43 |
|
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: 147.23 E-value: 1.30e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 21 LEVRHVTKRYGG----LTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQLPERrarsG 96
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPDR----G 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 97 VrrTFQRAQLYSRLSVEDNVLTAMEWRGGGGGLLADlfaapgrrrreaerreYALSVLAACGLADLRHKPAGALPIGQAR 176
Cdd:cd03293 77 Y--VFQQDALLPWLTVLDNVALGLELQGVPKAEARE----------------RAEELLELVGLSGFENAYPHQLSGGMRQ 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521297957 177 LVELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRL-RTTGVAVVLVEHDVGFVMGQSDRVVVLN 243
Cdd:cd03293 139 RVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIwRETGKTVLLVTHDIDEAVFLADRVVVLS 206
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
21-259 |
1.65e-43 |
|
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: 147.71 E-value: 1.65e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 21 LEVRHVTKRYGGLT-AISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQLP--ERRARSGV 97
Cdd:cd03256 1 IEVENLSKTYPNGKkALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGkaLRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 98 RRTFQRAQLYSRLSVEDNVLTAMEWRGGGGGLLADLFaapgrrrrEAERREYALSVLAACGLADLRHKPAGALPIGQARL 177
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGRLGRRSTWRSLFGLF--------PKEEKQRALAALERVGLLDKAYQRADQLSGGQQQR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 178 VELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLRTT-GVAVVLVEHDVGFVMGQSDRVVVLNLGSVLAEGTPDEI 256
Cdd:cd03256 153 VAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
|
...
gi 521297957 257 QAH 259
Cdd:cd03256 233 TDE 235
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
21-260 |
2.33e-43 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 147.06 E-value: 2.33e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 21 LEVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVT---RQLPERRARSG- 96
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTdskKDINKLRRKVGm 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 97 VrrtFQRAQLYSRLSVEDNVLTAMEWRGGGGGLLADlfaapgrrrreaerrEYALSVLAACGLADLRHKPAGALPIGQAR 176
Cdd:COG1126 82 V---FQQFNLFPHLTVLENVTLAPIKVKKMSKAEAE---------------ERAMELLERVGLADKADAYPAQLSGGQQQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 177 LVELARAIADRPRLLLLDEPTSGLsahETELFGE---QIQRLRTTGVAVVLVEHDVGFVMGQSDRVVVLNLGSVLAEGTP 253
Cdd:COG1126 144 RVAIARALAMEPKVMLFDEPTSAL---DPELVGEvldVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPP 220
|
....*..
gi 521297957 254 DEIQAHP 260
Cdd:COG1126 221 EEFFENP 227
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
22-243 |
2.66e-43 |
|
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: 146.52 E-value: 2.66e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 22 EVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQ------LPERRars 95
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKErkrigyVPQRR--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 96 GVRRTFqraqlysRLSVEDNVLTAM--EWRGGGGGLLADlFAApgrrrreaerreyALSVLAACGLADLRHKPAGALPIG 173
Cdd:cd03235 78 SIDRDF-------PISVRDVVLMGLygHKGLFRRLSKAD-KAK-------------VDEALERVGLSELADRQIGELSGG 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 174 QARLVELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLRTTGVAVVLVEHDVGFVMGQSDRVVVLN 243
Cdd:cd03235 137 QQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLN 206
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
5-260 |
1.07e-42 |
|
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: 151.98 E-value: 1.07e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 5 ATSTDSSVAGVTTEPALEVRHVTKRY-----GGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFL 79
Cdd:COG1123 245 AARGRAAPAAAAAEPLLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILF 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 80 DGVDVTRQLPERRARsgVRRTFQ------RAQLYSRLSVEDNVLTAMewRGGGGGLLADLFAApgrrrreaerreyALSV 153
Cdd:COG1123 325 DGKDLTKLSRRSLRE--LRRRVQmvfqdpYSSLNPRMTVGDIIAEPL--RLHGLLSRAERRER-------------VAEL 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 154 LAACGL-ADLRHKPAGALPIGQARLVELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRL-RTTGVAVVLVEHDVGF 231
Cdd:COG1123 388 LERVGLpPDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLqRELGLTYLFISHDLAV 467
|
250 260
....*....|....*....|....*....
gi 521297957 232 VMGQSDRVVVLNLGSVLAEGTPDEIQAHP 260
Cdd:COG1123 468 VRYIADRVAVMYDGRIVEDGPTEEVFANP 496
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
20-261 |
1.62e-42 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 148.30 E-value: 1.62e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 20 ALEVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQLPERRarsGVRR 99
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDR---NIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 100 TFQRAQLYSRLSVEDNVLTAMEWRGGGGGLLADLfaapgrrrreaerreyALSVLAACGLADLRHKPAGALPIGQARLVE 179
Cdd:COG3839 80 VFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRR----------------VREAAELLGLEDLLDRKPKQLSGGQRQRVA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 180 LARAIADRPRLLLLDEPTSGLSAH-----ETELFGEQiQRLRTTgvaVVLVEHDVGFVMGQSDRVVVLNLGSVLAEGTPD 254
Cdd:COG3839 144 LGRALVREPKVFLLDEPLSNLDAKlrvemRAEIKRLH-RRLGTT---TIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPE 219
|
....*..
gi 521297957 255 EIQAHPA 261
Cdd:COG3839 220 ELYDRPA 226
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
19-228 |
4.26e-42 |
|
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: 143.00 E-value: 4.26e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 19 PALEVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQLPERRARSGVr 98
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAY- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 99 rTFQRAQLYSRLSVEDNVltamewrgggggllaDLFAApgrRRREAERREYALSVLAACGLADLRHKPAGALPIGQARLV 178
Cdd:COG4133 80 -LGHADGLKPELTVRENL---------------RFWAA---LYGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRV 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 521297957 179 ELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLRTTGVAVVLVEHD 228
Cdd:COG4133 141 ALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQ 190
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
21-256 |
3.21e-41 |
|
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: 141.10 E-value: 3.21e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 21 LEVRHVTKRYGGL--TAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQLPERRARSGVr 98
Cdd:cd03263 1 LQIRNLTKTYKKGtkPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGY- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 99 rTFQRAQLYSRLSVEDNVLtamewrggggglladLFA-APGRRRREAERReyALSVLAACGLADLRHKPAGALPIGQARL 177
Cdd:cd03263 80 -CPQFDALFDELTVREHLR---------------FYArLKGLPKSEIKEE--VELLLRVLGLTDKANKRARTLSGGMKRK 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521297957 178 VELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLRtTGVAVVLVEHDVGFVMGQSDRVVVLNLGSVLAEGTPDEI 256
Cdd:cd03263 142 LSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVR-KGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
21-251 |
4.96e-41 |
|
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: 140.43 E-value: 4.96e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 21 LEVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRqLPERRARSGVrrT 100
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQK-NIEALRRIGA--L 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 101 FQRAQLYSRLSVEDNVLTAmewrgggggllADLFAAPGRRRReaerreyalSVLAACGLADLRHKPAGALPIGQARLVEL 180
Cdd:cd03268 78 IEAPGFYPNLTARENLRLL-----------ARLLGIRKKRID---------EVLDVVGLKDSAKKKVKGFSLGMKQRLGI 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 521297957 181 ARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLRTTGVAVVLVEHDVGFVMGQSDRVVVLNLGSVLAEG 251
Cdd:cd03268 138 ALALLGNPDLLILDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
20-261 |
1.37e-40 |
|
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: 140.17 E-value: 1.37e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 20 ALEVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQLPERRarsGVRR 99
Cdd:cd03296 2 SIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQER---NVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 100 TFQRAQLYSRLSVEDNVLTAMEWRGGGGGLLADLFAAPgrrrreaerreyALSVLAACGLADLRHKPAGALPIGQARLVE 179
Cdd:cd03296 79 VFQHYALFRHMTVFDNVAFGLRVKPRSERPPEAEIRAK------------VHELLKLVQLDWLADRYPAQLSGGQRQRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 180 LARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLR-TTGVAVVLVEHDVGFVMGQSDRVVVLNLGSVLAEGTPDEIQA 258
Cdd:cd03296 147 LARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHdELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYD 226
|
...
gi 521297957 259 HPA 261
Cdd:cd03296 227 HPA 229
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
21-266 |
4.88e-40 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 141.82 E-value: 4.88e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 21 LEVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQLPERRarsgvRRT 100
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLPPRE-----RRV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 101 ---FQRAQLYSRLSVEDNVLTAMEWRGGGGGLLADLfaapgrrrreaerreyALSVLAACGLADL-RHKPA---GalpiG 173
Cdd:COG1118 78 gfvFQHYALFPHMTVAENIAFGLRVRPPSKAEIRAR----------------VEELLELVQLEGLaDRYPSqlsG----G 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 174 QARLVELARAIADRPRLLLLDEPTSGLSAH-----ETELFgeqiQRLRTTGVAVVLVEHDVGFVMGQSDRVVVLNLGSVL 248
Cdd:COG1118 138 QRQRVALARALAVEPEVLLLDEPFGALDAKvrkelRRWLR----RLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIE 213
|
250
....*....|....*...
gi 521297957 249 AEGTPDEIQAHPAVRAAY 266
Cdd:COG1118 214 QVGTPDEVYDRPATPFVA 231
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
16-255 |
1.78e-39 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 143.24 E-value: 1.78e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 16 TTEPALEVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQLPERRARS 95
Cdd:COG3845 1 MMPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAIAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 96 GVRRTFQRAQLYSRLSVEDNVLTAMEWRGGGGGLLADLFAApgrrrreaerreyALSVLAACGLA-DLrHKPAGALPIGQ 174
Cdd:COG3845 81 GIGMVHQHFMLVPNLTVAENIVLGLEPTKGGRLDRKAARAR-------------IRELSERYGLDvDP-DAKVEDLSVGE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 175 ARLVELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLRTTGVAVVLVEHDVGFVMGQSDRVVVLNLGSVLAEGTPD 254
Cdd:COG3845 147 QQRVEILKALYRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTA 226
|
.
gi 521297957 255 E 255
Cdd:COG3845 227 E 227
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
21-268 |
3.93e-39 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 136.56 E-value: 3.93e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 21 LEVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQLPERRARSGVRRT 100
Cdd:PRK10895 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 101 FQRAQLYSRLSVEDNVLTAMEWRGggggllaDLfaapgrrrREAERREYALSVLAACGLADLRHKPAGALPIGQARLVEL 180
Cdd:PRK10895 84 PQEASIFRRLSVYDNLMAVLQIRD-------DL--------SAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 181 ARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLRTTGVAVVLVEHDVGFVMGQSDRVVVLNLGSVLAEGTPDEIQAHP 260
Cdd:PRK10895 149 ARALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDE 228
|
....*...
gi 521297957 261 AVRAAYLG 268
Cdd:PRK10895 229 HVKRVYLG 236
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
18-256 |
8.72e-39 |
|
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: 135.60 E-value: 8.72e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 18 EPALEVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGA---VF---LDGVDVtrqlPER 91
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdvrLFgerRGGEDV----WEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 92 RARSGVRRTFQRAQLYSRLSVEDNVLTAmewrggggglladLFAAPGR-RRREAERREYALSVLAACGLADLRHKPAGAL 170
Cdd:COG1119 77 RKRIGLVSPALQLRFPRDETVLDVVLSG-------------FFDSIGLyREPTDEQRERARELLELLGLAHLADRPFGTL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 171 PIGQARLVELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRL-RTTGVAVVLVEHDV-----GFvmgqsDRVVVLNL 244
Cdd:COG1119 144 SQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLaAEGAPTLVLVTHHVeeippGI-----THVLLLKD 218
|
250
....*....|..
gi 521297957 245 GSVLAEGTPDEI 256
Cdd:COG1119 219 GRVVAAGPKEEV 230
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
21-251 |
1.04e-38 |
|
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: 134.33 E-value: 1.04e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 21 LEVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQ-------LPERRA 93
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAarnrigyLPEERG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 94 rsgvrrtfqraqLYSRLSVEDNVLtamewrgggggLLADLFAAPgrrrrEAERREYALSVLAACGLADLRHKPAGALPIG 173
Cdd:cd03269 81 ------------LYPKMKVIDQLV-----------YLAQLKGLK-----KEEARRRIDEWLERLELSEYANKRVEELSKG 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521297957 174 QARLVELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLRTTGVAVVLVEHDVGFVMGQSDRVVVLNLGSVLAEG 251
Cdd:cd03269 133 NQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
21-251 |
3.57e-38 |
|
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: 133.09 E-value: 3.57e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 21 LEVRHVTKRYGGLTAISDVSLRVDPGeVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQLPERRARSGvrrt 100
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIG---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 101 F--QRAQLYSRLSVEDnVLTAMEWRGGGGGLLADlfaapgrrrreaerrEYALSVLAACGLADLRHKPAGALPIGQARLV 178
Cdd:cd03264 76 YlpQEFGVYPNFTVRE-FLDYIAWLKGIPSKEVK---------------ARVDEVLELVNLGDRAKKKIGSLSGGMRRRV 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 521297957 179 ELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLRTTGVaVVLVEHDVGFVMGQSDRVVVLNLGSVLAEG 251
Cdd:cd03264 140 GIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRI-VILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
21-245 |
3.86e-38 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 133.04 E-value: 3.86e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 21 LEVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQLPE-RRARSGVRR 99
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNiNELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 100 TFQRAQLYSRLSVEDNVLTAMEWRGGGGGLLADlfaapgrrrreaerrEYALSVLAACGLADLRHKPAGALPIGQARLVE 179
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPIKVKGMSKAEAE---------------ERALELLEKVGLADKADAYPAQLSGGQQQRVA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521297957 180 LARAIADRPRLLLLDEPTSGLsahETELFGE---QIQRLRTTGVAVVLVEHDVGFVMGQSDRVVVLNLG 245
Cdd:cd03262 146 IARALAMNPKVMLFDEPTSAL---DPELVGEvldVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDG 211
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
21-260 |
1.26e-37 |
|
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: 132.32 E-value: 1.26e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 21 LEVRHVTKRYGG----LTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVT----RQLPERR 92
Cdd:cd03258 2 IELKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTllsgKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 93 ARSGVrrTFQRAQLYSRLSVEDNVLTAME-WRGGGGGLLADlfaapgrrrreaerreyALSVLAACGLADLRHKPAGALP 171
Cdd:cd03258 82 RRIGM--IFQHFNLLSSRTVFENVALPLEiAGVPKAEIEER-----------------VLELLELVGLEDKADAYPAQLS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 172 IGQARLVELARAIADRPRLLLLDEPTSGLSAHETelfgEQIQRL-----RTTGVAVVLVEHDVGFVMGQSDRVVVLNLGS 246
Cdd:cd03258 143 GGQKQRVGIARALANNPKVLLCDEATSALDPETT----QSILALlrdinRELGLTIVLITHEMEVVKRICDRVAVMEKGE 218
|
250
....*....|....
gi 521297957 247 VLAEGTPDEIQAHP 260
Cdd:cd03258 219 VVEEGTVEEVFANP 232
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
22-245 |
2.58e-37 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 129.29 E-value: 2.58e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 22 EVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTrQLPERRARSGVRRTF 101
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIA-KLPLEELRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 102 QraqlysrLSVednvltamewrggggglladlfaapgrrrreaerreyalsvlaacgladlrhkpagalpiGQARLVELA 181
Cdd:cd00267 80 Q-------LSG------------------------------------------------------------GQRQRVALA 92
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521297957 182 RAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLRTTGVAVVLVEHDVGFVMGQSDRVVVLNLG 245
Cdd:cd00267 93 RALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
21-266 |
3.64e-37 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 131.78 E-value: 3.64e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 21 LEVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQLPERRARsgvrrt 100
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELAR------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 101 fQRAQL--YSRLS----VEDNVLtamewrggggglladLFAAPGRRRREAERREyALSVLAACGLADLRHKPAGALPIG- 173
Cdd:COG4559 76 -RRAVLpqHSSLAfpftVEEVVA---------------LGRAPHGSSAAQDRQI-VREALALVGLAHLAGRSYQTLSGGe 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 174 QARlVELARAIA-------DRPRLLLLDEPTSGLS-AHETELFgEQIQRLRTTGVAVVLVEHDVGFVMGQSDRVVVLNLG 245
Cdd:COG4559 139 QQR-VQLARVLAqlwepvdGGPRWLFLDEPTSALDlAHQHAVL-RLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQG 216
|
250 260
....*....|....*....|.
gi 521297957 246 SVLAEGTPDEIQAHPAVRAAY 266
Cdd:COG4559 217 RLVAQGTPEEVLTDELLERVY 237
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
21-247 |
3.74e-37 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 130.56 E-value: 3.74e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 21 LEVRHVTKRY-GGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRqLPeRRARSGVRR 99
Cdd:COG2884 2 IRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSR-LK-RREIPYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 100 T----FQRAQLYSRLSVEDNVLTAMEWRGGGGGLLADLfaapgrrrreaerreyALSVLAACGLADLRHKPAGALPIGQA 175
Cdd:COG2884 80 RigvvFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRR----------------VREVLDLVGLSDKAKALPHELSGGEQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 521297957 176 RLVELARAIADRPRLLLLDEPTSGLSaHET-----ELFgEQIQRLrttGVAVVLVEHDVGFVMGQSDRVVVLNLGSV 247
Cdd:COG2884 144 QRVAIARALVNRPELLLADEPTGNLD-PETsweimELL-EEINRR---GTTVLIATHDLELVDRMPKRVLELEDGRL 215
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
15-261 |
7.86e-37 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 133.92 E-value: 7.86e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 15 VTTEPALEVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQLPERRAr 94
Cdd:PRK09452 9 SSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRH- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 95 sgVRRTFQRAQLYSRLSVEDNVltamewrggggglladlfaAPGRRRREAERREYALSVLAACGLADL----RHKPAgAL 170
Cdd:PRK09452 88 --VNTVFQSYALFPHMTVFENV-------------------AFGLRMQKTPAAEITPRVMEALRMVQLeefaQRKPH-QL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 171 PIGQARLVELARAIADRPRLLLLDEPTSGLS-----AHETELfgEQIQrlRTTGVAVVLVEHDVGFVMGQSDRVVVLNLG 245
Cdd:PRK09452 146 SGGQQQRVAIARAVVNKPKVLLLDESLSALDyklrkQMQNEL--KALQ--RKLGITFVFVTHDQEEALTMSDRIVVMRDG 221
|
250
....*....|....*.
gi 521297957 246 SVLAEGTPDEIQAHPA 261
Cdd:PRK09452 222 RIEQDGTPREIYEEPK 237
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
18-265 |
9.03e-37 |
|
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: 136.19 E-value: 9.03e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 18 EPALEVRHVTKRY--GGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPT---SGAVFLDGVDVTRQLPERR 92
Cdd:COG1123 2 TPLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 93 ARSgVRRTFQ--RAQLySRLSVEDNVLTAMEWRGGGGGLLADLfaapgrrrreaerreyALSVLAACGLADLRHKPAGAL 170
Cdd:COG1123 82 GRR-IGMVFQdpMTQL-NPVTVGDQIAEALENLGLSRAEARAR----------------VLELLEAVGLERRLDRYPHQL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 171 PIGQARLVELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRL-RTTGVAVVLVEHDVGFVMGQSDRVVVLNLGSVLA 249
Cdd:COG1123 144 SGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELqRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVE 223
|
250
....*....|....*.
gi 521297957 250 EGTPDEIQAHPAVRAA 265
Cdd:COG1123 224 DGPPEEILAAPQALAA 239
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
21-261 |
1.96e-36 |
|
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: 129.34 E-value: 1.96e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 21 LEVRHVTKRYGGLT-AISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQLPERRARSgVRR 99
Cdd:cd03295 1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRK-IGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 100 TFQRAQLYSRLSVEDN---VLTAMEWRGGGGGLLADlfaapgrrrreaerreyalSVLAACGL--ADLRHKPAGALPIGQ 174
Cdd:cd03295 80 VIQQIGLFPHMTVEENialVPKLLKWPKEKIRERAD-------------------ELLALVGLdpAEFADRYPHELSGGQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 175 ARLVELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRL-RTTGVAVVLVEHDV--GFVMGqsDRVVVLNLGSVLAEG 251
Cdd:cd03295 141 QQRVGVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLqQELGKTIVFVTHDIdeAFRLA--DRIAIMKNGEIVQVG 218
|
250
....*....|
gi 521297957 252 TPDEIQAHPA 261
Cdd:cd03295 219 TPDEILRSPA 228
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
21-243 |
4.24e-36 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 127.62 E-value: 4.24e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 21 LEVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQLPERrARSGVRRT 100
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPE-WRRQVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 101 FQRAQLYsrlsvEDNVltamewrgggggllADLFAAPGRRRREAERREYALSVLAACGL-ADLRHKPAGALPIGQARLVE 179
Cdd:COG4619 80 PQEPALW-----GGTV--------------RDNLPFPFQLRERKFDRERALELLERLGLpPDILDKPVERLSGGERQRLA 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 521297957 180 LARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLRT-TGVAVVLVEHDVGFVMGQSDRVVVLN 243
Cdd:COG4619 141 LIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAeEGRAVLWVSHDPEQIERVADRVLTLE 205
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
21-251 |
4.90e-36 |
|
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: 127.87 E-value: 4.90e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 21 LEVRHVTKRY----GGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQLPERRARSG 96
Cdd:cd03266 2 ITADALTKRFrdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 97 VrrTFQRAQLYSRLSVEDNVLtamewrgggggLLADLFAAPGRRRREaerreyALSVLAA-CGLADLRHKPAGALPIGQA 175
Cdd:cd03266 82 F--VSDSTGLYDRLTARENLE-----------YFAGLYGLKGDELTA------RLEELADrLGMEELLDRRVGGFSTGMR 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 521297957 176 RLVELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLRTTGVAVVLVEHDVGFVMGQSDRVVVLNLGSVLAEG 251
Cdd:cd03266 143 QKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
21-256 |
5.36e-36 |
|
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: 128.07 E-value: 5.36e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 21 LEVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTP-----PTSGAVFLDGVDVtrqLPERRARS 95
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDI---YDLDVDVL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 96 GVRRT----FQRAQLYsRLSVEDNVltAMEWRGGGGGLLADLFAApgrrrreaerreyALSVLAACGLAD--LRHKPAGA 169
Cdd:cd03260 78 ELRRRvgmvFQKPNPF-PGSIYDNV--AYGLRLHGIKLKEELDER-------------VEEALRKAALWDevKDRLHALG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 170 LPIGQARLVELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLRTTgVAVVLVEHDvgfvMGQ----SDRVVVLNLG 245
Cdd:cd03260 142 LSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHN----MQQaarvADRTAFLLNG 216
|
250
....*....|.
gi 521297957 246 SVLAEGTPDEI 256
Cdd:cd03260 217 RLVEFGPTEQI 227
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
15-255 |
6.79e-36 |
|
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: 127.94 E-value: 6.79e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 15 VTTEPALEVRHVTKRYGG----LTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTrQLPE 90
Cdd:COG4181 3 SSSAPIIELRGLTKTVGTgageLTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLF-ALDE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 91 RrARSGVRR-----TFQRAQLYSRLSVEDNVLTAMEWRGGgggllADLFAApgrrrreaerreyALSVLAACGLAD-LRH 164
Cdd:COG4181 82 D-ARARLRArhvgfVFQSFQLLPTLTALENVMLPLELAGR-----RDARAR-------------ARALLERVGLGHrLDH 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 165 KPAGaLPIGQARLVELARAIADRPRLLLLDEPTSGLSAHEtelfGEQIQRL-----RTTGVAVVLVEHDVGfVMGQSDRV 239
Cdd:COG4181 143 YPAQ-LSGGEQQRVALARAFATEPAILFADEPTGNLDAAT----GEQIIDLlfelnRERGTTLVLVTHDPA-LAARCDRV 216
|
250
....*....|....*.
gi 521297957 240 VVLNLGSVLAEGTPDE 255
Cdd:COG4181 217 LRLRAGRLVEDTAATA 232
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
20-264 |
1.43e-35 |
|
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: 127.23 E-value: 1.43e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 20 ALEVRHVTKRYG----GLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQLPERRARS 95
Cdd:COG1124 1 MLEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 96 gVRRTFQ--RAQLYSRLSVEDnvltamewrggggglladLFAAPGRRRREAERREYALSVLAACGL-ADLRHKPAGALPI 172
Cdd:COG1124 81 -VQMVFQdpYASLHPRHTVDR------------------ILAEPLRIHGLPDREERIAELLEQVGLpPSFLDRYPHQLSG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 173 GQARLVELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLR-TTGVAVVLVEHDVGFVMGQSDRVVVLNLGSVLAEG 251
Cdd:COG1124 142 GQRQRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLReERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEEL 221
|
250
....*....|....*.
gi 521297957 252 TPDEIQA---HPAVRA 264
Cdd:COG1124 222 TVADLLAgpkHPYTRE 237
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
22-256 |
1.75e-35 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 127.12 E-value: 1.75e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 22 EVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQLPERRAR--SGVRr 99
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKrlAILR- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 100 tfQRAQLYSRLSVEDNV-----------LTAMEWRGGGGglladlfaapgrrrreaerreyALSVLaacGLADLRHKPAG 168
Cdd:COG4604 82 --QENHINSRLTVRELVafgrfpyskgrLTAEDREIIDE----------------------AIAYL---DLEDLADRYLD 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 169 ALPIGQARLVELARAIADRPRLLLLDEPTSGLS-AHETELFGeQIQRL-RTTGVAVVLVEHDVGFVMGQSDRVVVLNLGS 246
Cdd:COG4604 135 ELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDmKHSVQMMK-LLRRLaDELGKTVVIVLHDINFASCYADHIVAMKDGR 213
|
250
....*....|
gi 521297957 247 VLAEGTPDEI 256
Cdd:COG4604 214 VVAQGTPEEI 223
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
19-266 |
2.74e-35 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 126.81 E-value: 2.74e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 19 PALEVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQLPERRARS-GV 97
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRrAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 98 RRtfQRAQLYSRLSVEDNV-LTAMEWRGGGGGLLADLFAApgrrrreaerreyalsvLAACGLADLRHKPAGALPIG-QA 175
Cdd:PRK13548 81 LP--QHSSLSFPFTVEEVVaMGRAPHGLSRAEDDALVAAA-----------------LAQVDLAHLAGRDYPQLSGGeQQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 176 RlVELARAIA------DRPRLLLLDEPTSGLS-AHETELFGEQIQRLRTTGVAVVLVEHDVGFVMGQSDRVVVLNLGSVL 248
Cdd:PRK13548 142 R-VQLARVLAqlwepdGPPRWLLLDEPTSALDlAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLV 220
|
250
....*....|....*...
gi 521297957 249 AEGTPDEIQAHPAVRAAY 266
Cdd:PRK13548 221 ADGTPAEVLTPETLRRVY 238
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
18-259 |
5.95e-35 |
|
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: 132.65 E-value: 5.95e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 18 EPALEVRHVTKRYGGLT--AISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVtRQLP--ERRA 93
Cdd:COG2274 471 KGDIELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDL-RQIDpaSLRR 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 94 RSGVrrTFQRAQLYSRlSVEDNVltamewrggggglladLFAAPGRRRREaerreyalsVLAACGLADL----RHKPAG- 168
Cdd:COG2274 550 QIGV--VLQDVFLFSG-TIRENI----------------TLGDPDATDEE---------IIEAARLAGLhdfiEALPMGy 601
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 169 ---------ALPIGQARLVELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLRtTGVAVVLVEHDVGFVMgQSDRV 239
Cdd:COG2274 602 dtvvgeggsNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLL-KGRTVIIIAHRLSTIR-LADRI 679
|
250 260
....*....|....*....|
gi 521297957 240 VVLNLGSVLAEGTPDEIQAH 259
Cdd:COG2274 680 IVLDKGRIVEDGTHEELLAR 699
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
21-247 |
1.46e-34 |
|
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: 123.90 E-value: 1.46e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 21 LEVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQLPERRarsGVRRT 100
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDR---DIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 101 FQRAQLYSRLSVEDNVLTAMEWRGGGGGLLAdlfaapgrrrreaerrEYALSVLAACGLADLRHKPAGALPIGQARLVEL 180
Cdd:cd03301 78 FQNYALYPHMTVYDNIAFGLKLRKVPKDEID----------------ERVREVAELLQIEHLLDRKPKQLSGGQRQRVAL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521297957 181 ARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRL-RTTGVAVVLVEHDVGFVMGQSDRVVVLNLGSV 247
Cdd:cd03301 142 GRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLqQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
19-268 |
2.31e-34 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 127.26 E-value: 2.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 19 PALEVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQLPERRArsgVR 98
Cdd:PRK11607 18 PLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRP---IN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 99 RTFQRAQLYSRLSVEDNVLTAMEWRGGGGGLLADLFAapgrrrreaerreyalSVLAACGLADLRHKPAGALPIGQARLV 178
Cdd:PRK11607 95 MMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVN----------------EMLGLVHMQEFAKRKPHQLSGGQRQRV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 179 ELARAIADRPRLLLLDEPTSGLSAHETELFG-EQIQRLRTTGVAVVLVEHDVGFVMGQSDRVVVLNLGSVLAEGTPDEIQ 257
Cdd:PRK11607 159 ALARSLAKRPKLLLLDEPMGALDKKLRDRMQlEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIY 238
|
250
....*....|...
gi 521297957 258 AHPAVR--AAYLG 268
Cdd:PRK11607 239 EHPTTRysAEFIG 251
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
19-268 |
1.05e-33 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 122.29 E-value: 1.05e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 19 PALEVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQLPERRARSGVR 98
Cdd:PRK11614 4 VMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 99 RTFQRAQLYSRLSVEDNVltAMEWrggggglladlFAAPGRRRREAERREYALSVLaacgLADLRHKPAGALPIGQARLV 178
Cdd:PRK11614 84 IVPEGRRVFSRMTVEENL--AMGG-----------FFAERDQFQERIKWVYELFPR----LHERRIQRAGTMSGGEQQML 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 179 ELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLRTTGVAVVLVEHDVGFVMGQSDRVVVLNLGSVLAEGTPDEIQA 258
Cdd:PRK11614 147 AIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLA 226
|
250
....*....|
gi 521297957 259 HPAVRAAYLG 268
Cdd:PRK11614 227 NEAVRSAYLG 236
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
21-260 |
2.54e-33 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 123.65 E-value: 2.54e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 21 LEVRHVTKRY----GGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTrQLPERRARsG 96
Cdd:COG1135 2 IELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLT-ALSERELR-A 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 97 VRRT----FQRAQLYSRLSVEDNVLTAMEW----RGGGGGLLADLfaapgrrrreaerreyalsvLAACGLADLRHK-PA 167
Cdd:COG1135 80 ARRKigmiFQHFNLLSSRTVAENVALPLEIagvpKAEIRKRVAEL--------------------LELVGLSDKADAyPS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 168 ---GalpiGQARLVELARAIADRPRLLLLDEPTSGLSAHETelfgEQIQRL-----RTTGVAVVLVEHDVGFVMGQSDRV 239
Cdd:COG1135 140 qlsG----GQKQRVGIARALANNPKVLLCDEATSALDPETT----RSILDLlkdinRELGLTIVLITHEMDVVRRICDRV 211
|
250 260
....*....|....*....|.
gi 521297957 240 VVLNLGSVLAEGTPDEIQAHP 260
Cdd:COG1135 212 AVLENGRIVEQGPVLDVFANP 232
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
36-198 |
5.10e-33 |
|
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: 117.75 E-value: 5.10e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 36 ISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQlPERRARSGVRRTFQRAQLYSRLSVEDN 115
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDD-ERKSLRKEIGYVFQDPQLFPRLTVREN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 116 VltamewrggggglladLFAAPGRRRREAERREYALSVLAACGLADLRHKPAGALPI----GQARLVELARAIADRPRLL 191
Cdd:pfam00005 80 L----------------RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVGERPGtlsgGQRQRVAIARALLTKPKLL 143
|
....*..
gi 521297957 192 LLDEPTS 198
Cdd:pfam00005 144 LLDEPTA 150
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
14-267 |
1.48e-32 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 124.39 E-value: 1.48e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 14 GVTTEPALEVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQLPERRA 93
Cdd:PRK15439 5 DTTAPPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 94 RSGVRRTFQRAQLYSRLSVEDNVLTAMEWRGGGGGLLADLFAAPGrrrreaerreyalsvlaaCGLaDLrHKPAGALPIG 173
Cdd:PRK15439 85 QLGIYLVPQEPLLFPNLSVKENILFGLPKRQASMQKMKQLLAALG------------------CQL-DL-DSSAGSLEVA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 174 QARLVELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLRTTGVAVVLVEHDVGFVMGQSDRVVVLNLGSVLAEGTP 253
Cdd:PRK15439 145 DRQIVEILRGLMRDSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKT 224
|
250 260
....*....|....*....|.
gi 521297957 254 DE------IQA-HPAVRAAYL 267
Cdd:PRK15439 225 ADlstddiIQAiTPAAREKSL 245
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
21-260 |
1.86e-32 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 119.04 E-value: 1.86e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 21 LEVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVT-RQLPERRARSGVRR 99
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdPKVDERLIRQEAGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 100 TFQRAQLYSRLSVEDNVLTA-MEWRGGGGGLLADLfaapgrrrreaerreyALSVLAACGLADLRHKPAGALPIGQARLV 178
Cdd:PRK09493 82 VFQQFYLFPHLTALENVMFGpLRVRGASKEEAEKQ----------------ARELLAKVGLAERAHHYPSELSGGQQQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 179 ELARAIADRPRLLLLDEPTSGLsahETELFGEQI---QRLRTTGVAVVLVEHDVGFVMGQSDRVVVLNLGSVLAEGTPDE 255
Cdd:PRK09493 146 AIARALAVKPKLMLFDEPTSAL---DPELRHEVLkvmQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQV 222
|
....*
gi 521297957 256 IQAHP 260
Cdd:PRK09493 223 LIKNP 227
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
22-247 |
3.92e-32 |
|
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: 117.36 E-value: 3.92e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 22 EVRHVTKRYGGLTAI-SDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQlpERRARSG-VRR 99
Cdd:cd03226 1 RIENISFSYKKGTEIlDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAK--ERRKSIGyVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 100 TFQRaQLYSRlSVEDNVLTAMEwrgggggllaDLFAAPGRrrreaerreyALSVLAACGLADLRHKPAGALPIGQARLVE 179
Cdd:cd03226 79 DVDY-QLFTD-SVREELLLGLK----------ELDAGNEQ----------AETVLKDLDLYALKERHPLSLSGGQKQRLA 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521297957 180 LARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLRTTGVAVVLVEHDVGFVMGQSDRVVVLNLGSV 247
Cdd:cd03226 137 IAAALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
21-245 |
4.00e-32 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 115.94 E-value: 4.00e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 21 LEVRHVTKRYGG--LTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTR-QLPERRARSGV 97
Cdd:cd03228 1 IEFKNVSFSYPGrpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDlDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 98 rrTFQRAQLYSRlSVEDNVLTAmewrggggglladlfaapgrrrreaerreyalsvlaacgladlrhkpagalpiGQARL 177
Cdd:cd03228 81 --VPQDPFLFSG-TIRENILSG-----------------------------------------------------GQRQR 104
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521297957 178 VELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLRtTGVAVVLVEHDVGfVMGQSDRVVVLNLG 245
Cdd:cd03228 105 IAIARALLRDPPILILDEATSALDPETEALILEALRALA-KGKTVIVIAHRLS-TIRDADRIIVLDDG 170
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
21-260 |
4.32e-32 |
|
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: 117.82 E-value: 4.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 21 LEVRHVTKRYGGLTaISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQLPERRARSGVrrt 100
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDISYV--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 101 FQRAQLYSRLSVEDNVLTAMEWRGGGGGLLAdlfaapgrrrreaerrEYALSVLAACGLADLRHKPAGALPIGQARLVEL 180
Cdd:cd03299 77 PQNYALFPHMTVYKNIAYGLKKRKVDKKEIE----------------RKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAI 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 181 ARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLR-TTGVAVVLVEHDVGFVMGQSDRVVVLNLGSVLAEGTPDEIQAH 259
Cdd:cd03299 141 ARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRkEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKK 220
|
.
gi 521297957 260 P 260
Cdd:cd03299 221 P 221
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
17-242 |
2.90e-31 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 120.80 E-value: 2.90e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 17 TEPALEVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTP--PTSGAVFLDGVDVTRQLPERRAR 94
Cdd:PRK13549 2 MEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPhgTYEGEIIFEGEELQASNIRDTER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 95 SGVRRTFQRAQLYSRLSVEDNVLTAMEWRggggglladlfaaPGRRRREAERREYALSVLAACGLADLRHKPAGALPIGQ 174
Cdd:PRK13549 82 AGIAIIHQELALVKELSVLENIFLGNEIT-------------PGGIMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQ 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521297957 175 ARLVELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLRTTGVAVVLVEHDVGFVMGQSDRVVVL 242
Cdd:PRK13549 149 QQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVI 216
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
22-260 |
5.40e-31 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 117.59 E-value: 5.40e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 22 EVRHVTKRYGG----LTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTrQLPE---RRAR 94
Cdd:PRK11153 3 ELKNISKVFPQggrtIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLT-ALSEkelRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 95 SGVRRTFQRAQLYSRLSVEDNVLTAMEwrgGGGGLLADLFAApgrrrreaerreyALSVLAACGLADLRHK-PAgALPIG 173
Cdd:PRK11153 82 RQIGMIFQHFNLLSSRTVFDNVALPLE---LAGTPKAEIKAR-------------VTELLELVGLSDKADRyPA-QLSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 174 QARLVELARAIADRPRLLLLDEPTSGLSAHETelfgEQIQRL-----RTTGVAVVLVEHDVGFVMGQSDRVVVLNLGSVL 248
Cdd:PRK11153 145 QKQRVAIARALASNPKVLLCDEATSALDPATT----RSILELlkdinRELGLTIVLITHEMDVVKRICDRVAVIDAGRLV 220
|
250
....*....|..
gi 521297957 249 AEGTPDEIQAHP 260
Cdd:PRK11153 221 EQGTVSEVFSHP 232
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
5-259 |
5.51e-31 |
|
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: 120.63 E-value: 5.51e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 5 ATSTDSSVAGVTTEPALEVRHVTKRY-GGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVD 83
Cdd:COG4988 321 AAPAGTAPLPAAGPPSIELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVD 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 84 VtRQLPERRARSGVRRTFQRAQLYSrLSVEDNVltamewrggggglladLFAAPGRRRREAerreyaLSVLAACGLAD-L 162
Cdd:COG4988 401 L-SDLDPASWRRQIAWVPQNPYLFA-GTIRENL----------------RLGRPDASDEEL------EAALEAAGLDEfV 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 163 RHKPAG-ALPI---------GQARLVELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLRtTGVAVVLVEHDVGfV 232
Cdd:COG4988 457 AALPDGlDTPLgeggrglsgGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLA-KGRTVILITHRLA-L 534
|
250 260
....*....|....*....|....*..
gi 521297957 233 MGQSDRVVVLNLGSVLAEGTPDEIQAH 259
Cdd:COG4988 535 LAQADRILVLDDGRIVEQGTHEELLAK 561
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
19-265 |
9.79e-31 |
|
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: 117.12 E-value: 9.79e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 19 PALEVRhVTKRYGGLTAisDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDG---VDVTRQL---PERR 92
Cdd:COG4148 1 MMLEVD-FRLRRGGFTL--DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlQDSARGIflpPHRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 93 ARSGVrrtFQRAQLYSRLSVEDNVLTAMeWRGGGGGLLADLfaapgrrrreaerreyaLSVLAACGLADLRHKPAGALPI 172
Cdd:COG4148 78 RIGYV---FQEARLFPHLSVRGNLLYGR-KRAPRAERRISF-----------------DEVVELLGIGHLLDRRPATLSG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 173 GQARLVELARAIADRPRLLLLDEPTSGL-SAHETELFGEqIQRLRT-TGVAVVLVEHDVGFVMGQSDRVVVLNLGSVLAE 250
Cdd:COG4148 137 GERQRVAIGRALLSSPRLLLMDEPLAALdLARKAEILPY-LERLRDeLDIPILYVSHSLDEVARLADHVVLLEQGRVVAS 215
|
250
....*....|....*
gi 521297957 251 GTPDEIQAHPAVRAA 265
Cdd:COG4148 216 GPLAEVLSRPDLLPL 230
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
21-268 |
2.29e-30 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 113.31 E-value: 2.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 21 LEVRHVTKRYGGLTAisDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQLPERRARSGVrrt 100
Cdd:COG3840 2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPVSML--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 101 FQRAQLYSRLSVEDNV---------LTAMEWrgggggllADLFAApgrrrreaerreyalsvLAACGLADLRHKPAGALP 171
Cdd:COG3840 77 FQENNLFPHLTVAQNIglglrpglkLTAEQR--------AQVEQA-----------------LERVGLAGLLDRLPGQLS 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 172 IGQARLVELARA-IADRPrLLLLDEPTSGLS-AHETELFGEQIQRLRTTGVAVVLVEHDVGFVMGQSDRVVVLNLGSVLA 249
Cdd:COG3840 132 GGQRQRVALARClVRKRP-ILLLDEPFSALDpALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAA 210
|
250 260
....*....|....*....|.
gi 521297957 250 EGTPDEIQAH--PAVRAAYLG 268
Cdd:COG3840 211 DGPTAALLDGepPPALAAYLG 231
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
21-245 |
7.19e-30 |
|
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: 116.85 E-value: 7.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 21 LEVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTP--PTSGAVFLDGVDVTRQLPERRARSGVR 98
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSPLKASNIRDTERAGIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 99 RTFQRAQLYSRLSVEDNVLTAMEwrggggglladlFAAPGRRRREAERREYALSVLAACGL-ADLRHKPAGALPIGQARL 177
Cdd:TIGR02633 82 IIHQELTLVPELSVAENIFLGNE------------ITLPGGRMAYNAMYLRAKNLLRELQLdADNVTRPVGDYGGGQQQL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521297957 178 VELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLRTTGVAVVLVEHDVGFVMGQSDRVVVLNLG 245
Cdd:TIGR02633 150 VEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDG 217
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
21-247 |
1.34e-29 |
|
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: 110.96 E-value: 1.34e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 21 LEVRHVTKRY-GGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVT----RQLPERRARS 95
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSdlrgRAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 96 GVrrTFQRAQLYSRLSVEDNVLTAMEWRGGGGGLLADLFAApgrrrreaerreyalsVLAACGLADLRHKPAGALPIGQA 175
Cdd:cd03292 81 GV--VFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPA----------------ALELVGLSHKHRALPAELSGGEQ 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 521297957 176 RLVELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLRTTGVAVVLVEHDVGFVMGQSDRVVVLNLGSV 247
Cdd:cd03292 143 QRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
21-251 |
1.55e-29 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 111.06 E-value: 1.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 21 LEVRHVTKRY----GGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTrQLPERRARsg 96
Cdd:cd03257 2 LEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLL-KLSRRLRK-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 97 VRRT-----FQRAQ--LYSRLSVEDNVltamewrgggggllADLFAAPGRRRREAERREYALSVLAACGLADLRhkpAGA 169
Cdd:cd03257 79 IRRKeiqmvFQDPMssLNPRMTIGEQI--------------AEPLRIHGKLSKKEARKEAVLLLLVGVGLPEEV---LNR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 170 LPI----GQARLVELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLRT-TGVAVVLVEHDVGFVMGQSDRVVVLNL 244
Cdd:cd03257 142 YPHelsgGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEeLGLTLLFITHDLGVVAKIADRVAVMYA 221
|
....*..
gi 521297957 245 GSVLAEG 251
Cdd:cd03257 222 GKIVEEG 228
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
21-268 |
1.65e-29 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 114.05 E-value: 1.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 21 LEVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQLPERRARSGVrrt 100
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDICMV--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 101 FQRAQLYSRLSVEDNVltamewrggggglladlfaAPGRRRREAERREYALSVLAACGLADLrhkpAG-------ALPIG 173
Cdd:PRK11432 84 FQSYALFPHMSLGENV-------------------GYGLKMLGVPKEERKQRVKEALELVDL----AGfedryvdQISGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 174 QARLVELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLRTT-GVAVVLVEHDVGFVMGQSDRVVVLNLGSVLAEGT 252
Cdd:PRK11432 141 QQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGS 220
|
250
....*....|....*...
gi 521297957 253 PDEIQAHPAVR--AAYLG 268
Cdd:PRK11432 221 PQELYRQPASRfmASFMG 238
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
17-263 |
1.14e-28 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 113.73 E-value: 1.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 17 TEPALEVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQLPERRARSG 96
Cdd:PRK09700 2 ATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 97 VRRTFQRAQLYSRLSVEDNV------------LTAMEWRGGGGGlladlfaapgrrrreaerreyALSVLAACGL-ADLR 163
Cdd:PRK09700 82 IGIIYQELSVIDELTVLENLyigrhltkkvcgVNIIDWREMRVR---------------------AAMMLLRVGLkVDLD 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 164 HKpAGALPIGQARLVELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLRTTGVAVVLVEHDVGFVMGQSDRVVVLN 243
Cdd:PRK09700 141 EK-VANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMK 219
|
250 260
....*....|....*....|
gi 521297957 244 LGSVLAEGTPDEIQAHPAVR 263
Cdd:PRK09700 220 DGSSVCSGMVSDVSNDDIVR 239
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
20-263 |
1.20e-28 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 111.71 E-value: 1.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 20 ALEVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRqLPERRARSGVrr 99
Cdd:PRK10851 2 SIEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSR-LHARDRKVGF-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 100 TFQRAQLYSRLSVEDNV---LTAMEWRGGGGGLLADlfaapgrrrreaerrEYALSVLAACGLADLRHKPAGALPIGQAR 176
Cdd:PRK10851 79 VFQHYALFRHMTVFDNIafgLTVLPRRERPNAAAIK---------------AKVTQLLEMVQLAHLADRYPAQLSGGQKQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 177 LVELARAIADRPRLLLLDEPTSGLSAH-ETEL--FGEQI-QRLRTTGvavVLVEHDVGFVMGQSDRVVVLNLGSVLAEGT 252
Cdd:PRK10851 144 RVALARALAVEPQILLLDEPFGALDAQvRKELrrWLRQLhEELKFTS---VFVTHDQEEAMEVADRVVVMSQGNIEQAGT 220
|
250
....*....|.
gi 521297957 253 PDEIQAHPAVR 263
Cdd:PRK10851 221 PDQVWREPATR 231
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
21-247 |
2.60e-28 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 106.15 E-value: 2.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 21 LEVRHVTKRYGGLTA--ISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQLP-ERRARSGV 97
Cdd:cd03246 1 LEVENVSFRYPGAEPpvLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPnELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 98 rrTFQRAQLYSRlSVEDNVLTAmewrggggglladlfaapgrrrreaerreyalsvlaacgladlrhkpagalpiGQARL 177
Cdd:cd03246 81 --LPQDDELFSG-SIAENILSG-----------------------------------------------------GQRQR 104
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 178 VELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLRTTGVAVVLVEHDVGfVMGQSDRVVVLNLGSV 247
Cdd:cd03246 105 LGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPE-TLASADRILVLEDGRV 173
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
23-251 |
3.05e-28 |
|
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: 107.80 E-value: 3.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 23 VRHVTKR-YGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQLPERRARSGVrrTF 101
Cdd:cd03267 23 LKSLFKRkYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGV--VF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 102 -QRAQLYSRLSVED--NVLTAMeWRGGGGGLLADLfaapgrrrreaerreYALSVLAACGlaDLRHKPAGALPIGQARLV 178
Cdd:cd03267 101 gQKTQLWWDLPVIDsfYLLAAI-YDLPPARFKKRL---------------DELSELLDLE--ELLDTPVRQLSLGQRMRA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521297957 179 ELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRL-RTTGVAVVLVEHDVGFVMGQSDRVVVLNLGSVLAEG 251
Cdd:cd03267 163 EIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYnRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
9-256 |
1.23e-27 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 108.76 E-value: 1.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 9 DSSVAGVTTEPALEVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQL 88
Cdd:PRK13536 30 KASIPGSMSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 89 PERRARSGVRRTFQRAQLysRLSVEDNVLT-----AMEWRGGGGGLLadlfaapgrrrreaerreyalSVLAACGLADLR 163
Cdd:PRK13536 110 RLARARIGVVPQFDNLDL--EFTVRENLLVfgryfGMSTREIEAVIP---------------------SLLEFARLESKA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 164 HKPAGALPIGQARLVELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLRTTGVAVVLVEHDVGFVMGQSDRVVVLN 243
Cdd:PRK13536 167 DARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLE 246
|
250
....*....|...
gi 521297957 244 LGSVLAEGTPDEI 256
Cdd:PRK13536 247 AGRKIAEGRPHAL 259
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
19-229 |
1.67e-27 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 106.48 E-value: 1.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 19 PALEVRHVTKRYGG----LTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQLPERrar 94
Cdd:COG4525 2 SMLTVRHVSVRYPGggqpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADR--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 95 sGVrrTFQRAQLYSRLSVEDNVLTAMEWRGGGGGLLADLfaapgrrrreaerreyALSVLAACGLADLRHKPAGALPIGQ 174
Cdd:COG4525 79 -GV--VFQKDALLPWLNVLDNVAFGLRLRGVPKAERRAR----------------AEELLALVGLADFARRRIWQLSGGM 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 175 ARLVELARAIADRPRLLLLDEPTSGLSAheteLFGEQIQRL-----RTTGVAVVLVEHDV 229
Cdd:COG4525 140 RQRVGIARALAADPRFLLMDEPFGALDA----LTREQMQELlldvwQRTGKGVFLITHSV 195
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
17-242 |
3.17e-27 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 109.62 E-value: 3.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 17 TEPALEVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVtrQLPERRA--R 94
Cdd:PRK11288 1 SSPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEM--RFASTTAalA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 95 SGVRRTFQRAQLYSRLSVEDNVLTAMewrggggglladlFAAPGRRRREAERREYALSVLAACGLADLRHKPAGALPIGQ 174
Cdd:PRK11288 79 AGVAIIYQELHLVPEMTVAENLYLGQ-------------LPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQ 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521297957 175 ARLVELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLRTTGVAVVLVEHDVGFVMGQSDRVVVL 242
Cdd:PRK11288 146 RQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVF 213
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
36-245 |
3.65e-27 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 104.86 E-value: 3.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 36 ISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQLPERRArsgvrrTFQRAQLYSRLSVEDN 115
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMV------VFQNYSLLPWLTVREN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 116 VLTAMEwrggggGLLADLfaapgrrrREAERREYALSVLAACGLADLRHKPAGALPIGQARLVELARAIADRPRLLLLDE 195
Cdd:TIGR01184 75 IALAVD------RVLPDL--------SKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDE 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 521297957 196 PTSGLSAHETELFGEQIQRL-RTTGVAVVLVEHDVGFVMGQSDRVVVLNLG 245
Cdd:TIGR01184 141 PFGALDALTRGNLQEELMQIwEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
28-261 |
4.03e-27 |
|
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: 107.51 E-value: 4.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 28 KRYGGLTAisDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGV---DVTRQL---PERRARSGVrrtF 101
Cdd:TIGR02142 7 KRLGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRtlfDSRKGIflpPEKRRIGYV---F 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 102 QRAQLYSRLSVEDNVLTAMeWRGGGGGLLADlFAApgrrrreaerreyalsVLAACGLADLRHKPAGALPIGQARLVELA 181
Cdd:TIGR02142 82 QEARLFPHLSVRGNLRYGM-KRARPSERRIS-FER----------------VIELLGIGHLLGRLPGRLSGGEKQRVAIG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 182 RAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLR-TTGVAVVLVEHDVGFVMGQSDRVVVLNLGSVLAEGTPDEIQAHP 260
Cdd:TIGR02142 144 RALLSSPRLLLMDEPLAALDDPRKYEILPYLERLHaEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASP 223
|
.
gi 521297957 261 A 261
Cdd:TIGR02142 224 D 224
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
26-261 |
4.40e-27 |
|
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: 105.80 E-value: 4.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 26 VTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTrQLPERRARSgVRRT----- 100
Cdd:cd03294 30 ILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIA-AMSRKELRE-LRRKkismv 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 101 FQRAQLYSRLSVEDNVLTAMEWRGGGGGLLAdlfaapgrrrreaerrEYALSVLAACGLADLRHKPAGALPIGQARLVEL 180
Cdd:cd03294 108 FQSFALLPHRTVLENVAFGLEVQGVPRAERE----------------ERAAEALELVGLEGWEHKYPDELSGGMQQRVGL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 181 ARAIADRPRLLLLDEPTSGLSA-----HETELFGEQIQRLRTtgvaVVLVEHDVGFVMGQSDRVVVLNLGSVLAEGTPDE 255
Cdd:cd03294 172 ARALAVDPDILLMDEAFSALDPlirreMQDELLRLQAELQKT----IVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEE 247
|
....*.
gi 521297957 256 IQAHPA 261
Cdd:cd03294 248 ILTNPA 253
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
20-255 |
4.48e-27 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 109.48 E-value: 4.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 20 ALEVRHVTKRYGGLT-AISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTR-QLPERRARSGV 97
Cdd:COG1132 339 EIEFENVSFSYPGDRpVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDlTLESLRRQIGV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 98 rrTFQRAQLYSRlSVEDNVltamewrggggglladLFAAPGRRRREaerreyalsVLAACGLADL----RHKPAG----- 168
Cdd:COG1132 419 --VPQDTFLFSG-TIRENI----------------RYGRPDATDEE---------VEEAAKAAQAhefiEALPDGydtvv 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 169 -----ALPIGQARLVELARAIADRPRLLLLDEPTSGLSAhETElfgEQIQR-LR--TTGVAVVLVEHDVGFVMgQSDRVV 240
Cdd:COG1132 471 gergvNLSGGQRQRIAIARALLKDPPILILDEATSALDT-ETE---ALIQEaLErlMKGRTTIVIAHRLSTIR-NADRIL 545
|
250
....*....|....*
gi 521297957 241 VLNLGSVLAEGTPDE 255
Cdd:COG1132 546 VLDDGRIVEQGTHEE 560
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
23-240 |
5.12e-27 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 109.00 E-value: 5.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 23 VRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLdgvdvtrqlperraRSGVRRTF- 101
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI--------------PKGLRIGYl 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 102 -QRAQLYSRLSVEDNVLTAMEWRGGGGGLLADLFAAPGRRRREAERRE-----------YAL-----SVLAACGLADLRH 164
Cdd:COG0488 67 pQEPPLDDDLTVLDTVLDGDAELRALEAELEELEAKLAEPDEDLERLAelqeefealggWEAearaeEILSGLGFPEEDL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 521297957 165 -KPAGALPIGQARLVELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLRTTgvaVVLVEHDVGFVmgqsDRVV 240
Cdd:COG0488 147 dRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGT---VLVVSHDRYFL----DRVA 216
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
20-229 |
1.36e-26 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 104.01 E-value: 1.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 20 ALEVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQLPERrarsGVrr 99
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER----GV-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 100 TFQRAQLYSRLSVEDNVLTAMEWRGGGGGLLADLfaapgrrrreaerreyALSVLAACGLADLRHKPAGALPIGQARLVE 179
Cdd:PRK11248 75 VFQNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEI----------------AHQMLKKVGLEGAEKRYIWQLSGGQRQRVG 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 521297957 180 LARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRL-RTTGVAVVLVEHDV 229
Cdd:PRK11248 139 IARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLwQETGKQVLLITHDI 189
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
21-258 |
1.92e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 104.16 E-value: 1.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 21 LEVRHVTKRYG-GLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDG--VDVTRQ-LPERRARSG 96
Cdd:PRK13636 6 LKVEELNYNYSdGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKgLMKLRESVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 97 VrrTFQRA--QLYSRLSVEDNVLTAMEWRGGGGGLLADLFAApgrrrreaerreyalsvLAACGLADLRHKPAGALPIGQ 174
Cdd:PRK13636 86 M--VFQDPdnQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNA-----------------LKRTGIEHLKDKPTHCLSFGQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 175 ARLVELARAIADRPRLLLLDEPTSGLSAHET-ELFGEQIQRLRTTGVAVVLVEHDVGFVMGQSDRVVVLNLGSVLAEGTP 253
Cdd:PRK13636 147 KKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVsEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNP 226
|
....*
gi 521297957 254 DEIQA 258
Cdd:PRK13636 227 KEVFA 231
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
14-259 |
2.57e-26 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 104.50 E-value: 2.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 14 GVTTEPALEVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQLPERRA 93
Cdd:PRK13537 1 GPMSVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 94 RSGVRRTFQraQLYSRLSVEDNVLTAMEWRGGGGGLLADLFAapgrrrreaerreyalSVLAACGLADLRHKPAGALPIG 173
Cdd:PRK13537 81 RVGVVPQFD--NLDPDFTVRENLLVFGRYFGLSAAAARALVP----------------PLLEFAKLENKADAKVGELSGG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 174 QARLVELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLRTTGVAVVLVEHDVGFVMGQSDRVVVLNLGSVLAEGTP 253
Cdd:PRK13537 143 MKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAP 222
|
....*.
gi 521297957 254 DEIQAH 259
Cdd:PRK13537 223 HALIES 228
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
21-247 |
4.19e-26 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 102.83 E-value: 4.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 21 LEVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVfLDGvdvtrQLPERRARSGVRRT 100
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAG-----TAPLAEAREDTRLM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 101 FQRAQLYSRLSVEDNVLTAM--EWRGGggglladlfaapgrrrreaerreyALSVLAACGLADLRHKPAGALPIGQARLV 178
Cdd:PRK11247 87 FQDARLLPWKKVIDNVGLGLkgQWRDA------------------------ALQALAAVGLADRANEWPAALSGGQKQRV 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 179 ELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRL-RTTGVAVVLVEHDVGFVMGQSDRVVVLNLGSV 247
Cdd:PRK11247 143 ALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLwQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
11-256 |
6.11e-26 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 102.42 E-value: 6.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 11 SVAGVTTEPALEVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTL-------FDIISGLTppTSGAVFLDGVD 83
Cdd:COG1117 2 TAPASTLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLlrclnrmNDLIPGAR--VEGEILLDGED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 84 V---TRQLPERRARSG-VrrtFQRAQLYSrLSVEDNVltAMEWRGGGGGLLADLFAApgrrrreaerreyALSVLAACGL 159
Cdd:COG1117 80 IydpDVDVVELRRRVGmV---FQKPNPFP-KSIYDNV--AYGLRLHGIKSKSELDEI-------------VEESLRKAAL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 160 AD-----LrHKPAGALPIGQA-RLVeLARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLRTTgVAVVLVEHDvgfvM 233
Cdd:COG1117 141 WDevkdrL-KKSALGLSGGQQqRLC-IARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD-YTIVIVTHN----M 213
|
250 260
....*....|....*....|....*..
gi 521297957 234 GQ----SDRVVVLNLGSVLAEGTPDEI 256
Cdd:COG1117 214 QQaarvSDYTAFFYLGELVEFGPTEQI 240
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
21-227 |
2.41e-25 |
|
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: 99.36 E-value: 2.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 21 LEVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQLPERrarsgvrrt 100
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEP--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 101 fQRAQLY-SRLSVEDNVLTAME----WRGGGGGLLADLFAApgrrrreaerreyalsvLAACGLADLRHKPAGALPIGQA 175
Cdd:TIGR01189 72 -HENILYlGHLPGLKPELSALEnlhfWAAIHGGAQRTIEDA-----------------LAAVGLTGFEDLPAAQLSAGQQ 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 521297957 176 RLVELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLRTTGVAVVLVEH 227
Cdd:TIGR01189 134 RRLALARLWLSRRPLWILDEPTTALDKAGVALLAGLLRAHLARGGIVLLTTH 185
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
17-260 |
3.41e-25 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 100.43 E-value: 3.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 17 TEPALEVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVT----------- 85
Cdd:PRK10619 2 SENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 86 ---RQLpeRRARSGVRRTFQRAQLYSRLSVEDNVLTAMEWRGGGGGLLAdlfaapgrrrreaerREYALSVLAACGLAD- 161
Cdd:PRK10619 82 adkNQL--RLLRTRLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQEA---------------RERAVKYLAKVGIDEr 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 162 LRHKPAGALPIGQARLVELARAIADRPRLLLLDEPTSGLsahETELFGEQI---QRLRTTGVAVVLVEHDVGFVMGQSDR 238
Cdd:PRK10619 145 AQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSAL---DPELVGEVLrimQQLAEEGKTMVVVTHEMGFARHVSSH 221
|
250 260
....*....|....*....|..
gi 521297957 239 VVVLNLGSVLAEGTPDEIQAHP 260
Cdd:PRK10619 222 VIFLHQGKIEEEGAPEQLFGNP 243
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
17-266 |
3.84e-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: 3.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 17 TEPALEVRHVTKRY--GGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVtRQLPERRAR 94
Cdd:COG4987 330 GGPSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDL-RDLDEDDLR 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 95 SGVRRTFQRAQLYSRlSVEDNVLtamewrggggglladlFAAPGRRRREaerreyALSVLAACGLAD-LRHKPAG----- 168
Cdd:COG4987 409 RRIAVVPQRPHLFDT-TLRENLR----------------LARPDATDEE------LWAALERVGLGDwLAALPDGldtwl 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 169 -----ALPIGQARLVELARAIADRPRLLLLDEPTSGLSAhETElfgEQI-QRLRTT--GVAVVLVEHD-VGfvMGQSDRV 239
Cdd:COG4987 466 geggrRLSGGERRRLALARALLRDAPILLLDEPTEGLDA-ATE---QALlADLLEAlaGRTVLLITHRlAG--LERMDRI 539
|
250 260
....*....|....*....|....*...
gi 521297957 240 VVLNLGSVLAEGTPDE-IQAHPAVRAAY 266
Cdd:COG4987 540 LVLEDGRIVEQGTHEElLAQNGRYRQLY 567
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
38-251 |
4.61e-25 |
|
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: 98.91 E-value: 4.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 38 DVSLRVD---PGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGV--DVTRQ---LPERRARSGVrrTFQRAQLYSR 109
Cdd:cd03297 12 DFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlFDSRKkinLPPQQRKIGL--VFQQYALFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 110 LSVEDNVLTAMewRGGGGGLLADLFAApgrrrreaerreyalsVLAACGLADLRHKPAGALPIGQARLVELARAIADRPR 189
Cdd:cd03297 90 LNVRENLAFGL--KRKRNREDRISVDE----------------LLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 521297957 190 LLLLDEPTSGLSAH-ETELFGEQIQRLRTTGVAVVLVEHDVGFVMGQSDRVVVLNLGSVLAEG 251
Cdd:cd03297 152 LLLLDEPFSALDRAlRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
31-229 |
5.15e-25 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 98.26 E-value: 5.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 31 GGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVdvtrqlPERRARSGVRRTFQRAQLYSRl 110
Cdd:TIGR01166 3 GGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGE------PLDYSRKGLLERRQRVGLVFQ- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 111 SVEDNVLTAMEWRGGGgglladlFAAPGRRRREAERREYALSVLAACGLADLRHKPAGALPIGQARLVELARAIADRPRL 190
Cdd:TIGR01166 76 DPDDQLFAADVDQDVA-------FGPLNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDV 148
|
170 180 190
....*....|....*....|....*....|....*....
gi 521297957 191 LLLDEPTSGLSAHETELFGEQIQRLRTTGVAVVLVEHDV 229
Cdd:TIGR01166 149 LLLDEPTAGLDPAGREQMLAILRRLRAEGMTVVISTHDV 187
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
21-267 |
5.17e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 100.15 E-value: 5.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 21 LEVRHVTKRY-GGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVT---RQLPERRARSG 96
Cdd:PRK13639 2 LETRDLKYSYpDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKydkKSLLEVRKTVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 97 VrrTFQRA--QLYSRlSVEDNVltamewrggggglladLFAAPGRRRREAERREYALSVLAACGLADLRHKPAGALPIGQ 174
Cdd:PRK13639 82 I--VFQNPddQLFAP-TVEEDV----------------AFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 175 ARLVELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLRTTGVAVVLVEHDVGFVMGQSDRVVVLNLGSVLAEGTPD 254
Cdd:PRK13639 143 KKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPK 222
|
250
....*....|....
gi 521297957 255 EIQAHP-AVRAAYL 267
Cdd:PRK13639 223 EVFSDIeTIRKANL 236
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
21-227 |
8.22e-25 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 98.02 E-value: 8.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 21 LEVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTrqLPERRARS---GV 97
Cdd:PRK13539 3 LEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDID--DPDVAEAChylGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 98 RRTFQRAqlysrLSVEDNVLTameWRGGGGGLLADLFAApgrrrreaerreyalsvLAACGLADLRHKPAGALPIGQARL 177
Cdd:PRK13539 81 RNAMKPA-----LTVAENLEF---WAAFLGGEELDIAAA-----------------LEAVGLAPLAHLPFGYLSAGQKRR 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 521297957 178 VELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLRTTGVAVVLVEH 227
Cdd:PRK13539 136 VALARLLVSNRPIWILDEPTAALDAAAVALFAELIRAHLAQGGIVIAATH 185
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
20-260 |
1.07e-24 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 98.67 E-value: 1.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 20 ALEVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGV--DVTRQLPE-----RR 92
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDItiDTARSLSQqkgliRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 93 ARSGVRRTFQRAQLYSRLSVEDNVLtamewrggggglladlfAAPGRRRREAERREYAL--SVLAACGLADLRHKPAGAL 170
Cdd:PRK11264 83 LRQHVGFVFQNFNLFPHRTVLENII-----------------EGPVIVKGEPKEEATARarELLAKVGLAGKETSYPRRL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 171 PIGQARLVELARAIADRPRLLLLDEPTSGLsahETELFGE---QIQRLRTTGVAVVLVEHDVGFVMGQSDRVVVLNLGSV 247
Cdd:PRK11264 146 SGGQQQRVAIARALAMRPEVILFDEPTSAL---DPELVGEvlnTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
|
250
....*....|...
gi 521297957 248 LAEGTPDEIQAHP 260
Cdd:PRK11264 223 VEQGPAKALFADP 235
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
13-258 |
1.38e-24 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 102.51 E-value: 1.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 13 AGVTTEPALEVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQLPERR 92
Cdd:NF033858 259 ADDDDEPAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIATR 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 93 ARSGvrrtF--QRAQLYSRLSVEDN-VLtamewrggggglLADLFAAPGRRRREAERReyalsVLAACGLADLRHKPAGA 169
Cdd:NF033858 339 RRVG----YmsQAFSLYGELTVRQNlEL------------HARLFHLPAAEIAARVAE-----MLERFDLADVADALPDS 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 170 LPIGQ-ARLvELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRL-RTTGVAVVLVEHdvgFvMGQS---DRVVVLNL 244
Cdd:NF033858 398 LPLGIrQRL-SLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLIELsREDGVTIFISTH---F-MNEAercDRISLMHA 472
|
250
....*....|....
gi 521297957 245 GSVLAEGTPDEIQA 258
Cdd:NF033858 473 GRVLASDTPAALVA 486
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
18-259 |
2.10e-24 |
|
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: 101.75 E-value: 2.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 18 EPALEVRHVTKRYGGLTA--ISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQLPERRARS 95
Cdd:COG4618 328 KGRLSVENLTVVPPGSKRpiLRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRH 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 96 gvrrtF----QRAQLYSRlSVEDNVltAMewrggggglladlFAAPGRRrreaerreyalSVLAACGLADLrHK-----P 166
Cdd:COG4618 408 -----IgylpQDVELFDG-TIAENI--AR-------------FGDADPE-----------KVVAAAKLAGV-HEmilrlP 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 167 AG----------ALPIGQARLVELARAIADRPRLLLLDEPTSGLSAhetelFGEQ-----IQRLRTTGVAVVLVEHDVGf 231
Cdd:COG4618 455 DGydtrigeggaRLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDD-----EGEAalaaaIRALKARGATVVVITHRPS- 528
|
250 260
....*....|....*....|....*...
gi 521297957 232 VMGQSDRVVVLNLGSVLAEGTPDEIQAH 259
Cdd:COG4618 529 LLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
21-256 |
3.21e-24 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 97.78 E-value: 3.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 21 LEVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQLPERRARS----- 95
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRlallp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 96 ---------GVRR--TFQRA---QLYSRLSVEDN--VLTAMEwrggggglladlfaapgrrrreaerreyalsvlaACGL 159
Cdd:PRK11231 83 qhhltpegiTVRElvAYGRSpwlSLWGRLSAEDNarVNQAME----------------------------------QTRI 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 160 ADLRHKPAGALPIGQARLVELARAIADRPRLLLLDEPTSGLS-AHETELFGeQIQRLRTTGVAVVLVEHDVGFVMGQSDR 238
Cdd:PRK11231 129 NHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDiNHQVELMR-LMRELNTQGKTVVTVLHDLNQASRYCDH 207
|
250
....*....|....*...
gi 521297957 239 VVVLNLGSVLAEGTPDEI 256
Cdd:PRK11231 208 LVVLANGHVMAQGTPEEV 225
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
21-200 |
3.89e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 97.46 E-value: 3.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 21 LEVRHVTKRYG-GL----TAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQLPERRARS 95
Cdd:COG1101 2 LELKNLSKTFNpGTvnekRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 96 gVRRTFQRAQL--YSRLSVEDNVLTAME------WRGGGGGLLADLFAApgrrrreaerreyALSVLAAcGLADLRHKPA 167
Cdd:COG1101 82 -IGRVFQDPMMgtAPSMTIEENLALAYRrgkrrgLRRGLTKKRRELFRE-------------LLATLGL-GLENRLDTKV 146
|
170 180 190
....*....|....*....|....*....|...
gi 521297957 168 GALPIGQARLVELARAIADRPRLLLLDEPTSGL 200
Cdd:COG1101 147 GLLSGGQRQALSLLMATLTKPKLLLLDEHTAAL 179
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
18-256 |
5.42e-24 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 100.49 E-value: 5.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 18 EPALEVRHVT-KRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQLPERRARSG 96
Cdd:COG3845 255 EVVLEVENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLG 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 97 VR-----RtfQRAQLYSRLSVEDN-VLTAMEWRGGGGGLLADLFAApgrrrreaerREYALSVLAAcglADLR----HKP 166
Cdd:COG3845 335 VAyipedR--LGRGLVPDMSVAENlILGRYRRPPFSRGGFLDRKAI----------RAFAEELIEE---FDVRtpgpDTP 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 167 AGALPIG-QARLVeLARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLRTTGVAVVLVEHDVGFVMGQSDRVVVLNLG 245
Cdd:COG3845 400 ARSLSGGnQQKVI-LARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEG 478
|
250
....*....|.
gi 521297957 246 SVLAEGTPDEI 256
Cdd:COG3845 479 RIVGEVPAAEA 489
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
20-253 |
5.52e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 97.50 E-value: 5.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 20 ALEVRHVTKRY-GGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTrQLPERRARSGVR 98
Cdd:PRK13647 4 IIEVEDLHFRYkDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVN-AENEKWVRSKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 99 RTFQRA--QLYSrLSVEDNVLtamewrggggglladlFAAPGRRRREAERREYALSVLAACGLADLRHKPAGALPIGQAR 176
Cdd:PRK13647 83 LVFQDPddQVFS-STVWDDVA----------------FGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKK 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 521297957 177 LVELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLRTTGVAVVLVEHDVGFVMGQSDRVVVLNLGSVLAEGTP 253
Cdd:PRK13647 146 RVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDK 222
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
29-242 |
1.02e-23 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 94.61 E-value: 1.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 29 RYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDG----------VDVTRQLPERRARSGVR 98
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGgarvayvpqrSEVPDSLPLTVRDLVAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 99 RTFQRAQLYSRLSVEDNVLTAmewrggggglladlfaapgrrrreaerreyalSVLAACGLADLRHKPAGALPIGQARLV 178
Cdd:NF040873 81 GRWARRGLWRRLTRDDRAAVD--------------------------------DALERVGLADLAGRQLGELSGGQRQRA 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521297957 179 ELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLRTTGVAVVLVEHDVGFVMgQSDRVVVL 242
Cdd:NF040873 129 LLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAEEHARGATVVVVTHDLELVR-RADPCVLL 191
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
18-247 |
1.30e-23 |
|
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: 94.04 E-value: 1.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 18 EPALEVRHVTKRYggltAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQLPERRARSGV 97
Cdd:cd03215 2 EPVLEVRGLSVKG----AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 98 ------RRtfqRAQLYSRLSVEDNVltamewrggggglladlfaapgrrrreaerreyALSVLAACGladlrhkpagalp 171
Cdd:cd03215 78 ayvpedRK---REGLVLDLSVAENI---------------------------------ALSSLLSGG------------- 108
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 521297957 172 iGQARLVeLARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLRTTGVAVVLVEHDVGFVMGQSDRVVVLNLGSV 247
Cdd:cd03215 109 -NQQKVV-LARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
35-256 |
2.31e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 95.88 E-value: 2.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 35 AISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQ---LPERRARSGVRRTFQRAQLY---- 107
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKkvkLSDIRKKVGLVFQYPEYQLFeeti 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 108 --------SRLSVEDN-----VLTAMEwrggggglladlfaapgrrrreaerreyalsvlaACGLA--DLRHKPAGALPI 172
Cdd:PRK13637 102 ekdiafgpINLGLSEEeienrVKRAMN----------------------------------IVGLDyeDYKDKSPFELSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 173 GQARLVELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLRTT-GVAVVLVEHDVGFVMGQSDRVVVLNLGSVLAEG 251
Cdd:PRK13637 148 GQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCELQG 227
|
....*
gi 521297957 252 TPDEI 256
Cdd:PRK13637 228 TPREV 232
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
20-259 |
2.73e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 96.31 E-value: 2.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 20 ALEVRHVTKRY----------GGL-----------TAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVF 78
Cdd:COG4586 1 IIEVENLSKTYrvyekepglkGALkglfrreyrevEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 79 LDGVDVTRQLPERRARSGVrrTF-QRAQLYSRLSVED--NVLTAM------EWRGGGggllaDLFAapgrrrreaerrey 149
Cdd:COG4586 81 VLGYVPFKRRKEFARRIGV--VFgQRSQLWWDLPAIDsfRLLKAIyripdaEYKKRL-----DELV-------------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 150 alSVLaacGLADLRHKPAGALPIGQARLVELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRL-RTTGVAVVLVEHD 228
Cdd:COG4586 140 --ELL---DLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYnRERGTTILLTSHD 214
|
250 260 270
....*....|....*....|....*....|.
gi 521297957 229 VGFVMGQSDRVVVLNLGSVLAEGTPDEIQAH 259
Cdd:COG4586 215 MDDIEALCDRVIVIDHGRIIYDGSLEELKER 245
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
18-256 |
2.81e-23 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 98.34 E-value: 2.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 18 EPALEVRHVTKRY-----GGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFL----DGVDVTRQL 88
Cdd:TIGR03269 277 EPIIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPG 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 89 PERRARSG--VRRTFQRAQLYSRLSVEDNVLTAMewrgggGGLLADLFAapgrrrreaerREYALSVLAACGLAD----- 161
Cdd:TIGR03269 357 PDGRGRAKryIGILHQEYDLYPHRTVLDNLTEAI------GLELPDELA-----------RMKAVITLKMVGFDEekaee 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 162 LRHKPAGALPIGQARLVELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLRT-TGVAVVLVEHDVGFVMGQSDRVV 240
Cdd:TIGR03269 420 ILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREeMEQTFIIVSHDMDFVLDVCDRAA 499
|
250
....*....|....*.
gi 521297957 241 VLNLGSVLAEGTPDEI 256
Cdd:TIGR03269 500 LMRDGKIVKIGDPEEI 515
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
16-242 |
2.93e-23 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 94.40 E-value: 2.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 16 TTEPALEVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQLPERRaRS 95
Cdd:PRK10247 3 ENSPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIY-RQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 96 GVRRTFQRAQLYSRlSVEDNVLtaMEWRGGGGGLLADLFAAPgrrrreaerreyalsvLAACGLAD-LRHKPAGALPIGQ 174
Cdd:PRK10247 82 QVSYCAQTPTLFGD-TVYDNLI--FPWQIRNQQPDPAIFLDD----------------LERFALPDtILTKNIAELSGGE 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521297957 175 ARLVELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRL-RTTGVAVVLVEHDVGFVmGQSDRVVVL 242
Cdd:PRK10247 143 KQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYvREQNIAVLWVTHDKDEI-NHADKVITL 210
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
21-251 |
3.62e-23 |
|
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: 93.71 E-value: 3.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 21 LEVRHVTKRYGglTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQLPERRARSGVrrt 100
Cdd:cd03298 1 VRLDKIRFSYG--EQPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSML--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 101 FQRAQLYSRLSVEDNVltamewrgggggllaDLFAAPGRRRREAERREYAlSVLAACGLADLRHKPAGALPIGQARLVEL 180
Cdd:cd03298 76 FQENNLFAHLTVEQNV---------------GLGLSPGLKLTAEDRQAIE-VALARVGLAGLEKRLPGELSGGERQRVAL 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 521297957 181 ARA-IADRPrLLLLDEPTSGLS-AHETELFGEQIQRLRTTGVAVVLVEHDVGFVMGQSDRVVVLNLGSVLAEG 251
Cdd:cd03298 140 ARVlVRDKP-VLLLDEPFAALDpALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
20-251 |
3.74e-23 |
|
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: 93.81 E-value: 3.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 20 ALEVRHVTKRYGG--LTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVtRQLPERRARSGV 97
Cdd:cd03245 2 RIEFRNVSFSYPNqeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDI-RQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 98 RRTFQRAQLYSRlSVEDNVltamewrggggglladLFAAPGRRRREAerreyaLSVLAACGLADL--RHkPAG------- 168
Cdd:cd03245 81 GYVPQDVTLFYG-TLRDNI----------------TLGAPLADDERI------LRAAELAGVTDFvnKH-PNGldlqige 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 169 ---ALPIGQARLVELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLrTTGVAVVLVEHDVGFvMGQSDRVVVLNLG 245
Cdd:cd03245 137 rgrGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQL-LGDKTLIIITHRPSL-LDLVDRIIVMDSG 214
|
....*.
gi 521297957 246 SVLAEG 251
Cdd:cd03245 215 RIVADG 220
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
16-263 |
5.74e-23 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 94.83 E-value: 5.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 16 TTEPALEVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTrQLPERR--- 92
Cdd:PRK11831 3 SVANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIP-AMSRSRlyt 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 93 ARSGVRRTFQRAQLYSRLSVEDNVltAMEWRGGGGGLLADLFAApgrrrreaerreyALSVLAACGLADLRHKPAGALPI 172
Cdd:PRK11831 82 VRKRMSMLFQSGALFTDMNVFDNV--AYPLREHTQLPAPLLHST-------------VMMKLEAVGLRGAAKLMPSELSG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 173 GQARLVELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLRTT-GVAVVLVEHDVGFVMGQSDRVVVLNLGSVLAEG 251
Cdd:PRK11831 147 GMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHG 226
|
250
....*....|..
gi 521297957 252 TPDEIQAHPAVR 263
Cdd:PRK11831 227 SAQALQANPDPR 238
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
21-227 |
7.23e-23 |
|
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: 92.94 E-value: 7.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 21 LEVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQLPErrarsgvrrt 100
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDS---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 101 FQRAQLY--------SRLSVEDNVltamewrgggggllaDLFAAPGRRRReaerreyALSVLAACGLADLRHKPAGALPI 172
Cdd:cd03231 71 IARGLLYlghapgikTTLSVLENL---------------RFWHADHSDEQ-------VEEALARVGLNGFEDRPVAQLSA 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 521297957 173 GQARLVELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLRTTGVAVVLVEH 227
Cdd:cd03231 129 GQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTH 183
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
21-257 |
8.47e-23 |
|
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: 92.59 E-value: 8.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 21 LEVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGL--TPPTSGAVFLDGVDVTRQLPERRARSGVR 98
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEERARLGIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 99 RTFQRAQLYSRLSVEDnvltamewrggggglladlFaapgrrrreaerreyalsvlaacgladLRHKPAGaLPIGQARLV 178
Cdd:cd03217 81 LAFQYPPEIPGVKNAD-------------------F---------------------------LRYVNEG-FSGGEKKRN 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 179 ELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLRTTGVAVVLVEHD---VGFVmgQSDRVVVLNLGSVLAEGTPDE 255
Cdd:cd03217 114 EILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHYqrlLDYI--KPDRVHVLYDGRIVKSGDKEL 191
|
..
gi 521297957 256 IQ 257
Cdd:cd03217 192 AL 193
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
19-247 |
9.07e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 97.06 E-value: 9.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 19 PALEVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLdGVDVtrqlperraRSGVr 98
Cdd:COG0488 314 KVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV---------KIGY- 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 99 rtFqrAQLYSRLSVEDNVLTAMeWRggggglladlfAAPGrrrreaERREYALSVLAACGLA-DLRHKPAGALPIGQ-AR 176
Cdd:COG0488 383 --F--DQHQEELDPDKTVLDEL-RD-----------GAPG------GTEQEVRGYLGRFLFSgDDAFKPVGVLSGGEkAR 440
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 521297957 177 LVeLARAIADRPRLLLLDEPTSglsaH---ET-ELFGEQIQRLrtTGvAVVLVEHDVGFVMGQSDRVVVLNLGSV 247
Cdd:COG0488 441 LA-LAKLLLSPPNVLLLDEPTN----HldiETlEALEEALDDF--PG-TVLLVSHDRYFLDRVATRILEFEDGGV 507
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
21-256 |
1.26e-22 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 92.93 E-value: 1.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 21 LEVRHVTKRYG--GLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQLPER-RARSGV 97
Cdd:cd03252 1 ITFEHVRFRYKpdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWlRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 98 rrTFQRAQLYSRlSVEDNVltamewrggggglladLFAAPGRRRReaerreyalSVLAACGLAD----LRHKPAG----- 168
Cdd:cd03252 81 --VLQENVLFNR-SIRDNI----------------ALADPGMSME---------RVIEAAKLAGahdfISELPEGydtiv 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 169 -----ALPIGQARLVELARAIADRPRLLLLDEPTSGLSaHETELFGEQIQRLRTTGVAVVLVEHDVGFVMgQSDRVVVLN 243
Cdd:cd03252 133 geqgaGLSGGQRQRIAIARALIHNPRILIFDEATSALD-YESEHAIMRNMHDICAGRTVIIIAHRLSTVK-NADRIIVME 210
|
250
....*....|...
gi 521297957 244 LGSVLAEGTPDEI 256
Cdd:cd03252 211 KGRIVEQGSHDEL 223
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
22-255 |
1.99e-22 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 92.29 E-value: 1.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 22 EVRHVTKRY-GGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVtRQLPERRARSGVRRT 100
Cdd:cd03254 4 EFENVNFSYdEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDI-RDISRKSLRSMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 101 FQRAQLYSRlSVEDNVL------TAMEWRGGGGGLLADLFaapgrrrreaerreyalsvlaacgladLRHKPAG------ 168
Cdd:cd03254 83 LQDTFLFSG-TIMENIRlgrpnaTDEEVIEAAKEAGAHDF---------------------------IMKLPNGydtvlg 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 169 ----ALPIGQARLVELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLRtTGVAVVLVEHDVGFVMgQSDRVVVLNL 244
Cdd:cd03254 135 enggNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLM-KGRTSIIIAHRLSTIK-NADKILVLDD 212
|
250
....*....|.
gi 521297957 245 GSVLAEGTPDE 255
Cdd:cd03254 213 GKIIEEGTHDE 223
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
19-266 |
2.15e-22 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 95.29 E-value: 2.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 19 PALEVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTrqlpERRARSGVR 98
Cdd:PRK09536 2 PMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVE----ALSARAASR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 99 RTFQRAQLYSrLSVEDNVLTAMEWRGGGGGLLADLFAAPGRRRREaerreyalSVLAACGLADLRHKPAGALPIGQARLV 178
Cdd:PRK09536 78 RVASVPQDTS-LSFEFDVRQVVEMGRTPHRSRFDTWTETDRAAVE--------RAMERTGVAQFADRPVTSLSGGERQRV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 179 ELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLRTTGVAVVLVEHDVGFVMGQSDRVVVLNLGSVLAEGTPDEIQA 258
Cdd:PRK09536 149 LLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLT 228
|
....*...
gi 521297957 259 HPAVRAAY 266
Cdd:PRK09536 229 ADTLRAAF 236
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
17-259 |
2.52e-22 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 93.16 E-value: 2.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 17 TEPALEVRHVTKRYGGLT--AISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQ-LPERRA 93
Cdd:PRK13635 2 KEEIIRVEHISFRYPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEEtVWDVRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 94 RSGVrrTFQRA-QLYSRLSVEDNVLTAMEWRGGGGGLLADLFAApgrrrreaerreyalsVLAACGLAD-LRHKPAgALP 171
Cdd:PRK13635 82 QVGM--VFQNPdNQFVGATVQDDVAFGLENIGVPREEMVERVDQ----------------ALRQVGMEDfLNREPH-RLS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 172 IGQARLVELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLR-TTGVAVVLVEHDVGFVmGQSDRVVVLNLGSVLAE 250
Cdd:PRK13635 143 GGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKeQKGITVLSITHDLDEA-AQADRVIVMNKGEILEE 221
|
....*....
gi 521297957 251 GTPDEIQAH 259
Cdd:PRK13635 222 GTPEEIFKS 230
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
18-261 |
2.67e-22 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 94.71 E-value: 2.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 18 EPALEVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTR----QLPERRa 93
Cdd:PRK10070 26 EQGLSKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKisdaELREVR- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 94 RSGVRRTFQRAQLYSRLSVEDNVLTAMEwrggggglladLFAAPGRRRREAerreyALSVLAACGLADLRHKPAGALPIG 173
Cdd:PRK10070 105 RKKIAMVFQSFALMPHMTVLDNTAFGME-----------LAGINAEERREK-----ALDALRQVGLENYAHSYPDELSGG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 174 QARLVELARAIADRPRLLLLDEPTSGL-----SAHETELFGEQIQRLRTtgvaVVLVEHDVGFVMGQSDRVVVLNLGSVL 248
Cdd:PRK10070 169 MRQRVGLARALAINPDILLMDEAFSALdplirTEMQDELVKLQAKHQRT----IVFISHDLDEAMRIGDRIAIMQNGEVV 244
|
250
....*....|...
gi 521297957 249 AEGTPDEIQAHPA 261
Cdd:PRK10070 245 QVGTPDEILNNPA 257
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
32-268 |
3.20e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 92.74 E-value: 3.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 32 GLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVT--RQLPERRARSGVRRTFQRAQLYSR 109
Cdd:PRK13644 14 GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGdfSKLQGIRKLVGIVFQNPETQFVGR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 110 lSVEDNVLTAMEwrgggggllaDLFAAPGRRRREAERReyalsvLAACGLADLRHKPAGALPIGQARLVELARAIADRPR 189
Cdd:PRK13644 94 -TVEEDLAFGPE----------NLCLPPIEIRKRVDRA------LAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPE 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521297957 190 LLLLDEPTSGLSAHETELFGEQIQRLRTTGVAVVLVEHDVGfVMGQSDRVVVLNLGSVLAEGTPDEIQAHPAVRaaYLG 268
Cdd:PRK13644 157 CLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLE-ELHDADRIIVMDRGKIVLEGEPENVLSDVSLQ--TLG 232
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
21-261 |
3.79e-22 |
|
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: 93.19 E-value: 3.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 21 LEVRHVTKRY----GGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPP---TSGAVFLDGVDVTRqLPERRA 93
Cdd:COG0444 2 LEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLK-LSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 94 RSgVRRT-----FQRAqlYS----RLSVEDNVLTAMewRGGGGGLLADLFAApgrrrreaerreyALSVLAACGLADlrh 164
Cdd:COG0444 81 RK-IRGReiqmiFQDP--MTslnpVMTVGDQIAEPL--RIHGGLSKAEARER-------------AIELLERVGLPD--- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 165 kPAGAL---PI----GQARLVELARAIADRPRLLLLDEPTSGLSAheT------ELFGEqIQrlRTTGVAVVLVEHDVGF 231
Cdd:COG0444 140 -PERRLdryPHelsgGMRQRVMIARALALEPKLLIADEPTTALDV--TiqaqilNLLKD-LQ--RELGLAILFITHDLGV 213
|
250 260 270
....*....|....*....|....*....|
gi 521297957 232 VMGQSDRVVVLNLGSVLAEGTPDEIQAHPA 261
Cdd:COG0444 214 VAEIADRVAVMYAGRIVEEGPVEELFENPR 243
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
13-268 |
4.56e-22 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 93.94 E-value: 4.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 13 AGVTtepaleVRHVTKRYGGlTAIS-DVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQLPER 91
Cdd:PRK11000 2 ASVT------LRNVTKAYGD-VVISkDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 92 RarsGVRRTFQRAQLYSRLSVEDNVLTAMEwrggggglladlfAAPGRRRREAERREYALSVLAACGLADLRHKpagALP 171
Cdd:PRK11000 75 R---GVGMVFQSYALYPHLSVAENMSFGLK-------------LAGAKKEEINQRVNQVAEVLQLAHLLDRKPK---ALS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 172 IGQARLVELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRL-RTTGVAVVLVEHDVGFVMGQSDRVVVLNLGSVLAE 250
Cdd:PRK11000 136 GGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLhKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQV 215
|
250 260
....*....|....*....|
gi 521297957 251 GTPDEIQAHPAVR--AAYLG 268
Cdd:PRK11000 216 GKPLELYHYPANRfvAGFIG 235
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
19-242 |
8.74e-22 |
|
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: 94.28 E-value: 8.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 19 PALEVRHVTKRYGGLT-AISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTrQLPERRARSGV 97
Cdd:TIGR02857 320 SSLEFSGVSVAYPGRRpALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLA-DADADSWRDQI 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 98 RRTFQRAQLYSRlSVEDNVltamewrggggglladLFAAPGRRRREAERreyalsVLAACGLADL-------RHKPAG-- 168
Cdd:TIGR02857 399 AWVPQHPFLFAG-TIAENI----------------RLARPDASDAEIRE------ALERAGLDEFvaalpqgLDTPIGeg 455
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 521297957 169 --ALPIGQARLVELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLRtTGVAVVLVEHDVGfVMGQSDRVVVL 242
Cdd:TIGR02857 456 gaGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALA-QGRTVLLVTHRLA-LAALADRIVVL 529
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
21-245 |
1.27e-21 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 89.48 E-value: 1.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 21 LEVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQLPErrarsgvrrt 100
Cdd:PRK13538 2 LEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDE---------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 101 FQRAQLY--------SRLSVEDNVLTAMewRGGGGGLLADLFAApgrrrreaerreyalsvLAACGLADLRHKPAGALPI 172
Cdd:PRK13538 72 YHQDLLYlghqpgikTELTALENLRFYQ--RLHGPGDDEALWEA-----------------LAQVGLAGFEDVPVRQLSA 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521297957 173 GQARLVELARAIADRPRLLLLDEPTSGLSAHETELFGEQI-QRLRTTGVAVVLVEHDVGFVmgqSDRVVVLNLG 245
Cdd:PRK13538 133 GQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALLaQHAEQGGMVILTTHQDLPVA---SDKVRKLRLG 203
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
36-251 |
2.36e-21 |
|
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: 89.25 E-value: 2.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 36 ISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGL---TPPTSGAVFLDGVDVTRQLPERRArSGVRrtfQRAQLYSRLSV 112
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRvegGGTTSGQILFNGQPRKPDQFQKCV-AYVR---QDDILLPGLTV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 113 EDNVL-TAMewrggggglladlFAAPGRRRREAERREYALSVLAACGLADLRHKPAGALPIGQARLVELARAIADRPRLL 191
Cdd:cd03234 99 RETLTyTAI-------------LRLPRKSSDAIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 521297957 192 LLDEPTSGLSAHETELFGEQIQRLRTTGVAVVLVEHDVGFVMGQS-DRVVVLNLGSVLAEG 251
Cdd:cd03234 166 ILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLfDRILLLSSGEIVYSG 226
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
16-261 |
2.89e-21 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 90.95 E-value: 2.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 16 TTEPALEVRHVTKRY---GGL--------TAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDV 84
Cdd:COG4608 3 MAEPLLEVRDLKKHFpvrGGLfgrtvgvvKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 85 TRqLPERRARSgVRRT----FQ--RAQLYSRLSVEDNVLTAMEWRGGGGGLLADlfaapgrrrreaerrEYALSVLAACG 158
Cdd:COG4608 83 TG-LSGRELRP-LRRRmqmvFQdpYASLNPRMTVGDIIAEPLRIHGLASKAERR---------------ERVAELLELVG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 159 L-ADLRHKPAGALPIGQARLVELARAIADRPRLLLLDEPTSGL----SAHETELFGEQIQRLrttGVAVVLVEHDVGFVM 233
Cdd:COG4608 146 LrPEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALdvsiQAQVLNLLEDLQDEL---GLTYLFISHDLSVVR 222
|
250 260
....*....|....*....|....*...
gi 521297957 234 GQSDRVVVLNLGSVLAEGTPDEIQAHPA 261
Cdd:COG4608 223 HISDRVAVMYLGKIVEIAPRDELYARPL 250
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
23-260 |
3.61e-21 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 89.40 E-value: 3.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 23 VRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVfldgvdvtrqlpERRARSGVRRTFQ 102
Cdd:PRK09544 7 LENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI------------KRNGKLRIGYVPQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 103 RAQLYSRLSVedNVLTAMEWRggggglladlfaaPGRRRREAerreyaLSVLAACGLADLRHKPAGALPIGQARLVELAR 182
Cdd:PRK09544 75 KLYLDTTLPL--TVNRFLRLR-------------PGTKKEDI------LPALKRVQAGHLIDAPMQKLSGGETQRVLLAR 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521297957 183 AIADRPRLLLLDEPTSGLSAHETELFGEQIQRLRTT-GVAVVLVEHDVGFVMGQSDRVVVLNlGSVLAEGTPDEIQAHP 260
Cdd:PRK09544 134 ALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCLN-HHICCSGTPEVVSLHP 211
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
16-266 |
7.54e-21 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 91.23 E-value: 7.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 16 TTEPALEVRHVTKRygglTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQLPERRARS 95
Cdd:COG1129 252 PGEVVLEVEGLSVG----GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDAIRA 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 96 GV------RRTfqraQ-LYSRLSVEDNV-LTAMewrgggggllaDLFAAPGRRRREaerreyALSVLAACGLADLRHKPA 167
Cdd:COG1129 328 GIayvpedRKG----EgLVLDLSIRENItLASL-----------DRLSRGGLLDRR------RERALAEEYIKRLRIKTP 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 168 GA-LPIG------QARLVeLARAIADRPRLLLLDEPTSGL--SAHEtELFgEQIQRLRTTGVAVVLVEHDVGFVMGQSDR 238
Cdd:COG1129 387 SPeQPVGnlsggnQQKVV-LAKWLATDPKVLILDEPTRGIdvGAKA-EIY-RLIRELAAEGKAVIVISSELPELLGLSDR 463
|
250 260
....*....|....*....|....*...
gi 521297957 239 VVVLNLGSVLAEGTPDEIQAHPAVRAAY 266
Cdd:COG1129 464 ILVMREGRIVGELDREEATEEAIMAAAT 491
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
17-257 |
3.63e-20 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 89.29 E-value: 3.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 17 TEPALEVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQLPERRARSG 96
Cdd:PRK10762 1 MQALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 97 VRRTFQRAQLYSRLSVEDNVLTAME---------WRgggggllaDLFAApgrrrreaerreyALSVLAACGLADLRHKPA 167
Cdd:PRK10762 81 IGIIHQELNLIPQLTIAENIFLGREfvnrfgridWK--------KMYAE-------------ADKLLARLNLRFSSDKLV 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 168 GALPIGQARLVELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLRTTGVAVVLVEHDVGFVMGQSDRVVVLNLGSV 247
Cdd:PRK10762 140 GELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQF 219
|
250
....*....|
gi 521297957 248 LAEGTPDEIQ 257
Cdd:PRK10762 220 IAEREVADLT 229
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
29-258 |
4.74e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 86.98 E-value: 4.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 29 RYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDG--VDVTRQ--LPERRARSGVRRTFQRA 104
Cdd:PRK13638 10 RYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpLDYSKRglLALRQQVATVFQDPEQQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 105 QLYSRLSVEdnvlTAMEWRgggggllaDLFAAPGRRRREAERreyALSVLAACGLadlRHKPAGALPIGQARLVELARAI 184
Cdd:PRK13638 90 IFYTDIDSD----IAFSLR--------NLGVPEAEITRRVDE---ALTLVDAQHF---RHQPIQCLSHGQKKRVAIAGAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 521297957 185 ADRPRLLLLDEPTSGLS-AHETELFGeQIQRLRTTGVAVVLVEHDVGFVMGQSDRVVVLNLGSVLAEGTPDEIQA 258
Cdd:PRK13638 152 VLQARYLLLDEPTAGLDpAGRTQMIA-IIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFA 225
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
15-256 |
5.75e-20 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 86.13 E-value: 5.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 15 VTTEPALEVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVD-VTRQL----- 88
Cdd:PRK11701 1 MMDQPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDgQLRDLyalse 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 89 PERR--ARS--GVRRTFQRAQLYSRLSVEDNV---LTAMEWRgggggLLADLFAApgrrrreaerreyALSVL-----AA 156
Cdd:PRK11701 81 AERRrlLRTewGFVHQHPRDGLRMQVSAGGNIgerLMAVGAR-----HYGDIRAT-------------AGDWLerveiDA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 157 CGLADLRHKPAGALpigQARLvELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRL-RTTGVAVVLVEHDVGFVMGQ 235
Cdd:PRK11701 143 ARIDDLPTTFSGGM---QQRL-QIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLvRELGLAVVIVTHDLAVARLL 218
|
250 260
....*....|....*....|.
gi 521297957 236 SDRVVVLNLGSVLAEGTPDEI 256
Cdd:PRK11701 219 AHRLLVMKQGRVVESGLTDQV 239
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
20-261 |
1.20e-19 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 86.82 E-value: 1.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 20 ALEVRHVTKRY-GGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQLPERRarsGVR 98
Cdd:PRK11650 3 GLKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADR---DIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 99 RTFQRAQLYSRLSVEDNvltaMEWrggggglladlfaapGRRRREAERREYALSVLAACGLADLRH----KPAgALPIGQ 174
Cdd:PRK11650 80 MVFQNYALYPHMSVREN----MAY---------------GLKIRGMPKAEIEERVAEAARILELEPlldrKPR-ELSGGQ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 175 ARLVELARAIADRPRLLLLDEPTSGLSAhetELFGE---QIQRL-RTTGVAVVLVEHDVGFVMGQSDRVVVLNLGSVLAE 250
Cdd:PRK11650 140 RQRVAMGRAIVREPAVFLFDEPLSNLDA---KLRVQmrlEIQRLhRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQI 216
|
250
....*....|.
gi 521297957 251 GTPDEIQAHPA 261
Cdd:PRK11650 217 GTPVEVYEKPA 227
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
21-242 |
1.76e-19 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 87.54 E-value: 1.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 21 LEVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTS--GAVFLDGvdvtrqlpERRARSGVR 98
Cdd:NF040905 2 LEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDG--------EVCRFKDIR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 99 RT--------FQRAQLYSRLSVEDNVLTAME--------WRGGGGGlladlfaapgrrrreaerreyALSVLAACGLADL 162
Cdd:NF040905 74 DSealgiviiHQELALIPYLSIAENIFLGNErakrgvidWNETNRR---------------------ARELLAKVGLDES 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 163 RHKPAGALPIGQARLVELARAIADRPRLLLLDEPTSGL----SAHETELfgeqIQRLRTTGVAVVLVEHDVGFVMGQSDR 238
Cdd:NF040905 133 PDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTAALneedSAALLDL----LLELKAQGITSIIISHKLNEIRRVADS 208
|
....
gi 521297957 239 VVVL 242
Cdd:NF040905 209 ITVL 212
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
25-245 |
1.79e-19 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 84.16 E-value: 1.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 25 HVTKRY-GGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTR----QLPERRARSGVrr 99
Cdd:PRK10908 6 HVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRlknrEVPFLRRQIGM-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 100 TFQRAQLYSRLSVEDNVLTAMewrggggglladlfaapgrrrreaerreyalsVLAACGLADLRHKPAGAL--------- 170
Cdd:PRK10908 84 IFQDHHLLMDRTVYDNVAIPL--------------------------------IIAGASGDDIRRRVSAALdkvglldka 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 171 ---PI----GQARLVELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLRTTGVAVVLVEHDVGFVMGQSDRVVVLN 243
Cdd:PRK10908 132 knfPIqlsgGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLS 211
|
..
gi 521297957 244 LG 245
Cdd:PRK10908 212 DG 213
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
25-256 |
2.88e-19 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 84.12 E-value: 2.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 25 HVTKRYGGLTAisdvslRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPtSGAVFLDGVDVTRQLPERRARsgvrrtfQRA 104
Cdd:COG4138 7 AVAGRLGPISA------QVNAGELIHLIGPNGAGKSTLLARMAGLLPG-QGEILLNGRPLSDWSAAELAR-------HRA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 105 qlYsrLSVEDNVLTAME-WRGGgggllaDLFAAPGRRRREAERREYALSvlAACGLADLRHKPAGALPIGQARLVELARA 183
Cdd:COG4138 73 --Y--LSQQQSPPFAMPvFQYL------ALHQPAGASSEAVEQLLAQLA--EALGLEDKLSRPLTQLSGGEWQRVRLAAV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 184 I-----ADRP--RLLLLDEPTSGLS-AHETELFGeQIQRLRTTGVAVVLVEHDVGFVMGQSDRVVVLNLGSVLAEGTPDE 255
Cdd:COG4138 141 LlqvwpTINPegQLLLLDEPMNSLDvAQQAALDR-LLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAE 219
|
.
gi 521297957 256 I 256
Cdd:COG4138 220 V 220
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
20-254 |
3.29e-19 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 83.91 E-value: 3.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 20 ALEVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDG--VDVTRQLPE---RRAR 94
Cdd:PRK11124 2 SIQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhFDFSKTPSDkaiRELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 95 SGVRRTFQRAQLYSRLSVEDNvltamewrggggglladLFAAP----GRRRREAERReyALSVLAACGLADLrhkpAGAL 170
Cdd:PRK11124 82 RNVGMVFQQYNLWPHLTVQQN-----------------LIEAPcrvlGLSKDQALAR--AEKLLERLRLKPY----ADRF 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 171 PI----GQARLVELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLRTTGVAVVLVEHDVGFVMGQSDRVVVLNLGS 246
Cdd:PRK11124 139 PLhlsgGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGH 218
|
....*...
gi 521297957 247 VLAEGTPD 254
Cdd:PRK11124 219 IVEQGDAS 226
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
21-258 |
8.01e-19 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 82.66 E-value: 8.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 21 LEVRHVTKRYGG--LTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDV-TRQLPERRARSGV 97
Cdd:cd03251 1 VEFKNVTFRYPGdgPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVrDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 98 rrTFQRAQLYSRlSVEDNVltamewrggggglladLFAAPGRRRREaerreyalsVLAACGLADL----RHKPAG----- 168
Cdd:cd03251 81 --VSQDVFLFND-TVAENI----------------AYGRPGATREE---------VEEAARAANAhefiMELPEGydtvi 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 169 -----ALPIGQARLVELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRL---RTTGVavvlVEHDVGFVMgQSDRVV 240
Cdd:cd03251 133 gergvKLSGGQRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLmknRTTFV----IAHRLSTIE-NADRIV 207
|
250
....*....|....*...
gi 521297957 241 VLNLGSVLAEGTPDEIQA 258
Cdd:cd03251 208 VLEDGKIVERGTHEELLA 225
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
17-266 |
9.03e-19 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 83.30 E-value: 9.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 17 TEPALEVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQLPERRARsg 96
Cdd:PRK10575 8 SDTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFAR-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 97 vrrtfQRAQLYSRLSVEDnvltAMEWRGGGGGLLADLFAAPGRRRREAERREYalSVLAACGLADLRHKPAGALPIGQAR 176
Cdd:PRK10575 86 -----KVAYLPQQLPAAE----GMTVRELVAIGRYPWHGALGRFGAADREKVE--EAISLVGLKPLAHRLVDSLSGGERQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 177 LVELARAIADRPRLLLLDEPTSGLS-AHETELFGeQIQRL-RTTGVAVVLVEHDVGFVMGQSDRVVVLNLGSVLAEGTPD 254
Cdd:PRK10575 155 RAWIAMLVAQDSRCLLLDEPTSALDiAHQVDVLA-LVHRLsQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPA 233
|
250
....*....|..
gi 521297957 255 EIQAHPAVRAAY 266
Cdd:PRK10575 234 ELMRGETLEQIY 245
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
39-256 |
1.03e-18 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 82.67 E-value: 1.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 39 VSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPpTSGAVFLDGVDV----TRQLPERRArsgvrrtfqraqlYsrLSVED 114
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQPLeawsAAELARHRA-------------Y--LSQQQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 115 NVLTAME-WRGGgggllaDLFAAPGRRRREAERREYALSvlAACGLADLRHKPAGALPIGQARLVELA-------RAIAD 186
Cdd:PRK03695 79 TPPFAMPvFQYL------TLHQPDKTRTEAVASALNEVA--EALGLDDKLGRSVNQLSGGEWQRVRLAavvlqvwPDINP 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 187 RPRLLLLDEPTSGLSAHETELFGEQIQRLRTTGVAVVLVEHDVGFVMGQSDRVVVLNLGSVLAEGTPDEI 256
Cdd:PRK03695 151 AGQLLLLDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEV 220
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
19-253 |
1.24e-18 |
|
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: 81.77 E-value: 1.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 19 PALEVRHVTKRY--GGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTrQLPERRARSg 96
Cdd:cd03244 1 GDIEFKNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDIS-KIGLHDLRS- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 97 vRRTF--QRAQLYSRlSVEDNVltamewrgggggllaDLFaapgrrrreaerREYA----LSVLAACGLADLRHKPAGAL 170
Cdd:cd03244 79 -RISIipQDPVLFSG-TIRSNL---------------DPF------------GEYSdeelWQALERVGLKEFVESLPGGL 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 171 P-----------IGQARLVELARAIADRPRLLLLDEPTSGLSaHETElfgEQIQR-LRT--TGVAVVLVEHDVGFVMgQS 236
Cdd:cd03244 130 DtvveeggenlsVGQRQLLCLARALLRKSKILVLDEATASVD-PETD---ALIQKtIREafKDCTVLTIAHRLDTII-DS 204
|
250
....*....|....*..
gi 521297957 237 DRVVVLNLGSVLAEGTP 253
Cdd:cd03244 205 DRILVLDKGRVVEFDSP 221
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
35-256 |
1.37e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 82.91 E-value: 1.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 35 AISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQLPER-----RARSGVRRTFQRAQLYsr 109
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKyirpvRKRIGMVFQFPESQLF-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 110 lsvEDNVLTAMEwrggggglladlFAAPGRRRREAERREYALSVLAACGLA-DLRHKPAGALPIGQARLVELARAIADRP 188
Cdd:PRK13646 100 ---EDTVEREII------------FGPKNFKMNLDEVKNYAHRLLMDLGFSrDVMSQSPFQMSGGQMRKIAIVSILAMNP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521297957 189 RLLLLDEPTSGLSAHETELFGEQIQRLRT-TGVAVVLVEHDVGFVMGQSDRVVVLNLGSVLAEGTPDEI 256
Cdd:PRK13646 165 DIIVLDEPTAGLDPQSKRQVMRLLKSLQTdENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKEL 233
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
16-256 |
1.63e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 82.73 E-value: 1.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 16 TTEPALEVRHVTKRYGGLT--AISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQ-LPERR 92
Cdd:PRK13632 3 NKSVMIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKEnLKEIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 93 ARSGVrrTFQRA--QLYSrLSVEDNVLTAMEWRGGGGGLLADLFAapgrrrreaerrEYALSVlaacGLADLRHKPAGAL 170
Cdd:PRK13632 83 KKIGI--IFQNPdnQFIG-ATVEDDIAFGLENKKVPPKKMKDIID------------DLAKKV----GMEDYLDKEPQNL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 171 PIGQARLVELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLRTTGVAVVL-VEHDVGFVMgQSDRVVVLNLGSVLA 249
Cdd:PRK13632 144 SGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLIsITHDMDEAI-LADKVIVFSEGKLIA 222
|
....*..
gi 521297957 250 EGTPDEI 256
Cdd:PRK13632 223 QGKPKEI 229
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
21-252 |
2.26e-18 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 81.98 E-value: 2.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 21 LEVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGL-----TPPTSGAVFLDGVDVTRQLPE--RRA 93
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgdkSAGSHIELLGRTVQREGRLARdiRKS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 94 RSGVRRTFQRAQLYSRLSVEDNVLTAmewrggggGLLADLFAAPGRRRREAERREYALSVLAACGLADLRHKPAGALPIG 173
Cdd:PRK09984 85 RANTGYIFQQFNLVNRLSVLENVLIG--------ALGSTPFWRTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 174 QARLVELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRL-RTTGVAVVLVEHDVGFVMGQSDRVVVLNLGSVLAEGT 252
Cdd:PRK09984 157 QQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDInQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGS 236
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
20-256 |
2.32e-18 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 81.67 E-value: 2.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 20 ALEVRHVTKRY----------------------GGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAV 77
Cdd:COG1134 4 MIEVENVSKSYrlyhepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 78 FLDG-----VDVTrqlperrarSGvrrtFQraqlySRLSVEDNV--------LTAMEwrggggglLADLFAApgrrrrea 144
Cdd:COG1134 84 EVNGrvsalLELG---------AG----FH-----PELTGRENIylngrllgLSRKE--------IDEKFDE-------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 145 erreyalsVLAACGLADLRHKPAGALPIG-QARLVeLARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLRTTGVAVV 223
Cdd:COG1134 130 --------IVEFAELGDFIDQPVKTYSSGmRARLA-FAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVI 200
|
250 260 270
....*....|....*....|....*....|...
gi 521297957 224 LVEHDVGFVMGQSDRVVVLNLGSVLAEGTPDEI 256
Cdd:COG1134 201 FVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEV 233
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
31-251 |
2.34e-18 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 80.29 E-value: 2.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 31 GGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPP--TSGAVFLDGVDVTRQLPerRARSG-VRrtfQRAQLY 107
Cdd:cd03213 20 SGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRPLDKRSF--RKIIGyVP---QDDILH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 108 SRLSVEDNVltamewrggggglladLFAApgrrrreaerreyALSVLAAcgladlrhkpagalpiGQARLVELARAIADR 187
Cdd:cd03213 95 PTLTVRETL----------------MFAA-------------KLRGLSG----------------GERKRVSIALELVSN 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 521297957 188 PRLLLLDEPTSGLSAHETELFGEQIQRLRTTGVAVVLVEHDV-GFVMGQSDRVVVLNLGSVLAEG 251
Cdd:cd03213 130 PSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQPsSEIFELFDKLLLLSQGRVIYFG 194
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
21-260 |
2.54e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 82.16 E-value: 2.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 21 LEVRHVTKRY-GGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQlPERRARSGVRR 99
Cdd:PRK13652 4 IETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKE-NIREVRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 100 TFQRA--QLYSRlSVEDNVLtamewrggggglladlFAAPGRRRREAERREYALSVLAACGLADLRHKPAGALPIGQARL 177
Cdd:PRK13652 83 VFQNPddQIFSP-TVEQDIA----------------FGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 178 VELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRL-RTTGVAVVLVEHDVGFVMGQSDRVVVLNLGSVLAEGTPDEI 256
Cdd:PRK13652 146 VAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLpETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEI 225
|
....
gi 521297957 257 QAHP 260
Cdd:PRK13652 226 FLQP 229
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
35-256 |
2.84e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 82.10 E-value: 2.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 35 AISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQ-----LPERRARSGVRRTFQRAQLYsr 109
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTsknkdIKQIRKKVGLVFQFPESQLF-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 110 lsvEDNVLTAMEwrggggglladlFAAPGRRRREAERREYALSVLAACGLA-DLRHKPAGALPIGQARLVELARAIADRP 188
Cdd:PRK13649 100 ---EETVLKDVA------------FGPQNFGVSQEEAEALAREKLALVGISeSLFEKNPFELSGGQMRRVAIAGILAMEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521297957 189 RLLLLDEPTSGLSAHETELFGEQIQRLRTTGVAVVLVEHDVGFVMGQSDRVVVLNLGSVLAEGTPDEI 256
Cdd:PRK13649 165 KILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDI 232
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
21-268 |
3.50e-18 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 80.78 E-value: 3.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 21 LEVRHVTKRYGGLTAISDvsLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQLPERRArsgVRRT 100
Cdd:PRK10771 2 LKLTDITWLYHHLPMRFD--LTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRP---VSML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 101 FQRAQLYSRLSVEDNVltamewrgggggllaDLFAAPGRRRREAERREYAlSVLAACGLADLRHKPAGALPIGQARLVEL 180
Cdd:PRK10771 77 FQENNLFSHLTVAQNI---------------GLGLNPGLKLNAAQREKLH-AIARQMGIEDLLARLPGQLSGGQRQRVAL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 181 ARAIADRPRLLLLDEPTSGLS-AHETELFGEQIQRLRTTGVAVVLVEHDVGFVMGQSDRVVVLNLGSVLAEGTPDEIQAH 259
Cdd:PRK10771 141 ARCLVREQPILLLDEPFSALDpALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLSG 220
|
....*....
gi 521297957 260 PAVRAAYLG 268
Cdd:PRK10771 221 KASASALLG 229
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
17-229 |
4.49e-18 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 80.59 E-value: 4.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 17 TEPALEVRHVTKRYGG----LTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQLPERR 92
Cdd:PRK10584 3 AENIVEVHHLKKSVGQgeheLSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 93 AR---SGVRRTFQRAQLYSRLSVEDNVLTAMEWRGGGGGLLADlfaapgrrrreaerreYALSVLAACGLAD-LRHKPAg 168
Cdd:PRK10584 83 AKlraKHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRN----------------GAKALLEQLGLGKrLDHLPA- 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 521297957 169 ALPIGQARLVELARAIADRPRLLLLDEPTSGLSAHEtelfGEQIQRL-----RTTGVAVVLVEHDV 229
Cdd:PRK10584 146 QLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQT----GDKIADLlfslnREHGTTLILVTHDL 207
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
35-256 |
6.30e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 81.32 E-value: 6.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 35 AISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVT-----RQLPERRARSGVRRTFQRAQLYsr 109
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSstskqKEIKPVRKKVGVVFQFPESQLF-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 110 lsvEDNVLTAMEwrggggglladlFAAPGRRRREAERREYALSVLAACGLA-DLRHKPAGALPIGQARLVELARAIADRP 188
Cdd:PRK13643 99 ---EETVLKDVA------------FGPQNFGIPKEKAEKIAAEKLEMVGLAdEFWEKSPFELSGGQMRRVAIAGILAMEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521297957 189 RLLLLDEPTSGLSAHETELFGEQIQRLRTTGVAVVLVEHDVGFVMGQSDRVVVLNLGSVLAEGTPDEI 256
Cdd:PRK13643 164 EVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDV 231
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
21-258 |
8.41e-18 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 82.54 E-value: 8.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 21 LEVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLT--PPTSGAV--------------------- 77
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRIiyhvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 78 ---------------FLDGVDVTRQLPERRARSGVRRTFqraQLYSRLSVEDNVLTAMEWRGGGGGLLADLfaapgrrrr 142
Cdd:TIGR03269 81 pcpvcggtlepeevdFWNLSDKLRRRIRKRIAIMLQRTF---ALYGDDTVLDNVLEALEEIGYEGKEAVGR--------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 143 eaerreyALSVLAACGLADLRHKPAGALPIGQARLVELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRL-RTTGVA 221
Cdd:TIGR03269 149 -------AVDLIEMVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvKASGIS 221
|
250 260 270
....*....|....*....|....*....|....*..
gi 521297957 222 VVLVEHDVGFVMGQSDRVVVLNLGSVLAEGTPDEIQA 258
Cdd:TIGR03269 222 MVLTSHWPEVIEDLSDKAIWLENGEIKEEGTPDEVVA 258
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
35-261 |
8.43e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 80.83 E-value: 8.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 35 AISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVT-----RQLPERRARSGVRRTFQRAQLYSR 109
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITagkknKKLKPLRKKVGIVFQFPEHQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 110 LSVEDNVLTAMEwrggggglladlFAAPgrrrrEAERREYALSVLAACGL-ADLRHKPAGALPIGQARLVELARAIADRP 188
Cdd:PRK13634 102 TVEKDICFGPMN------------FGVS-----EEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIAGVLAMEP 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521297957 189 RLLLLDEPTSGLSAHETELFGEQIQRL-RTTGVAVVLVEHDVGFVMGQSDRVVVLNLGSVLAEGTPDEIQAHPA 261
Cdd:PRK13634 165 EVLVLDEPTAGLDPKGRKEMMEMFYKLhKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
34-256 |
1.48e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 80.13 E-value: 1.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 34 TAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDV--TRQLPERRARSGVrrTFQRA--QLYSR 109
Cdd:PRK13633 24 LALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTsdEENLWDIRNKAGM--VFQNPdnQIVAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 110 LsVEDNVLTAMEwrgggggllaDLFAAPgrrRREAERREYALSvlaACGLADLRHKPAGALPIGQARLVELARAIADRPR 189
Cdd:PRK13633 102 I-VEEDVAFGPE----------NLGIPP---EEIRERVDESLK---KVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521297957 190 LLLLDEPTSGLSAHETELFGEQIQRL-RTTGVAVVLVEHDVGFVMgQSDRVVVLNLGSVLAEGTPDEI 256
Cdd:PRK13633 165 CIIFDEPTAMLDPSGRREVVNTIKELnKKYGITIILITHYMEEAV-EADRIIVMDSGKVVMEGTPKEI 231
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
21-240 |
1.80e-17 |
|
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: 76.72 E-value: 1.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 21 LEVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVdvtrqlperrarsgvrrt 100
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST------------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 101 fQRAQLYSRLSvednvltamewrggggglladlfaapGrrrreaerreyalsvlaacgladlrhkpagalpiGQARLVEL 180
Cdd:cd03221 63 -VKIGYFEQLS--------------------------G----------------------------------GEKMRLAL 81
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 181 ARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLRTTgvaVVLVEHDVGFVmgqsDRVV 240
Cdd:cd03221 82 AKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPGT---VILVSHDRYFL----DQVA 134
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
38-265 |
1.87e-17 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 81.69 E-value: 1.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 38 DVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVtRQLPERRARSGVRRTFQRAQLYSRlSVEDNVL 117
Cdd:TIGR00958 499 GLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPL-VQYDHHYLHRQVALVGQEPVLFSG-SVRENIA 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 118 TAMEwrgggGGLLADLFAAPGRRRREAERREYALSVLAACGladlrhkPAGA-LPIGQARLVELARAIADRPRLLLLDEP 196
Cdd:TIGR00958 577 YGLT-----DTPDEEIMAAAKAANAHDFIMEFPNGYDTEVG-------EKGSqLSGGQKQRIAIARALVRKPRVLILDEA 644
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521297957 197 TSGLSAHETELFGEQIQRLRTTgvaVVLVEHDVGFVMgQSDRVVVLNLGSVLAEGTPDEIQAHPAVRAA 265
Cdd:TIGR00958 645 TSALDAECEQLLQESRSRASRT---VLLIAHRLSTVE-RADQILVLKKGSVVEMGTHKQLMEDQGCYKH 709
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
21-258 |
2.02e-17 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 81.69 E-value: 2.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 21 LEVRHVTKRY----GGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQLPERRARsg 96
Cdd:PRK10535 5 LELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQ-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 97 VRR-----TFQRAQLYSRLSVEDNVltamewrgggggLLADLFAAPGRRRREAErreyALSVLAACGLADLRHKPAGALP 171
Cdd:PRK10535 83 LRRehfgfIFQRYHLLSHLTAAQNV------------EVPAVYAGLERKQRLLR----AQELLQRLGLEDRVEYQPSQLS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 172 IGQARLVELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLRTTGVAVVLVEHDvGFVMGQSDRVVVLNLGSVLAEG 251
Cdd:PRK10535 147 GGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHD-PQVAAQAERVIEIRDGEIVRNP 225
|
....*..
gi 521297957 252 TPDEIQA 258
Cdd:PRK10535 226 PAQEKVN 232
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
20-259 |
2.30e-17 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 81.32 E-value: 2.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 20 ALEVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTrqlpERRARsgvRR 99
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMA----DARHR---RA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 100 TFQR----AQ-----LYSRLSVEDNV--------LTAME--WRggggglLADLfaapgrrrreaerreyalsvLAACGLA 160
Cdd:NF033858 74 VCPRiaymPQglgknLYPTLSVFENLdffgrlfgQDAAErrRR------IDEL--------------------LRATGLA 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 161 DLRHKPAGALPIGQARLVELARAIADRPRLLLLDEPTSG---LSAHEtelFGEQIQRLRTTGVAV-VLV-----EHDVGF 231
Cdd:NF033858 128 PFADRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGvdpLSRRQ---FWELIDRIRAERPGMsVLVataymEEAERF 204
|
250 260
....*....|....*....|....*...
gi 521297957 232 vmgqsDRVVVLNLGSVLAEGTPDEIQAH 259
Cdd:NF033858 205 -----DWLVAMDAGRVLATGTPAELLAR 227
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
21-264 |
4.87e-17 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 78.58 E-value: 4.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 21 LEVRHVTKRYGG---------LTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQlpER 91
Cdd:PRK10419 4 LNVSGLSHHYAHgglsgkhqhQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKL--NR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 92 RARSGVRRT----FQRA--QLYSRLSVEDNVLTAMewRGGGGGLLADLFAApgrrrreaerreyALSVLAACGLAD-LRH 164
Cdd:PRK10419 82 AQRKAFRRDiqmvFQDSisAVNPRKTVREIIREPL--RHLLSLDKAERLAR-------------ASEMLRAVDLDDsVLD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 165 KPAGALPIGQARLVELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLRT-TGVAVVLVEHDVGFVMGQSDRVVVLN 243
Cdd:PRK10419 147 KRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQqFGTACLFITHDLRLVERFCQRVMVMD 226
|
250 260
....*....|....*....|...
gi 521297957 244 LGSVLAEGTPDEIQA--HPAVRA 264
Cdd:PRK10419 227 NGQIVETQPVGDKLTfsSPAGRV 249
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
22-255 |
7.95e-17 |
|
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: 77.19 E-value: 7.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 22 EVRHVTKRY---GGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVtRQLPERRARSGVR 98
Cdd:cd03249 2 EFKNVSFRYpsrPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDI-RDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 99 RTFQRAQLYSRlSVEDNVLtamewrggggglladlFAAPGRRRReaerreyalSVLAACGLADLrHKPAGALPI------ 172
Cdd:cd03249 81 LVSQEPVLFDG-TIAENIR----------------YGKPDATDE---------EVEEAAKKANI-HDFIMSLPDgydtlv 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 173 ---------GQARLVELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLRtTGVAVVLVEHDVGFVMGqSDRVVVLN 243
Cdd:cd03249 134 gergsqlsgGQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAM-KGRTTIVIAHRLSTIRN-ADLIAVLQ 211
|
250
....*....|..
gi 521297957 244 LGSVLAEGTPDE 255
Cdd:cd03249 212 NGQVVEQGTHDE 223
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
33-260 |
2.04e-16 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 77.44 E-value: 2.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 33 LTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQLPE--RRARSGVRRTFQR--AQLYS 108
Cdd:PRK15079 34 LKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDewRAVRSDIQMIFQDplASLNP 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 109 RLSVednvltamewrgggggllADLFAAPGRR----RREAERREYALSVLAACGLAD-----LRHKPAGalpiGQARLVE 179
Cdd:PRK15079 114 RMTI------------------GEIIAEPLRTyhpkLSRQEVKDRVKAMMLKVGLLPnlinrYPHEFSG----GQCQRIG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 180 LARAIADRPRLLLLDEPTSGL----SAHETELFgEQIQRlrTTGVAVVLVEHDVGFVMGQSDRVVVLNLGSVLAEGTPDE 255
Cdd:PRK15079 172 IARALILEPKLIICDEPVSALdvsiQAQVVNLL-QQLQR--EMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDE 248
|
....*
gi 521297957 256 IQAHP 260
Cdd:PRK15079 249 VYHNP 253
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
19-253 |
2.41e-16 |
|
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: 78.90 E-value: 2.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 19 PALEVRHVTKRY--GGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQLPERRARSG 96
Cdd:TIGR01257 927 PGVCVKNLVKIFepSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLG 1006
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 97 VrrTFQRAQLYSRLSVEDNVltamewrggggglladLFAAPGRRRREAERREYALSVLAACGLADLRHKPAGALPIGQAR 176
Cdd:TIGR01257 1007 M--CPQHNILFHHLTVAEHI----------------LFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQR 1068
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521297957 177 LVELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLRtTGVAVVLVEH--DVGFVMGqsDRVVVLNLGSVLAEGTP 253
Cdd:TIGR01257 1069 KLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYR-SGRTIIMSTHhmDEADLLG--DRIAIISQGRLYCSGTP 1144
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
25-256 |
3.45e-16 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 76.18 E-value: 3.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 25 HVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQLPERRARSgVRRTFQRA 104
Cdd:PRK10253 12 QLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARR-IGLLAQNA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 105 QLYSRLSVEDNVLTA--------MEWRGGGGGLLAdlfaapgrrrreaerreyalSVLAACGLADLRHKPAGALPIGQAR 176
Cdd:PRK10253 91 TTPGDITVQELVARGryphqplfTRWRKEDEEAVT--------------------KAMQATGITHLADQSVDTLSGGQRQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 177 LVELARAIADRPRLLLLDEPTSGLS-AHETELFgEQIQRL-RTTGVAVVLVEHDVGFVMGQSDRVVVLNLGSVLAEGTPD 254
Cdd:PRK10253 151 RAWIAMVLAQETAIMLLDEPTTWLDiSHQIDLL-ELLSELnREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPK 229
|
..
gi 521297957 255 EI 256
Cdd:PRK10253 230 EI 231
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
20-256 |
3.50e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 76.38 E-value: 3.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 20 ALEVRHVTKRY--GGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGA---VFLDGVDVT-RQLPERRA 93
Cdd:PRK13640 5 IVEFKHVSFTYpdSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTaKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 94 RSGVrrTFQRA-QLYSRLSVEDNVLTAMEWRGGGGGLLADLFAapgrrrreaerreyalSVLAACGLADLRHKPAGALPI 172
Cdd:PRK13640 85 KVGI--VFQNPdNQFVGATVGDDVAFGLENRAVPRPEMIKIVR----------------DVLADVGMLDYIDSEPANLSG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 173 GQARLVELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLRT-TGVAVVLVEHDVGfVMGQSDRVVVLNLGSVLAEG 251
Cdd:PRK13640 147 GQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKkNNLTVISITHDID-EANMADQVLVLDDGKLLAQG 225
|
....*
gi 521297957 252 TPDEI 256
Cdd:PRK13640 226 SPVEI 230
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
21-250 |
3.73e-16 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 77.74 E-value: 3.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 21 LEVRHVTKrygglTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQLPERRARSGV--- 97
Cdd:PRK10762 258 LKVDNLSG-----PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLANGIvyi 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 98 ---RRtfqRAQLYSRLSVEDNV-LTAMewrgggggllaDLFAAPGrrrreaERREYALSVLAACGLADL-------RHKP 166
Cdd:PRK10762 333 sedRK---RDGLVLGMSVKENMsLTAL-----------RYFSRAG------GSLKHADEQQAVSDFIRLfniktpsMEQA 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 167 AGALPIGQARLVELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLRTTGVAVVLVEHDVGFVMGQSDRVVVLNLGS 246
Cdd:PRK10762 393 IGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGR 472
|
....
gi 521297957 247 VLAE 250
Cdd:PRK10762 473 ISGE 476
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
13-228 |
4.00e-16 |
|
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: 77.79 E-value: 4.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 13 AGVTTEPALEVRHVTKRY-GGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTrQLPER 91
Cdd:TIGR02868 327 AVGLGKPTLELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVS-SLDQD 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 92 RARSGVRRTFQRAQLYSRlSVEDNVltamewrggggglladLFAAPGRRRREaerreyALSVLAACGLAD-LRHKPAG-- 168
Cdd:TIGR02868 406 EVRRRVSVCAQDAHLFDT-TVRENL----------------RLARPDATDEE------LWAALERVGLADwLRALPDGld 462
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 169 --------ALPIGQARLVELARAIADRPRLLLLDEPTSGLSAhETELfgEQIQRLR--TTGVAVVLVEHD 228
Cdd:TIGR02868 463 tvlgeggaRLSGGERQRLALARALLADAPILLLDEPTEHLDA-ETAD--ELLEDLLaaLSGRTVVLITHH 529
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
21-256 |
5.22e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 75.92 E-value: 5.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 21 LEVRHVTKRYGGLT---AISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQ-LPERRARSG 96
Cdd:PRK13650 5 IEVKNLTFKYKEDQekyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEEnVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 97 VrrTFQRA-QLYSRLSVEDNVLTAMEWRGGGGGLLADlfaapgrrrreaeRREYALSVLaacGLADLRHKPAGALPIGQA 175
Cdd:PRK13650 85 M--VFQNPdNQFVGATVEDDVAFGLENKGIPHEEMKE-------------RVNEALELV---GMQDFKEREPARLSGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 176 RLVELARAIADRPRLLLLDEPTSGLSAH-ETELFGeQIQRLRTT-GVAVVLVEHDVGFVmGQSDRVVVLNLGSVLAEGTP 253
Cdd:PRK13650 147 QRVAIAGAVAMRPKIIILDEATSMLDPEgRLELIK-TIKGIRDDyQMTVISITHDLDEV-ALSDRVLVMKNGQVESTSTP 224
|
...
gi 521297957 254 DEI 256
Cdd:PRK13650 225 REL 227
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
28-251 |
5.29e-16 |
|
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: 74.88 E-value: 5.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 28 KRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGvDVTRQLperRARSGvrrtFQraqly 107
Cdd:cd03220 30 GEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG-RVSSLL---GLGGG----FN----- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 108 SRLSVEDNVLTAMEWRGGGGGLLADLFAapgrrrreaerreyalSVLAACGLADLRHKPAGALPIG-QARLvELARAIAD 186
Cdd:cd03220 97 PELTGRENIYLNGRLLGLSRKEIDEKID----------------EIIEFSELGDFIDLPVKTYSSGmKARL-AFAIATAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521297957 187 RPRLLLLDEPTSGLSAHetelFGEQ----IQRLRTTGVAVVLVEHDVGFVMGQSDRVVVLNLGSVLAEG 251
Cdd:cd03220 160 EPDILLIDEVLAVGDAA----FQEKcqrrLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
21-255 |
8.53e-16 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 74.57 E-value: 8.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 21 LEVRHVTKRYG-GLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTR-QLPERRARSGV- 97
Cdd:cd03253 1 IEFENVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREvTLDSLRRAIGVv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 98 -------RRTFQRAQLYSRLSV-EDNVLTAMEwrggggglladlfAAPGRRRREAERREYAlSVLAACGLadlrhKPAGa 169
Cdd:cd03253 81 pqdtvlfNDTIGYNIRYGRPDAtDEEVIEAAK-------------AAQIHDKIMRFPDGYD-TIVGERGL-----KLSG- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 170 lpiGQARLVELARAIADRPRLLLLDEPTSGLSAH-ETELFgEQIQRL---RTTgvavVLVEHDVGFVMgQSDRVVVLNLG 245
Cdd:cd03253 141 ---GEKQRVAIARAILKNPPILLLDEATSALDTHtEREIQ-AALRDVskgRTT----IVIAHRLSTIV-NADKIIVLKDG 211
|
250
....*....|
gi 521297957 246 SVLAEGTPDE 255
Cdd:cd03253 212 RIVERGTHEE 221
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
16-266 |
1.15e-15 |
|
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: 76.26 E-value: 1.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 16 TTEPALEVRHVTKRY-----------GGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPpTSGAVFLDGVDV 84
Cdd:COG4172 271 DAPPLLEARDLKVWFpikrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDL 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 85 TRqLPERRARSgVRRTFQ------RAQLYSRLSVEDNVltamewrgggggllADLFAAPGRRRREAERREYALSVLAACG 158
Cdd:COG4172 350 DG-LSRRALRP-LRRRMQvvfqdpFGSLSPRMTVGQII--------------AEGLRVHGPGLSAAERRARVAEALEEVG 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 159 L-ADLRHKPAGALPIGQARLVELARAIADRPRLLLLDEPTSGL----SAHETELFGEqIQRLRttGVAVVLVEHDVGFVM 233
Cdd:COG4172 414 LdPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALdvsvQAQILDLLRD-LQREH--GLAYLFISHDLAVVR 490
|
250 260 270
....*....|....*....|....*....|...
gi 521297957 234 GQSDRVVVLNLGSVLAEGTPDEIQAHPavRAAY 266
Cdd:COG4172 491 ALAHRVMVMKDGKVVEQGPTEQVFDAP--QHPY 521
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
21-256 |
1.26e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 75.12 E-value: 1.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 21 LEVRHVTKRYGG-----LTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAV---FLD------------ 80
Cdd:PRK13651 3 IKVKNIVKIFNKklpteLKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewiFKDeknkkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 81 -GVDVTRQLPER---------RARSGVRRTFQRAQLYSRlSVEDNVLtamewrggggglladlFAAPGRRRREAERREYA 150
Cdd:PRK13651 83 vLEKLVIQKTRFkkikkikeiRRRVGVVFQFAEYQLFEQ-TIEKDII----------------FGPVSMGVSKEEAKKRA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 151 LSVLAACGLAD--LRHKPAGaLPIGQARLVELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLRTTGVAVVLVEHD 228
Cdd:PRK13651 146 AKYIELVGLDEsyLQRSPFE-LSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHD 224
|
250 260
....*....|....*....|....*...
gi 521297957 229 VGFVMGQSDRVVVLNLGSVLAEGTPDEI 256
Cdd:PRK13651 225 LDNVLEWTKRTIFFKDGKIIKDGDTYDI 252
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
21-253 |
1.74e-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: 72.83 E-value: 1.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 21 LEVRHVTKRYGG--LTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRqLPERRARSGVR 98
Cdd:cd03369 7 IEVENLSVRYAPdlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDIST-IPLEDLRSSLT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 99 RTFQRAQLYSRlSVEDNVLTAMEWrgggggLLADLFAApgrrrreaerreyalsvlaacgladLRHKPAGA-LPIGQARL 177
Cdd:cd03369 86 IIPQDPTLFSG-TIRSNLDPFDEY------SDEEIYGA-------------------------LRVSEGGLnLSQGQRQL 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 521297957 178 VELARAIADRPRLLLLDEPTSGLSAHETELFGEQIqRLRTTGVAVVLVEHDVGFVMgQSDRVVVLNLGSVLAEGTP 253
Cdd:cd03369 134 LCLARALLKRPRVLVLDEATASIDYATDALIQKTI-REEFTNSTILTIAHRLRTII-DYDKILVMDAGEVKEYDHP 207
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-260 |
2.07e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 73.79 E-value: 2.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 21 LEVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLT-----PPTSGAVFLDGVDVTRqLPERRARS 95
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIelypeARVSGEVYLDGQDIFK-MDVIELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 96 GVRRTFQRAQLYSRLSVEDNVLTAMEWRGGGGGLlADLFAAPGRRRREAERREYALSVLAAcgladlrhkPAGALPIGQA 175
Cdd:PRK14247 83 RVQMVFQIPNPIPNLSIFENVALGLKLNRLVKSK-KELQERVRWALEKAQLWDEVKDRLDA---------PAGKLSGGQQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 176 RLVELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLRTTgVAVVLVEHDVGFVMGQSDRVVVLNLGSVLAEGTPDE 255
Cdd:PRK14247 153 QRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTRE 231
|
....*
gi 521297957 256 IQAHP 260
Cdd:PRK14247 232 VFTNP 236
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
19-260 |
2.32e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 73.98 E-value: 2.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 19 PALEVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLF-------DIISGLTppTSGAVFLDGVDV--TRQLP 89
Cdd:PRK14271 20 PAMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLrtlnrmnDKVSGYR--YSGDVLLGGRSIfnYRDVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 90 ERRARSGVrrTFQRAQLYSrLSVEDNVLTAMewRGGGGGLLADLFAApgrrrreaerreyALSVLAACGLADLRHKPAGA 169
Cdd:PRK14271 98 EFRRRVGM--LFQRPNPFP-MSIMDNVLAGV--RAHKLVPRKEFRGV-------------AQARLTEVGLWDAVKDRLSD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 170 LPI----GQARLVELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLrTTGVAVVLVEHDVGFVMGQSDRVVVLNLG 245
Cdd:PRK14271 160 SPFrlsgGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSL-ADRLTVIIVTHNLAQAARISDRAALFFDG 238
|
250
....*....|....*
gi 521297957 246 SVLAEGTPDEIQAHP 260
Cdd:PRK14271 239 RLVEEGPTEQLFSSP 253
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
38-247 |
3.26e-15 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 72.50 E-value: 3.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 38 DVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTrQLPERRARSGVRRTFQRAQLYSRlSVEDNVL 117
Cdd:cd03248 32 DVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPIS-QYEHKYLHSKVSLVGQEPVLFAR-SLQDNIA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 118 TAMEWRGGGGGLLADLFAAPGRRrreaerreyaLSVLAACGLADLRHKpAGALPIGQARLVELARAIADRPRLLLLDEPT 197
Cdd:cd03248 110 YGLQSCSFECVKEAAQKAHAHSF----------ISELASGYDTEVGEK-GSQLSGGQKQRVAIARALIRNPQVLILDEAT 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 521297957 198 SGLSAhETELFGEQIQRLRTTGVAVVLVEHDVGFVMgQSDRVVVLNLGSV 247
Cdd:cd03248 179 SALDA-ESEQQVQQALYDWPERRTVLVIAHRLSTVE-RADQILVLDGGRI 226
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
36-256 |
7.05e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 72.55 E-value: 7.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 36 ISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQ-----LPERRARSGVRRTFQRAQLYsrl 110
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPEtgnknLKKLRKKVSLVFQFPEAQLF--- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 111 svEDNVLTAMEwrggggglladlFAAPGRRRREAERREYALSVLAACGLA-DLRHKPAGALPIGQARLVELARAIADRPR 189
Cdd:PRK13641 100 --ENTVLKDVE------------FGPKNFGFSEDEAKEKALKWLKKVGLSeDLISKSPFELSGGQMRRVAIAGVMAYEPE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 521297957 190 LLLLDEPTSGLSAHETELFGEQIQRLRTTGVAVVLVEHDVGFVMGQSDRVVVLNLGSVLAEGTPDEI 256
Cdd:PRK13641 166 ILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEI 232
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
21-77 |
7.51e-15 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 73.82 E-value: 7.51e-15
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 521297957 21 LEVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAV 77
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTI 379
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
19-229 |
7.88e-15 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 71.77 E-value: 7.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 19 PALEVRHVTKRY--GGLTA--ISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQLPERRAR 94
Cdd:PRK11629 4 ILLQCDNLCKRYqeGSVQTdvLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 95 SGVRR---TFQRAQLYSRLSVEDNVltAMEWRGGGgglladlfAAPGRRRREaerreyALSVLAACGLADLRHKPAGALP 171
Cdd:PRK11629 84 LRNQKlgfIYQFHHLLPDFTALENV--AMPLLIGK--------KKPAEINSR------ALEMLAAVGLEHRANHRPSELS 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 521297957 172 IGQARLVELARAIADRPRLLLLDEPTSGLSAHET----ELFGEQIQRlrtTGVAVVLVEHDV 229
Cdd:PRK11629 148 GGERQRVAIARALVNNPRLVLADEPTGNLDARNAdsifQLLGELNRL---QGTAFLVVTHDL 206
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
21-77 |
1.20e-14 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 73.23 E-value: 1.20e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 521297957 21 LEVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAV 77
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTI 381
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
24-245 |
1.67e-14 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 72.84 E-value: 1.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 24 RHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQLPERRARSGVRRTFQR 103
Cdd:PRK10982 2 SNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGISMVHQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 104 AQLYSRLSVEDNVltameWrggggglladLFAAPGRRRREAERREY--ALSVLAACGL-ADLRHKPAgALPIGQARLVEL 180
Cdd:PRK10982 82 LNLVLQRSVMDNM-----W----------LGRYPTKGMFVDQDKMYrdTKAIFDELDIdIDPRAKVA-TLSVSQMQMIEI 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 521297957 181 ARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLRTTGVAVVLVEHDVGFVMGQSDRVVVLNLG 245
Cdd:PRK10982 146 AKAFSYNAKIVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDG 210
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-260 |
5.52e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 69.69 E-value: 5.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 13 AGVTTEPALEVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTP------PTSGAVFLDGVDVTR 86
Cdd:PRK14246 3 AGKSAEDVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 87 qLPERRARSGVRRTFQRAQLYSRLSVEDNVLTAMEWRGGGGGLLADLFAAPGRRRREAERREYalsvlaacglaDLRHKP 166
Cdd:PRK14246 83 -IDAIKLRKEVGMVFQQPNPFPHLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVY-----------DRLNSP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 167 AGALPIGQARLVELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLRTTgVAVVLVEHDVGFVMGQSDRVVVLNLGS 246
Cdd:PRK14246 151 ASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGE 229
|
250
....*....|....
gi 521297957 247 VLAEGTPDEIQAHP 260
Cdd:PRK14246 230 LVEWGSSNEIFTSP 243
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
17-251 |
7.85e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 69.53 E-value: 7.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 17 TEPALEVRHVTKRY-GGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQLpERRARS 95
Cdd:PRK15056 3 QQAGIVVNDVTVTWrNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQAL-QKNLVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 96 GVRRTFQRAQLYSRLsVEDNVLTA----MEW-RGGGGGLLADLFAApgrrrreaerreyalsvLAACGLADLRHKPAGAL 170
Cdd:PRK15056 82 YVPQSEEVDWSFPVL-VEDVVMMGryghMGWlRRAKKRDRQIVTAA-----------------LARVDMVEFRHRQIGEL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 171 PIGQARLVELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLRTTGVAVVLVEHDVGFVMGQSDRVVVLNlGSVLAE 250
Cdd:PRK15056 144 SGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMVK-GTVLAS 222
|
.
gi 521297957 251 G 251
Cdd:PRK15056 223 G 223
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
17-260 |
8.34e-14 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 69.99 E-value: 8.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 17 TEPALEVRHVTKRY----------GGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTR 86
Cdd:PRK11308 2 QQPLLQAIDLKKHYpvkrglfkpeRLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 87 qlPERRARSGVRRT----FQR--AQLYSRLSVEDNV---------LTAMEWRGGggglladlfaapgrrrreaerreyAL 151
Cdd:PRK11308 82 --ADPEAQKLLRQKiqivFQNpyGSLNPRKKVGQILeepllintsLSAAERREK------------------------AL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 152 SVLAACGLadlRHKPAGALPI----GQARLVELARAIADRPRLLLLDEPTSGLS----AHETELFGEQIQRLrttGVAVV 223
Cdd:PRK11308 136 AMMAKVGL---RPEHYDRYPHmfsgGQRQRIAIARALMLDPDVVVADEPVSALDvsvqAQVLNLMMDLQQEL---GLSYV 209
|
250 260 270
....*....|....*....|....*....|....*..
gi 521297957 224 LVEHDVGFVMGQSDRVVVLNLGSVLAEGTPDEIQAHP 260
Cdd:PRK11308 210 FISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNP 246
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
18-246 |
9.41e-14 |
|
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: 68.61 E-value: 9.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 18 EPALEVRHVTKRY-----GG--LTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLD----GVDVTr 86
Cdd:COG4778 2 TTLLEVENLSKTFtlhlqGGkrLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggWVDLA- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 87 QLPERRARSgVRRT-------FQRAqlYSRLSVEDNV---LTAMEWRGGGGGLLAdlfaapgrrrreaerreyaLSVLAA 156
Cdd:COG4778 81 QASPREILA-LRRRtigyvsqFLRV--IPRVSALDVVaepLLERGVDREEARARA-------------------RELLAR 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 157 CGLAD-LRHKPAGALPIGQARLVELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLRTTGVAVVLVEHDVGFVMGQ 235
Cdd:COG4778 139 LNLPErLWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAV 218
|
250
....*....|.
gi 521297957 236 SDRVVVLNLGS 246
Cdd:COG4778 219 ADRVVDVTPFS 229
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
20-259 |
1.23e-13 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 70.38 E-value: 1.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 20 ALEVRHVTKRYGGLT-AISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVtRQLperrARSGVR 98
Cdd:PRK13657 334 AVEFDDVSFSYDNSRqGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDI-RTV----TRASLR 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 99 RT----FQRAQLYSRlSVEDNVL------TAMEWRGGGGGLLADLFAAPGRRrreaerreyalsvlaacGLADLRHKPAG 168
Cdd:PRK13657 409 RNiavvFQDAGLFNR-SIEDNIRvgrpdaTDEEMRAAAERAQAHDFIERKPD-----------------GYDTVVGERGR 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 169 ALPIGQARLVELARAIADRPRLLLLDEPTSGLSAhETE----LFGEQIQRLRTTGVavvlVEHDVGFVMgQSDRVVVLNL 244
Cdd:PRK13657 471 QLSGGERQRLAIARALLKDPPILILDEATSALDV-ETEakvkAALDELMKGRTTFI----IAHRLSTVR-NADRILVFDN 544
|
250
....*....|....*
gi 521297957 245 GSVLAEGTPDEIQAH 259
Cdd:PRK13657 545 GRVVESGSFDELVAR 559
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
37-245 |
1.81e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 69.69 E-value: 1.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 37 SDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDV----TRQ--------LPERRARSGvrrtfqra 104
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEInalsTAQrlarglvyLPEDRQSSG-------- 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 105 qLYSRLSVEDNVLTAMEWRGGggglladLFAAPGRRRREAERREYALSVlaACGLADlrhKPAGALPIGQARLVELARAI 184
Cdd:PRK15439 352 -LYLDAPLAWNVCALTHNRRG-------FWIKPARENAVLERYRRALNI--KFNHAE---QAARTLSGGNQQKVLIAKCL 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 521297957 185 ADRPRLLLLDEPTSGLSAHETELFGEQIQRLRTTGVAVVLVEHDVGFVMGQSDRVVVLNLG 245
Cdd:PRK15439 419 EASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQG 479
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
4-252 |
2.33e-13 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 70.04 E-value: 2.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 4 VATSTDSSVAGVTTEPALEVRHVTKRYGGLT--AISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDG 81
Cdd:TIGR01257 1921 VAEERQRIISGGNKTDILRLNELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAG 2000
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 82 VDVTRQLPERRARSGVRRTFQRAqlysrlsveDNVLTAMEwrggGGGLLADLFAAPGRRRREAERREyalsvLAACGLAD 161
Cdd:TIGR01257 2001 KSILTNISDVHQNMGYCPQFDAI---------DDLLTGRE----HLYLYARLRGVPAEEIEKVANWS-----IQSLGLSL 2062
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 162 LRHKPAGALPIGQARLVELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLRTTGVAVVLVEHDVGFVMGQSDRVVV 241
Cdd:TIGR01257 2063 YADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAI 2142
|
250
....*....|.
gi 521297957 242 LNLGSVLAEGT 252
Cdd:TIGR01257 2143 MVKGAFQCLGT 2153
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
16-256 |
2.46e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 68.24 E-value: 2.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 16 TTEPALEVRHVTKRYGGLTA--ISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQ-LPERR 92
Cdd:PRK13648 3 DKNSIIVFKNVSFQYQSDASftLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDnFEKLR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 93 ARSGVrrTFQRAQ-LYSRLSVEDNVLTAMEwrggggglladLFAAPGRRRREAERreyalSVLAACGLADLRHKPAGALP 171
Cdd:PRK13648 83 KHIGI--VFQNPDnQFVGSIVKYDVAFGLE-----------NHAVPYDEMHRRVS-----EALKQVDMLERADYEPNALS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 172 IGQARLVELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLRTT-GVAVVLVEHDVGFVMGqSDRVVVLNLGSVLAE 250
Cdd:PRK13648 145 GGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEhNITIISITHDLSEAME-ADHVIVMNKGTVYKE 223
|
....*.
gi 521297957 251 GTPDEI 256
Cdd:PRK13648 224 GTPTEI 229
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
18-250 |
4.56e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 68.40 E-value: 4.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 18 EPALEVRHVTKRygGLTaiSDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQLPERRARSGV 97
Cdd:PRK11288 255 EVRLRLDGLKGP--GLR--EPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRAGI 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 98 -----RRTFQraQLYSRLSVEDNV-LTAMEWRgggggLLADLFAAPGRRRREAERREYALSVLAACgladlRHKPAGALP 171
Cdd:PRK11288 331 mlcpeDRKAE--GIIPVHSVADNInISARRHH-----LRAGCLINNRWEAENADRFIRSLNIKTPS-----REQLIMNLS 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 172 IGQARLVELARAIADRPRLLLLDEPTSGL---SAHETElfgEQIQRLRTTGVAVVLVEHDVGFVMGQSDRVVVLNLGSVL 248
Cdd:PRK11288 399 GGNQQKAILGRWLSEDMKVILLDEPTRGIdvgAKHEIY---NVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIA 475
|
..
gi 521297957 249 AE 250
Cdd:PRK11288 476 GE 477
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
35-246 |
4.96e-13 |
|
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: 65.95 E-value: 4.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 35 AISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGvdvtrqlperrarsGVRRTFQRAQLYSRlSVED 114
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG--------------SIAYVSQEPWIQNG-TIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 115 NVLtamewrggggglladlFAAPgrrrreAERREYaLSVLAACGL-ADLRHKPAGALPI----------GQ-ARlVELAR 182
Cdd:cd03250 85 NIL----------------FGKP------FDEERY-EKVIKACALePDLEILPDGDLTEigekginlsgGQkQR-ISLAR 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 521297957 183 AIADRPRLLLLDEPTSGLSAH-ETELFGEQIQRLRTTGVAVVLVEHDVGFVMgQSDRVVVLNLGS 246
Cdd:cd03250 141 AVYSDADIYLLDDPLSAVDAHvGRHIFENCILGLLLNNKTRILVTHQLQLLP-HADQIVVLDNGR 204
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
19-260 |
8.75e-13 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 67.24 E-value: 8.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 19 PALEVRHVT----KRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPP----TSGAVFLDGVDVTRQLPE 90
Cdd:COG4170 2 PLLDIRNLTieidTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGIDLLKLSPR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 91 RRaRSGVRR----TFQRAQ--LYSRLSVEDNVLTAM-------------EWRGGggglladlfaapgrrrreaerreYAL 151
Cdd:COG4170 82 ER-RKIIGReiamIFQEPSscLDPSAKIGDQLIEAIpswtfkgkwwqrfKWRKK-----------------------RAI 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 152 SVLAACGLADlrHKP-----AGALPIGQARLVELARAIADRPRLLLLDEPTSGLSAhETELfgeQIQRL-----RTTGVA 221
Cdd:COG4170 138 ELLHRVGIKD--HKDimnsyPHELTEGECQKVMIAMAIANQPRLLIADEPTNAMES-TTQA---QIFRLlarlnQLQGTS 211
|
250 260 270
....*....|....*....|....*....|....*....
gi 521297957 222 VVLVEHDVGFVMGQSDRVVVLNLGSVLAEGTPDEIQAHP 260
Cdd:COG4170 212 ILLISHDLESISQWADTITVLYCGQTVESGPTEQILKSP 250
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
36-227 |
1.26e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 64.97 E-value: 1.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 36 ISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQlperRARSGVRRTF--QRAQLYSRLSVE 113
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKD----LCTYQKQLCFvgHRSGINPYLTLR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 114 DNVLTamewrgggggllaDLFAAPGrrrreaerreyALSVLAACGLADLRHK---PAGALPIGQARLVELARAIADRPRL 190
Cdd:PRK13540 93 ENCLY-------------DIHFSPG-----------AVGITELCRLFSLEHLidyPCGLLSSGQKRQVALLRLWMSKAKL 148
|
170 180 190
....*....|....*....|....*....|....*..
gi 521297957 191 LLLDEPTSGLSAHETELFGEQIQRLRTTGVAVVLVEH 227
Cdd:PRK13540 149 WLLDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSH 185
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
25-228 |
1.31e-12 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 67.27 E-value: 1.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 25 HVTKRYGGLTAI-SDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGavfldgvdvtrqlpERRARSGVRRTF-- 101
Cdd:TIGR03719 9 RVSKVVPPKKEIlKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNG--------------EARPQPGIKVGYlp 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 102 QRAQLYSRLSVEDNVLTAMEWRGGGGG---LLADLFAAPGRRRREAERREYAL-SVLAACGLADLRHK----------PA 167
Cdd:TIGR03719 75 QEPQLDPTKTVRENVEEGVAEIKDALDrfnEISAKYAEPDADFDKLAAEQAELqEIIDAADAWDLDSQleiamdalrcPP 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 521297957 168 GALPI-----GQARLVELARAIADRPRLLLLDEPTSGLSAhETELFGEQ-IQRLRTTgvaVVLVEHD 228
Cdd:TIGR03719 155 WDADVtklsgGERRRVALCRLLLSKPDMLLLDEPTNHLDA-ESVAWLERhLQEYPGT---VVAVTHD 217
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
21-265 |
7.24e-12 |
|
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: 64.85 E-value: 7.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 21 LEVRHVT---------KRyggltaISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPT-SGAVFLDGVDVTRQLPE 90
Cdd:TIGR02633 258 LEARNLTcwdvinphrKR------VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNPA 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 91 RRARSG---VRRTFQRAQLYSRLSVEDNVLTAMEWRGGGGGLLADlfaapGRRRREAERREYALSVLAACglADLrhkPA 167
Cdd:TIGR02633 332 QAIRAGiamVPEDRKRHGIVPILGVGKNITLSVLKSFCFKMRIDA-----AAELQIIGSAIQRLKVKTAS--PFL---PI 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 168 GALPIGQARLVELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLRTTGVAVVLVEHDVGFVMGQSDRVVVLNLGSV 247
Cdd:TIGR02633 402 GRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
250
....*....|....*...
gi 521297957 248 LAEGTPDEIQAHPAVRAA 265
Cdd:TIGR02633 482 KGDFVNHALTQEQVLAAA 499
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
17-200 |
7.71e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 63.64 E-value: 7.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 17 TEPALEVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDII---SGLTP--PTSGAVFLDGVDV------T 85
Cdd:PRK14239 2 TEPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrmNDLNPevTITGSIVYNGHNIysprtdT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 86 RQLperraRSGVRRTFQRAQLYSrLSVEDNVLTAMewRGGGGGLLADLFAApgrrrreaerreYALSVLAAC---GLADL 162
Cdd:PRK14239 82 VDL-----RKEIGMVFQQPNPFP-MSIYENVVYGL--RLKGIKDKQVLDEA------------VEKSLKGASiwdEVKDR 141
|
170 180 190
....*....|....*....|....*....|....*...
gi 521297957 163 RHKPAGALPIGQARLVELARAIADRPRLLLLDEPTSGL 200
Cdd:PRK14239 142 LHDSALGLSGGQQQRVCIARVLATSPKIILLDEPTSAL 179
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
21-258 |
1.24e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 63.19 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 21 LEVRHVTKRY---GGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQlPERRARSGV 97
Cdd:PRK13642 5 LEVENLVFKYekeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAE-NVWNLRRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 98 RRTFQRA-QLYSRLSVEDNVLTAMEwrggggglladlfaapGRRRREAERREYALSVLAACGLADLRHKPAGALPIGQAR 176
Cdd:PRK13642 84 GMVFQNPdNQFVGATVEDDVAFGME----------------NQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 177 LVELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLRTT-GVAVVLVEHDVGfVMGQSDRVVVLNLGSVLAEGTPDE 255
Cdd:PRK13642 148 RVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKyQLTVLSITHDLD-EAASSDRILVMKAGEIIKEAAPSE 226
|
...
gi 521297957 256 IQA 258
Cdd:PRK13642 227 LFA 229
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
34-250 |
1.24e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 62.67 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 34 TAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTP--PTSGAVFLDGVDVTRQLPerrarsgvrrtfqraqLYSRLS 111
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVPDNQFGREAS----------------LIDAIG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 112 VEDNVLTAMEwrggggglladlfaapgrrrreaerreyalsVLAACGLAD---LRHKPAgALPIGQARLVELARAIADRP 188
Cdd:COG2401 108 RKGDFKDAVE-------------------------------LLNAVGLSDavlWLRRFK-ELSTGQKFRFRLALLLAERP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521297957 189 RLLLLDEPTSGLSAHETELFGEQIQRL-RTTGVAVVLVEHDVGFVMG-QSDRVVVLNLGSVLAE 250
Cdd:COG2401 156 KLLVIDEFCSHLDRQTAKRVARNLQKLaRRAGITLVVATHHYDVIDDlQPDLLIFVGYGGVPEE 219
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
19-264 |
1.68e-11 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 63.28 E-value: 1.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 19 PALEVRHVTKRY----GGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPP----TSGAVFLDGVDVTRQLP- 89
Cdd:PRK15093 2 PLLDIRNLTIEFktsdGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDnwrvTADRMRFDDIDLLRLSPr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 90 ERRARSG--VRRTFQRAQlySRLSVEDNVLTAMewrggggglladLFAAPGRRRREAERREY------ALSVLAACGLAD 161
Cdd:PRK15093 82 ERRKLVGhnVSMIFQEPQ--SCLDPSERVGRQL------------MQNIPGWTYKGRWWQRFgwrkrrAIELLHRVGIKD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 162 lrHKPA-GALPI----GQARLVELARAIADRPRLLLLDEPTSGLSAhETElfgEQIQRLRT-----TGVAVVLVEHDVGF 231
Cdd:PRK15093 148 --HKDAmRSFPYelteGECQKVMIAIALANQPRLLIADEPTNAMEP-TTQ---AQIFRLLTrlnqnNNTTILLISHDLQM 221
|
250 260 270
....*....|....*....|....*....|....*.
gi 521297957 232 VMGQSDRVVVLNLGSVLAEGTPDEIQA---HPAVRA 264
Cdd:PRK15093 222 LSQWADKINVLYCGQTVETAPSKELVTtphHPYTQA 257
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
15-255 |
2.24e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 63.69 E-value: 2.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 15 VTTEPALEVRHVTKRY--GGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTrQLPERR 92
Cdd:PRK11160 333 AADQVSLTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIA-DYSEAA 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 93 ARSGVRRTFQRAQLYSRlSVEDNVltamewrggggglladLFAAPGRRRReaerreyALS-VLAACGLADLRHKPAG--- 168
Cdd:PRK11160 412 LRQAISVVSQRVHLFSA-TLRDNL----------------LLAAPNASDE-------ALIeVLQQVGLEKLLEDDKGlna 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 169 -------ALPIGQARLVELARAIADRPRLLLLDEPTSGLSAhETElfgEQIQRL---RTTGVAVVLVEHDVgFVMGQSDR 238
Cdd:PRK11160 468 wlgeggrQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDA-ETE---RQILELlaeHAQNKTVLMITHRL-TGLEQFDR 542
|
250
....*....|....*..
gi 521297957 239 VVVLNLGSVLAEGTPDE 255
Cdd:PRK11160 543 ICVMDNGQIIEQGTHQE 559
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
25-264 |
4.61e-11 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 62.20 E-value: 4.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 25 HVTKRYGGLTAISDVSLrvdPGE-VCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDG---VDVTRQL---PERRaRSGV 97
Cdd:PRK11144 5 NFKQQLGDLCLTVNLTL---PAQgITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlFDAEKGIclpPEKR-RIGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 98 rrTFQRAQLYSRLSVEDNVLTAMewrgggGGLLADLFAapgrrrreaerreyalSVLAACGLADLRHKPAGALPIGQARL 177
Cdd:PRK11144 81 --VFQDARLFPHYKVRGNLRYGM------AKSMVAQFD----------------KIVALLGIEPLLDRYPGSLSGGEKQR 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 178 VELARAIADRPRLLLLDEPTSGLSA-HETELFgEQIQRL-RTTGVAVVLVEHDVGFVMGQSDRVVVLNLGSVLAEGTPDE 255
Cdd:PRK11144 137 VAIGRALLTAPELLLMDEPLASLDLpRKRELL-PYLERLaREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEE 215
|
....*....
gi 521297957 256 IQAHPAVRA 264
Cdd:PRK11144 216 VWASSAMRP 224
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
25-256 |
6.82e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 61.00 E-value: 6.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 25 HVTKRYGglTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISG-LTPP-------TSGAVFLDGVDVTRQLPERRARsg 96
Cdd:PRK13547 8 HVARRHR--AILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdLTGGgaprgarVTGDVTLNGEPLAAIDAPRLAR-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 97 vRRTF--QRAQLYSRLSVEDNVLTAmewRGGGGGLLADLFAAPGRRrreaerreyALSVLAACGLADLRHKPAGALPIGQ 174
Cdd:PRK13547 84 -LRAVlpQAAQPAFAFSAREIVLLG---RYPHARRAGALTHRDGEI---------AWQALALAGATALVGRDVTTLSGGE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 175 ARLVELARAIAD---------RPRLLLLDEPTSGLS-AHETELFgEQIQRL-RTTGVAVVLVEHDVGFVMGQSDRVVVLN 243
Cdd:PRK13547 151 LARVQFARVLAQlwpphdaaqPPRYLLLDEPTAALDlAHQHRLL-DTVRRLaRDWNLGVLAIVHDPNLAARHADRIAMLA 229
|
250
....*....|...
gi 521297957 244 LGSVLAEGTPDEI 256
Cdd:PRK13547 230 DGAIVAHGAPADV 242
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
35-256 |
8.48e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 61.18 E-value: 8.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 35 AISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLD------GVDVTRQLPERRARSGVRRTFQRAQLYS 108
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGdyaipaNLKKIKEVKRLRKEIGLVFQFPEYQLFQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 109 RlSVEDNVltamewrggggglladlfaAPGRRRREAERREYALSVLAACGLADLRHKPAGALPI----GQARLVELARAI 184
Cdd:PRK13645 106 E-TIEKDI-------------------AFGPVNLGENKQEAYKKVPELLKLVQLPEDYVKRSPFelsgGQKRRVALAGII 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 521297957 185 ADRPRLLLLDEPTSGLSAHETELFGEQIQRL-RTTGVAVVLVEHDVGFVMGQSDRVVVLNLGSVLAEGTPDEI 256
Cdd:PRK13645 166 AMDGNTLVLDEPTGGLDPKGEEDFINLFERLnKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEI 238
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
21-256 |
8.74e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 61.02 E-value: 8.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 21 LEVRHVT-----KRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFL-DGVDVTRQLPERRAR 94
Cdd:PRK13631 22 LRVKNLYcvfdeKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgDIYIGDKKNNHELIT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 95 SGVRRTFQRA-QLYSRLSVednVLTAMEWRGGGGGLLADLFAAP-GRRRREAERREYALSVLAACGLAD--LRHKPAGaL 170
Cdd:PRK13631 102 NPYSKKIKNFkELRRRVSM---VFQFPEYQLFKDTIEKDIMFGPvALGVKKSEAKKLAKFYLNKMGLDDsyLERSPFG-L 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 171 PIGQARLVELARAIADRPRLLLLDEPTSGLS-AHETELFgEQIQRLRTTGVAVVLVEHDVGFVMGQSDRVVVLNLGSVLA 249
Cdd:PRK13631 178 SGGQKRRVAIAGILAIQPEILIFDEPTAGLDpKGEHEMM-QLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILK 256
|
....*..
gi 521297957 250 EGTPDEI 256
Cdd:PRK13631 257 TGTPYEI 263
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
18-200 |
9.17e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 61.57 E-value: 9.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 18 EPALEVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPT-------------SGAVFLD---- 80
Cdd:PRK10938 258 EPRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPQGysndltlfgrrrgSGETIWDikkh 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 81 -GVdVTRQLP-ERRARSGVRRT-----FQRAQLYSRLSVEDNVLtAMEWrggggglladlfaapgrrrreaerreyalsv 153
Cdd:PRK10938 338 iGY-VSSSLHlDYRVSTSVRNVilsgfFDSIGIYQAVSDRQQKL-AQQW------------------------------- 384
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 521297957 154 LAACGLAD-LRHKPAGALPIGQARLVELARAIADRPRLLLLDEPTSGL 200
Cdd:PRK10938 385 LDILGIDKrTADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGL 432
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
36-255 |
1.26e-10 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 61.22 E-value: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 36 ISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPP---TSGAVFLDGVDVTRQlpERRARSGVRRtfQRAQLYSRLSV 112
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPIDAK--EMRAISAYVQ--QDDLFIPTLTV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 113 EDNVLTAMEWRGgggglladlfaapGRRRREAERREYALSVLAACGLADLRHKPAGA------LPIGQARLVELARAIAD 186
Cdd:TIGR00955 117 REHLMFQAHLRM-------------PRRVTKKEKRERVDEVLQALGLRKCANTRIGVpgrvkgLSGGERKRLAFASELLT 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 521297957 187 RPRLLLLDEPTSGL---SAHETElfgEQIQRLRTTGVAVVLVEHDVGF-VMGQSDRVVVLNLGSVLAEGTPDE 255
Cdd:TIGR00955 184 DPPLLFCDEPTSGLdsfMAYSVV---QVLKGLAQKGKTIICTIHQPSSeLFELFDKIILMAEGRVAYLGSPDQ 253
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
21-250 |
1.94e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 60.71 E-value: 1.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 21 LEVRHVT---------KRyggltaISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTP-PTSGAVFLDGVDVT----R 86
Cdd:PRK13549 260 LEVRNLTawdpvnphiKR------VDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKirnpQ 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 87 Q--------LPERRARSGvrrtfqraqLYSRLSVEDNVLTAmewrggggglLADLFAAPGRRRREAERREYALSVlaacg 158
Cdd:PRK13549 334 QaiaqgiamVPEDRKRDG---------IVPVMGVGKNITLA----------ALDRFTGGSRIDDAAELKTILESI----- 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 159 lADLRHK-PAGALPIG------QARLVeLARAIADRPRLLLLDEPTSGL---SAHET-ELFGEQIQRlrttGVAVVLVEH 227
Cdd:PRK13549 390 -QRLKVKtASPELAIArlsggnQQKAV-LAKCLLLNPKILILDEPTRGIdvgAKYEIyKLINQLVQQ----GVAIIVISS 463
|
250 260
....*....|....*....|...
gi 521297957 228 DVGFVMGQSDRVVVLNLGSVLAE 250
Cdd:PRK13549 464 ELPEVLGLSDRVLVMHEGKLKGD 486
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
16-261 |
1.96e-10 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 60.47 E-value: 1.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 16 TTEPALEVRHVTKRYGG----LTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPP----TSGAVFLDGVDVTrQ 87
Cdd:COG4172 2 MSMPLLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDpaahPSGSILFDGQDLL-G 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 88 LPERRARsGVR-----RTFQR------------AQLYSRLSVEDNvLTAMEWRGGggglladlfaapgrrrreaerreyA 150
Cdd:COG4172 81 LSERELR-RIRgnriaMIFQEpmtslnplhtigKQIAEVLRLHRG-LSGAAARAR------------------------A 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 151 LSVLAACGLADLRhKPAGALPI----GQARLVELARAIADRPRLLLLDEPTSGL----SAhetelfgeQIQRL-----RT 217
Cdd:COG4172 135 LELLERVGIPDPE-RRLDAYPHqlsgGQRQRVMIAMALANEPDLLIADEPTTALdvtvQA--------QILDLlkdlqRE 205
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 521297957 218 TGVAVVLVEHDVGFVMGQSDRVVVLNLGSVLAEGTPDEIQAHPA 261
Cdd:COG4172 206 LGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAELFAAPQ 249
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
18-260 |
2.00e-10 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 59.80 E-value: 2.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 18 EPALEVRHVTK---------RYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTrqL 88
Cdd:PRK15112 2 ETLLEVRNLSKtfryrtgwfRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLH--F 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 89 PERRARSG-VRRTFQRAQlysrlsvednvlTAMEWRggggGLLADLFAAPGRRRREAERREYALSVLAACGLADLRHKPA 167
Cdd:PRK15112 80 GDYSYRSQrIRMIFQDPS------------TSLNPR----QRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLLPDHA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 168 G----ALPIGQARLVELARAIADRPRLLLLDEPTSGLS-AHETELFGEQIQRLRTTGVAVVLVEHDVGFVMGQSDRVVVL 242
Cdd:PRK15112 144 SyyphMLAPGQKQRLGLARALILRPKVIIADEALASLDmSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVM 223
|
250
....*....|....*...
gi 521297957 243 NLGSVLAEGTPDEIQAHP 260
Cdd:PRK15112 224 HQGEVVERGSTADVLASP 241
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
19-237 |
2.34e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 59.28 E-value: 2.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 19 PALEVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTpPTSGAVFLDG-VDVTRQ-LPERRA--- 93
Cdd:PRK14258 6 PAIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMN-ELESEVRVEGrVEFFNQnIYERRVnln 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 94 --RSGVRRTFQRAQLYSrLSVEDNVLTAME---WRGGGGGLLAdlfaapgrrrreaerreyalsVLAACGLADL------ 162
Cdd:PRK14258 85 rlRRQVSMVHPKPNLFP-MSVYDNVAYGVKivgWRPKLEIDDI---------------------VESALKDADLwdeikh 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 521297957 163 -RHKPAGALPIGQARLVELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLR-TTGVAVVLVEHDVGFVMGQSD 237
Cdd:PRK14258 143 kIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlRSELTMVIVSHNLHQVSRLSD 219
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
6-250 |
5.36e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 59.41 E-value: 5.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 6 TSTDSSVAGVTTEPALEVRHVTKRYGGltAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVT 85
Cdd:PRK09700 251 NAMKENVSNLAHETVFEVRNVTSRDRK--KVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIS 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 86 RQLPERRARSG---VRRTFQRAQLYSRLSVEDNVLTAMEWRGGGGGLLADLFaAPGRRRREAERREYALSVlaACGLADl 162
Cdd:PRK09700 329 PRSPLDAVKKGmayITESRRDNGFFPNFSIAQNMAISRSLKDGGYKGAMGLF-HEVDEQRTAENQRELLAL--KCHSVN- 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 163 rhKPAGALPIGQARLVELARAIADRPRLLLLDEPTSGLS-AHETELFgEQIQRLRTTGVAVVLVEHDVGFVMGQSDRVVV 241
Cdd:PRK09700 405 --QNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDvGAKAEIY-KVMRQLADDGKVILMVSSELPEIITVCDRIAV 481
|
....*....
gi 521297957 242 LNLGSVLAE 250
Cdd:PRK09700 482 FCEGRLTQI 490
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
21-251 |
6.52e-10 |
|
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: 56.94 E-value: 6.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 21 LEVRHVTKRYGG--LTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQLPERRARSGVR 98
Cdd:cd03247 1 LSINNVSFSYPEqeQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 99 RtfQRAQLYSRlSVEDNVltamewrggggglladlfaapgrrrreaerreyalsvlaacgladlrhkpaGA-LPIGQARL 177
Cdd:cd03247 81 N--QRPYLFDT-TLRNNL---------------------------------------------------GRrFSGGERQR 106
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521297957 178 VELARAIADRPRLLLLDEPTSGLSAhETELfgeQIQRL---RTTGVAVVLVEHD-VGfvMGQSDRVVVLNLGSVLAEG 251
Cdd:cd03247 107 LALARILLQDAPIVLLDEPTVGLDP-ITER---QLLSLifeVLKDKTLIWITHHlTG--IEHMDKILFLENGKIIMQG 178
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
20-77 |
8.97e-10 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 58.75 E-value: 8.97e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 521297957 20 ALEVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAV 77
Cdd:PRK15064 319 ALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV 376
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
36-223 |
8.97e-10 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 56.87 E-value: 8.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 36 ISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPP--TSGAVFLDGvdvtRQLPErrarsgvrrTFQRAQLYSR-LSV 112
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAgvITGEILING----RPLDK---------NFQRSTGYVEqQDV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 113 EDNVLTAMEwrgggggllADLFAApgrrrreaerreyalsvlaacglaDLRhkpagALPIGQARLVELARAIADRPRLLL 192
Cdd:cd03232 90 HSPNLTVRE---------ALRFSA------------------------LLR-----GLSVEQRKRLTIGVELAAKPSILF 131
|
170 180 190
....*....|....*....|....*....|.
gi 521297957 193 LDEPTSGLSAHETELFGEQIQRLRTTGVAVV 223
Cdd:cd03232 132 LDEPTSGLDSQAAYNIVRFLKKLADSGQAIL 162
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
5-227 |
1.15e-09 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 58.28 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 5 ATSTDSSVAGVTTEPALEVRHVT-KRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVD 83
Cdd:COG4178 347 ALPEAASRIETSEDGALALEDLTlRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGA 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 84 VTRQLPER--------RArsgvrrtfqrAQLY--SRLSVEDNVLTAmewrggggglladlfaapgrrrreaerreyalsV 153
Cdd:COG4178 427 RVLFLPQRpylplgtlRE----------ALLYpaTAEAFSDAELRE---------------------------------A 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 154 LAACGLADLRHKP------AGALPIG-QARLVeLARAIADRPRLLLLDEPTSGLSAH-ETELFgeqiQRLRTT--GVAVV 223
Cdd:COG4178 464 LEAVGLGHLAERLdeeadwDQVLSLGeQQRLA-FARLLLHKPDWLFLDEATSALDEEnEAALY----QLLREElpGTTVI 538
|
....
gi 521297957 224 LVEH 227
Cdd:COG4178 539 SVGH 542
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
39-267 |
2.29e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 57.55 E-value: 2.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 39 VSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTsGAVFLDGVDVtRQLPERRARSGVRRTFQRAQLYSRlSVEDNVLT 118
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GSLKINGIEL-RELDPESWRKHLSWVGQNPQLPHG-TLRDNVLL 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 119 AmewrgGGGGLLADLFAApgrrrreaERREYALSVLAAC--GLADLRHKPAGALPIGQARLVELARAIADRPRLLLLDEP 196
Cdd:PRK11174 446 G-----NPDASDEQLQQA--------LENAWVSEFLPLLpqGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEP 512
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 521297957 197 TSGLSAHETELFGEQIQRLrTTGVAVVLVEHDVGFVMgQSDRVVVLNLGSVLAEGTPDEIQAHPAVRAAYL 267
Cdd:PRK11174 513 TASLDAHSEQLVMQALNAA-SRRQTTLMVTHQLEDLA-QWDQIWVMQDGQIVQQGDYAELSQAGGLFATLL 581
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
34-261 |
2.42e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 57.41 E-value: 2.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 34 TAISDVSLRVDPGEVCGFIGPNGAGKTT----LFDIIsgltpPTSGAVFLDGVDVtrQLPERRARSGVRRTFQ------R 103
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQPL--HNLNRRQLLPVRHRIQvvfqdpN 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 104 AQLYSRLSVEDNVLTAMEwrggggGLLADLFAApgrrrreaERREYALSVLAACGL-ADLRHKPAGALPIGQARLVELAR 182
Cdd:PRK15134 373 SSLNPRLNVLQIIEEGLR------VHQPTLSAA--------QREQQVIAVMEEVGLdPETRHRYPAEFSGGQRQRIAIAR 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 183 AIADRPRLLLLDEPTSGL----SAHETELFGEQIQRLRttgVAVVLVEHDVGFVMGQSDRVVVLNLGSVLAEGTPDEIQA 258
Cdd:PRK15134 439 ALILKPSLIILDEPTSSLdktvQAQILALLKSLQQKHQ---LAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFA 515
|
...
gi 521297957 259 HPA 261
Cdd:PRK15134 516 APQ 518
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
26-228 |
3.25e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 57.05 E-value: 3.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 26 VTKRYGGLTAI-SDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSG-AVFLDGVDVTrQLPerrarsgvrrtfQR 103
Cdd:PRK11819 12 VSKVVPPKKQIlKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGeARPAPGIKVG-YLP------------QE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 104 AQLYSRLSVEDNVLTAM-EWRGGGGG--LLADLFAAPGRRRREAERREYAL-SVLAACGLADLRHK----------PAGA 169
Cdd:PRK11819 79 PQLDPEKTVRENVEEGVaEVKAALDRfnEIYAAYAEPDADFDALAAEQGELqEIIDAADAWDLDSQleiamdalrcPPWD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521297957 170 LPI-----GQARLVELARAIADRPRLLLLDEPTSGLSAhETELFGEqiQRLRTTGVAVVLVEHD 228
Cdd:PRK11819 159 AKVtklsgGERRRVALCRLLLEKPDMLLLDEPTNHLDA-ESVAWLE--QFLHDYPGTVVAVTHD 219
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-260 |
3.74e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 56.00 E-value: 3.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 20 ALEVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTL---FDIISGLTPPT--SGAVFLDGVDV-TRQLPERRA 93
Cdd:PRK14267 4 AIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLlrtFNRLLELNEEArvEGEVRLFGRNIySPDVDPIEV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 94 RSGVRRTFQRAQLYSRLSVEDNVLTAMEWRGGGGGLLAdlfaapgrrrrEAERREYALSVLAacgLAD-----LRHKPaG 168
Cdd:PRK14267 84 RREVGMVFQYPNPFPHLTIYDNVAIGVKLNGLVKSKKE-----------LDERVEWALKKAA---LWDevkdrLNDYP-S 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 169 ALPIGQARLVELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLRTTgVAVVLVEHDVGFVMGQSDRVVVLNLGSVL 248
Cdd:PRK14267 149 NLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLGKLI 227
|
250
....*....|..
gi 521297957 249 AEGTPDEIQAHP 260
Cdd:PRK14267 228 EVGPTRKVFENP 239
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
166-256 |
5.71e-09 |
|
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: 56.56 E-value: 5.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 166 PAGALPIGQARLVELARAIADR---PRLLLLDEPTSGLSAHETELFGEQIQRLRTTGVAVVLVEHDVGfVMGQSDRVVVL 242
Cdd:TIGR00630 826 PATTLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNLD-VIKTADYIIDL 904
|
90 100
....*....|....*....|
gi 521297957 243 ------NLGSVLAEGTPDEI 256
Cdd:TIGR00630 905 gpeggdGGGTVVASGTPEEV 924
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
17-239 |
6.54e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 55.17 E-value: 6.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 17 TEPALEVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLF-------DIISGLTppTSGAVFLDGVDVTRQ-- 87
Cdd:PRK14243 7 TETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILrcfnrlnDLIPGFR--VEGKVTFHGKNLYAPdv 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 88 -LPERRARSGVrrTFQRAQLYSRlSVEDNVltAMEWRGGGGGLLADlfaapgrrrreaERREYALSVLAACGLADLRHKP 166
Cdd:PRK14243 85 dPVEVRRRIGM--VFQKPNPFPK-SIYDNI--AYGARINGYKGDMD------------ELVERSLRQAALWDEVKDKLKQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521297957 167 AG-ALPIGQARLVELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLRTTgVAVVLVEHDvgfvMGQSDRV 239
Cdd:PRK14243 148 SGlSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHN----MQQAARV 216
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
16-102 |
6.85e-09 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 55.03 E-value: 6.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 16 TTEPALEVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGlTPP---TSGAVFLDGVDVTRQLPERR 92
Cdd:CHL00131 3 KNKPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG-HPAykiLEGDILFKGESILDLEPEER 81
|
90
....*....|
gi 521297957 93 ARSGVRRTFQ 102
Cdd:CHL00131 82 AHLGIFLAFQ 91
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
31-256 |
1.07e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 55.75 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 31 GGLTAISDVSLR---------------VDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRqlperRARS 95
Cdd:PLN03232 1232 RGSIKFEDVHLRyrpglppvlhglsffVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAK-----FGLT 1306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 96 GVRRTF----QRAQLYSRlSVEDNVLTAMEwrggggGLLADLFAApgrrrreaerreyalsvLAACGLAD-LRHKPAG-- 168
Cdd:PLN03232 1307 DLRRVLsiipQSPVLFSG-TVRFNIDPFSE------HNDADLWEA-----------------LERAHIKDvIDRNPFGld 1362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 169 --------ALPIGQARLVELARAIADRPRLLLLDEPTSGLSAHETELFGEQIqRLRTTGVAVVLVEHDVGFVMgQSDRVV 240
Cdd:PLN03232 1363 aevseggeNFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTI-REEFKSCTMLVIAHRLNTII-DCDKIL 1440
|
250
....*....|....*.
gi 521297957 241 VLNLGSVLAEGTPDEI 256
Cdd:PLN03232 1441 VLSSGQVLEYDSPQEL 1456
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
20-257 |
1.34e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 54.74 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 20 ALEVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTtlfdiiSGLTPptsgaVFLDGVDVTRQLPERRARSGVRR 99
Cdd:NF000106 13 AVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**------RGALP-----AHV*GPDAGRRPWRF*TWCANRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 100 TFQRAQLYSRlSVEDNVLTAMEWRGGGGGLLADLFAAPGRRRREAERREYALSVLAACGLADLRHKPagalpiGQARLVE 179
Cdd:NF000106 82 ALRRTIG*HR-PVR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSG------GMRRRLD 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521297957 180 LARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLRTTGVAVVLVEHDVGFVMGQSDRVVVLNLGSVLAEGTPDEIQ 257
Cdd:NF000106 155 LAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELK 232
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
13-261 |
1.66e-08 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 54.35 E-value: 1.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 13 AGVTTEPALEVRHVTKRY----GGLTAISDVSLRVDPGEVCGFIGPNGAGKT-TLFDIIsGLTPP---TSGAVFLDGVDV 84
Cdd:PRK09473 5 AQQQADALLDVKDLRVTFstpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALM-GLLAAngrIGGSATFNGREI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 85 TrQLPER-----RARSgVRRTFQ--RAQLYSRLSVEDNVLTAMEWRGGGGGLLAdlfaapgrrrreaerreYALSV--LA 155
Cdd:PRK09473 84 L-NLPEKelnklRAEQ-ISMIFQdpMTSLNPYMRVGEQLMEVLMLHKGMSKAEA-----------------FEESVrmLD 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 156 ACGLADLR-------HKPAGalpiGQARLVELARAIADRPRLLLLDEPTSGL----SAHETELFGEQIQRLRTtgvAVVL 224
Cdd:PRK09473 145 AVKMPEARkrmkmypHEFSG----GMRQRVMIAMALLCRPKLLIADEPTTALdvtvQAQIMTLLNELKREFNT---AIIM 217
|
250 260 270
....*....|....*....|....*....|....*..
gi 521297957 225 VEHDVGFVMGQSDRVVVLNLGSVLAEGTPDEIQAHPA 261
Cdd:PRK09473 218 ITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQPS 254
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
21-256 |
1.95e-08 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 54.95 E-value: 1.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 21 LEVRHVTKRY-GGLT-AISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVtrqlperrARSGVR 98
Cdd:TIGR00957 1285 VEFRNYCLRYrEDLDlVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNI--------AKIGLH 1356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 99 rtfqraQLYSRLSV--EDNVLTAMEWRGGGggllaDLFAAPGRRRREAERREYALSVLAACGLADLRHKPAGA---LPIG 173
Cdd:TIGR00957 1357 ------DLRFKITIipQDPVLFSGSLRMNL-----DPFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGgenLSVG 1425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 174 QARLVELARAIADRPRLLLLDEPTSGLSAHETELFGEQIqRLRTTGVAVVLVEHDVGFVMGQSdRVVVLNLGSVLAEGTP 253
Cdd:TIGR00957 1426 QRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTI-RTQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAP 1503
|
...
gi 521297957 254 DEI 256
Cdd:TIGR00957 1504 SNL 1506
|
|
| BCA_ABC_TP_C |
pfam12399 |
Branched-chain amino acid ATP-binding cassette transporter; This domain family is found in ... |
247-268 |
1.96e-08 |
|
Branched-chain amino acid ATP-binding cassette transporter; This domain family is found in bacteria, archaea and eukaryotes, and is approximately 30 amino acids in length. The family is found in association with pfam00005. There is a conserved AYLG sequence motif. This family is the C terminal of an ATP dependent branched-chain amino acid transporter. This domain is essential for LPS transport, through critical interactions with Walker A and switch helix domains.
Pssm-ID: 463560 Cd Length: 25 Bit Score: 48.79 E-value: 1.96e-08
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
20-252 |
2.19e-08 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 54.72 E-value: 2.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 20 ALEVRHVTKRY-GGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTrQLPERRARSGVR 98
Cdd:PRK10790 340 RIDIDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLS-SLSHSVLRQGVA 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 99 RTFQ-----RAQLYSRLSVEDNVLTAMEWRGGGGGLLADLfaapgrrrreaerreyalsvlaACGLADLRHKPAG----A 169
Cdd:PRK10790 419 MVQQdpvvlADTFLANVTLGRDISEEQVWQALETVQLAEL----------------------ARSLPDGLYTPLGeqgnN 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 170 LPIGQARLVELARAIADRPRLLLLDEPTSGLSAHeTElfgEQIQ------RLRTTgvaVVLVEHDVGFVMgQSDRVVVLN 243
Cdd:PRK10790 477 LSVGQKQLLALARVLVQTPQILILDEATANIDSG-TE---QAIQqalaavREHTT---LVVIAHRLSTIV-EADTILVLH 548
|
....*....
gi 521297957 244 LGSVLAEGT 252
Cdd:PRK10790 549 RGQAVEQGT 557
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
151-251 |
3.30e-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: 51.94 E-value: 3.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 151 LSVLAACGLADLR-HKPAGALPIGQARLVELARAIADRPR--LLLLDEPTSGLSAHETELFGEQIQRLRTTGVAVVLVEH 227
Cdd:cd03238 68 LQFLIDVGLGYLTlGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEH 147
|
90 100 110
....*....|....*....|....*....|
gi 521297957 228 DVgFVMGQSDRVVVL------NLGSVLAEG 251
Cdd:cd03238 148 NL-DVLSSADWIIDFgpgsgkSGGKVVFSG 176
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
14-251 |
3.61e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 54.12 E-value: 3.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 14 GVTTEPALEVRHVTKRygglTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTS--GAVFLDGVDVTRQLper 91
Cdd:PLN03211 66 GHKPKISDETRQIQER----TILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTKQI--- 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 92 rarsgVRRTFQRAQ---LYSRLSVEDNVLTAMEWRGGGGGLLADLFAApgrrrreaerreyALSVLAACGLADLRHKPAG 168
Cdd:PLN03211 139 -----LKRTGFVTQddiLYPHLTVRETLVFCSLLRLPKSLTKQEKILV-------------AESVISELGLTKCENTIIG 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 169 ALPI-----GQARLVELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLRTTGVAVVLVEHDVGFVMGQS-DRVVVL 242
Cdd:PLN03211 201 NSFIrgisgGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMfDSVLVL 280
|
....*....
gi 521297957 243 NLGSVLAEG 251
Cdd:PLN03211 281 SEGRCLFFG 289
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
21-87 |
3.69e-08 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 53.65 E-value: 3.69e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 521297957 21 LEVRHVTKRYGGLT-----AISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQ 87
Cdd:COG4615 328 LELRGVTYRYPGEDgdegfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTAD 399
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
173-264 |
7.10e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 52.44 E-value: 7.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 173 GQARLVELARAIADRPRLLLLDEPTSGL----SAHETELFGEQIQRlrtTGVAVVLVEHDVGFVMGQSDRVVVLNLGSVL 248
Cdd:PRK11022 157 GMSQRVMIAMAIACRPKLLIADEPTTALdvtiQAQIIELLLELQQK---ENMALVLITHDLALVAEAAHKIIVMYAGQVV 233
|
90
....*....|....*....
gi 521297957 249 AEGTPDEI---QAHPAVRA 264
Cdd:PRK11022 234 ETGKAHDIfraPRHPYTQA 252
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
13-253 |
7.26e-08 |
|
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: 52.86 E-value: 7.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 13 AGVTTEPALEVRHVTKRYGGLtaisdvSLRVDPG-----EVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLD------- 80
Cdd:COG1245 334 REKEEETLVEYPDLTKSYGGF------SLEVEGGeiregEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDlkisykp 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 81 -----GVDVT-RQLPERRARSGVRRTFQRAQLYSRLSVEdnvltamewrggggglladlfaapgrrrreaerreyalsvl 154
Cdd:COG1245 408 qyispDYDGTvEEFLRSANTDDFGSSYYKTEIIKPLGLE----------------------------------------- 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 155 aacglaDLRHKPAGALPIGqarlvELAR-AI-------ADrprLLLLDEPtsglSAHeteLFGEQ-------IQRL-RTT 218
Cdd:COG1245 447 ------KLLDKNVKDLSGG-----ELQRvAIaaclsrdAD---LYLLDEP----SAH---LDVEQrlavakaIRRFaENR 505
|
250 260 270
....*....|....*....|....*....|....*
gi 521297957 219 GVAVVLVEHDVGFVMGQSDRVVVLnlgsvlaEGTP 253
Cdd:COG1245 506 GKTAMVVDHDIYLIDYISDRLMVF-------EGEP 533
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
35-81 |
1.12e-07 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 52.20 E-value: 1.12e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 521297957 35 AISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDG 81
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG 85
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
173-261 |
1.51e-07 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 51.95 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 173 GQARLVELARAIADRPR---LLLLDEPTSGLSAHETELFGEQIQRLRTTGVAVVLVEH--DVgfvMGQSDRVVVL----- 242
Cdd:COG0178 830 GEAQRVKLASELSKRSTgktLYILDEPTTGLHFHDIRKLLEVLHRLVDKGNTVVVIEHnlDV---IKTADWIIDLgpegg 906
|
90 100
....*....|....*....|
gi 521297957 243 -NLGSVLAEGTPDEIQAHPA 261
Cdd:COG0178 907 dGGGEIVAEGTPEEVAKVKA 926
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
21-110 |
1.76e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 51.90 E-value: 1.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 21 LEVRHVTKRYGGLT-AISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQLPE--RRARSGV 97
Cdd:PRK10522 323 LELRNVTFAYQDNGfSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEdyRKLFSAV 402
|
90
....*....|...
gi 521297957 98 rrtFQRAQLYSRL 110
Cdd:PRK10522 403 ---FTDFHLFDQL 412
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
41-247 |
2.09e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 51.49 E-value: 2.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 41 LRVDPGE-VCgFIGPNGAGKTTLFDIISGLTPPTSGAVFLDG-VDVTR--QLPERRAR--------SGVRRTFQRAQLYS 108
Cdd:PRK11147 24 LHIEDNErVC-LVGRNGAGKSTLMKILNGEVLLDDGRIIYEQdLIVARlqQDPPRNVEgtvydfvaEGIEEQAEYLKRYH 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 109 RLS--VE----DNVLTAMEwRGGGGGLLADLFAAPGRRRreaerreyalSVLAACGL-ADlrhKPAGALPIGQARLVELA 181
Cdd:PRK11147 103 DIShlVEtdpsEKNLNELA-KLQEQLDHHNLWQLENRIN----------EVLAQLGLdPD---AALSSLSGGWLRKAALG 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 521297957 182 RAIADRPRLLLLDEPTSGLSAhETELFGEQIqrLRTTGVAVVLVEHDVGFVMGQSDRVVVLNLGSV 247
Cdd:PRK11147 169 RALVSNPDVLLLDEPTNHLDI-ETIEWLEGF--LKTFQGSIIFISHDRSFIRNMATRIVDLDRGKL 231
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
165-268 |
2.45e-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: 51.55 E-value: 2.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 165 KPAGALPIGQARLVELARAIADRPR--LLLLDEPTSGLSAHETELFGEQIQRLRTTGVAVVLVEHDVGfVMGQSDRVVVL 242
Cdd:TIGR00630 484 RAAGTLSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDED-TIRAADYVIDI 562
|
90 100 110
....*....|....*....|....*....|...
gi 521297957 243 NLGS------VLAEGTPDEIQAHP-AVRAAYLG 268
Cdd:TIGR00630 563 GPGAgehggeVVASGTPEEILANPdSLTGQYLS 595
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
15-253 |
5.32e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 50.19 E-value: 5.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 15 VTTEPALEVRHVTKRYGGLtaisdvSLRVDPG-----EVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLD--------- 80
Cdd:PRK13409 335 SERETLVEYPDLTKKLGDF------SLEVEGGeiyegEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPElkisykpqy 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 81 ---GVDVTRQLPERRARSGVRRTFQRAQLYSRLsvednvltamewrggggglladlfaapgrrrreaerreyalsvlaac 157
Cdd:PRK13409 409 ikpDYDGTVEDLLRSITDDLGSSYYKSEIIKPL----------------------------------------------- 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 158 GLADLRHKPAGALPIGQARLVELARAIADRPRLLLLDEPtsglSAHeteLFGEQ-------IQRL-RTTGVAVVLVEHDV 229
Cdd:PRK13409 442 QLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEP----SAH---LDVEQrlavakaIRRIaEEREATALVVDHDI 514
|
250 260
....*....|....*....|....
gi 521297957 230 GFVMGQSDRVVVLnlgsvlaEGTP 253
Cdd:PRK13409 515 YMIDYISDRLMVF-------EGEP 531
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
166-253 |
5.42e-07 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 49.54 E-value: 5.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 166 PAGALPIGQARLVELARAIADRPR---LLLLDEPTSGLSAHETELFGEQIQRLRTTGVAVVLVEHDVGfVMGQSDRVVVL 242
Cdd:cd03271 166 PATTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLD-VIKCADWIIDL 244
|
90
....*....|....*..
gi 521297957 243 ------NLGSVLAEGTP 253
Cdd:cd03271 245 gpeggdGGGQVVASGTP 261
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
42-223 |
5.45e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 49.08 E-value: 5.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 42 RVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQlpeRRARSgVRRTFQRAQLYSRLSVEDNV--LTA 119
Cdd:PRK13543 33 HVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRG---DRSRF-MAYLGHLPGLKADLSTLENLhfLCG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 120 MEWRGGGGGlladlfaaPGrrrreaerreyalSVLAACGLADLRHKPAGALPIGQARLVELARAIADRPRLLLLDEPTSG 199
Cdd:PRK13543 109 LHGRRAKQM--------PG-------------SALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYAN 167
|
170 180
....*....|....*....|....*
gi 521297957 200 LSAHETELFGEQIQ-RLRTTGVAVV 223
Cdd:PRK13543 168 LDLEGITLVNRMISaHLRGGGAALV 192
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
35-81 |
6.00e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 49.43 E-value: 6.00e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 521297957 35 AISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDG 81
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG 85
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
38-241 |
9.76e-07 |
|
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: 48.56 E-value: 9.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 38 DVSLRVDPG-----EVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQLPERRARSGVRrtfQRAQLYSRLsv 112
Cdd:cd03237 12 EFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYIKADYEGT---VRDLLSSIT-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 113 eDNVLTAMEWRGgggglladlfaapgrrrreaerreyalSVLAACGLADLRHKPAGALPIGQARLVELARAIADRPRLLL 192
Cdd:cd03237 87 -KDFYTHPYFKT---------------------------EIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYL 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 193 LDEPtsglSAH-ETElfgeqiQRLRTTGV----------AVVLVEHDVGFVMGQSDRVVV 241
Cdd:cd03237 139 LDEP----SAYlDVE------QRLMASKVirrfaennekTAFVVEHDIIMIDYLADRLIV 188
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
31-247 |
1.33e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 49.09 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 31 GGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVF--------------LDGVDVTRQ--LPERRAR 94
Cdd:PLN03073 520 GGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFrsakvrmavfsqhhVDGLDLSSNplLYMMRCF 599
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 95 SGVRRTFQRAQLYSrlsvednvltamewrggggglladlFAAPGrrrreaerreyalsvlaacglaDLRHKPAGALPIGQ 174
Cdd:PLN03073 600 PGVPEQKLRAHLGS-------------------------FGVTG----------------------NLALQPMYTLSGGQ 632
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 521297957 175 ARLVELARAIADRPRLLLLDEPTSGLSAHETELFgeqIQRLRTTGVAVVLVEHDVGFVMGQSDRVVVLNLGSV 247
Cdd:PLN03073 633 KSRVAFAKITFKKPHILLLDEPSNHLDLDAVEAL---IQGLVLFQGGVLMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
39-102 |
1.52e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 48.25 E-value: 1.52e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 521297957 39 VSLRVDPGEVCGFIGPNGAGKTTLFDIISGLT--PPTSGAVFLDGVDVTRQLPERRARSGVRRTFQ 102
Cdd:PRK09580 20 LNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRAGEGIFMAFQ 85
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
32-246 |
2.21e-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: 47.33 E-value: 2.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 32 GLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQLPE---RRARSGVRRTFQRAQLYS 108
Cdd:cd03290 13 GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEatrSRNRYSVAYAAQKPWLLN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 109 RlSVEDNVltamewrggggglladLFAAPgrrrreAERREYAlSVLAACGL-ADLRHKPAG----------ALPIGQARL 177
Cdd:cd03290 93 A-TVEENI----------------TFGSP------FNKQRYK-AVTDACSLqPDIDLLPFGdqteigergiNLSGGQRQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 521297957 178 VELARAIADRPRLLLLDEPTSGLSAHETE-LFGEQIQR-LRTTGVAVVLVEHDVGFVMgQSDRVVVLNLGS 246
Cdd:cd03290 149 ICVARALYQNTNIVFLDDPFSALDIHLSDhLMQEGILKfLQDDKRTLVLVTHKLQYLP-HADWIIAMKDGS 218
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
166-256 |
2.52e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 48.49 E-value: 2.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 166 PAG-ALPIGQARLVELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLRTTG-VAVVLVEHDVGFVMgQSDRVVVLN 243
Cdd:PTZ00265 1354 PYGkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdKTIITIAHRIASIK-RSDKIVVFN 1432
|
90
....*....|....*...
gi 521297957 244 ----LGS-VLAEGTPDEI 256
Cdd:PTZ00265 1433 npdrTGSfVQAHGTHEEL 1450
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
173-261 |
2.96e-06 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 48.15 E-value: 2.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 173 GQARLVELARAIADRPR---LLLLDEPTSGLSAHETELFGEQIQRLRTTGVAVVLVEH--DVgfvMGQSDRVVVL----- 242
Cdd:PRK00349 834 GEAQRVKLAKELSKRSTgktLYILDEPTTGLHFEDIRKLLEVLHRLVDKGNTVVVIEHnlDV---IKTADWIIDLgpegg 910
|
90 100
....*....|....*....|
gi 521297957 243 -NLGSVLAEGTPDEIQAHPA 261
Cdd:PRK00349 911 dGGGEIVATGTPEEVAKVEA 930
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
193-267 |
3.82e-06 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 47.71 E-value: 3.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 193 LDEPTSGLSAHETELFGEQIQRLRTTGVAVVLVEHDVGfVMGQSDRVVVL------NLGSVLAEGTPDEIQAHPA-VRAA 265
Cdd:COG0178 511 LDEPSIGLHQRDNDRLIETLKRLRDLGNTVIVVEHDED-TIRAADYIIDIgpgageHGGEVVAQGTPEEILKNPDsLTGQ 589
|
..
gi 521297957 266 YL 267
Cdd:COG0178 590 YL 591
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
155-264 |
3.90e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 47.90 E-value: 3.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 155 AACGLAdLRHKPAG----ALPIGQARLVELAR---AIADRPRLLLLDEPTSGLSAHETELFGEQIQRLRTTGVAVVLVEH 227
Cdd:PRK00635 792 ALCSLG-LDYLPLGrplsSLSGGEIQRLKLAYellAPSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEH 870
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 521297957 228 DVgFVMGQSDRVVVL-----NLGS-VLAEGTPDE-IQAH-PAVRA 264
Cdd:PRK00635 871 NM-HVVKVADYVLELgpeggNLGGyLLASCSPEElIHLHtPTAKA 914
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
39-256 |
5.74e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 47.43 E-value: 5.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 39 VSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTR-QLPERRARSGVrrTFQRAQLYSRlSVEDNVL 117
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKfGLMDLRKVLGI--IPQAPVLFSG-TVRFNLD 1334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 118 TAMEwrggggGLLADLFAApgrrrreaerreyalsvLAACGLAD-LRHKPAGA----------LPIGQARLVELARAIAD 186
Cdd:PLN03130 1335 PFNE------HNDADLWES-----------------LERAHLKDvIRRNSLGLdaevseagenFSVGQRQLLSLARALLR 1391
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 187 RPRLLLLDEPTSGLSAHETELFGEQIqRLRTTGVAVVLVEHDVGFVMgQSDRVVVLNLGSVLAEGTPDEI 256
Cdd:PLN03130 1392 RSKILVLDEATAAVDVRTDALIQKTI-REEFKSCTMLIIAHRLNTII-DCDRILVLDAGRVVEFDTPENL 1459
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
21-229 |
7.37e-06 |
|
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: 46.39 E-value: 7.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 21 LEVRHVTKRY--GGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTpPTSGAVFLDGVD-VTRQLPERRARSGV 97
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLL-NTEGDIQIDGVSwNSVPLQKWRKAFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 98 rrTFQRAQLYSRlSVEDNVLTAMEWRGGGGGLLAD-------LFAAPGRRRREAERREYALSvlaacgladlrHkpagal 170
Cdd:cd03289 82 --IPQKVFIFSG-TFRKNLDPYGKWSDEEIWKVAEevglksvIEQFPGQLDFVLVDGGCVLS-----------H------ 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 521297957 171 piGQARLVELARAIADRPRLLLLDEPtsglSAHeteLFGEQIQRLRTT------GVAVVLVEHDV 229
Cdd:cd03289 142 --GHKQLMCLARSVLSKAKILLLDEP----SAH---LDPITYQVIRKTlkqafaDCTVILSEHRI 197
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
18-256 |
1.02e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 46.26 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 18 EPALEVRHVTKRygGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQLPERRARSG- 96
Cdd:PRK10982 248 EVILEVRNLTSL--RQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAINHGf 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 97 --VRRTFQRAQLYSRLSVEDNVLTAmewrggggglLADLFAAPGRRRREAERREYALSVLAACGLADLRHKPA-GALPIG 173
Cdd:PRK10982 326 alVTEERRSTGIYAYLDIGFNSLIS----------NIRNYKNKVGLLDNSRMKSDTQWVIDSMRVKTPGHRTQiGSLSGG 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 174 QARLVELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRLRTTGVAVVLVEHDVGFVMGQSDRVVVLNLGSV-----L 248
Cdd:PRK10982 396 NQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLVagivdT 475
|
....*...
gi 521297957 249 AEGTPDEI 256
Cdd:PRK10982 476 KTTTQNEI 483
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
6-251 |
1.04e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 46.39 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 6 TSTDSSVAGvttEPALEVRHVTKRY---GGLT--------AISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTS 74
Cdd:PRK10261 302 IEQDTVVDG---EPILQVRNLVTRFplrSGLLnrvtrevhAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQG 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 75 GAVFLDGVDVTrQLPERRARSgVRRTFQ------RAQLYSRLSVEDNVLTAMEWRGGGGGLLADLFAApgrrrreaerre 148
Cdd:PRK10261 379 GEIIFNGQRID-TLSPGKLQA-LRRDIQfifqdpYASLDPRQTVGDSIMEPLRVHGLLPGKAAAARVA------------ 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 149 yalSVLAACGLadlrhKPAGALPI------GQARLVELARAIADRPRLLLLDEPTSGLsahETELFGEQIQRL----RTT 218
Cdd:PRK10261 445 ---WLLERVGL-----LPEHAWRYphefsgGQRQRICIARALALNPKVIIADEAVSAL---DVSIRGQIINLLldlqRDF 513
|
250 260 270
....*....|....*....|....*....|...
gi 521297957 219 GVAVVLVEHDVGFVMGQSDRVVVLNLGSVLAEG 251
Cdd:PRK10261 514 GIAYLFISHDMAVVERISHRVAVMYLGQIVEIG 546
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
192-267 |
1.93e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 45.98 E-value: 1.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 192 LLDEPTSGLSAHETELFGEQIQRLRTTGVAVVLVEHDVGFVmGQSDRVVVLNLGS------VLAEGTPDEIQAHP-AVRA 264
Cdd:PRK00635 501 ILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDEQMI-SLADRIIDIGPGAgifggeVLFNGSPREFLAKSdSLTA 579
|
...
gi 521297957 265 AYL 267
Cdd:PRK00635 580 KYL 582
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
21-229 |
2.22e-05 |
|
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: 45.67 E-value: 2.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 21 LEVRHVTKRY--GGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTpPTSGAVFLDGV---DVTRQlpERRARS 95
Cdd:TIGR01271 1218 MDVQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLL-STEGEIQIDGVswnSVTLQ--TWRKAF 1294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 96 GV--------RRTFqRAQL--YSRLSVEDnvltamEWRGGGGGLLADLFAA-PGRRRREAERREYALSVlaacgladlrh 164
Cdd:TIGR01271 1295 GVipqkvfifSGTF-RKNLdpYEQWSDEE------IWKVAEEVGLKSVIEQfPDKLDFVLVDGGYVLSN----------- 1356
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 521297957 165 kpagalpiGQARLVELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRlRTTGVAVVLVEHDV 229
Cdd:TIGR01271 1357 --------GHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQ-SFSNCTVILSEHRV 1412
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
36-256 |
2.30e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 45.74 E-value: 2.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 36 ISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAvfldGVDVtrqlperraRSGVRRTFQRAQLYSRlSVEDN 115
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETS----SVVI---------RGSVAYVPQVSWIFNA-TVREN 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 116 VLTAMEWRGGGGGLLADLFAapgrrrreaerREYALSVLAACGLADLRHKPAGaLPIGQARLVELARAIADRPRLLLLDE 195
Cdd:PLN03232 699 ILFGSDFESERYWRAIDVTA-----------LQHDLDLLPGRDLTEIGERGVN-ISGGQKQRVSMARAVYSNSDIYIFDD 766
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 521297957 196 PTSGLSAHETELFGEQIQRLRTTGVAVVLVEHDVGFvMGQSDRVVVLNLGSVLAEGTPDEI 256
Cdd:PLN03232 767 PLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQLHF-LPLMDRIILVSEGMIKEEGTFAEL 826
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
40-225 |
2.32e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 45.01 E-value: 2.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 40 SLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGavfldgvdvtrqlpERRARsgvrrtFQRAqlySRLSVED-NVLT 118
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSG--------------ERQSQ------FSHI---TRLSFEQlQKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 119 AMEWRGGGGgllaDLFAAPGRRRREAERREYALSV--------LAA-CGLADLRHKPAGALPIGQARLVELARAIADRPR 189
Cdd:PRK10938 80 SDEWQRNNT----DMLSPGEDDTGRTTAEIIQDEVkdparceqLAQqFGITALLDRRFKYLSTGETRKTLLCQALMSEPD 155
|
170 180 190
....*....|....*....|....*....|....*.
gi 521297957 190 LLLLDEPTSGLSAHETELFGEQIQRLRTTGVAVVLV 225
Cdd:PRK10938 156 LLILDEPFDGLDVASRQQLAELLASLHQSGITLVLV 191
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
19-79 |
3.24e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 44.78 E-value: 3.24e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 521297957 19 PALEVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFL 79
Cdd:PRK10636 311 PLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL 371
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
36-77 |
3.32e-05 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 43.30 E-value: 3.32e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 521297957 36 ISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAV 77
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI 58
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
36-258 |
4.19e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 44.73 E-value: 4.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 36 ISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLdgvdvtrqlperrARSGVRRTFQRAQLYSRlSVEDN 115
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVV-------------IRGTVAYVPQVSWIFNA-TVRDN 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 116 VLTAMEWRGGGGGLLADLFAapgrrrreaerREYALSVLAACGLADLRHKPAGaLPIGQARLVELARAIADRPRLLLLDE 195
Cdd:PLN03130 699 ILFGSPFDPERYERAIDVTA-----------LQHDLDLLPGGDLTEIGERGVN-ISGGQKQRVSMARAVYSNSDVYIFDD 766
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521297957 196 PTSGLSAH------ETELFGEQIQRLRttgvavVLVEHDVGFvMGQSDRVVVLNLGSVLAEGTPDEIQA 258
Cdd:PLN03130 767 PLSALDAHvgrqvfDKCIKDELRGKTR------VLVTNQLHF-LSQVDRIILVHEGMIKEEGTYEELSN 828
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
149-267 |
5.16e-05 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 44.55 E-value: 5.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 149 YALSVLAACGL-ADLRHKPAG----------ALPIGQARLVELARAIADRPRLLLLDEPTSGLSAHETELFGEQI--QRL 215
Cdd:TIGR00957 729 YYQQVLEACALlPDLEILPSGdrteigekgvNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVigPEG 808
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 521297957 216 RTTGVAVVLVEHDVGFvMGQSDRVVVLNLGSVLAEGTPDEIQAHPAVRAAYL 267
Cdd:TIGR00957 809 VLKNKTRILVTHGISY-LPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEFL 859
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
17-261 |
5.73e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 43.93 E-value: 5.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 17 TEPALEVRH--VTKRYGGL--TAISDVSLRVDPGEVCGFIGPNGAGKT-TLFDIISGL-TPP---TSGAVFLDGVDVTRQ 87
Cdd:PRK15134 2 TQPLLAIENlsVAFRQQQTvrTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLpSPPvvyPSGDIRFHGESLLHA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 88 lPERRARsGVR-----RTFQ------------RAQLYSRLSVEDNVLTAmewrggggglladlfAAPGRrrreaerreyA 150
Cdd:PRK15134 82 -SEQTLR-GVRgnkiaMIFQepmvslnplhtlEKQLYEVLSLHRGMRRE---------------AARGE----------I 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 151 LSVL-------AACGLADLRHKPAGalpiGQARLVELARAIADRPRLLLLDEPTSGL----SAHETELFGEQIQRLrttG 219
Cdd:PRK15134 135 LNCLdrvgirqAAKRLTDYPHQLSG----GERQRVMIAMALLTRPELLIADEPTTALdvsvQAQILQLLRELQQEL---N 207
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 521297957 220 VAVVLVEHDVGFVMGQSDRVVVLNLGSVLAEGTPDEIQAHPA 261
Cdd:PRK15134 208 MGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPT 249
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
4-259 |
6.47e-05 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 43.36 E-value: 6.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 4 VATSTDSSVAGVTTEpaLEVRHVTKRYGGL--TAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDG 81
Cdd:cd03288 5 ISGSSNSGLVGLGGE--IKIHDLCVRYENNlkPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 82 VDVTRqLPERRARSGVRRTFQRAQLYS-----RLSVEDNVLTAMEWRGGGGGLLADLFAA-PGrrrreaerreyalsvla 155
Cdd:cd03288 83 IDISK-LPLHTLRSRLSIILQDPILFSgsirfNLDPECKCTDDRLWEALEIAQLKNMVKSlPG----------------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 156 acGLADLRHKPAGALPIGQARLVELARAIADRPRLLLLDEPTSGLsahetELFGEQI-QRLRTTGVA---VVLVEHDVGF 231
Cdd:cd03288 145 --GLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASI-----DMATENIlQKVVMTAFAdrtVVTIAHRVST 217
|
250 260
....*....|....*....|....*...
gi 521297957 232 VMgQSDRVVVLNLGSVLAEGTPDEIQAH 259
Cdd:cd03288 218 IL-DADLVLVLSRGILVECDTPENLLAQ 244
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
173-264 |
8.29e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 43.69 E-value: 8.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 173 GQARLVELARAIADRPRLLLLDEPTSGLSAHETELFGEQIQRL-RTTGVAVVLVEHDVGFVMGQSDRVVVLNLGSVLAEG 251
Cdd:PRK10261 172 GMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLqKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETG 251
|
90
....*....|....*.
gi 521297957 252 TPDEI---QAHPAVRA 264
Cdd:PRK10261 252 SVEQIfhaPQHPYTRA 267
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
151-240 |
1.12e-04 |
|
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: 42.24 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 151 LSVLAACGLADLR-HKPAGALPIGQARLVELARAIADRPR--LLLLDEPTSGLSAHETELFGEQIQRLRTTGVAVVLVEH 227
Cdd:cd03270 118 LGFLVDVGLGYLTlSRSAPTLSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEH 197
|
90
....*....|...
gi 521297957 228 DVGfVMGQSDRVV 240
Cdd:cd03270 198 DED-TIRAADHVI 209
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
36-264 |
1.13e-04 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 42.38 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 36 ISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPP----TSGAVFLDGVDVtrqlperrARSGVR-RTFQraqlysrl 110
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPV--------APCALRgRKIA-------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 111 SVEDNVLTAMEWRGGGGGLLADLFAAPGRRRREAErreyALSVLAACGLADlRHKPAGALPI----GQARLVELARAIAD 186
Cdd:PRK10418 83 TIMQNPRSAFNPLHTMHTHARETCLALGKPADDAT----LTAALEAVGLEN-AARVLKLYPFemsgGMLQRMMIALALLC 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 187 RPRLLLLDEPTSGLSAHETELFGEQIQRL-RTTGVAVVLVEHDVGFVMGQSDRVVVLNLGSVLAEGTPDEI---QAHPAV 262
Cdd:PRK10418 158 EAPFIIADEPTTDLDVVAQARILDLLESIvQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLfnaPKHAVT 237
|
..
gi 521297957 263 RA 264
Cdd:PRK10418 238 RS 239
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
21-84 |
1.38e-04 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 42.70 E-value: 1.38e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 521297957 21 LEVRHVTKRYGG--LTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDV 84
Cdd:PRK11176 342 IEFRNVTFTYPGkeVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDL 407
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
37-73 |
3.72e-04 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 37.96 E-value: 3.72e-04
10 20 30
....*....|....*....|....*....|....*...
gi 521297957 37 SDVSLRVDPGEVCGFIGPNGAGKTTLFD-IISGLTPPT 73
Cdd:pfam13555 13 DGHTIPIDPRGNTLLTGPSGSGKSTLLDaIQTLLVPAK 50
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
22-77 |
4.74e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 41.09 E-value: 4.74e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 521297957 22 EVRHVTKRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAV 77
Cdd:PRK11147 321 EMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI 376
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
40-66 |
5.16e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 40.68 E-value: 5.16e-04
10 20
....*....|....*....|....*..
gi 521297957 40 SLRVDPGEVCGFIGPNGAGKTTLFDII 66
Cdd:COG4637 15 DLELPLGPLTVLIGANGSGKSNLLDAL 41
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
17-85 |
5.58e-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: 39.86 E-value: 5.58e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521297957 17 TEPALevrhvTKRYGgltaisDVSLRVDP-----GEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVT 85
Cdd:cd03222 2 LYPDC-----VKRYG------VFFLLVELgvvkeGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPV 64
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
36-78 |
7.43e-04 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 40.37 E-value: 7.43e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 521297957 36 ISDVSLRVDPGEVCgFIGPNGAGKTTLFDIISGLTPPTSGAVF 78
Cdd:COG3593 14 IKDLSIELSDDLTV-LVGENNSGKSSILEALRLLLGPSSSRKF 55
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
50-80 |
7.95e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 40.65 E-value: 7.95e-04
10 20 30
....*....|....*....|....*....|.
gi 521297957 50 GFIGPNGAGKTTLFDIISGLTPPTSGAVFLD 80
Cdd:PRK15064 31 GLIGANGCGKSTFMKILGGDLEPSAGNVSLD 61
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
34-97 |
8.57e-04 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 40.47 E-value: 8.57e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 521297957 34 TAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTR-QLPERRARSGV 97
Cdd:PRK10789 329 PALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKlQLDSWRSRLAV 393
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
34-227 |
9.16e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 39.47 E-value: 9.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 34 TAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPTSGAVFLDGVDVTRQlperrARSGVRRTFQRAQLYSRLSVE 113
Cdd:PRK13541 14 KNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNI-----AKPYCTYIGHNLGLKLEMTVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 114 DNVLTAMEwrggGGGLLADLFAApgrrrreaerreyalsvLAACGLADLRHKPAGALPIGQARLVELARAIADRPRLLLL 193
Cdd:PRK13541 89 ENLKFWSE----IYNSAETLYAA-----------------IHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLL 147
|
170 180 190
....*....|....*....|....*....|....
gi 521297957 194 DEPTSGLSAHETELFGEQIQRLRTTGVAVVLVEH 227
Cdd:PRK13541 148 DEVETNLSKENRDLLNNLIVMKANSGGIVLLSSH 181
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
173-247 |
1.02e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 40.53 E-value: 1.02e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 521297957 173 GQARLVELARAI-ADRPrLLLLDEPTSGLSAHETELFGEQIQRLRTTGVAVVLVEHDVgFVMGQSDRVVVLNLGSV 247
Cdd:PTZ00243 786 GQKARVSLARAVyANRD-VYLLDDPLSALDAHVGERVVEECFLGALAGKTRVLATHQV-HVVPRADYVVALGDGRV 859
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
45-72 |
1.38e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 39.79 E-value: 1.38e-03
10 20
....*....|....*....|....*...
gi 521297957 45 PGEVCGFIGPNGAGKTTLFDIISGLTPP 72
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGELIP 125
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
45-92 |
1.50e-03 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 38.12 E-value: 1.50e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 521297957 45 PGEVCGFIGPNGAGKTTLFDIISG-LTPPTSGAVFLDGVDVTRQLPERR 92
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALAReLGPPGGGVIYIDGEDILEEVLDQL 49
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
45-71 |
1.55e-03 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 39.77 E-value: 1.55e-03
10 20
....*....|....*....|....*...
gi 521297957 45 PGEVCGFIGPNGAGKTTLFDIISG-LTP 71
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGeLKP 125
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
28-83 |
2.09e-03 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 38.40 E-value: 2.09e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 521297957 28 KRYGGLTAISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTPPT---SGAVFLDGVD 83
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIP 73
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
45-75 |
3.69e-03 |
|
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: 37.73 E-value: 3.69e-03
10 20 30
....*....|....*....|....*....|.
gi 521297957 45 PGEVCGFIGPNGAGKTTLFDIISGLTPPTSG 75
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLKPNLG 55
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| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
50-69 |
4.93e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 37.75 E-value: 4.93e-03
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
193-267 |
6.37e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 37.74 E-value: 6.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 193 LDEPTSGLsaHE--TELFGEQIQRLRTTGVAVVLVEHDVGfVMGQSDRVVVL------NLGSVLAEGTPDEIQAHPA-VR 263
Cdd:PRK00349 515 LDEPSIGL--HQrdNDRLIETLKHLRDLGNTLIVVEHDED-TIRAADYIVDIgpgagvHGGEVVASGTPEEIMKNPNsLT 591
|
....
gi 521297957 264 AAYL 267
Cdd:PRK00349 592 GQYL 595
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
36-227 |
7.21e-03 |
|
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: 37.42 E-value: 7.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 36 ISDVSLRVDPGEVCGFIGPNGAGKTTLFDIISGLTP--------PTSGAVFLdgvdvtrqLPERRARSgvRRTFqRAQLY 107
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPvyggrltkPAKGKLFY--------VPQRPYMT--LGTL-RDQII 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521297957 108 SRLSVEDnvltaMEWRgggGGLLADLFAapgrrrreaerreyalsVLAACGLADLRHKPAG---------ALPIGQARLV 178
Cdd:TIGR00954 537 YPDSSED-----MKRR---GLSDKDLEQ-----------------ILDNVQLTHILEREGGwsavqdwmdVLSGGEKQRI 591
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 521297957 179 ELARAIADRPRLLLLDEPTSGLSaheTELFGEQIQRLRTTGVAVVLVEH 227
Cdd:TIGR00954 592 AMARLFYHKPQFAILDECTSAVS---VDVEGYMYRLCREFGITLFSVSH 637
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