|
Name |
Accession |
Description |
Interval |
E-value |
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-221 |
4.87e-103 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 300.44 E-value: 4.87e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 4 IDVKNLTKTYKKNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQSKEIRQNVGYLPS 83
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 84 EVHFYDDMKVIDLLKYSAGFY---KKFNQKRMKELAERLDLD--LHKKIEDLSFGNRKKVGIVQALLHEPKLLILDEPTG 158
Cdd:COG1131 81 EPALYPDLTVRENLRFFARLYglpRKEARERIDELLELFGLTdaADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1021811607 159 GLDPLMQNTFFEILTEEREKGTTIIFSSHILSEVQKMCDRVAIIKEGELVKVETIENLTKNNL 221
Cdd:COG1131 161 GLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARLL 223
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-286 |
5.54e-89 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 266.97 E-value: 5.54e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 3 IIDVKNLTKTYKKNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIvkqSKEIRQNVGYLP 82
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPL---DPEDRRRIGYLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 83 SEVHFYDDMKVIDLLKYSA---GFYKKFNQKRMKELAERLDLD--LHKKIEDLSFGNRKKVGIVQALLHEPKLLILDEPT 157
Cdd:COG4152 78 EERGLYPKMKVGEQLVYLArlkGLSKAEAKRRADEWLERLGLGdrANKKVEELSKGNQQKVQLIAALLHDPELLILDEPF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 158 GGLDPLMQNTFFEILTEEREKGTTIIFSSHILSEVQKMCDRVAIIKEGELV---KVETIENLTKNNlkNITITFEQTNAI 234
Cdd:COG4152 158 SGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVlsgSVDEIRRQFGRN--TLRLEADGDAGW 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1021811607 235 DFDLEGIVKKEINGS--EMMLLYSGDIKTLLNQL-NTMPVQDLLIEEPSLEEVFI 286
Cdd:COG4152 236 LRALPGVTVVEEDGDgaELKLEDGADAQELLRALlARGPVREFEEVRPSLNEIFI 290
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-207 |
1.30e-80 |
|
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: 241.15 E-value: 1.30e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 4 IDVKNLTKTYKKNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQSKEIRQNVGYLPS 83
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 84 EVHFYDDMKVIDLLKYSAgfykkfnqkrmkelaerldldlhkkiedlsfGNRKKVGIVQALLHEPKLLILDEPTGGLDPL 163
Cdd:cd03230 81 EPSLYENLTVRENLKLSG-------------------------------GMKQRLALAQALLHDPELLILDEPTSGLDPE 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1021811607 164 MQNTFFEILTEEREKGTTIIFSSHILSEVQKMCDRVAIIKEGEL 207
Cdd:cd03230 130 SRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
4-228 |
2.13e-80 |
|
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: 243.23 E-value: 2.13e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 4 IDVKNLTKTYKKNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQSKEIRQNVGYLPS 83
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGVLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 84 EVHFYDDMKVIDLLKYSAGFYKKF---NQKRMKELAERLDLD--LHKKIEDLSFGNRKKVGIVQALLHEPKLLILDEPTG 158
Cdd:COG4555 82 ERGLYDRLTVRENIRYFAELYGLFdeeLKKRIEELIELLGLEefLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTN 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1021811607 159 GLDPLMQNTFFEILTEEREKGTTIIFSSHILSEVQKMCDRVAIIKEGELVKVETI----ENLTKNNLKNITITF 228
Cdd:COG4555 162 GLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLdelrEEIGEENLEDAFVAL 235
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
3-208 |
3.86e-67 |
|
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: 208.38 E-value: 3.86e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 3 IIDVKNLTKTYKKNRGIV----NLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQSKEIRQNV 78
Cdd:cd03266 1 MITADALTKRFRDVKKTVqavdGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 79 GYLPSEVHFYDDMKVIDLLKYSAGFY--KKFNQK-RMKELAERLDLD--LHKKIEDLSFGNRKKVGIVQALLHEPKLLIL 153
Cdd:cd03266 81 GFVSDSTGLYDRLTARENLEYFAGLYglKGDELTaRLEELADRLGMEelLDRRVGGFSTGMRQKVAIARALVHDPPVLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1021811607 154 DEPTGGLDPLMQNTFFEILTEEREKGTTIIFSSHILSEVQKMCDRVAIIKEGELV 208
Cdd:cd03266 161 DEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVV 215
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-208 |
8.72e-67 |
|
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: 207.13 E-value: 8.72e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 4 IDVKNLTKTYKKNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIvkqSKEIRQNVGYLPS 83
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPL---DIAARNRIGYLPE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 84 EVHFYDDMKVIDLLKYSA---GFYKKFNQKRMKELAERLDLDLH--KKIEDLSFGNRKKVGIVQALLHEPKLLILDEPTG 158
Cdd:cd03269 78 ERGLYPKMKVIDQLVYLAqlkGLKKEEARRRIDEWLERLELSEYanKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFS 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1021811607 159 GLDPLMQNTFFEILTEEREKGTTIIFSSHILSEVQKMCDRVAIIKEGELV 208
Cdd:cd03269 158 GLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAV 207
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-290 |
1.18e-63 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 203.01 E-value: 1.18e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 3 IIDVKNLTKTYK---KNRGIV------------------NLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSAT 61
Cdd:COG4586 1 IIEVENLSKTYRvyeKEPGLKgalkglfrreyreveavdDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 62 IFGKDIVKQSKEIRQNVGylpseVHF------YDDMKVIDLLKYSAGFY----KKFnQKRMKELAERLDLD--LHKKIED 129
Cdd:COG4586 81 VLGYVPFKRRKEFARRIG-----VVFgqrsqlWWDLPAIDSFRLLKAIYripdAEY-KKRLDELVELLDLGelLDTPVRQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 130 LSFGNRKKVGIVQALLHEPKLLILDEPTGGLDPLMQNTFFEILTEE-REKGTTIIFSSHILSEVQKMCDRVAIIKEGELV 208
Cdd:COG4586 155 LSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYnRERGTTILLTSHDMDDIEALCDRVIVIDHGRII 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 209 KVETIENLTKN--NLKNITITFEQTNAIDFDLEGIVKKEINGSEMMLLYSG--DIKTLLNQL-NTMPVQDLLIEEPSLEE 283
Cdd:COG4586 235 YDGSLEELKERfgPYKTIVLELAEPVPPLELPRGGEVIEREGNRVRLEVDPreSLAEVLARLlARYPVRDLTIEEPPIEE 314
|
....*..
gi 1021811607 284 VFIHYYE 290
Cdd:COG4586 315 VIRRIYK 321
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-208 |
3.59e-63 |
|
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: 198.19 E-value: 3.59e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 4 IDVKNLTKTYKKNRGIVNLTFSVEEGeIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQSKEIRQNVGYLPS 83
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 84 EVHFYDDMKVIDLLKYSAgFYKKFNQKRMKELAERL--DLDL----HKKIEDLSFGNRKKVGIVQALLHEPKLLILDEPT 157
Cdd:cd03264 80 EFGVYPNFTVREFLDYIA-WLKGIPSKEVKARVDEVleLVNLgdraKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1021811607 158 GGLDPLMQNTFFEILTEEREkGTTIIFSSHILSEVQKMCDRVAIIKEGELV 208
Cdd:cd03264 159 AGLDPEERIRFRNLLSELGE-DRIVILSTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
4-216 |
2.69e-62 |
|
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: 196.05 E-value: 2.69e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 4 IDVKNLTKTYKKNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQSKEIRQNVGYLPS 83
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 84 EVHFYDDMKVIDLLKYSAGFYKKFNQKRMKELAERLD-LDL----HKKIEDLSFGNRKKVGIVQALLHEPKLLILDEPTG 158
Cdd:cd03265 81 DLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDfVGLleaaDRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1021811607 159 GLDPLMQNTFFEILTE-EREKGTTIIFSSHILSEVQKMCDRVAIIKEGELVKVETIENL 216
Cdd:cd03265 161 GLDPQTRAHVWEYIEKlKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
11-288 |
9.61e-62 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 197.61 E-value: 9.61e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 11 KTYKKNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQSKEIRQNVGYLPSEVHFYDD 90
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVRRSIGIVPQYASVDED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 91 MKVIDLLKYSAGFY---KKFNQKRMKELAERLDL--DLHKKIEDLSFGNRKKVGIVQALLHEPKLLILDEPTGGLDPLMQ 165
Cdd:TIGR01188 81 LTGRENLEMMGRLYglpKDEAEERAEELLELFELgeAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 166 NTFFEILTEEREKGTTIIFSSHILSEVQKMCDRVAIIKEGELVKVETIENLtKNNLKNITITFEQTNAIDFDLE-GIVKK 244
Cdd:TIGR01188 161 RAIWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEEL-KRRLGKDTLESRPRDIQSLKVEvSMLIA 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1021811607 245 EI----NGSEMMLLYSGDIKTLLNQL-------------NTMPVQDLLIEEPSLEEVFIHY 288
Cdd:TIGR01188 240 ELgetgLGLLAVTVDSDRIKILVPDGdetvpeiveaairNGIRIRSISTERPSLDDVFLKL 300
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-208 |
3.34e-59 |
|
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: 187.81 E-value: 3.34e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 4 IDVKNLTKTYKKNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKqSKEIRQNVGYLPS 83
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQK-NIEALRRIGALIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 84 EVHFYDDMKVIDLLKYSAgFYKKFNQKRMKELAERLDLDL--HKKIEDLSFGNRKKVGIVQALLHEPKLLILDEPTGGLD 161
Cdd:cd03268 80 APGFYPNLTARENLRLLA-RLLGIRKKRIDEVLDVVGLKDsaKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1021811607 162 PLMQNTFFEILTEEREKGTTIIFSSHILSEVQKMCDRVAIIKEGELV 208
Cdd:cd03268 159 PDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLI 205
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-208 |
9.04e-58 |
|
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: 184.63 E-value: 9.04e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 4 IDVKNLTKTYKKNRGIV--NLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQSKEIRQNVGYL 81
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAvdDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 82 PSEVHFYDDMKVIDLLKYSA---GFYKKFNQKRMKELAERLDL--DLHKKIEDLSFGNRKKVGIVQALLHEPKLLILDEP 156
Cdd:cd03263 81 PQFDALFDELTVREHLRFYArlkGLPKSEIKEEVELLLRVLGLtdKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1021811607 157 TGGLDPLMQNTFFEILTEEReKGTTIIFSSHILSEVQKMCDRVAIIKEGELV 208
Cdd:cd03263 161 TSGLDPASRRAIWDLILEVR-KGRSIILTTHSMDEAEALCDRIAIMSDGKLR 211
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-222 |
1.10e-53 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 174.89 E-value: 1.10e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 1 MKIIDVKNLTKTYKKNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQskeiRQNVGY 80
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA----RRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 81 LPSEVHFYDD--MKVIDL----LKYSAGFYKKFNQK---RMKELAERLDLD--LHKKIEDLSFGNRKKVGIVQALLHEPK 149
Cdd:COG1121 80 VPQRAEVDWDfpITVRDVvlmgRYGRRGLFRRPSRAdreAVDEALERVGLEdlADRPIGELSGGQQQRVLLARALAQDPD 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1021811607 150 LLILDEPTGGLDPLMQNTFFEILTEEREKGTTIIFSSHILSEVQKMCDRVAIIKEGELVKVETIENLTKNNLK 222
Cdd:COG1121 160 LLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLVAHGPPEEVLTPENLS 232
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
4-208 |
1.07e-48 |
|
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: 161.73 E-value: 1.07e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 4 IDVKNLTKTYK------------------KNRGIV---NLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATI 62
Cdd:cd03267 1 IEVSNLSKSYRvyskepgligslkslfkrKYREVEalkGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 63 FGKDIVKQSKEIRQNVGY-LPSEVHFYDDMKVIDLLKYSAGFYK----KFnQKRMKELAERLDLD--LHKKIEDLSFGNR 135
Cdd:cd03267 81 AGLVPWKRRKKFLRRIGVvFGQKTQLWWDLPVIDSFYLLAAIYDlppaRF-KKRLDELSELLDLEelLDTPVRQLSLGQR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1021811607 136 KKVGIVQALLHEPKLLILDEPTGGLDPLMQNTFFEILTEE-REKGTTIIFSSHILSEVQKMCDRVAIIKEGELV 208
Cdd:cd03267 160 MRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYnRERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
6-203 |
2.96e-48 |
|
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: 160.01 E-value: 2.96e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 6 VKNLTKTYKKNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQSKEIrqnvGYLP--S 83
Cdd:cd03235 2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKRI----GYVPqrR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 84 EVHFYDDMKVIDLLK----YSAGFYKKFNQKRMKELAERLD----LDL-HKKIEDLSFGNRKKVGIVQALLHEPKLLILD 154
Cdd:cd03235 78 SIDRDFPISVRDVVLmglyGHKGLFRRLSKADKAKVDEALErvglSELaDRQIGELSGGQQQRVLLARALVQDPDLLLLD 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1021811607 155 EPTGGLDPLMQNTFFEILTEEREKGTTIIFSSHILSEVQKMCDRVAIIK 203
Cdd:cd03235 158 EPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLN 206
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
3-208 |
1.12e-47 |
|
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: 158.82 E-value: 1.12e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 3 IIDVKNLTKTYKKNRGIV----NLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQSKEI---- 74
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVkaldDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLrkir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 75 RQNVGYLP----SEVHFYddMKVID-----LLKYSAGFYKKFNQKRMKELAERLDLD---LHKKIEDLSFGNRKKVGIVQ 142
Cdd:cd03257 81 RKEIQMVFqdpmSSLNPR--MTIGEqiaepLRIHGKLSKKEARKEAVLLLLVGVGLPeevLNRYPHELSGGQRQRVAIAR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1021811607 143 ALLHEPKLLILDEPTGGLDPLMQNTFFEILTEER-EKGTTIIFSSHILSEVQKMCDRVAIIKEGELV 208
Cdd:cd03257 159 ALALNPKLLIADEPTSALDVSVQAQILDLLKKLQeELGLTLLFITHDLGVVAKIADRVAVMYAGKIV 225
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-208 |
4.60e-46 |
|
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: 161.99 E-value: 4.60e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 3 IIDVKNLTKTYK-KNRGIV----NLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQS----KE 73
Cdd:COG1123 260 LLEVRNLSKRYPvRGKGGVravdDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrslRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 74 IRQNVGYLpsevhFYD-------DMKVIDLLKYSAGFYKKFN----QKRMKELAERLDLD---LHKKIEDLSFGNRKKVG 139
Cdd:COG1123 340 LRRRVQMV-----FQDpysslnpRMTVGDIIAEPLRLHGLLSraerRERVAELLERVGLPpdlADRYPHELSGGQRQRVA 414
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 140 IVQALLHEPKLLILDEPTGGLDPLMQNTFFEILTEEREK-GTTIIFSSHILSEVQKMCDRVAIIKEGELV 208
Cdd:COG1123 415 IARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDGRIV 484
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-209 |
1.33e-45 |
|
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: 153.64 E-value: 1.33e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 4 IDVKNLTKTYKKNRGIV-NLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQS-KEIRQNVGYL 81
Cdd:COG1122 1 IELENLSFSYPGGTPALdDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNlRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 82 ---PsevhfyDDM----KVIDLLKYS---AGFYKKFNQKRMKELAERLDLD--LHKKIEDLSFGNRKKVGIVQALLHEPK 149
Cdd:COG1122 81 fqnP------DDQlfapTVEEDVAFGpenLGLPREEIRERVEEALELVGLEhlADRPPHELSGGQKQRVAIAGVLAMEPE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 150 LLILDEPTGGLDPLMQNTFFEILTEEREKGTTIIFSSHILSEVQKMCDRVAIIKEGELVK 209
Cdd:COG1122 155 VLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVA 214
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-209 |
3.50e-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: 150.66 E-value: 3.50e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 5 DVKNLTKTYKKNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQS-KEIRQNVGYLPs 83
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSpKELARKIAYVP- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 84 evhfyddmKVIDLLkysagfykkfnqkRMKELAERLdldlhkkIEDLSFGNRKKVGIVQALLHEPKLLILDEPTGGLDPL 163
Cdd:cd03214 80 --------QALELL-------------GLAHLADRP-------FNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIA 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1021811607 164 MQNTFFEILTEE-REKGTTIIFSSHILSEVQKMCDRVAIIKEGELVK 209
Cdd:cd03214 132 HQIELLELLRRLaRERGKTVVMVLHDLNLAARYADRVILLKDGRIVA 178
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-224 |
6.93e-45 |
|
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: 152.51 E-value: 6.93e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 3 IIDVKNLTKTYKKNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQS-KEIRQNVGYL 81
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSrRELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 82 PSEVHFYDDMKVIDLLKYS----AGFYKKFNQK---RMKELAERLDLD--LHKKIEDLSFGNRKKVGIVQALLHEPKLLI 152
Cdd:COG1120 81 PQEPPAPFGLTVRELVALGryphLGLFGRPSAEdreAVEEALERTGLEhlADRPVDELSGGERQRVLIARALAQEPPLLL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1021811607 153 LDEPTGGLDPLMQNTFFEILTEE-REKGTTIIFSSHILSEVQKMCDRVAIIKEGELVKVETIEN-LTKNNLKNI 224
Cdd:COG1120 161 LDEPTSHLDLAHQLEVLELLRRLaRERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEvLTPELLEEV 234
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
6-206 |
8.54e-45 |
|
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: 148.93 E-value: 8.54e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 6 VKNLTKTYKKNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVK-QSKEIRQNVGYLPSe 84
Cdd:cd00267 2 IENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKlPLEELRRRIGYVPQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 85 vhfyddmkvidllkysagfykkfnqkrmkelaerldldlhkkiedLSFGNRKKVGIVQALLHEPKLLILDEPTGGLDPLM 164
Cdd:cd00267 81 ---------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPAS 115
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1021811607 165 QNTFFEILTEEREKGTTIIFSSHILSEVQKMCDRVAIIKEGE 206
Cdd:cd00267 116 RERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
3-220 |
9.05e-44 |
|
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: 148.97 E-value: 9.05e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 3 IIDVKNLTKTYKKNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQS----KEIRQNV 78
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSekelYELRRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 79 GYLpsevhF-----YDDMKVID-----LLKYSagfykKFNQKRMKELA-ERLDL-----DLHKKIEDLSFGNRKKVGIVQ 142
Cdd:COG1127 85 GML-----FqggalFDSLTVFEnvafpLREHT-----DLSEAEIRELVlEKLELvglpgAADKMPSELSGGMRKRVALAR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1021811607 143 ALLHEPKLLILDEPTGGLDPLMQNTFFE-ILTEEREKGTTIIFSSHILSEVQKMCDRVAIIKEGELVKVETIENLTKNN 220
Cdd:COG1127 155 ALALDPEILLYDEPTAGLDPITSAVIDElIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASD 233
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-192 |
1.10e-43 |
|
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: 148.01 E-value: 1.10e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 4 IDVKNLTKTYKKNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQSKEIRQNVGYLPS 83
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYLGH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 84 EVHFYDDMKVIDLLKYSAGFYK-KFNQKRMKELAERLDLD--LHKKIEDLSFGNRKKVGIVQALLHEPKLLILDEPTGGL 160
Cdd:COG4133 83 ADGLKPELTVRENLRFWAALYGlRADREAIDEALEAVGLAglADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTAL 162
|
170 180 190
....*....|....*....|....*....|..
gi 1021811607 161 DPLMQNTFFEILTEEREKGTTIIFSSHILSEV 192
Cdd:COG4133 163 DAAGVALLAELIAAHLARGGAVLLTTHQPLEL 194
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-206 |
2.30e-43 |
|
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: 146.18 E-value: 2.30e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 4 IDVKNLTKTYKKNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDI---VKQSKEIRQNVGY 80
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLtdlEDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 81 LPSEVHFYDDMKVIDLLKYSagfykkfnqkrmkelaerldldlhkkiedLSFGNRKKVGIVQALLHEPKLLILDEPTGGL 160
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG-----------------------------LSGGQQQRVALARALAMDPDVLLLDEPTSAL 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1021811607 161 DPLMQNTFFEILTEEREK-GTTIIFSSHILSEVQKMCDRVAIIKEGE 206
Cdd:cd03229 132 DPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
3-219 |
5.98e-43 |
|
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: 146.96 E-value: 5.98e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 3 IIDVKNLTKTYKKNRGIV----NLTFSVEEGEIFGFIGPNGAGKSTTIRtLLNFL-YPTSGSATIFGKDIVKQSK----E 73
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVtalkDVSLSVPKGEIFGIIGRSGAGKSTLIR-CINGLeRPTSGSVLVDGTDLTLLSGkelrK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 74 IRQNVGYLPSEVHFYDDMKVIDLLKYS---AGFYKKFNQKRMKELAERLDL-DLHKK-IEDLSFGNRKKVGIVQALLHEP 148
Cdd:cd03258 80 ARRRIGMIFQHFNLLSSRTVFENVALPleiAGVPKAEIEERVLELLELVGLeDKADAyPAQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1021811607 149 KLLILDEPTGGLDPLMQNTFFEILTE-EREKGTTIIFSSHILSEVQKMCDRVAIIKEGELVKVETIENLTKN 219
Cdd:cd03258 160 KVLLCDEATSALDPETTQSILALLRDiNRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFAN 231
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-219 |
2.26e-42 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 145.52 E-value: 2.26e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 4 IDVKNLTKTYKKNRGIV-NLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQSK-EIRQNVGYL 81
Cdd:cd03295 1 IEFENVTKRYGGGKKAVnNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPvELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 82 PSEVHFYDDMKVID-------LLKYSagfyKKFNQKRMKELAERLDLD----LHKKIEDLSFGNRKKVGIVQALLHEPKL 150
Cdd:cd03295 81 IQQIGLFPHMTVEEnialvpkLLKWP----KEKIRERADELLALVGLDpaefADRYPHELSGGQQQRVGVARALAADPPL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1021811607 151 LILDEPTGGLDPL----MQNTFFEIlteEREKGTTIIFSSHILSEVQKMCDRVAIIKEGELVKVETIENLTKN 219
Cdd:cd03295 157 LLMDEPFGALDPItrdqLQEEFKRL---QQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRS 226
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
6-206 |
2.91e-42 |
|
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: 144.15 E-value: 2.91e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 6 VKNLTKTYKKNRGIV--NLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQS-KEIRQNVGYL- 81
Cdd:cd03225 2 LKNLSFSYPDGARPAldDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSlKELRRKVGLVf 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 82 --PsevhfyDDM----KVIDLLKYSA---GFYKKFNQKRMKELAERLDLD--LHKKIEDLSFGNRKKVGIVQALLHEPKL 150
Cdd:cd03225 82 qnP------DDQffgpTVEEEVAFGLenlGLPEEEIEERVEEALELVGLEglRDRSPFTLSGGQKQRVAIAGVLAMDPDI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1021811607 151 LILDEPTGGLDPLMQNTFFEILTEEREKGTTIIFSSHILSEVQKMCDRVAIIKEGE 206
Cdd:cd03225 156 LLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-216 |
3.22e-42 |
|
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: 144.95 E-value: 3.22e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 4 IDVKNLTKTYKKNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQS----KEIRQNVG 79
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSeaelYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 80 YLpsevhF-----YDDMKVID-----LLKYSagfykKFNQKRMKELA-ERLDL-----DLHKKIEDLSFGNRKKVGIVQA 143
Cdd:cd03261 81 ML-----FqsgalFDSLTVFEnvafpLREHT-----RLSEEEIREIVlEKLEAvglrgAEDLYPAELSGGMKKRVALARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1021811607 144 LLHEPKLLILDEPTGGLDPLMQNTFFE-ILTEEREKGTTIIFSSHILSEVQKMCDRVAIIKEGELVKVETIENL 216
Cdd:cd03261 151 LALDPELLLYDEPTAGLDPIASGVIDDlIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEEL 224
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-210 |
1.18e-41 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 142.66 E-value: 1.18e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 4 IDVKNLTKTYKKNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQSKEIRqNVGYLPS 83
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERR-NIGMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 84 EVHFYDDMKVIDLLKY---SAGFYKKFNQKRMKELAERLDLD--LHKKIEDLSFGNRKKVGIVQALLHEPKLLILDEPTG 158
Cdd:cd03259 80 DYALFPHLTVAENIAFglkLRGVPKAEIRARVRELLELVGLEglLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1021811607 159 GLDPL----MQNTFFEILteeREKGTTIIFSSHILSEVQKMCDRVAIIKEGELVKV 210
Cdd:cd03259 160 ALDAKlreeLREELKELQ---RELGITTIYVTHDQEEALALADRIAVMNEGRIVQV 212
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
4-218 |
5.19e-41 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 141.38 E-value: 5.19e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 4 IDVKNLTKTYKKNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIvkqSKEIRQNVGYLPS 83
Cdd:TIGR03740 1 LETKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPW---TRKDLHKIGSLIE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 84 EVHFYDDMKVIDLLKYSAgFYKKFNQKRMKELAERLDL--DLHKKIEDLSFGNRKKVGIVQALLHEPKLLILDEPTGGLD 161
Cdd:TIGR03740 78 SPPLYENLTARENLKVHT-TLLGLPDSRIDEVLNIVDLtnTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEPTNGLD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 162 PLMQNTFFEILTEEREKGTTIIFSSHILSEVQKMCDRVAIIKEGELV---KVETIENLTK 218
Cdd:TIGR03740 157 PIGIQELRELIRSFPEQGITVILSSHILSEVQQLADHIGIISEGVLGyqgKINKSENLEK 216
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-208 |
2.04e-40 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 146.71 E-value: 2.04e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 3 IIDVKNLTKTY---KKNRGIvnlTFSVEEGEIFGFIGPNGAGKSttirTLLNFLY----PTSGSATIFGKDI-VKQSKE- 73
Cdd:COG3845 5 ALELRGITKRFggvVANDDV---SLTVRPGEIHALLGENGAGKS----TLMKILYglyqPDSGEILIDGKPVrIRSPRDa 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 74 IRQNVGYlpseV--HF--YDDMKVID--LLKYSAGFYKKFNQK----RMKELAER--LDLDLHKKIEDLSFGNRKKVGIV 141
Cdd:COG3845 78 IALGIGM----VhqHFmlVPNLTVAEniVLGLEPTKGGRLDRKaaraRIRELSERygLDVDPDAKVEDLSVGEQQRVEIL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1021811607 142 QALLHEPKLLILDEPTGGLDPLMQNTFFEILTEEREKGTTIIFSSHILSEVQKMCDRVAIIKEGELV 208
Cdd:COG3845 154 KALYRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVV 220
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-207 |
2.07e-40 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 139.93 E-value: 2.07e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 4 IDVKNLTKTYKKNRGIV----NLTFSVEEGEIFGFIGPNGAGKSTtirtLLNFLY----PTSGSATIFGKDIVK-----Q 70
Cdd:cd03255 1 IELKNLSKTYGGGGEKVqalkGVSLSIEKGEFVAIVGPSGSGKST----LLNILGgldrPTSGEVRVDGTDISKlsekeL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 71 SKEIRQNVGYLPSEVHFYDDMKVIDLLKYSAGFYKKFNQKRM---KELAERLDLD--LHKKIEDLSFGNRKKVGIVQALL 145
Cdd:cd03255 77 AAFRRRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERReraEELLERVGLGdrLNHYPSELSGGQQQRVAIARALA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1021811607 146 HEPKLLILDEPTGGLDPLMQNTFFEILTEE-REKGTTIIFSSHILsEVQKMCDRVAIIKEGEL 207
Cdd:cd03255 157 NDPKIILADEPTGNLDSETGKEVMELLRELnKEAGTTIVVVTHDP-ELAEYADRIIELRDGKI 218
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
3-205 |
2.65e-39 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 139.56 E-value: 2.65e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 3 IIDVKNLTKTYKKNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQSKEIRQNVGYLP 82
Cdd:PRK13537 7 PIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGVVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 83 SEVHFYDDMKVID-LLKYSAGFYKKFNQ--KRMKELAE--RLDLDLHKKIEDLSFGNRKKVGIVQALLHEPKLLILDEPT 157
Cdd:PRK13537 87 QFDNLDPDFTVREnLLVFGRYFGLSAAAarALVPPLLEfaKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPT 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1021811607 158 GGLDPLMQNTFFEILTEEREKGTTIIFSSHILSEVQKMCDRVAIIKEG 205
Cdd:PRK13537 167 TGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEG 214
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
3-211 |
9.40e-39 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 135.57 E-value: 9.40e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 3 IIDVKNLTKTYKKNRGIV-NLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQSKE----IRQN 77
Cdd:COG2884 1 MIRFENVSKRYPGGREALsDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRReipyLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 78 VGYLPSEVHFYDDMKVIDLLKYS---AGFYKKFNQKRMKELAERLDLD--LHKKIEDLSFGNRKKVGIVQALLHEPKLLI 152
Cdd:COG2884 81 IGVVFQDFRLLPDRTVYENVALPlrvTGKSRKEIRRRVREVLDLVGLSdkAKALPHELSGGEQQRVAIARALVNRPELLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1021811607 153 LDEPTGGLDPLMQNTFFEILTEEREKGTTIIFSSHILSEVQKMCDRVAIIKEGELVKVE 211
Cdd:COG2884 161 ADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDE 219
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
2-208 |
1.54e-38 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 135.95 E-value: 1.54e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 2 KIIDVKNLTKTYKKNRGIV-NLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQS----KEIRQ 76
Cdd:COG3638 1 PMLELRNLSKRYPGGTPALdDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRgralRRLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 77 NVGYLPSEVHFYDDMKVID-----------LLKYSAGFYKKfnqkRMKELA----ERLDLD--LHKKIEDLSFGNRKKVG 139
Cdd:COG3638 81 RIGMIFQQFNLVPRLSVLTnvlagrlgrtsTWRSLLGLFPP----EDRERAlealERVGLAdkAYQRADQLSGGQQQRVA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 140 IVQALLHEPKLLILDEPTGGLDPLMQNTFFEILTEE-REKGTTIIFSSHILSEVQKMCDRVAIIKEGELV 208
Cdd:COG3638 157 IARALVQEPKLILADEPVASLDPKTARQVMDLLRRIaREDGITVVVNLHQVDLARRYADRIIGLRDGRVV 226
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-219 |
2.75e-38 |
|
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: 134.48 E-value: 2.75e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 4 IDVKNLTKTYKKNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQSKE--IRQNVGYL 81
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHerARAGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 82 PSEVHFYDDMKVIDLLKYSAGFYKKFNQKRMKE--------LAERLdldlHKKIEDLSFGNRKKVGIVQALLHEPKLLIL 153
Cdd:cd03224 81 PEGRRIFPELTVEENLLLGAYARRRAKRKARLErvyelfprLKERR----KQLAGTLSGGEQQMLAIARALMSRPKLLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1021811607 154 DEPTGGLDPLMQNTFFEILTEEREKGTTIIFSSHILSEVQKMCDRVAIIKEGELVKVETIENLTKN 219
Cdd:cd03224 157 DEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-221 |
4.43e-37 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 137.46 E-value: 4.43e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 3 IIDVKNLTKTYKKNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQS-KEIRQN-VGY 80
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSpRDAQAAgIAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 81 LPSEVHFYDDMKV-----IDLLKYSAGFykkFNQKRMKELAERL------DLDLHKKIEDLSFGNRKKVGIVQALLHEPK 149
Cdd:COG1129 84 IHQELNLVPNLSVaenifLGREPRRGGL---IDWRAMRRRARELlarlglDIDPDTPVGDLSVAQQQLVEIARALSRDAR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1021811607 150 LLILDEPTGGLDPLMQNTFFEILTEEREKGTTIIFSSHILSEVQKMCDRVAIIKEGELVKVETIENLTKNNL 221
Cdd:COG1129 161 VLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAELTEDEL 232
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-286 |
7.66e-37 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 133.80 E-value: 7.66e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 4 IDVKNLTKTYKkNRGIVN-LTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQSKEIRQNVGYLP 82
Cdd:PRK13536 42 IDLAGVSKSYG-DKAVVNgLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARARIGVVP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 83 SevhfYDDMKVI-----DLLKYsaGFYKKFNQKRMKE----LAE--RLDLDLHKKIEDLSFGNRKKVGIVQALLHEPKLL 151
Cdd:PRK13536 121 Q----FDNLDLEftvreNLLVF--GRYFGMSTREIEAvipsLLEfaRLESKADARVSDLSGGMKRRLTLARALINDPQLL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 152 ILDEPTGGLDPLMQNTFFEILTEEREKGTTIIFSSHILSEVQKMCDRVAIIKEGELVKVETIENLTKNNLKNITITFEQT 231
Cdd:PRK13536 195 ILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDEHIGCQVIEIYGG 274
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 232 NAidFDLEGIVKK-----EINGsEMMLLYSGDIKTLLNQLNTMPVQDLLIEEPSLEEVFI 286
Cdd:PRK13536 275 DP--HELSSLVKPyarriEVSG-ETLFCYAPDPEQVRVQLRGRAGLRLLQRPPNLEDVFL 331
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
3-218 |
9.70e-37 |
|
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: 130.97 E-value: 9.70e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 3 IIDVKNLTKTYKKNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSG-SATIFGKDIVKQS-KEIRQNVGY 80
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDvWELRKRIGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 81 LPSEVH--FYDDMKVIDLL---KY-SAGFYKKFN---QKRMKELAERLDLD--LHKKIEDLSFGNRKKVGIVQALLHEPK 149
Cdd:COG1119 83 VSPALQlrFPRDETVLDVVlsgFFdSIGLYREPTdeqRERARELLELLGLAhlADRPFGTLSQGEQRRVLIARALVKDPE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1021811607 150 LLILDEPTGGLDPLMQNTFFEILTEE-REKGTTIIFSSHILSEVQKMCDRVAIIKEGELV------KVETIENLTK 218
Cdd:COG1119 163 LLILDEPTAGLDLGARELLLALLDKLaAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVaagpkeEVLTSENLSE 238
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-224 |
1.17e-36 |
|
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: 130.77 E-value: 1.17e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 4 IDVKNLTKTYKKNRGIV-NLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQSKE----IRQNV 78
Cdd:cd03256 1 IEVENLSKTYPNGKKALkDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKalrqLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 79 GYLPSEVHFYDDMKVID-----------LLKYSAGFYKKFNQKRMKELAERLDLD--LHKKIEDLSFGNRKKVGIVQALL 145
Cdd:cd03256 81 GMIFQQFNLIERLSVLEnvlsgrlgrrsTWRSLFGLFPKEEKQRALAALERVGLLdkAYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 146 HEPKLLILDEPTGGLDPLMQNTFFEILTE-EREKGTTIIFSSHILSEVQKMCDRVAIIKEGELVKVETIENLTKNNLKNI 224
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQVMDLLKRiNREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTDEVLDEI 240
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
3-208 |
8.86e-36 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 130.97 E-value: 8.86e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 3 IIDVKNLTKTYKKNRGIV----NLTFSVEEGEIFGFIGPNGAGKSTTIRtLLNFL-YPTSGSATIFGKDIVKQSK----E 73
Cdd:COG1135 1 MIELENLSKTFPTKGGPVtaldDVSLTIEKGEIFGIIGYSGAGKSTLIR-CINLLeRPTSGSVLVDGVDLTALSErelrA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 74 IRQNVGYLPSevHF--------YDDmkvIDL-LKYsAGFYKKFNQKRMKELAERLDLD--LHKKIEDLSFGNRKKVGIVQ 142
Cdd:COG1135 80 ARRKIGMIFQ--HFnllssrtvAEN---VALpLEI-AGVPKAEIRKRVAELLELVGLSdkADAYPSQLSGGQKQRVGIAR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 143 ALLHEPKLLILDEPTGGLDPlmqNTFFEILT---EEREK-GTTIIFSSHILSEVQKMCDRVAIIKEGELV 208
Cdd:COG1135 154 ALANNPKVLLCDEATSALDP---ETTRSILDllkDINRElGLTIVLITHEMDVVRRICDRVAVLENGRIV 220
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-208 |
1.14e-35 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 133.88 E-value: 1.14e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 3 IIDVKNLTKTYKKNRGIV--NLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPT---SGSATIFGKDIVKQSKEIR-Q 76
Cdd:COG1123 4 LLEVRDLSVRYPGGDVPAvdGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRgR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 77 NVGYLPSE-------VHFYDDM-KVIDLLKYSagfyKKFNQKRMKELAERLDLD--LHKKIEDLSFGNRKKVGIVQALLH 146
Cdd:COG1123 84 RIGMVFQDpmtqlnpVTVGDQIaEALENLGLS----RAEARARVLELLEAVGLErrLDRYPHQLSGGQRQRVAIAMALAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1021811607 147 EPKLLILDEPTGGLDPLMQNTFFEILTE-EREKGTTIIFSSHILSEVQKMCDRVAIIKEGELV 208
Cdd:COG1123 160 DPDLLIADEPTTALDVTTQAEILDLLRElQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIV 222
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
18-219 |
8.77e-35 |
|
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: 126.60 E-value: 8.77e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 18 GIVNLTFSVEEGEIFGFIGPNGAGKSTTIRtLLNFLY-PTSGSATIFGKDIVKQSK----EIR--------QNVGYLPse 84
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLR-CINRLIePTSGKVLIDGQDIAAMSRkelrELRrkkismvfQSFALLP-- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 85 vHfyddMKVIDLLKYS---AGFYKKFNQKRMKELAERLDL--DLHKKIEDLSFGNRKKVGIVQALLHEPKLLILDEPTGG 159
Cdd:cd03294 116 -H----RTVLENVAFGlevQGVPRAEREERAAEALELVGLegWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSA 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1021811607 160 LDPL----MQNTFFEIlteEREKGTTIIFSSHILSEVQKMCDRVAIIKEGELVKVETIENLTKN 219
Cdd:cd03294 191 LDPLirreMQDELLRL---QAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-214 |
9.04e-35 |
|
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: 125.28 E-value: 9.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 4 IDVKNLTKTYKKNRGIV----NLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQSKEIrqnvG 79
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVtaleDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPDR----G 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 80 YLPSEVHFYDDMKVID----LLKySAGFYKKFNQKRMKELAERLDLD--LHKKIEDLSFGNRKKVGIVQALLHEPKLLIL 153
Cdd:cd03293 77 YVFQQDALLPWLTVLDnvalGLE-LQGVPKAEARERAEELLELVGLSgfENAYPHQLSGGMRQRVALARALAVDPDVLLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1021811607 154 DEPTGGLDPL----MQNTFFEILteeREKGTTIIFSSHILSEVQKMCDRVAIIKE--GELVKVETIE 214
Cdd:cd03293 156 DEPFSALDALtreqLQEELLDIW---RETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIVAEVEVD 219
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
3-208 |
9.30e-35 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 125.87 E-value: 9.30e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 3 IIDVKNLTKTYKKNR-GIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQSK----EIRQN 77
Cdd:TIGR02315 1 MLEVENLSKVYPNGKqALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGkklrKLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 78 VGYLPSEVHFYDDMKVID-----------LLKYSAGFYKKFNQKRMKELAERLDLD--LHKKIEDLSFGNRKKVGIVQAL 144
Cdd:TIGR02315 81 IGMIFQHYNLIERLTVLEnvlhgrlgykpTWRSLLGRFSEEDKERALSALERVGLAdkAYQRADQLSGGQQQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1021811607 145 LHEPKLLILDEPTGGLDPLMQNTFFEILTE-EREKGTTIIFSSHILSEVQKMCDRVAIIKEGELV 208
Cdd:TIGR02315 161 AQQPDLILADEPIASLDPKTSKQVMDYLKRiNKEDGITVIINLHQVDLAKKYADRIVGLKAGEIV 225
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
4-219 |
9.97e-35 |
|
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: 125.53 E-value: 9.97e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 4 IDVKNLTKTYKkNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQSKEIRqNVGYLPS 83
Cdd:cd03299 1 LKVENLSKDWK-EFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKR-DISYVPQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 84 EVHFYDDMKVIDLLKYsaGFYKKFNQK-----RMKELAERLDLD--LHKKIEDLSFGNRKKVGIVQALLHEPKLLILDEP 156
Cdd:cd03299 79 NYALFPHMTVYKNIAY--GLKKRKVDKkeierKVLEIAEMLGIDhlLNRKPETLSGGEQQRVAIARALVVNPKILLLDEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1021811607 157 TGGLDPLMQNTFFEILTEEREK-GTTIIFSSHILSEVQKMCDRVAIIKEGELVKVETIENLTKN 219
Cdd:cd03299 157 FSALDVRTKEKLREELKKIRKEfGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-208 |
1.35e-34 |
|
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: 125.24 E-value: 1.35e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 4 IDVKNLTKTYKknrGIV---NLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIV-KQSKEIR---- 75
Cdd:cd03219 1 LEVRGLTKRFG---GLValdDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITgLPPHEIArlgi 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 76 ----QNVGYLPSevhfyddMKVIDLL--------KYSAGFYKKFNQ-----KRMKELAERLDLD--LHKKIEDLSFGNRK 136
Cdd:cd03219 78 grtfQIPRLFPE-------LTVLENVmvaaqartGSGLLLARARREerearERAEELLERVGLAdlADRPAGELSYGQQR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1021811607 137 KVGIVQALLHEPKLLILDEPTGGLDPLMQNTFFEILTEEREKGTTIIFSSHILSEVQKMCDRVAIIKEGELV 208
Cdd:cd03219 151 RLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVI 222
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-208 |
2.81e-34 |
|
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: 124.77 E-value: 2.81e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 1 MKIIDVKNLTKTYKKNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQS-KEI----- 74
Cdd:COG0411 2 DPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPpHRIarlgi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 75 -R--QNVGYLPS----E-----VHFYDDMKVIDLLKYSAGFYK--KFNQKRMKELAERLDLD--LHKKIEDLSFGNRKKV 138
Cdd:COG0411 82 aRtfQNPRLFPEltvlEnvlvaAHARLGRGLLAALLRLPRARReeREARERAEELLERVGLAdrADEPAGNLSYGQQRRL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1021811607 139 GIVQALLHEPKLLILDEPTGGLDPLMQNTFFEILTE-EREKGTTIIFSSHILSEVQKMCDRVAIIKEGELV 208
Cdd:COG0411 162 EIARALATEPKLLLLDEPAAGLNPEETEELAELIRRlRDERGITILLIEHDMDLVMGLADRIVVLDFGRVI 232
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-206 |
7.62e-34 |
|
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: 121.34 E-value: 7.62e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 4 IDVKNLTKTYKKNRGIV--NLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVK-QSKEIRQNVGY 80
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVlkDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDlDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 81 LPSEVHFYDDMkvidllkysagfykkfnqkrmkeLAERLdldlhkkiedLSFGNRKKVGIVQALLHEPKLLILDEPTGGL 160
Cdd:cd03228 81 VPQDPFLFSGT-----------------------IRENI----------LSGGQRQRIAIARALLRDPPILILDEATSAL 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1021811607 161 DPLMQNTFFEILTEEReKGTTIIFSSHILSEVqKMCDRVAIIKEGE 206
Cdd:cd03228 128 DPETEALILEALRALA-KGKTVIVIAHRLSTI-RDADRIIVLDDGR 171
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
21-157 |
1.62e-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: 119.67 E-value: 1.62e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 21 NLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQSKEI-RQNVGYLPSEVHFYDDMKVIDLLKY 99
Cdd:pfam00005 3 NVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSlRKEIGYVFQDPQLFPRLTVRENLRL 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1021811607 100 SAGFYKKFNQK---RMKELAERLDLD------LHKKIEDLSFGNRKKVGIVQALLHEPKLLILDEPT 157
Cdd:pfam00005 83 GLLLKGLSKREkdaRAEEALEKLGLGdladrpVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
21-218 |
1.68e-33 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 129.47 E-value: 1.68e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 21 NLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQSKEIRQNVGYLPSEVHFYDDMKVIDLLKYS 100
Cdd:NF033858 284 HVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIATRRRVGYMSQAFSLYGELTVRQNLELH 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 101 AGFY---KKFNQKRMKELAERLDLD--LHKKIEDLSFGNRKKVGIVQALLHEPKLLILDEPTGGLDPLMQNTFFEILTE- 174
Cdd:NF033858 364 ARLFhlpAAEIAARVAEMLERFDLAdvADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLIEl 443
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1021811607 175 EREKGTTIIFSSHILSEVQKmCDRVAIIKEGELVKVETIENLTK 218
Cdd:NF033858 444 SREDGVTIFISTHFMNEAER-CDRISLMHAGRVLASDTPAALVA 486
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-212 |
2.33e-33 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 122.95 E-value: 2.33e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 4 IDVKNLTKTYKKN-----RGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRtLLN-FLYPTSGSATIFGKDIV----KQSKE 73
Cdd:TIGR04521 1 IKLKNVSYIYQPGtpfekKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQ-HLNgLLKPTSGTVTIDGRDITakkkKKLKD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 74 IRQNVGYL---PSEVHF----YDDMkvidllkysA------GFYKKFNQKRMKELAERLDLD---LHKKIEDLSFGNRKK 137
Cdd:TIGR04521 80 LRKKVGLVfqfPEHQLFeetvYKDI---------AfgpknlGLSEEEAEERVKEALELVGLDeeyLERSPFELSGGQMRR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1021811607 138 VGIVQALLHEPKLLILDEPTGGLDPLMQNTFFEILTE-EREKGTTIIFSSHILSEVQKMCDRVAIIKEGELVKVET 212
Cdd:TIGR04521 151 VAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRlHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGT 226
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-208 |
5.52e-33 |
|
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: 118.69 E-value: 5.52e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 4 IDVKNLTKTYKKNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKdivkqskeirqnvgylps 83
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGK------------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 84 EVHFYDDMKvidllkysagfykkfnqkrmkelAERLdldlhkKIE---DLSFGNRKKVGIVQALLHEPKLLILDEPTGGL 160
Cdd:cd03216 63 EVSFASPRD-----------------------ARRA------GIAmvyQLSVGERQMVEIARALARNARLLILDEPTAAL 113
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1021811607 161 DPLMQNTFFEILTEEREKGTTIIFSSHILSEVQKMCDRVAIIKEGELV 208
Cdd:cd03216 114 TPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-208 |
2.82e-32 |
|
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: 121.31 E-value: 2.82e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 3 IIDVKNLTKTYKKNRGIV----NLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNfLYP----TSGSATIFGKDIVKQSKE- 73
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVkavdGVSFDVRRGETLGLVGESGSGKSTLARAILG-LLPppgiTSGEILFDGEDLLKLSEKe 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 74 ---IR--------QN----------VGYLpsevhfyddmkVIDLLKYSAGFYKKFNQKRMKELAERLDLDLHKKIED--- 129
Cdd:COG0444 80 lrkIRgreiqmifQDpmtslnpvmtVGDQ-----------IAEPLRIHGGLSKAEARERAIELLERVGLPDPERRLDryp 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 130 --LSFGNRKKVGIVQALLHEPKLLILDEPTGGLDPLMQNTFFEILTE-EREKGTTIIFSSHILSEVQKMCDRVAIIKEGE 206
Cdd:COG0444 149 heLSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDlQRELGLAILFITHDLGVVAEIADRVAVMYAGR 228
|
..
gi 1021811607 207 LV 208
Cdd:COG0444 229 IV 230
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-208 |
2.91e-32 |
|
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: 118.93 E-value: 2.91e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 1 MKIIDVKNLTKTYKKNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQSKE--IRQNV 78
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHriARLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 79 GYLPSEVHFYDDMKVIDLLKysAGFYKKFNQKRMKELAER-LDL--DLHKKIE----DLSFGNRKKVGIVQALLHEPKLL 151
Cdd:COG0410 81 GYVPEGRRIFPSLTVEENLL--LGAYARRDRAEVRADLERvYELfpRLKERRRqragTLSGGEQQMLAIGRALMSRPKLL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1021811607 152 ILDEPTGGLDPLMQNTFFEILTEEREKGTTIIFSSHILSEVQKMCDRVAIIKEGELV 208
Cdd:COG0410 159 LLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIV 215
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-207 |
4.59e-32 |
|
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: 118.41 E-value: 4.59e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 4 IDVKNLTKTYKKNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQ--SKEIRQNVGYL 81
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLpmHKRARLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 82 PSEVHFYDDMKV---IDLLKYSAGFYKKFNQKRMKELAERLDLD--LHKKIEDLSFGNRKKVGIVQALLHEPKLLILDEP 156
Cdd:cd03218 81 PQEASIFRKLTVeenILAVLEIRGLSKKEREEKLEELLEEFHIThlRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1021811607 157 TGGLDPLMQNTFFEILTEEREKGTTIIFSSHILSEVQKMCDRVAIIKEGEL 207
Cdd:cd03218 161 FAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKV 211
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-208 |
1.73e-31 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 117.30 E-value: 1.73e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 1 MKIIDVKNLTKTYKKNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDI--VKQSKEIRQNV 78
Cdd:PRK10895 1 MATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDIslLPLHARARRGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 79 GYLPSEVHFYDDMKVIDLLKYSAGFYKKFNQKRMKELAERLDLDLH-KKIED-----LSFGNRKKVGIVQALLHEPKLLI 152
Cdd:PRK10895 81 GYLPQEASIFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHiEHLRDsmgqsLSGGERRRVEIARALAANPKFIL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1021811607 153 LDEPTGGLDPLMQNTFFEILTEEREKGTTIIFSSHILSEVQKMCDRVAIIKEGELV 208
Cdd:PRK10895 161 LDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLI 216
|
|
| PQQ_ABC_ATP |
TIGR03864 |
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of ... |
4-208 |
4.50e-31 |
|
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of this protein family are the ATP-binding subunit of an ABC transporter system that is associated with PQQ biosynthesis and PQQ-dependent alcohol dehydrogenases. While this family shows homology to several efflux ABC transporter subunits, the presence of a periplasmic substrate-binding protein and association with systems for catabolism of alcohols suggests a role in import rather than detoxification. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 274822 [Multi-domain] Cd Length: 236 Bit Score: 115.85 E-value: 4.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 4 IDVKNLTKTYKKNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQSKEIRQNVGylps 83
Cdd:TIGR03864 2 LEVAGLSFRYGARRALDDVSFTVRPGRFVALLGPNGAGKSTLFSLLTRLYVAQSGQISVAGHDLRRAPRAALARLG---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 84 eVHFYD-----DMKVIDLLKYSA---GFYKKFNQKRMKELAERLDLD--LHKKIEDLSFGNRKKVGIVQALLHEPKLLIL 153
Cdd:TIGR03864 78 -VVFQQptldlDLSVRQNLRYHAalhGLSRAEARARIAELLARLGLAerADDKVRELNGGHRRRVEIARALLHRPALLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1021811607 154 DEPTGGLDP---LMQNTFFEILTeeREKGTTIIFSSHILSEVQKMcDRVAIIKEGELV 208
Cdd:TIGR03864 157 DEPTVGLDPasrAAITAHVRALA--RDQGLSVLWATHLVDEIEAS-DRLVVLHRGRVL 211
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-217 |
4.66e-31 |
|
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: 121.06 E-value: 4.66e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 3 IIDVKNLTKTYKK-NRGIV----NLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATI-FGKDIVKQSK---- 72
Cdd:TIGR03269 279 IIKVRNVSKRYISvDRGVVkavdNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrVGDEWVDMTKpgpd 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 73 ---EIRQNVGYLPSEVHFYDDMKVIDLLKYSAGFYKKFNQKRMK------------ELAERLdldLHKKIEDLSFGNRKK 137
Cdd:TIGR03269 359 grgRAKRYIGILHQEYDLYPHRTVLDNLTEAIGLELPDELARMKavitlkmvgfdeEKAEEI---LDKYPDELSEGERHR 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 138 VGIVQALLHEPKLLILDEPTGGLDPLMQNTFFE-ILTEEREKGTTIIFSSHILSEVQKMCDRVAIIKEGELVKV----ET 212
Cdd:TIGR03269 436 VALAQVLIKEPRIVILDEPTGTMDPITKVDVTHsILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIgdpeEI 515
|
....*
gi 1021811607 213 IENLT 217
Cdd:TIGR03269 516 VEELT 520
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-212 |
4.86e-31 |
|
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: 115.80 E-value: 4.86e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 4 IDVKNLTKTYKKNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIV------KQSKEIRQN 77
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITnlpphkRPVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 78 VGYLPsevHfyddMKVIDLLKYS---AGFYKKFNQKRMKELAERLDLD--LHKKIEDLSFGNRKKVGIVQALLHEPKLLI 152
Cdd:cd03300 81 YALFP---H----LTVFENIAFGlrlKKLPKAEIKERVAEALDLVQLEgyANRKPSQLSGGQQQRVAIARALVNEPKVLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1021811607 153 LDEPTGGLD-PLMQNTFFEILTEEREKGTTIIFSSHILSEVQKMCDRVAIIKEGELVKVET 212
Cdd:cd03300 154 LDEPLGALDlKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGT 214
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-208 |
5.53e-31 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 115.36 E-value: 5.53e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 4 IDVKNLTKTYKKNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTL--LNFLY---PTSGSATIFGKDIVKQ-------- 70
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLnrLNDLIpgaPDEGEVLLDGKDIYDLdvdvlelr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 71 -------------SKEIRQNVGYLPSeVHFYDDMKVIDLLKYSAgfykkfnqKRMKELAERLDLDLHKKieDLSFGNRKK 137
Cdd:cd03260 81 rrvgmvfqkpnpfPGSIYDNVAYGLR-LHGIKLKEELDERVEEA--------LRKAALWDEVKDRLHAL--GLSGGQQQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1021811607 138 VGIVQALLHEPKLLILDEPTGGLDPLMQNTFFEILTEEREKgTTIIFSSHILSEVQKMCDRVAIIKEGELV 208
Cdd:cd03260 150 LCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLV 219
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
6-207 |
1.94e-30 |
|
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: 120.89 E-value: 1.94e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 6 VKNLTKTYKK-NRGIV---NLTFSveEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQSKEIRQNVGYL 81
Cdd:TIGR01257 931 VKNLVKIFEPsGRPAVdrlNITFY--ENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMC 1008
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 82 PSEVHFYDDMKVIDLLKYSAGFYKKFNQKRMKELAERL-DLDLHKK----IEDLSFGNRKKVGIVQALLHEPKLLILDEP 156
Cdd:TIGR01257 1009 PQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLeDTGLHHKrneeAQDLSGGMQRKLSVAIAFVGDAKVVVLDEP 1088
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1021811607 157 TGGLDPLMQNTFFEILTEEREkGTTIIFSSHILSEVQKMCDRVAIIKEGEL 207
Cdd:TIGR01257 1089 TSGVDPYSRRSIWDLLLKYRS-GRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
4-220 |
2.65e-30 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 119.94 E-value: 2.65e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 4 IDVKNLTKTYKKNRGIV--NLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIvKQ--SKEIRQNVG 79
Cdd:COG2274 474 IELENVSFRYPGDSPPVldNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDL-RQidPASLRRQIG 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 80 YLPSEVHFY---------------DDMKVIDLLKySAGFYkkfnqkrmkELAERLDLDLHKKIED----LSFGNRKKVGI 140
Cdd:COG2274 553 VVLQDVFLFsgtirenitlgdpdaTDEEIIEAAR-LAGLH---------DFIEALPMGYDTVVGEggsnLSGGQRQRLAI 622
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 141 VQALLHEPKLLILDEPTGGLDPLMQNTFFEILtEEREKGTTIIFSSHILSEVqKMCDRVAIIKEGELVKVETIENLTKNN 220
Cdd:COG2274 623 ARALLRNPRILILDEATSALDAETEAIILENL-RRLLKGRTVIIIAHRLSTI-RLADRIIVLDKGRIVEDGTHEELLARK 700
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
4-208 |
3.24e-30 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 113.96 E-value: 3.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 4 IDVKNLTKTYKKNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLlNFL-YPTSGSATI------FGKDI-VKQSKEIR 75
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVL-NLLeMPRSGTLNIagnhfdFSKTPsDKAIRELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 76 QNVGYLPSEVHFYDDMKVIDLLKYS----AGFYKKFNQKRMKELAERLDLD-------LHkkiedLSFGNRKKVGIVQAL 144
Cdd:PRK11124 82 RNVGMVFQQYNLWPHLTVQQNLIEApcrvLGLSKDQALARAEKLLERLRLKpyadrfpLH-----LSGGQQQRVAIARAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1021811607 145 LHEPKLLILDEPTGGLDPLMQNTFFEILTEEREKGTTIIFSSHILSEVQKMCDRVAIIKEGELV 208
Cdd:PRK11124 157 MMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIV 220
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-210 |
7.41e-30 |
|
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: 111.96 E-value: 7.41e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 4 IDVKNLTKTYKKNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQSKEIRqNVGYLPS 83
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDR-DIAMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 84 EVHFYDDMKVIDLLKY---SAGFYKKFNQKRMKELAERLDLD--LHKKIEDLSFGNRKKVGIVQALLHEPKLLILDEPTG 158
Cdd:cd03301 80 NYALYPHMTVYDNIAFglkLRKVPKDEIDERVREVAELLQIEhlLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1021811607 159 GLDPLMQntfFEILTE----EREKGTTIIFSSHILSEVQKMCDRVAIIKEGELVKV 210
Cdd:cd03301 160 NLDAKLR---VQMRAElkrlQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQI 212
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
3-208 |
4.03e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 111.75 E-value: 4.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 3 IIDVKNLTKTYKK-NRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQS-KEIRQNVGY 80
Cdd:PRK13647 4 IIEVEDLHFRYKDgTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENeKWVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 81 LpsevhFYD-DMKVIDLLKYSAGFYKKFNQK-RMKELAERLDLDL---------HKKIEDLSFGNRKKVGIVQALLHEPK 149
Cdd:PRK13647 84 V-----FQDpDDQVFSSTVWDDVAFGPVNMGlDKDEVERRVEEALkavrmwdfrDKPPYHLSYGQKKRVAIAGVLAMDPD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1021811607 150 LLILDEPTGGLDPLMQNTFFEILTEEREKGTTIIFSSHILSEVQKMCDRVAIIKEGELV 208
Cdd:PRK13647 159 VIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVL 217
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
4-208 |
5.55e-29 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 112.97 E-value: 5.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 4 IDVKNLTKTYKKNRGIV----NLTFSVEEGEIFGFIGPNGAGKSTTIRtLLNFL-YPTSGSATIFGKDIVKQSK----EI 74
Cdd:PRK11153 2 IELKNISKVFPQGGRTIhalnNVSLHIPAGEIFGVIGASGAGKSTLIR-CINLLeRPTSGRVLVDGQDLTALSEkelrKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 75 RQNVGYLPSevHFYddmkvidLLkyS--------------AGFYKKFNQKRMKELAERLDL-DLHKKI-EDLSFGNRKKV 138
Cdd:PRK11153 81 RRQIGMIFQ--HFN-------LL--SsrtvfdnvalplelAGTPKAEIKARVTELLELVGLsDKADRYpAQLSGGQKQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1021811607 139 GIVQALLHEPKLLILDEPTGGLDPLMQNTFFEILTE-EREKGTTIIFSSHILSEVQKMCDRVAIIKEGELV 208
Cdd:PRK11153 150 AIARALASNPKVLLCDEATSALDPATTRSILELLKDiNRELGLTIVLITHEMDVVKRICDRVAVIDAGRLV 220
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
4-220 |
7.81e-29 |
|
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: 115.25 E-value: 7.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 4 IDVKNLTKTYKKNRGIV--NLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQS-KEIRQNVGY 80
Cdd:COG4987 334 LELEDVSFRYPGAGRPVldGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDeDDLRRRIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 81 LPSEVHFYD---------------DMKVIDLLKysagfykkfnQKRMKELAERLDLDLHKKIED----LSFGNRKKVGIV 141
Cdd:COG4987 414 VPQRPHLFDttlrenlrlarpdatDEELWAALE----------RVGLGDWLAALPDGLDTWLGEggrrLSGGERRRLALA 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1021811607 142 QALLHEPKLLILDEPTGGLDPLMQNTFFEILtEEREKGTTIIFSSHILSEVQKMcDRVAIIKEGELVKVETIENLTKNN 220
Cdd:COG4987 484 RALLRDAPILLLDEPTEGLDAATEQALLADL-LEALAGRTVLLITHRLAGLERM-DRILVLEDGRIVEQGTHEELLAQN 560
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
4-208 |
1.03e-28 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 109.72 E-value: 1.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 4 IDVKNLTKTYKKNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLlNFL-YPTSGSATIFGKDI-------VKQSKEIR 75
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVL-NLLeTPDSGQLNIAGHQFdfsqkpsEKAIRLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 76 QNVGYLPSEVHFYDDMKVIDLLKYS----AGFYKKFNQKRMKELAERLDLD-------LHkkiedLSFGNRKKVGIVQAL 144
Cdd:COG4161 82 QKVGMVFQQYNLWPHLTVMENLIEApckvLGLSKEQAREKAMKLLARLRLTdkadrfpLH-----LSGGQQQRVAIARAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1021811607 145 LHEPKLLILDEPTGGLDPLMQNTFFEILTEEREKGTTIIFSSHILSEVQKMCDRVAIIKEGELV 208
Cdd:COG4161 157 MMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRII 220
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-207 |
3.17e-28 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 108.58 E-value: 3.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 1 MKIIDVKNLTKTYKKnRGIVN-LTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQS--KEIRQN 77
Cdd:COG1137 1 MMTLEAENLVKSYGK-RTVVKdVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPmhKRARLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 78 VGYLPSEVHFYDDMKVID-------LLKYSagfyKKFNQKRMKELAERLDLD--LHKKIEDLSFGNRKKVGIVQALLHEP 148
Cdd:COG1137 80 IGYLPQEASIFRKLTVEDnilavleLRKLS----KKEREERLEELLEEFGIThlRKSKAYSLSGGERRRVEIARALATNP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1021811607 149 KLLILDEPTGGLDPL----MQntffEILTEEREKGTTIIFSSHILSEVQKMCDRVAIIKEGEL 207
Cdd:COG1137 156 KFILLDEPFAGVDPIavadIQ----KIIRHLKERGIGVLITDHNVRETLGICDRAYIISEGKV 214
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
4-220 |
4.49e-28 |
|
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: 112.93 E-value: 4.49e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 4 IDVKNLTKTYKKNRGIV-NLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQSKE-IRQNVGYL 81
Cdd:COG4988 337 IELEDVSFSYPGGRPALdGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPAsWRRQIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 82 PSEVHFY---------------DDMKVIDLLKySAGFYkkfnqkrmkELAERLDLDLHKKIED----LSFGNRKKVGIVQ 142
Cdd:COG4988 417 PQNPYLFagtirenlrlgrpdaSDEELEAALE-AAGLD---------EFVAALPDGLDTPLGEggrgLSGGQAQRLALAR 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 143 ALLHEPKLLILDEPTGGLDPlmqNTFFEILTEERE--KGTTIIFSSHILSEVQKMcDRVAIIKEGELVKVETIENLTKNN 220
Cdd:COG4988 487 ALLRDAPLLLLDEPTAHLDA---ETEAEILQALRRlaKGRTVILITHRLALLAQA-DRILVLDDGRIVEQGTHEELLAKN 562
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-207 |
8.54e-28 |
|
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: 106.85 E-value: 8.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 4 IDVKNLTKTYKKNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLlNFL-YPTSGSATIFGKDIVKQSK---EIRQNVG 79
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCI-NLLeEPDSGTIIIDGLKLTDDKKninELRQKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 80 YLPSEVHFYDDMKVIDLLKYSAGFYKKFNQKRMKELAERLdLDL-------HKKIEDLSFGNRKKVGIVQALLHEPKLLI 152
Cdd:cd03262 80 MVFQQFNLFPHLTVLENITLAPIKVKGMSKAEAEERALEL-LEKvgladkaDAYPAQLSGGQQQRVAIARALAMNPKVML 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1021811607 153 LDEPTGGLDPLMQNTFFEILTEEREKGTTIIFSSHILSEVQKMCDRVAIIKEGEL 207
Cdd:cd03262 159 FDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
4-208 |
1.18e-27 |
|
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: 106.52 E-value: 1.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 4 IDVKNLTKTYK--KNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIvKQ--SKEIRQNVG 79
Cdd:cd03245 3 IEFRNVSFSYPnqEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDI-RQldPADLRRNIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 80 YLPSEVH-FYDDMKviDLLKYSAGFYkkfNQKRMKELAER-------------LDLDLHKKIEDLSFGNRKKVGIVQALL 145
Cdd:cd03245 82 YVPQDVTlFYGTLR--DNITLGAPLA---DDERILRAAELagvtdfvnkhpngLDLQIGERGRGLSGGQRQAVALARALL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1021811607 146 HEPKLLILDEPTGGLDPLMQNTFFEILTEEREkGTTIIFSSHILSEVQkMCDRVAIIKEGELV 208
Cdd:cd03245 157 NDPPILLLDEPTSAMDMNSEERLKERLRQLLG-DKTLIIITHRPSLLD-LVDRIIVMDSGRIV 217
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
4-207 |
1.44e-27 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 105.95 E-value: 1.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 4 IDVKNLTKTYKKN-RGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIV----KQSKEIRQNV 78
Cdd:cd03292 1 IEFINVTKTYPNGtAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSdlrgRAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 79 GYLPSEVHFYDDMKVIDLLKYS---AGFYKKFNQKRMKELAERLDLDlHKK---IEDLSFGNRKKVGIVQALLHEPKLLI 152
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFAlevTGVPPREIRKRVPAALELVGLS-HKHralPAELSGGEQQRVAIARAIVNSPTILI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1021811607 153 LDEPTGGLDPLMQNTFFEILTEEREKGTTIIFSSHILSEVQKMCDRVAIIKEGEL 207
Cdd:cd03292 160 ADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3-207 |
2.51e-27 |
|
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: 104.44 E-value: 2.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 3 IIDVKNLTKTYKKNrgivNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQSKE--IRQNVGY 80
Cdd:cd03215 4 VLEVRGLSVKGAVR----DVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRdaIRAGIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 81 LPSEvhfyddmkvidllkysagfykkfnqkRMKE-------LAERLDLDLHkkiedLSFGNRKKVGIVQALLHEPKLLIL 153
Cdd:cd03215 80 VPED--------------------------RKREglvldlsVAENIALSSL-----LSGGNQQKVVLARWLARDPRVLIL 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1021811607 154 DEPTGGLDPLMQNTFFEILTEEREKGTTIIFSSHILSEVQKMCDRVAIIKEGEL 207
Cdd:cd03215 129 DEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
22-187 |
3.19e-27 |
|
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: 104.43 E-value: 3.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 22 LTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQSK---EIRQNVGYL---PSEVHFYDDM-KVI 94
Cdd:TIGR01166 11 LNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDYSRKgllERRQRVGLVfqdPDDQLFAADVdQDV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 95 DLLKYSAGFYKKFNQKRMKELAERLDLD--LHKKIEDLSFGNRKKVGIVQALLHEPKLLILDEPTGGLDPLMQNTFFEIL 172
Cdd:TIGR01166 91 AFGPLNLGLSEAEVERRVREALTAVGASglRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPAGREQMLAIL 170
|
170
....*....|....*
gi 1021811607 173 TEEREKGTTIIFSSH 187
Cdd:TIGR01166 171 RRLRAEGMTVVISTH 185
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
4-208 |
6.48e-27 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 103.78 E-value: 6.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 4 IDVKNLTKTYKKNRG------IVNLTFSVEEGEIFGFIGPNGAGKSTtirtLLNFL------YPTSGSATIFGKDIVKQS 71
Cdd:cd03213 4 LSFRNLTVTVKSSPSksgkqlLKNVSGKAKPGELTAIMGPSGAGKST----LLNALagrrtgLGVSGEVLINGRPLDKRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 72 keIRQNVGYLPSEVHFYDDMKVIDLLKYSAgfykkfnqkrmkelaerldldlhkKIEDLSFGNRKKVGIVQALLHEPKLL 151
Cdd:cd03213 80 --FRKIIGYVPQDDILHPTLTVRETLMFAA------------------------KLRGLSGGERKRVSIALELVSNPSLL 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1021811607 152 ILDEPTGGLDPLMQNTFFEILTEEREKGTTIIFSSHILS-EVQKMCDRVAIIKEGELV 208
Cdd:cd03213 134 FLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQPSsEIFELFDKLLLLSQGRVI 191
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
3-209 |
8.22e-27 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 105.27 E-value: 8.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 3 IIDVKNLTKTY-------KKNRGIV--NLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVK---- 69
Cdd:TIGR02769 2 LLEVRDVTHTYrtgglfgAKQRAPVltNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQldrk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 70 QSKEIRQNVGYL----PSEVHFYDDMKVI--DLLKYSAGFYKKFNQKRMKELAERLDL---DLHKKIEDLSFGNRKKVGI 140
Cdd:TIGR02769 82 QRRAFRRDVQLVfqdsPSAVNPRMTVRQIigEPLRHLTSLDESEQKARIAELLDMVGLrseDADKLPRQLSGGQLQRINI 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 141 VQALLHEPKLLILDEPTGGLDPLMQNTFFEILTEEREK-GTTIIFSSHILSEVQKMCDRVAIIKEGELVK 209
Cdd:TIGR02769 162 ARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAfGTAYLFITHDLRLVQSFCQRVAVMDKGQIVE 231
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
4-219 |
9.55e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 105.90 E-value: 9.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 4 IDVKNLTKTYKKN-----RGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQS---KEIR 75
Cdd:PRK13637 3 IKIENLTHIYMEGtpfekKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKvklSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 76 QNVGYL---PSEVHFYDDM-KVIDLLKYSAGFYKKFNQKRMKELAERLDLDLHKKIE----DLSFGNRKKVGIVQALLHE 147
Cdd:PRK13637 83 KKVGLVfqyPEYQLFEETIeKDIAFGPINLGLSEEEIENRVKRAMNIVGLDYEDYKDkspfELSGGQKRRVAIAGVVAME 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1021811607 148 PKLLILDEPTGGLDPL-MQNTFFEILTEEREKGTTIIFSSHILSEVQKMCDRVAIIKEGELVKVETIENLTKN 219
Cdd:PRK13637 163 PKILILDEPTAGLDPKgRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKE 235
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
3-288 |
9.72e-27 |
|
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: 110.10 E-value: 9.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 3 IIDVKNLTKTYK--KNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQSKEIRQNVGY 80
Cdd:TIGR01257 1937 ILRLNELTKVYSgtSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNMGY 2016
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 81 LPSevhfYDdmKVIDLLKYSAGFY-----KKFNQKRMKELA----ERLDLDLH--KKIEDLSFGNRKKVGIVQALLHEPK 149
Cdd:TIGR01257 2017 CPQ----FD--AIDDLLTGREHLYlyarlRGVPAEEIEKVAnwsiQSLGLSLYadRLAGTYSGGNKRKLSTAIALIGCPP 2090
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 150 LLILDEPTGGLDP----LMQNTFFEILTEERekgtTIIFSSHILSEVQKMCDRVAIIKEGELVKVETIENLTKNNLKNIT 225
Cdd:TIGR01257 2091 LVLLDEPTTGMDPqarrMLWNTIVSIIREGR----AVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSKFGDGYI 2166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 226 ITFEQTNAIDfDL---------------EGIVKKEINGSEMMLLYSGDIKTLLNQLNTMPVQDLLIEEPS-----LEEVF 285
Cdd:TIGR01257 2167 VTMKIKSPKD-DLlpdlnpveqffqgnfPGSVQRERHYNMLQFQVSSSSLARIFQLLISHKDSLLIEEYSvtqttLDQVF 2245
|
...
gi 1021811607 286 IHY 288
Cdd:TIGR01257 2246 VNF 2248
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
3-208 |
1.16e-26 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 104.71 E-value: 1.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 3 IIDVKNLTKTYKKNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQS-KEIRQNVGYL 81
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSsRQLARRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 82 PSEVHFYDDMKVIDLLKYSAGFY----------------KKFNQKRMKELAERldldlhkKIEDLSFGNRKKVGIVQALL 145
Cdd:PRK11231 82 PQHHLTPEGITVRELVAYGRSPWlslwgrlsaednarvnQAMEQTRINHLADR-------RLTDLSGGQRQRAFLAMVLA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1021811607 146 HEPKLLILDEPTGGLDPLMQNTFFEILTEEREKGTTIIFSSHILSEVQKMCDRVAIIKEGELV 208
Cdd:PRK11231 155 QDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVM 217
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
5-208 |
3.02e-26 |
|
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: 102.34 E-value: 3.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 5 DVKNLTKTYKKNRGIV-NLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIvkQSKEIRQNVGYLPS 83
Cdd:cd03226 1 RIENISFSYKKGTEILdDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI--KAKERRKSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 84 EV--HFYDDmKVIDLLKYSAGFYKKFNQKRMKELAerlDLDLHKKIE----DLSFGNRKKVGIVQALLHEPKLLILDEPT 157
Cdd:cd03226 79 DVdyQLFTD-SVREELLLGLKELDAGNEQAETVLK---DLDLYALKErhplSLSGGQKQRLAIAAALLSGKDLLIFDEPT 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1021811607 158 GGLDPLMQNTFFEILTEEREKGTTIIFSSHILSEVQKMCDRVAIIKEGELV 208
Cdd:cd03226 155 SGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-221 |
3.60e-26 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 107.03 E-value: 3.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 3 IIDVKNLTKtykkNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQS--KEIRQNVGY 80
Cdd:COG1129 256 VLEVEGLSV----GGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSprDAIRAGIAY 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 81 LPSevhfyD--------DMKVID------LLKYSAGFYkkFNQKRMKELAE----RLDL---DLHKKIEDLSFGNRKKVG 139
Cdd:COG1129 332 VPE-----DrkgeglvlDLSIREnitlasLDRLSRGGL--LDRRRERALAEeyikRLRIktpSPEQPVGNLSGGNQQKVV 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 140 IVQALLHEPKLLILDEPTGGLDPLMQNTFFEILTEEREKGTTIIFSSHILSEVQKMCDRVAIIKEGELVKVETIENLTKN 219
Cdd:COG1129 405 LAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIVGELDREEATEE 484
|
..
gi 1021811607 220 NL 221
Cdd:COG1129 485 AI 486
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
4-207 |
4.96e-26 |
|
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: 100.75 E-value: 4.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 4 IDVKNLTKTYKKNRGIV--NLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQ-SKEIRQNVGY 80
Cdd:cd03246 1 LEVENVSFRYPGAEPPVlrNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWdPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 81 LPSEVHFYDDmkvidllkysagfykkfnqkrmkELAERLdldlhkkiedLSFGNRKKVGIVQALLHEPKLLILDEPTGGL 160
Cdd:cd03246 81 LPQDDELFSG-----------------------SIAENI----------LSGGQRQRLGLARALYGNPRILVLDEPNSHL 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1021811607 161 DPLMQNTFFEILTEEREKGTTIIFSSHILsEVQKMCDRVAIIKEGEL 207
Cdd:cd03246 128 DVEGERALNQAIAALKAAGATRIVIAHRP-ETLASADRILVLEDGRV 173
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-219 |
5.99e-26 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 102.65 E-value: 5.99e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 1 MKIIDVKNLTKTYKKNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIV--KQSKEIRQNV 78
Cdd:PRK11614 3 KVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITdwQTAKIMREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 79 GYLPSEVHFYDDMKVIDLLKYsAGFYKKFNQ-----KRMKELAERLDLDLHKKIEDLSFGNRKKVGIVQALLHEPKLLIL 153
Cdd:PRK11614 83 AIVPEGRRVFSRMTVEENLAM-GGFFAERDQfqeriKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1021811607 154 DEPTGGLDPLMQNTFFEILTEEREKGTTIIFSSHILSEVQKMCDRVAIIKEGELVKVETIENLTKN 219
Cdd:PRK11614 162 DEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLAN 227
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
2-221 |
1.03e-25 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 106.02 E-value: 1.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 2 KIIDVKNLTKTYKKNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQSKEIRQNVGYl 81
Cdd:PRK09700 4 PYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLGI- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 82 pseVHFYDDMKVIDLLKYSAGFY------KKF------NQKRMKELAE----RLDL--DLHKKIEDLSFGNRKKVGIVQA 143
Cdd:PRK09700 83 ---GIIYQELSVIDELTVLENLYigrhltKKVcgvniiDWREMRVRAAmmllRVGLkvDLDEKVANLSISHKQMLEIAKT 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1021811607 144 LLHEPKLLILDEPTGGLDPLMQNTFFEILTEEREKGTTIIFSSHILSEVQKMCDRVAIIKEGELVKVETIENLTKNNL 221
Cdd:PRK09700 160 LMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSNDDI 237
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
3-222 |
1.49e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 102.46 E-value: 1.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 3 IIDVKNLTKTYKKNRGIVN-LTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQSK---EIRQNV 78
Cdd:PRK13639 1 ILETRDLKYSYPDGTEALKgINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKsllEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 79 GYL---PSEVHFYDDMKV-IDLLKYSAGFYKKFNQKRMKELAERLDLD--LHKKIEDLSFGNRKKVGIVQALLHEPKLLI 152
Cdd:PRK13639 81 GIVfqnPDDQLFAPTVEEdVAFGPLNLGLSKEEVEKRVKEALKAVGMEgfENKPPHHLSGGQKKRVAIAGILAMKPEIIV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1021811607 153 LDEPTGGLDPLMQNTFFEILTEEREKGTTIIFSSHILSEVQKMCDRVAIIKEGELVKVET-------IENLTKNNLK 222
Cdd:PRK13639 161 LDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTpkevfsdIETIRKANLR 237
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-216 |
1.65e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 102.19 E-value: 1.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 1 MKIIDVKNLTKTYKKNRGIV-NLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQS-KEIRQNV 78
Cdd:PRK13652 1 MHLIETRDLCYSYSGSKEALnNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENiREVRKFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 79 GYL---PSEVHFYDDMKV-IDLLKYSAGFYKKFNQKRMKELAERLDL-DLHKKI-EDLSFGNRKKVGIVQALLHEPKLLI 152
Cdd:PRK13652 81 GLVfqnPDDQIFSPTVEQdIAFGPINLGLDEETVAHRVSSALHMLGLeELRDRVpHHLSGGEKKRVAIAGVIAMEPQVLV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1021811607 153 LDEPTGGLDPLMQNTFFEILTEEREK-GTTIIFSSHILSEVQKMCDRVAIIKEGELVKVETIENL 216
Cdd:PRK13652 161 LDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
8-221 |
2.06e-25 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 104.99 E-value: 2.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 8 NLTKTYKKNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQS--KEIRQNVGYLPSEV 85
Cdd:PRK11288 9 GIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASttAALAAGVAIIYQEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 86 HFYDDMKVID-----LLKYSAGFykkFNQKRMKELA----ERL--DLDLHKKIEDLSFGNRKKVGIVQALLHEPKLLILD 154
Cdd:PRK11288 89 HLVPEMTVAEnlylgQLPHKGGI---VNRRLLNYEAreqlEHLgvDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1021811607 155 EPTGGLDPLMQNTFFEILTEEREKGTTIIFSSHILSEVQKMCDRVAIIKEGELVKV-ETIENLTKNNL 221
Cdd:PRK11288 166 EPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVATfDDMAQVDRDQL 233
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-221 |
3.54e-25 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 104.36 E-value: 3.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 3 IIDVKNLTKTYKKNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQSKEIRQNVG-YL 81
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLGiYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 82 -PSEVHFYDDMKVID-----LLKYSAgfykkfNQKRMKELAERLD--LDLHKKIEDLSFGNRKKVGIVQALLHEPKLLIL 153
Cdd:PRK15439 91 vPQEPLLFPNLSVKEnilfgLPKRQA------SMQKMKQLLAALGcqLDLDSSAGSLEVADRQIVEILRGLMRDSRILIL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1021811607 154 DEPTGGLDPLMQNTFFEILTEEREKGTTIIFSSHILSEVQKMCDRVAIIKEGELVKVETIENLTKNNL 221
Cdd:PRK15439 165 DEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTDDI 232
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
3-208 |
5.11e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 101.08 E-value: 5.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 3 IIDVKNLTKTYKKNRGIVN-LTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQSK---EIRQNV 78
Cdd:PRK13636 5 ILKVEELNYNYSDGTHALKgININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKglmKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 79 GYL---PSEVHF----YDDmkvIDLLKYSAGFYKKFNQKRMKELAERLDLD--LHKKIEDLSFGNRKKVGIVQALLHEPK 149
Cdd:PRK13636 85 GMVfqdPDNQLFsasvYQD---VSFGAVNLKLPEDEVRKRVDNALKRTGIEhlKDKPTHCLSFGQKKRVAIAGVLVMEPK 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 150 LLILDEPTGGLDPLMQNTFFEILTE-EREKGTTIIFSSHILSEVQKMCDRVAIIKEGELV 208
Cdd:PRK13636 162 VLVLDEPTAGLDPMGVSEIMKLLVEmQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVI 221
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1-209 |
7.66e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 100.93 E-value: 7.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 1 MKIIdVKNLTKTYKKN-----RGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDI-------- 67
Cdd:PRK13651 1 MQIK-VKNIVKIFNKKlptelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEknkkktke 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 68 -----------------VKQSKEIRQNVG--YLPSEVHFYDDM--KVIDLLKYSAGFYKKFNQKRMKELAERLDLD---L 123
Cdd:PRK13651 80 kekvleklviqktrfkkIKKIKEIRRRVGvvFQFAEYQLFEQTieKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDesyL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 124 HKKIEDLSFGNRKKVGIVQALLHEPKLLILDEPTGGLDPLMQNTFFEILTEEREKGTTIIFSSHILSEVQKMCDRVAIIK 203
Cdd:PRK13651 160 QRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFK 239
|
....*.
gi 1021811607 204 EGELVK 209
Cdd:PRK13651 240 DGKIIK 245
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
4-208 |
1.09e-24 |
|
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: 97.38 E-value: 1.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 4 IDVKNLTKTYKKNRGIV--NLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQSKEIRQNVGYL 81
Cdd:cd03247 1 LSINNVSFSYPEQEQQVlkNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 82 PSEVHFYDDmkvidllkysagfykkfnqKRMKELAERLdldlhkkiedlSFGNRKKVGIVQALLHEPKLLILDEPTGGLD 161
Cdd:cd03247 81 NQRPYLFDT-------------------TLRNNLGRRF-----------SGGERQRLALARILLQDAPIVLLDEPTVGLD 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1021811607 162 PLMQ----NTFFEILteereKGTTIIFSSHILSEVQKMcDRVAIIKEGELV 208
Cdd:cd03247 131 PITErqllSLIFEVL-----KDKTLIWITHHLTGIEHM-DKILFLENGKII 175
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
14-208 |
1.32e-24 |
|
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: 98.50 E-value: 1.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 14 KKNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFL---YPTSGSATIFGKDIVKQskEIRQNVGYLPSEVHFYDD 90
Cdd:cd03234 18 KYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVeggGTTSGQILFNGQPRKPD--QFQKCVAYVRQDDILLPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 91 MKVIDLLKYSAGF--YKKFNQKRMKELAERLDLDL-------HKKIEDLSFGNRKKVGIVQALLHEPKLLILDEPTGGLD 161
Cdd:cd03234 96 LTVRETLTYTAILrlPRKSSDAIRKKRVEDVLLRDlaltrigGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1021811607 162 PLMQNTFFEILTEEREKGTTIIFSSHI-LSEVQKMCDRVAIIKEGELV 208
Cdd:cd03234 176 SFTALNLVSTLSQLARRNRIVILTIHQpRSDLFRLFDRILLLSSGEIV 223
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
18-248 |
1.95e-24 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 101.65 E-value: 1.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 18 GIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQS----KEI-RQNVGYLPSEVHFYDDMK 92
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISdaelREVrRKKIAMVFQSFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 93 VIDLLKYS---AGFYKKFNQKRMKELAERLDLD--LHKKIEDLSFGNRKKVGIVQALLHEPKLLILDEPTGGLDPLMQNT 167
Cdd:PRK10070 123 VLDNTAFGmelAGINAEERREKALDALRQVGLEnyAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 168 FFEILTEEREKGT-TIIFSSHILSEVQKMCDRVAIIKEGELVKVETIENLTKNNLKNITITFEQTNAID--FDLEGIVKK 244
Cdd:PRK10070 203 MQDELVKLQAKHQrTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGVDISqvFSAKDIARR 282
|
....
gi 1021811607 245 EING 248
Cdd:PRK10070 283 TPNG 286
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
4-222 |
2.27e-24 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 99.19 E-value: 2.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 4 IDVKNLTKTYKK-NRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIvkqSKEIRQN-VGYL 81
Cdd:PRK15056 7 IVVNDVTVTWRNgHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPT---RQALQKNlVAYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 82 PS--EVHFYDDMKVIDLL---KYS-AGFY---KKFNQKRMKELAERLD-LDL-HKKIEDLSFGNRKKVGIVQALLHEPKL 150
Cdd:PRK15056 84 PQseEVDWSFPVLVEDVVmmgRYGhMGWLrraKKRDRQIVTAALARVDmVEFrHRQIGELSGGQKKRVFLARAIAQQGQV 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1021811607 151 LILDEPTGGLDPLMQNTFFEILTEEREKGTTIIFSSHILSEVQKMCDRVAIIKEGELVKVETIENLTKNNLK 222
Cdd:PRK15056 164 ILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGPTETTFTAENLE 235
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-205 |
8.06e-24 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 98.64 E-value: 8.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 1 MKIIDVKNLTKTYKKNRGIV----NLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYP---TSGSATIFGKDIV----K 69
Cdd:PRK09473 10 DALLDVKDLRVTFSTPDGDVtavnDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREILnlpeK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 70 QSKEIR-QNVGYLpsevhFYDDM-------KVIDLLKYSAGFYKKFNQK-------------RMKELAERLDLDLHkkie 128
Cdd:PRK09473 90 ELNKLRaEQISMI-----FQDPMtslnpymRVGEQLMEVLMLHKGMSKAeafeesvrmldavKMPEARKRMKMYPH---- 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1021811607 129 DLSFGNRKKVGIVQALLHEPKLLILDEPTGGLDPLMQNTFFEILTE-EREKGTTIIFSSHILSEVQKMCDRVAIIKEG 205
Cdd:PRK09473 161 EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNElKREFNTAIIMITHDLGVVAGICDKVLVMYAG 238
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-218 |
9.37e-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: 9.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 3 IIDVKNLTktYKKNRGIV---NLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQS-KEIRQN- 77
Cdd:COG3845 257 VLEVENLS--VRDDRGVPalkDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSpRERRRLg 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 78 VGYLPSEVHFY---DDMKVID--LLK--YSAGFYKKF--NQKRMKELAERL----DL---DLHKKIEDLSFGNRKKVGIV 141
Cdd:COG3845 335 VAYIPEDRLGRglvPDMSVAEnlILGryRRPPFSRGGflDRKAIRAFAEELieefDVrtpGPDTPARSLSGGNQQKVILA 414
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1021811607 142 QALLHEPKLLILDEPTGGLDPLMQNTFFEILTEEREKGTTIIFSSHILSEVQKMCDRVAIIKEGELVKVETIENLTK 218
Cdd:COG3845 415 RELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRIVGEVPAAEATR 491
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
3-210 |
1.29e-23 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 98.75 E-value: 1.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 3 IIDVKNLTKTYKKNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDI--------------- 67
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLshvppyqrpinmmfq 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 68 -----------------VKQSK----EIRQNVGYLPSEVHfyddmkvidllkysagfykkfnqkrMKELAERldldlhkK 126
Cdd:PRK11607 99 syalfphmtveqniafgLKQDKlpkaEIASRVNEMLGLVH-------------------------MQEFAKR-------K 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 127 IEDLSFGNRKKVGIVQALLHEPKLLILDEPTGGLDP----LMQNTFFEILteEReKGTTIIFSSHILSEVQKMCDRVAII 202
Cdd:PRK11607 147 PHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKklrdRMQLEVVDIL--ER-VGVTCVMVTHDQEEAMTMAGRIAIM 223
|
....*...
gi 1021811607 203 KEGELVKV 210
Cdd:PRK11607 224 NRGKFVQI 231
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
4-219 |
1.30e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 97.21 E-value: 1.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 4 IDVKNLTKTYK-----KNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQS-----KE 73
Cdd:PRK13641 3 IKFENVDYIYSpgtpmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETgnknlKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 74 IRQNVG--YLPSEVHFYDD--MKVIDLLKYSAGFYKKFNQKRMKELAERLDLD---LHKKIEDLSFGNRKKVGIVQALLH 146
Cdd:PRK13641 83 LRKKVSlvFQFPEAQLFENtvLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSedlISKSPFELSGGQMRRVAIAGVMAY 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1021811607 147 EPKLLILDEPTGGLDPLMQNTFFEILTEEREKGTTIIFSSHILSEVQKMCDRVAIIKEGELVKVETIENLTKN 219
Cdd:PRK13641 163 EPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSD 235
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
21-219 |
2.67e-23 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 99.41 E-value: 2.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 21 NLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQ-------------------SKEIRQNVGYl 81
Cdd:TIGR00958 499 GLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYdhhylhrqvalvgqepvlfSGSVRENIAY- 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 82 psEVHFYDDMKVIDLLKysAGFYKKFnqkrMKELAERLDLDLHKKIEDLSFGNRKKVGIVQALLHEPKLLILDEPTGGLD 161
Cdd:TIGR00958 578 --GLTDTPDEEIMAAAK--AANAHDF----IMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALD 649
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1021811607 162 PLMQNTFFEiltEEREKGTTIIFSSHILSEVQKmCDRVAIIKEGELVKVETIENLTKN 219
Cdd:TIGR00958 650 AECEQLLQE---SRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMED 703
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
4-208 |
6.95e-23 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 97.93 E-value: 6.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 4 IDVKNLTKTYKKNRGIV-NLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDI--VKQsKEIRQNVGY 80
Cdd:COG1132 340 IEFENVSFSYPGDRPVLkDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIrdLTL-ESLRRQIGV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 81 LPSEVH-F--------------YDDMKVIDLLKySAGFYkkfnqkrmkELAERLDLDLHKKIED----LSFGNRKKVGIV 141
Cdd:COG1132 419 VPQDTFlFsgtirenirygrpdATDEEVEEAAK-AAQAH---------EFIEALPDGYDTVVGErgvnLSGGQRQRIAIA 488
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1021811607 142 QALLHEPKLLILDEPTGGLDP----LMQNTFFEILteereKGTTIIFSSHILSEVqKMCDRVAIIKEGELV 208
Cdd:COG1132 489 RALLKDPPILILDEATSALDTeteaLIQEALERLM-----KGRTTIVIAHRLSTI-RNADRILVLDDGRIV 553
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-161 |
1.11e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 97.44 E-value: 1.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 6 VKNLTKTYKKNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIfgkdivkqSKEIRqnVGYLPSEV 85
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI--------PKGLR--IGYLPQEP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 86 HFYDDMKVID-----------LLK-----YSAGFYKKFNQKRMKELAERLD----------------------LDLHKKI 127
Cdd:COG0488 71 PLDDDLTVLDtvldgdaelraLEAeleelEAKLAEPDEDLERLAELQEEFEalggweaearaeeilsglgfpeEDLDRPV 150
|
170 180 190
....*....|....*....|....*....|....
gi 1021811607 128 EDLSFGNRKKVGIVQALLHEPKLLILDEPTGGLD 161
Cdd:COG0488 151 SELSGGWRRRVALARALLSEPDLLLLDEPTNHLD 184
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
4-209 |
1.15e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 94.43 E-value: 1.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 4 IDVKNLTKTYK-----KNRGIVNLTFSVEEGEIFGFIGPNGAGKSTtIRTLLNFLY-PTSGSATIFGKDIVKQS-----K 72
Cdd:PRK13649 3 INLQNVSYTYQagtpfEGRALFDVNLTIEDGSYTAFIGHTGSGKST-IMQLLNGLHvPTQGSVRVDDTLITSTSknkdiK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 73 EIRQNVGYlpseVHFYDDMKVID--LLKYSAGFYKKF--NQKRMKELA-ERLDL-----DLHKKIE-DLSFGNRKKVGIV 141
Cdd:PRK13649 82 QIRKKVGL----VFQFPESQLFEetVLKDVAFGPQNFgvSQEEAEALArEKLALvgiseSLFEKNPfELSGGQMRRVAIA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1021811607 142 QALLHEPKLLILDEPTGGLDPLMQNTFFEILTEEREKGTTIIFSSHILSEVQKMCDRVAIIKEGELVK 209
Cdd:PRK13649 158 GILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVL 225
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
4-208 |
1.90e-22 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 92.90 E-value: 1.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 4 IDVKNLTKTYkkNRGIVNLTFSVEEGEIFGFIGPNGAGKSttirTLLN----FLYPTSGSATIFGKDIVKQSKE------ 73
Cdd:COG3840 2 LRLDDLTYRY--GDFPLRFDLTIAAGERVAILGPSGAGKS----TLLNliagFLPPDSGRILWNGQDLTALPPAerpvsm 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 74 ------------IRQNVGyL---PSevhfyddmkvidlLKYSAGfykkfNQKRMKELAERLDLD--LHKKIEDLSFGNRK 136
Cdd:COG3840 76 lfqennlfphltVAQNIG-LglrPG-------------LKLTAE-----QRAQVEQALERVGLAglLDRLPGQLSGGQRQ 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1021811607 137 KVGIVQALLHEPKLLILDEPTGGLDPLMQNtffEILT--EE--REKGTTIIFSSHILSEVQKMCDRVAIIKEGELV 208
Cdd:COG3840 137 RVALARCLVRKRPILLLDEPFSALDPALRQ---EMLDlvDElcRERGLTVLMVTHDPEDAARIADRVLLVADGRIA 209
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
28-209 |
2.40e-22 |
|
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: 92.36 E-value: 2.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 28 EGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQSKEI-----RQNVGYLPSEVHFYDDMKVIDLLKYSAG 102
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKInlppqQRKIGLVFQQYALFPHLNVRENLAFGLK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 103 FYKKFNQK-RMKELAERLDLD--LHKKIEDLSFGNRKKVGIVQALLHEPKLLILDEPTGGLDPLMQNTFFEILTEEREK- 178
Cdd:cd03297 102 RKRNREDRiSVDELLDLLGLDhlLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKKNl 181
|
170 180 190
....*....|....*....|....*....|.
gi 1021811607 179 GTTIIFSSHILSEVQKMCDRVAIIKEGELVK 209
Cdd:cd03297 182 NIPVIFVTHDLSEAEYLADRIVVMEDGRLQY 212
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-205 |
2.65e-22 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 95.29 E-value: 2.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 1 MKIIDVKNLTKTYKKNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQS-KEIRQNVG 79
Cdd:PRK09536 1 MPMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSaRAASRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 80 YLPSE--VHF-YDDMKVIDLLKYSA----GFYKKFNQKRMKELAERLDLD--LHKKIEDLSFGNRKKVGIVQALLHEPKL 150
Cdd:PRK09536 81 SVPQDtsLSFeFDVRQVVEMGRTPHrsrfDTWTETDRAAVERAMERTGVAqfADRPVTSLSGGERQRVLLARALAQATPV 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1021811607 151 LILDEPTGGLDPLMQNTFFEILTEEREKGTTIIFSSHILSEVQKMCDRVAIIKEG 205
Cdd:PRK09536 161 LLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADG 215
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
3-208 |
3.30e-22 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 92.36 E-value: 3.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 3 IIDVKNLTKTYKKNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTlLNFL-YPTSGSATIFGKDIVKQSKEI---RQNV 78
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRC-INLLeEPDSGTITVDGEDLTDSKKDInklRRKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 79 GYlpseV--HF--YDDMKVID--------LLKYSagfyKKFNQKRMKELAERLDLD--LHKKIEDLSFGNRKKVGIVQAL 144
Cdd:COG1126 80 GM----VfqQFnlFPHLTVLEnvtlapikVKKMS----KAEAEERAMELLERVGLAdkADAYPAQLSGGQQQRVAIARAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1021811607 145 LHEPKLLILDEPTGGLDPLMQNTFFEILTEEREKGTTIIFSSHILSEVQKMCDRVAIIKEGELV 208
Cdd:COG1126 152 AMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIV 215
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
4-208 |
3.80e-22 |
|
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: 91.83 E-value: 3.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 4 IDVKNLTKTY---------KKNRGIV-------------NLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSAT 61
Cdd:cd03220 1 IELENVSKSYptykggsssLKKLGILgrkgevgefwalkDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 62 IFGKDivkqSKEIRQNVGYLPsevhfydDMKVIDLLKYSAGFY---KKFNQKRMKELAERLDL--DLHKKIEDLSFGNRK 136
Cdd:cd03220 81 VRGRV----SSLLGLGGGFNP-------ELTGRENIYLNGRLLglsRKEIDEKIDEIIEFSELgdFIDLPVKTYSSGMKA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1021811607 137 KVGIVQALLHEPKLLILDEPTGGLDPLMQNTFFEILTEEREKGTTIIFSSHILSEVQKMCDRVAIIKEGELV 208
Cdd:cd03220 150 RLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIR 221
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
2-208 |
3.88e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 95.90 E-value: 3.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 2 KIIDVKNLTKTYKKNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSatifgkdiVKQSKEIRqnVGYL 81
Cdd:COG0488 314 KVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGT--------VKLGETVK--IGYF 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 82 PSEVHFYD-DMKVIDLLkysAGFYKKFNQKRMKELAERLDL---DLHKKIEDLSFGNRKKVGIVQALLHEPKLLILDEPT 157
Cdd:COG0488 384 DQHQEELDpDKTVLDEL---RDGAPGGTEQEVRGYLGRFLFsgdDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPT 460
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1021811607 158 GGLDPLMQntffEILTE--EREKGtTIIFSSHILSEVQKMCDRVAIIKEGELV 208
Cdd:COG0488 461 NHLDIETL----EALEEalDDFPG-TVLLVSHDRYFLDRVATRILEFEDGGVR 508
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
18-208 |
4.04e-22 |
|
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: 91.40 E-value: 4.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 18 GIVNLTFS--VEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDiVKQSKEIRQNVGYLPSEVHFYDDMKV-- 93
Cdd:cd03298 11 GEQPMHFDltFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVD-VTAAPPADRPVSMLFQENNLFAHLTVeq 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 94 -IDL-----LKYSAgfykkFNQKRMKELAERLDLD--LHKKIEDLSFGNRKKVGIVQALLHEPKLLILDEPTGGLDPLMQ 165
Cdd:cd03298 90 nVGLglspgLKLTA-----EDRQAIEVALARVGLAglEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1021811607 166 NTFFEILTE-EREKGTTIIFSSHILSEVQKMCDRVAIIKEGELV 208
Cdd:cd03298 165 AEMLDLVLDlHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIA 208
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
21-208 |
4.39e-22 |
|
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: 95.59 E-value: 4.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 21 NLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQSKE-IRQNVGYLPSEVHFY----------- 88
Cdd:COG4618 350 GVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREeLGRHIGYLPQDVELFdgtiaeniarf 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 89 ---DDMKVIDLLKySAGfykkfnqkrMKELAERLDLDLHKKIED----LSFGNRKKVGIVQALLHEPKLLILDEPTGGLD 161
Cdd:COG4618 430 gdaDPEKVVAAAK-LAG---------VHEMILRLPDGYDTRIGEggarLSGGQRQRIGLARALYGDPRLVVLDEPNSNLD 499
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1021811607 162 P-----LMQntffeILTEEREKGTTIIFSSH---ILSEvqkmCDRVAIIKEGELV 208
Cdd:COG4618 500 DegeaaLAA-----AIRALKARGATVVVITHrpsLLAA----VDKLLVLRDGRVQ 545
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1-219 |
5.85e-22 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 93.43 E-value: 5.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 1 MKIIDVKNLTKTYKKNRGI------VNLTFSveEGEIFGFIGPNGAGKSTTIRTLLNFLYP----TSGSATIFGKDIVKQ 70
Cdd:COG4170 1 MPLLDIRNLTIEIDTPQGRvkavdrVSLTLN--EGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGIDLLKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 71 S-KEIRQNVG------------YL-PSEVHFYDDMKVIDLLKYSAGFYKKFNQ--KRMKELAERLDLDLHKKIED----- 129
Cdd:COG4170 79 SpRERRKIIGreiamifqepssCLdPSAKIGDQLIEAIPSWTFKGKWWQRFKWrkKRAIELLHRVGIKDHKDIMNsyphe 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 130 LSFGNRKKVGIVQALLHEPKLLILDEPTGGLDPLMQNTFFEILTE-EREKGTTIIFSSHILSEVQKMCDRVAIIKEGELV 208
Cdd:COG4170 159 LTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARlNQLQGTSILLISHDLESISQWADTITVLYCGQTV 238
|
250
....*....|.
gi 1021811607 209 KVETIENLTKN 219
Cdd:COG4170 239 ESGPTEQILKS 249
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-212 |
7.09e-22 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 94.85 E-value: 7.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 3 IIDVKNLTKtyKKNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQSK---------- 72
Cdd:PRK09700 265 VFEVRNVTS--RDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPldavkkgmay 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 73 --EIRQNVGYLPSeVHFYDDMKVIDLLKYSA--GFYKKFNQKRMKELAE--RLDLDL-----HKKIEDLSFGNRKKVGIV 141
Cdd:PRK09700 343 itESRRDNGFFPN-FSIAQNMAISRSLKDGGykGAMGLFHEVDEQRTAEnqRELLALkchsvNQNITELSGGNQQKVLIS 421
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1021811607 142 QALLHEPKLLILDEPTGGLDPLMQNTFFEILTEEREKGTTIIFSSHILSEVQKMCDRVAIIKEGELVKVET 212
Cdd:PRK09700 422 KWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQILT 492
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
4-220 |
8.84e-22 |
|
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: 91.06 E-value: 8.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 4 IDVKNLTKTY--KKNRGIV-NLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQS-KEIRQNVG 79
Cdd:cd03249 1 IEFKNVSFRYpsRPDVPILkGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNlRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 80 YLPSEVHFYdDMKVIDLLKYSAGFYKKFNQKRMKELAErldldLHKKIED---------------LSFGNRKKVGIVQAL 144
Cdd:cd03249 81 LVSQEPVLF-DGTIAENIRYGKPDATDEEVEEAAKKAN-----IHDFIMSlpdgydtlvgergsqLSGGQKQRIAIARAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 145 LHEPKLLILDEPTGGLDP----LMQNTFfeiltEEREKGTTIIFSSHILSEVQKmCDRVAIIKEGELVKVETIENLTKNN 220
Cdd:cd03249 155 LRNPKILLLDEATSALDAesekLVQEAL-----DRAMKGRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGTHDELMAQK 228
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
4-212 |
2.02e-21 |
|
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: 90.48 E-value: 2.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 4 IDVKNLTKTYKKNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQSKEIRqNVGYLPS 83
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQER-NVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 84 EVHFYDDMKVIDLLKYSAGFYKKFN-------QKRMKELAERLDLD-LHKKI-EDLSFGNRKKVGIVQALLHEPKLLILD 154
Cdd:cd03296 82 HYALFRHMTVFDNVAFGLRVKPRSErppeaeiRAKVHELLKLVQLDwLADRYpAQLSGGQRQRVALARALAVEPKVLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1021811607 155 EPTGGLDPLMQNTFFEILTE-EREKGTTIIFSSHILSEVQKMCDRVAIIKEGELVKVET 212
Cdd:cd03296 162 EPFGALDAKVRKELRRWLRRlHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGT 220
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
4-208 |
2.70e-21 |
|
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: 89.48 E-value: 2.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 4 IDVKNLTKTYKKNRGIV--NLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQS-KEIRQNVGY 80
Cdd:cd03244 3 IEFKNVSLRYRPNLPPVlkNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGlHDLRSRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 81 LPSEV--------------HFYDDMKVIDLLKysagfykkfnQKRMKELAERLDLDLHKKIED----LSFGNRKKVGIVQ 142
Cdd:cd03244 83 IPQDPvlfsgtirsnldpfGEYSDEELWQALE----------RVGLKEFVESLPGGLDTVVEEggenLSVGQRQLLCLAR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 143 ALLHEPKLLILDEPTGGLDP----LMQNTffeilTEEREKGTTIIFSSHILSEVQKmCDRVAIIKEGELV 208
Cdd:cd03244 153 ALLRKSKILVLDEATASVDPetdaLIQKT-----IREAFKDCTVLTIAHRLDTIID-SDRILVLDKGRVV 216
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-216 |
4.76e-21 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 92.42 E-value: 4.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 3 IIDVKNLTktykkNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQSKEIRQNVG--Y 80
Cdd:PRK15439 268 VLTVEDLT-----GEGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGlvY 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 81 LPSEVH----FYD---DMKVIDLLKYSAGFYkkfnQKRMKELA--ERLDLDLHKKIED-------LSFGNRKKVGIVQAL 144
Cdd:PRK15439 343 LPEDRQssglYLDaplAWNVCALTHNRRGFW----IKPARENAvlERYRRALNIKFNHaeqaartLSGGNQQKVLIAKCL 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 145 LHEPKLLILDEPTGGLDPLMQNTFFEILTEEREKGTTIIFSSHILSEVQKMCDRVAIIKEGEL--------VKVETIENL 216
Cdd:PRK15439 419 EASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEIsgaltgaaINVDTIMRL 498
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
3-221 |
5.02e-21 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 92.30 E-value: 5.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 3 IIDVKNLTKTYKKNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRtLLNFLYPT---SGSATIFGKDIvkQSKEIRQN-- 77
Cdd:PRK13549 5 LLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMK-VLSGVYPHgtyEGEIIFEGEEL--QASNIRDTer 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 78 --VGYLPSEVHFYDDMKVI-------DLLKYSAGFYKKFNQKRMKELAE-RLDLDLHKKIEDLSFGNRKKVGIVQALLHE 147
Cdd:PRK13549 82 agIAIIHQELALVKELSVLeniflgnEITPGGIMDYDAMYLRAQKLLAQlKLDINPATPVGNLGLGQQQLVEIAKALNKQ 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1021811607 148 PKLLILDEPTGGLDPLMQNTFFEILTEEREKGTTIIFSSHILSEVQKMCDRVAIIKEGELVKVETIENLTKNNL 221
Cdd:PRK13549 162 ARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAGMTEDDI 235
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
7-208 |
9.22e-21 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 89.28 E-value: 9.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 7 KNLTKTYKKNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVK-QSKEIRQNVGYLPSEV 85
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHyASKEVARRIGLLAQNA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 86 HFYDDMKVIDLLKYSAGFYKKFNQKRMKELAERLDLDLH---------KKIEDLSFGNRKKVGIVQALLHEPKLLILDEP 156
Cdd:PRK10253 91 TTPGDITVQELVARGRYPHQPLFTRWRKEDEEAVTKAMQatgithladQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1021811607 157 TGGLDPLMQNTFFEILTE-EREKGTTIIFSSHILSEVQKMCDRVAIIKEGELV 208
Cdd:PRK10253 171 TTWLDISHQIDLLELLSElNREKGYTLAAVLHDLNQACRYASHLIALREGKIV 223
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
4-216 |
9.47e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 89.69 E-value: 9.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 4 IDVKNLTKTYKKN-----RGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIV-----KQSKE 73
Cdd:PRK13634 3 ITFQKVEHRYQYKtpferRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITagkknKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 74 IRQNVGYL---PSEVHFYDDM-KVIDLLKYSAGFYKKFNQKRMKELAERLDLD---LHKKIEDLSFGNRKKVGIVQALLH 146
Cdd:PRK13634 83 LRKKVGIVfqfPEHQLFEETVeKDICFGPMNFGVSEEDAKQKAREMIELVGLPeelLARSPFELSGGQMRRVAIAGVLAM 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1021811607 147 EPKLLILDEPTGGLDPLMQNTFFEILTE-EREKGTTIIFSSHILSEVQKMCDRVAIIKEGELVKVETIENL 216
Cdd:PRK13634 163 EPEVLVLDEPTAGLDPKGRKEMMEMFYKlHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREI 233
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
4-216 |
1.07e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 89.45 E-value: 1.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 4 IDVKNLTKTYKKN-----RGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQSKE----- 73
Cdd:PRK13646 3 IRFDNVSYTYQKGtpyehQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDkyirp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 74 IRQNVG--YLPSEVHFYDDMKVIDLLKYSAGFykKFNQKRMKELAERLDLDL-------HKKIEDLSFGNRKKVGIVQAL 144
Cdd:PRK13646 83 VRKRIGmvFQFPESQLFEDTVEREIIFGPKNF--KMNLDEVKNYAHRLLMDLgfsrdvmSQSPFQMSGGQMRKIAIVSIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1021811607 145 LHEPKLLILDEPTGGLDPLMQNTFFEILTE-EREKGTTIIFSSHILSEVQKMCDRVAIIKEGELVKVETIENL 216
Cdd:PRK13646 161 AMNPDIIVLDEPTAGLDPQSKRQVMRLLKSlQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKEL 233
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-213 |
1.13e-20 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 88.98 E-value: 1.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 1 MKIIDVKNLTKTY-------KKNRGIV--NLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVK-- 69
Cdd:PRK10419 1 MTLLNVSGLSHHYahgglsgKHQHQTVlnNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKln 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 70 --QSKEIRQNVGYL----PSEVHFYDDMKVI--DLLKYSAGFYKKFNQKRMKELAERLDLD---LHKKIEDLSFGNRKKV 138
Cdd:PRK10419 81 raQRKAFRRDIQMVfqdsISAVNPRKTVREIirEPLRHLLSLDKAERLARASEMLRAVDLDdsvLDKRPPQLSGGQLQRV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1021811607 139 GIVQALLHEPKLLILDEPTGGLDPLMQNTFFEILTEEREK-GTTIIFSSHILSEVQKMCDRVAIIKEGELVKVETI 213
Cdd:PRK10419 161 CLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPV 236
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
22-218 |
1.26e-20 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 88.36 E-value: 1.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 22 LTFSVEEGEIFGFIGPNGAGKSTtirtLLNF---LYPTSGSATIFGKDIVKQSK-EIRQNVGYLPSEVHFYDDMKVIDLL 97
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKST----LLARmagLLPGQGEILLNGRPLSDWSAaELARHRAYLSQQQSPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 98 K--YSAGFYKKFNQKRMKELAERLDLD--LHKKIEDLSFGNRKKVGIVQALLH-------EPKLLILDEPTGGLDPLMQN 166
Cdd:COG4138 91 AlhQPAGASSEAVEQLLAQLAEALGLEdkLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMNSLDVAQQA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1021811607 167 TFFEILTEEREKGTTIIFSSHILSEVQKMCDRVAIIKEGELV------KVETIENLTK 218
Cdd:COG4138 171 ALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVasgetaEVMTPENLSE 228
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-210 |
1.41e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 88.89 E-value: 1.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 2 KIIDVKNLTKTYK--KNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQS-KEIRQNV 78
Cdd:PRK13632 6 VMIKVENVSFSYPnsENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENlKEIRKKI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 79 G---------YLPSEVHfyDDMkvidllkysaGF---YKKFNQKRMK----ELAERLDLD--LHKKIEDLSFGNRKKVGI 140
Cdd:PRK13632 86 GiifqnpdnqFIGATVE--DDI----------AFgleNKKVPPKKMKdiidDLAKKVGMEdyLDKEPQNLSGGQKQRVAI 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1021811607 141 VQALLHEPKLLILDEPTGGLDPLMQNTFFEILTEEREKGT-TIIFSSHILSEVQKmCDRVAIIKEGELVKV 210
Cdd:PRK13632 154 ASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLISITHDMDEAIL-ADKVIVFSEGKLIAQ 223
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
2-214 |
1.90e-20 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 87.83 E-value: 1.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 2 KIIDVKNLTKTY------------------KKNRGIV----NLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGS 59
Cdd:COG1134 3 SMIEVENVSKSYrlyhepsrslkelllrrrRTRREEFwalkDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 60 ATIFGKdivkqskeI----------------RQNV-------GYLPSEV-HFYDDM-------KVIDL-LK-YSAGfykk 106
Cdd:COG1134 83 VEVNGR--------VsallelgagfhpeltgRENIylngrllGLSRKEIdEKFDEIvefaelgDFIDQpVKtYSSG---- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 107 fnqkrMK-ELAerldldlhkkiedlsFGnrkkvgiVQALLhEPKLLILDEPTGGLDPLMQNTFFEILTEEREKGTTIIFS 185
Cdd:COG1134 151 -----MRaRLA---------------FA-------VATAV-DPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFV 202
|
250 260
....*....|....*....|....*....
gi 1021811607 186 SHILSEVQKMCDRVAIIKEGELVKVETIE 214
Cdd:COG1134 203 SHSMGAVRRLCDRAIWLEKGRLVMDGDPE 231
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
4-220 |
2.39e-20 |
|
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: 87.28 E-value: 2.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 4 IDVKNLTKTYKKNRGIV-NLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQS-KEIRQNVGYL 81
Cdd:cd03254 3 IEFENVNFSYDEKKPVLkDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISrKSLRSMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 82 PSEVHFY---------------DDMKVIDLLKysagfykkfnQKRMKELAERLDLDLHKKI----EDLSFGNRKKVGIVQ 142
Cdd:cd03254 83 LQDTFLFsgtimenirlgrpnaTDEEVIEAAK----------EAGAHDFIMKLPNGYDTVLgengGNLSQGERQLLAIAR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1021811607 143 ALLHEPKLLILDEPTGGLDPLMQNTFFEILTEEREKGTTIIFsSHILSEVQKmCDRVAIIKEGELVKVETIENLTKNN 220
Cdd:cd03254 153 AMLRDPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIII-AHRLSTIKN-ADKILVLDDGKIIEEGTHDELLAKK 228
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
4-199 |
3.15e-20 |
|
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: 90.42 E-value: 3.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 4 IDVKNLTKTYK-KNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQS-KEIRQNVGYL 81
Cdd:TIGR02857 322 LEFSGVSVAYPgRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADaDSWRDQIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 82 PSEVHFYDDMkvidlLKYSAGFYKKF-NQKRMKELAERLDLD---------LHKKIED----LSFGNRKKVGIVQALLHE 147
Cdd:TIGR02857 402 PQHPFLFAGT-----IAENIRLARPDaSDAEIREALERAGLDefvaalpqgLDTPIGEggagLSGGQAQRLALARAFLRD 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1021811607 148 PKLLILDEPTGGLDPLMQNTFFEILtEEREKGTTIIFSSHILsEVQKMCDRV 199
Cdd:TIGR02857 477 APLLLLDEPTAHLDAETEAEVLEAL-RALAQGRTVLLVTHRL-ALAALADRI 526
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
4-216 |
5.04e-20 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 86.52 E-value: 5.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 4 IDVKNLTKTYKKNRGIV--NLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQS-KEIRQNVGY 80
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVlrDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTlASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 81 LPSEVHFYDDmKVIDLLKYSagfykKFNQKR-----------MKELAERLDLDLHKKIED----LSFGNRKKVGIVQALL 145
Cdd:cd03251 81 VSQDVFLFND-TVAENIAYG-----RPGATReeveeaaraanAHEFIMELPEGYDTVIGErgvkLSGGQRQRIAIARALL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1021811607 146 HEPKLLILDEPTGGLDP----LMQNTfFEILTEERekgTTIIFsSHILSEVQKmCDRVAIIKEGELVKVETIENL 216
Cdd:cd03251 155 KDPPILILDEATSALDTeserLVQAA-LERLMKNR---TTFVI-AHRLSTIEN-ADRIVVLEDGKIVERGTHEEL 223
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-209 |
7.43e-20 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 86.34 E-value: 7.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 1 MKIIDVKNLTKTYKKNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLlNFL-YPTSGSATI------FGKDIVKQS-- 71
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCI-NLLeQPEAGTIRVgditidTARSLSQQKgl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 72 -KEIRQNVGYLPSEVHFYDDMKVIDLLKYSAGFYKKFNQKRMKELAERL--DLDLHKKiED-----LSFGNRKKVGIVQA 143
Cdd:PRK11264 80 iRQLRQHVGFVFQNFNLFPHRTVLENIIEGPVIVKGEPKEEATARARELlaKVGLAGK-ETsyprrLSGGQQQRVAIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1021811607 144 LLHEPKLLILDEPTGGLDPLMQNtffEILTEER---EKGTTIIFSSHILSEVQKMCDRVAIIKEGELVK 209
Cdd:PRK11264 159 LAMRPEVILFDEPTSALDPELVG---EVLNTIRqlaQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVE 224
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
4-208 |
7.79e-20 |
|
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: 86.13 E-value: 7.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 4 IDVKNLTKTYKKNRGIV-NLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDI--VKQSkEIRQNVGY 80
Cdd:cd03253 1 IEFENVTFAYDPGRPVLkDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIreVTLD-SLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 81 LPSEVHFYDDmKVIDLLKY---SAgfykkfNQKRMKELAERldLDLHKKIEDLSFGNRKKVG---------------IVQ 142
Cdd:cd03253 80 VPQDTVLFND-TIGYNIRYgrpDA------TDEEVIEAAKA--AQIHDKIMRFPDGYDTIVGerglklsggekqrvaIAR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1021811607 143 ALLHEPKLLILDEPTGGLDplmQNTFFEILTEERE--KGTTIIFSSHILSEVqKMCDRVAIIKEGELV 208
Cdd:cd03253 151 AILKNPPILLLDEATSALD---THTEREIQAALRDvsKGRTTIVIAHRLSTI-VNADKIIVLKDGRIV 214
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
3-207 |
8.98e-20 |
|
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: 85.60 E-value: 8.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 3 IIDVKNLTKTYKkNRG----IVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDI----------- 67
Cdd:cd03248 11 IVKFQNVTFAYP-TRPdtlvLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPIsqyehkylhsk 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 68 ---VKQ-----SKEIRQNVGY-LPSEvhfyDDMKVIDLL-KYSAGFYkkfnqkrMKELAERLDLDLHKKIEDLSFGNRKK 137
Cdd:cd03248 90 vslVGQepvlfARSLQDNIAYgLQSC----SFECVKEAAqKAHAHSF-------ISELASGYDTEVGEKGSQLSGGQKQR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 138 VGIVQALLHEPKLLILDEPTGGLDPLMQNTFFEILTEEREKgTTIIFSSHILSEVQKmCDRVAIIKEGEL 207
Cdd:cd03248 159 VAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPER-RTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
3-205 |
1.11e-19 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 87.70 E-value: 1.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 3 IIDVKNLTKTYKKNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQSKEIR------Q 76
Cdd:PRK09452 14 LVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRhvntvfQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 77 NVGYLPsevHfyddMKVIDLLKYSAGFYKKFNQK---------RMKELAERLDldlhKKIEDLSFGNRKKVGIVQALLHE 147
Cdd:PRK09452 94 SYALFP---H----MTVFENVAFGLRMQKTPAAEitprvmealRMVQLEEFAQ----RKPHQLSGGQQQRVAIARAVVNK 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1021811607 148 PKLLILDEPTGGLD----PLMQNtffEILTEEREKGTTIIFSSHILSEVQKMCDRVAIIKEG 205
Cdd:PRK09452 163 PKVLLLDESLSALDyklrKQMQN---ELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDG 221
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
21-220 |
1.19e-19 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 85.62 E-value: 1.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 21 NLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQSKE-IRQNVGY-LPSEVHFYDDMKV-IDLL 97
Cdd:cd03252 20 NISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAwLRRQVGVvLQENVLFNRSIRDnIALA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 98 KYSAGFYKKFNQKRM-------KELAERLDLDLHKKIEDLSFGNRKKVGIVQALLHEPKLLILDEPTGGLD-----PLMQ 165
Cdd:cd03252 100 DPGMSMERVIEAAKLagahdfiSELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDyesehAIMR 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1021811607 166 NtFFEILteereKGTTIIFSSHILSEVqKMCDRVAIIKEGELVKVETIENLTKNN 220
Cdd:cd03252 180 N-MHDIC-----AGRTVIIIAHRLSTV-KNADRIIVMEKGRIVEQGSHDELLAEN 227
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
4-187 |
2.12e-19 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 87.76 E-value: 2.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 4 IDVKNLTKTYKKNRGIVNLTFSVEEGEIFGFIGPNGAGKSTtirtLLNFL---YPT--SGSATIFGKDivKQSKE----I 74
Cdd:PRK10938 261 IVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKST----LLSLItgdHPQgySNDLTLFGRR--RGSGEtiwdI 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 75 RQNVGYLPSEVH----------------FYDdmkvidllkySAGFYKKFNQKRMKELAERLD-LDLHKKIED-----LSF 132
Cdd:PRK10938 335 KKHIGYVSSSLHldyrvstsvrnvilsgFFD----------SIGIYQAVSDRQQKLAQQWLDiLGIDKRTADapfhsLSW 404
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1021811607 133 GNRKKVGIVQALLHEPKLLILDEPTGGLDPL---MQNTFFEILTEEREkgTTIIFSSH 187
Cdd:PRK10938 405 GQQRLALIVRALVKHPTLLILDEPLQGLDPLnrqLVRRFVDVLISEGE--TQLLFVSH 460
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
3-205 |
2.21e-19 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 84.76 E-value: 2.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 3 IIDVKNLTKTYKKNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLlNFLYPTSGSATIFG----KDIVKQSKEIRQNV 78
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCI-NKLEEITSGDLIVDglkvNDPKVDERLIRQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 79 GYLPSEVHFYDDMKVIDllkySAGFYKKFNQKRMKELAERLDLDLHKKI----------EDLSFGNRKKVGIVQALLHEP 148
Cdd:PRK09493 80 GMVFQQFYLFPHLTALE----NVMFGPLRVRGASKEEAEKQARELLAKVglaerahhypSELSGGQQQRVAIARALAVKP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1021811607 149 KLLILDEPTGGLDPLMQNTFFEILTEEREKGTTIIFSSHILSEVQKMCDRVAIIKEG 205
Cdd:PRK09493 156 KLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKG 212
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-232 |
3.30e-19 |
|
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: 87.19 E-value: 3.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 3 IIDVKNLTKTYKKNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRtLLNFLYPT---SGSATIFGKDIVKQS--KEIRQN 77
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMK-ILSGVYPHgtwDGEIYWSGSPLKASNirDTERAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 78 VGYLPSEVHFYDDMKVID-------------LLKYSAGFykkfnqKRMKELAERLDLD---LHKKIEDLSFGNRKKVGIV 141
Cdd:TIGR02633 80 IVIIHQELTLVPELSVAEniflgneitlpggRMAYNAMY------LRAKNLLRELQLDadnVTRPVGDYGGGQQQLVEIA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 142 QALLHEPKLLILDEPTGGLDPLMQNTFFEILTEEREKGTTIIFSSHILSEVQKMCDRVAIIKEGELVKVETIENLTKNNL 221
Cdd:TIGR02633 154 KALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSEDDI 233
|
250
....*....|.
gi 1021811607 222 KNITITFEQTN 232
Cdd:TIGR02633 234 ITMMVGREITS 244
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-216 |
3.43e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 85.17 E-value: 3.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 1 MKIIDVKNLTKTYKKNRG---IVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQSK-EIRQ 76
Cdd:PRK13650 2 SNIIEVKNLTFKYKEDQEkytLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVwDIRH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 77 NVGY-------------LPSEVHFYDDMKVIDLlkysagfykKFNQKRMKELAERLDLDLHKKIED--LSFGNRKKVGIV 141
Cdd:PRK13650 82 KIGMvfqnpdnqfvgatVEDDVAFGLENKGIPH---------EEMKERVNEALELVGMQDFKEREParLSGGQKQRVAIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1021811607 142 QALLHEPKLLILDEPTGGLDPLMQNTFFEILTEEREK-GTTIIFSSHILSEVqKMCDRVAIIKEGELVKVETIENL 216
Cdd:PRK13650 153 GAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDEV-ALSDRVLVMKNGQVESTSTPREL 227
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
3-199 |
3.76e-19 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 84.40 E-value: 3.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 3 IIDVKNLTKTYKKNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSatifgkdiVKQSKEIRqnVGYLP 82
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGV--------IKRNGKLR--IGYVP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 83 SEVHFYDDM--KVIDLLKYSAGFYKKFNQKRMKEL-AERLdldLHKKIEDLSFGNRKKVGIVQALLHEPKLLILDEPTGG 159
Cdd:PRK09544 74 QKLYLDTTLplTVNRFLRLRPGTKKEDILPALKRVqAGHL---IDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQG 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1021811607 160 LDPLMQNTFFEILTEER-EKGTTIIFSSHILSEVQKMCDRV 199
Cdd:PRK09544 151 VDVNGQVALYDLIDQLRrELDCAVLMVSHDLHLVMAKTDEV 191
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-208 |
3.98e-19 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 87.05 E-value: 3.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 1 MKIIDVKNLTKTYKKNRGIV----NLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFL-YP---TSGSATIFGKDIVKQS- 71
Cdd:COG4172 4 MPLLSVEDLSVAFGQGGGTVeavkGVSFDIAAGETLALVGESGSGKSVTALSILRLLpDPaahPSGSILFDGQDLLGLSe 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 72 KEIRQ----NVGYLpsevhFYDDM-----------KVIDLLKYSAGFYKKFNQKRMKELAERLDL-DLHKKIED----LS 131
Cdd:COG4172 84 RELRRirgnRIAMI-----FQEPMtslnplhtigkQIAEVLRLHRGLSGAAARARALELLERVGIpDPERRLDAyphqLS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1021811607 132 FGNRKKVGIVQALLHEPKLLILDEPTGGLDPLMQNTFFEILTE-EREKGTTIIFSSHILSEVQKMCDRVAIIKEGELV 208
Cdd:COG4172 159 GGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDlQRELGMALLLITHDLGVVRRFADRVAVMRQGEIV 236
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-216 |
4.34e-19 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 85.62 E-value: 4.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 1 MKIIDVKNLTKTYKKNRGIVN----LTFSVEEGEIFGFIGPNGAGKSTTIRTLLNF----LYPTSGSATIFGKDIVKQS- 71
Cdd:PRK15093 1 MPLLDIRNLTIEFKTSDGWVKavdrVSMTLTEGEIRGLVGESGSGKSLIAKAICGVtkdnWRVTADRMRFDDIDLLRLSp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 72 ----KEIRQNVGYL---------PSEVHFYDDMKVIDLLKYSAGFYKKFN--QKRMKELAERLDLDLHKKIE-----DLS 131
Cdd:PRK15093 81 rerrKLVGHNVSMIfqepqscldPSERVGRQLMQNIPGWTYKGRWWQRFGwrKRRAIELLHRVGIKDHKDAMrsfpyELT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 132 FGNRKKVGIVQALLHEPKLLILDEPTGGLDPLMQNTFFEILTE-EREKGTTIIFSSHILSEVQKMCDRVAIIKEGELVKV 210
Cdd:PRK15093 161 EGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRlNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVET 240
|
....*.
gi 1021811607 211 ETIENL 216
Cdd:PRK15093 241 APSKEL 246
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
11-219 |
4.42e-19 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 85.53 E-value: 4.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 11 KTYKKNRGIvnlTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQS----KEIRQNVgylpsEVH 86
Cdd:PRK15079 32 KTLKAVDGV---TLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKddewRAVRSDI-----QMI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 87 FYDD-------MKVID-----LLKYSAGFYKKFNQKRMKELAERLDLdLHKKI----EDLSFGNRKKVGIVQALLHEPKL 150
Cdd:PRK15079 104 FQDPlaslnprMTIGEiiaepLRTYHPKLSRQEVKDRVKAMMLKVGL-LPNLInrypHEFSGGQCQRIGIARALILEPKL 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 151 LILDEPTGGLDPLMQNTFFEILTE-EREKGTTIIFSSHILSEVQKMCDRVAIIKEGELVKVETIENLTKN 219
Cdd:PRK15079 183 IICDEPVSALDVSIQAQVVNLLQQlQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHN 252
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
8-207 |
4.45e-19 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 83.71 E-value: 4.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 8 NLTKTYKKNR----GIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQSK----EIR-QNV 78
Cdd:PRK11629 10 NLCKRYQEGSvqtdVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSaakaELRnQKL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 79 GYLPSEVHFYDDMKVID-----LLkySAGFYKKFNQKRMKEL--AERLDLDLHKKIEDLSFGNRKKVGIVQALLHEPKLL 151
Cdd:PRK11629 90 GFIYQFHHLLPDFTALEnvampLL--IGKKKPAEINSRALEMlaAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLV 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1021811607 152 ILDEPTGGLDPLMQNTFFEILTE-EREKGTTIIFSSHILSEVQKMcDRVAIIKEGEL 207
Cdd:PRK11629 168 LADEPTGNLDARNADSIFQLLGElNRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRL 223
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-208 |
4.92e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 84.68 E-value: 4.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 2 KIIDVKNLTKTYK--KNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGK--------DIVKQS 71
Cdd:PRK13635 4 EIIRVEHISFRYPdaATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMvlseetvwDVRRQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 72 KEIRQN-----VG-YLPSEVHF--------YDDM--KVIDLLKysagfykkfnQKRMKELAERldlDLHKkiedLSFGNR 135
Cdd:PRK13635 84 GMVFQNpdnqfVGaTVQDDVAFglenigvpREEMveRVDQALR----------QVGMEDFLNR---EPHR----LSGGQK 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1021811607 136 KKVGIVQALLHEPKLLILDEPTGGLDPLMQNTFFEILTE-EREKGTTIIFSSHILSEVQKmCDRVAIIKEGELV 208
Cdd:PRK13635 147 QRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQlKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEIL 219
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
7-217 |
7.70e-19 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 85.94 E-value: 7.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 7 KNLTKTYKKNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDI-VKQSKEIRQN-VGYLPSE 84
Cdd:PRK10982 2 SNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdFKSSKEALENgISMVHQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 85 VHFYDDMKVID---LLKY-SAGFYkkFNQKRM----KELAERLDLDL--HKKIEDLSFGNRKKVGIVQALLHEPKLLILD 154
Cdd:PRK10982 82 LNLVLQRSVMDnmwLGRYpTKGMF--VDQDKMyrdtKAIFDELDIDIdpRAKVATLSVSQMQMIEIAKAFSYNAKIVIMD 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1021811607 155 EPTGGLDPLMQNTFFEILTEEREKGTTIIFSSHILSEVQKMCDRVAIIKEGELVKVETIENLT 217
Cdd:PRK10982 160 EPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGLT 222
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
13-208 |
9.35e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 83.90 E-value: 9.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 13 YKKNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIvKQSKE----IRQNVGYL---PSEV 85
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL-DYSKRgllaLRQQVATVfqdPEQQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 86 HFYDDMKViDLlkysagfykKFNQKRM----KELAERLDLDL---------HKKIEDLSFGNRKKVGIVQALLHEPKLLI 152
Cdd:PRK13638 90 IFYTDIDS-DI---------AFSLRNLgvpeAEITRRVDEALtlvdaqhfrHQPIQCLSHGQKKRVAIAGALVLQARYLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1021811607 153 LDEPTGGLDPLMQNTFFEILTEEREKGTTIIFSSHILSEVQKMCDRVAIIKEGELV 208
Cdd:PRK13638 160 LDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQIL 215
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
22-221 |
1.22e-18 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 83.06 E-value: 1.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 22 LTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLyPTSGSATIFGKDIVKQS-KEIRQNVGYLPSEVHFYDDMKVIDLLKYS 100
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSaAELARHRAYLSQQQTPPFAMPVFQYLTLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 101 --AGFYKKFNQKRMKELAERLDLD--LHKKIEDLSFGNRKKVGIVQALLH-------EPKLLILDEPTGGLDPLMQNTFF 169
Cdd:PRK03695 94 qpDKTRTEAVASALNEVAEALGLDdkLGRSVNQLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPMNSLDVAQQAALD 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1021811607 170 EILTEEREKGTTIIFSSHILSEVQKMCDRVAIIKEGELV-KVETIENLTKNNL 221
Cdd:PRK03695 174 RLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLaSGRRDEVLTPENL 226
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
3-208 |
1.39e-18 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 85.51 E-value: 1.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 3 IIDVKNLTKTYKKNRGI----------VN-LTFSVEEGEIFGFIGPNGAGKSTTIRTLLNfLYPTSGSATIFGKDIVKQS 71
Cdd:COG4172 275 LLEARDLKVWFPIKRGLfrrtvghvkaVDgVSLTLRRGETLGLVGESGSGKSTLGLALLR-LIPSEGEIRFDGQDLDGLS 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 72 --------KEI-------------RQNVGYLPSE---VHFyddmkvidllkysAGFYKKFNQKRMKELAERLDLD---LH 124
Cdd:COG4172 354 rralrplrRRMqvvfqdpfgslspRMTVGQIIAEglrVHG-------------PGLSAAERRARVAEALEEVGLDpaaRH 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 125 KKIEDLSFGNRKKVGIVQALLHEPKLLILDEPTGGLDPLMQNTFFEILTE-EREKGTTIIFSSHILSEVQKMCDRVAIIK 203
Cdd:COG4172 421 RYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDlQREHGLAYLFISHDLAVVRALAHRVMVMK 500
|
....*
gi 1021811607 204 EGELV 208
Cdd:COG4172 501 DGKVV 505
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
20-209 |
1.39e-18 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 82.81 E-value: 1.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 20 VNLTfsVEEGEIFGFIGPNGAGKSTTIRTLL-NFLY-PTSGSATIFGKDIVKQSKEIRQNVG------YlPSEVhfyDDM 91
Cdd:COG0396 19 VNLT--IKPGEVHAIMGPNGSGKSTLAKVLMgHPKYeVTSGSILLDGEDILELSPDERARAGiflafqY-PVEI---PGV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 92 KVIDLLKYSAG------FYKKFNQKRMKELAERLDLD---LHKKI-EDLSFGNRKKVGIVQALLHEPKLLILDEPTGGLD 161
Cdd:COG0396 93 SVSNFLRTALNarrgeeLSAREFLKLLKEKMKELGLDedfLDRYVnEGFSGGEKKRNEILQMLLLEPKLAILDETDSGLD 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1021811607 162 PLMQNTFFEILTEEREKGTTIIFSSH---ILSEVQkmCDRVAIIKEGELVK 209
Cdd:COG0396 173 IDALRIVAEGVNKLRSPDRGILIITHyqrILDYIK--PDFVHVLVDGRIVK 221
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
3-212 |
1.55e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 83.63 E-value: 1.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 3 IIDVKNLTKTYKKN-----RGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIfgKDIV-------KQ 70
Cdd:PRK13643 1 MIKFEKVNYTYQPNspfasRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTV--GDIVvsstskqKE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 71 SKEIRQNVG--YLPSEVHFYDD--MKVIDLLKYSAGFYKKFNQKRMKELAERLDLD---LHKKIEDLSFGNRKKVGIVQA 143
Cdd:PRK13643 79 IKPVRKKVGvvFQFPESQLFEEtvLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLAdefWEKSPFELSGGQMRRVAIAGI 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1021811607 144 LLHEPKLLILDEPTGGLDPLMQNTFFEILTEEREKGTTIIFSSHILSEVQKMCDRVAIIKEGELVKVET 212
Cdd:PRK13643 159 LAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGT 227
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
4-207 |
1.70e-18 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 85.06 E-value: 1.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 4 IDVKNLTKTykknrGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQSKE--IRQNVGYL 81
Cdd:PRK10762 258 LKVDNLSGP-----GVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQdgLANGIVYI 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 82 pSEVHFYD----DMKVIDLLKYSAGFYKKFNQKRMKELAERLDLD------------LHKKIEDLSFGNRKKVGIVQALL 145
Cdd:PRK10762 333 -SEDRKRDglvlGMSVKENMSLTALRYFSRAGGSLKHADEQQAVSdfirlfniktpsMEQAIGLLSGGNQQKVAIARGLM 411
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1021811607 146 HEPKLLILDEPTGGLDPLMQNTFFEILTEEREKGTTIIFSSHILSEVQKMCDRVAIIKEGEL 207
Cdd:PRK10762 412 TRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-208 |
1.88e-18 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 82.47 E-value: 1.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 4 IDVKNLTKTYKKNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQSKE----IRqnvG 79
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWelarRR---A 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 80 YLP--SEVHF-YDDMKVIDLLKYSAGFYKKFNQKRMKELAERLDLD--LHKKIEDLSFGNRKKVGIVQAL--LHE----- 147
Cdd:COG4559 79 VLPqhSSLAFpFTVEEVVALGRAPHGSSAAQDRQIVREALALVGLAhlAGRSYQTLSGGEQQRVQLARVLaqLWEpvdgg 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1021811607 148 PKLLILDEPTGGLDPLMQNTFFEILTEEREKGTTIIFSSHILSEVQKMCDRVAIIKEGELV 208
Cdd:COG4559 159 PRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLV 219
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-208 |
1.99e-18 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 82.39 E-value: 1.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 3 IIDVKNLTKTYKKNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTL--LNFLYP---TSGSATIFGKDIVKQSK---EI 74
Cdd:COG1117 11 KIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrMNDLIPgarVEGEILLDGEDIYDPDVdvvEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 75 RQNVGY-------LPSEVhfYDDmkVIDLLKYsAGFYKKfnqKRMKELAERL-----------DlDLHKKIEDLSFGNRK 136
Cdd:COG1117 91 RRRVGMvfqkpnpFPKSI--YDN--VAYGLRL-HGIKSK---SELDEIVEESlrkaalwdevkD-RLKKSALGLSGGQQQ 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1021811607 137 KVGIVQALLHEPKLLILDEPTGGLDPLMQNTFFEILTEEREKgTTIIFSSHILSEVQKMCDRVAIIKEGELV 208
Cdd:COG1117 162 RLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD-YTIVIVTHNMQQAARVSDYTAFFYLGELV 232
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
3-207 |
3.88e-18 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 81.98 E-value: 3.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 3 IIDVKNLTKTYKKNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLY--PTSGS-ATIFGKDIVKQ---SKEIRQ 76
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdKSAGShIELLGRTVQREgrlARDIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 77 N---VGYLPSEVHFYDDMKVID-----------LLKYSAGFYKKFNQKRMKELAERLDLD--LHKKIEDLSFGNRKKVGI 140
Cdd:PRK09984 84 SranTGYIFQQFNLVNRLSVLEnvligalgstpFWRTCFSWFTREQKQRALQALTRVGMVhfAHQRVSTLSGGQQQRVAI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1021811607 141 VQALLHEPKLLILDEPTGGLDPLMQNTFFEILTE-EREKGTTIIFSSHILSEVQKMCDRVAIIKEGEL 207
Cdd:PRK09984 164 ARALMQQAKVILADEPIASLDPESARIVMDTLRDiNQNDGITVVVTLHQVDYALRYCERIVALRQGHV 231
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-246 |
4.20e-18 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 84.08 E-value: 4.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 4 IDVKNLTKTYKKNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTL--LNFLYPTSG----------------------- 58
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGriiyhvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 59 -------SATIFGKDIVKQSKEIRQNVG-----YLPSEVHFYDDMKVIDLLKYS---AGFYKKFNQKRMKELAERLDLDl 123
Cdd:TIGR03269 81 pcpvcggTLEPEEVDFWNLSDKLRRRIRkriaiMLQRTFALYGDDTVLDNVLEAleeIGYEGKEAVGRAVDLIEMVQLS- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 124 HKKIE---DLSFGNRKKVGIVQALLHEPKLLILDEPTGGLDPLMQNTFFEILTEE-REKGTTIIFSSHILSEVQKMCDRV 199
Cdd:TIGR03269 160 HRITHiarDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvKASGISMVLTSHWPEVIEDLSDKA 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1021811607 200 AIIKEGELVKVETIENLtknnlknITITFEQTNAIDFDLEGIVKKEI 246
Cdd:TIGR03269 240 IWLENGEIKEEGTPDEV-------VAVFMEGVSEVEKECEVEVGEPI 279
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
23-208 |
5.34e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 83.42 E-value: 5.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 23 TFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQS--KEIRQNVGYLPsevhfyDDMK-------- 92
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSprDAIRAGIMLCP------EDRKaegiipvh 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 93 -VIDLLKYSA-GFYKKF----NQKRMKELAERLDLDL-------HKKIEDLSFGNRKKVgIVQALLHEP-KLLILDEPTG 158
Cdd:PRK11288 347 sVADNINISArRHHLRAgcliNNRWEAENADRFIRSLniktpsrEQLIMNLSGGNQQKA-ILGRWLSEDmKVILLDEPTR 425
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1021811607 159 GLDPLMQNTFFEILTEEREKGTTIIFSSHILSEVQKMCDRVAIIKEGELV 208
Cdd:PRK11288 426 GIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIA 475
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
4-208 |
5.93e-18 |
|
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: 80.15 E-value: 5.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 4 IDVKNLTKTYKKN--RGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQSKE-IRQNVGY 80
Cdd:cd03369 7 IEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEdLRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 81 LPSE-VHF-------------YDDMKVIDLLKYSAGFykkfnqkrmkelaerldldlhkkiEDLSFGNRKKVGIVQALLH 146
Cdd:cd03369 87 IPQDpTLFsgtirsnldpfdeYSDEEIYGALRVSEGG------------------------LNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1021811607 147 EPKLLILDEPTGGL----DPLMQNTFFEILTeerekGTTIIFSSHILSEVQKmCDRVAIIKEGELV 208
Cdd:cd03369 143 RPRVLVLDEATASIdyatDALIQKTIREEFT-----NSTILTIAHRLRTIID-YDKILVMDAGEVK 202
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-219 |
7.14e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 81.04 E-value: 7.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 4 IDVKNLTKTYKKNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTL-----LNFLYPTSGSATIFGKDIVKQSK---EIR 75
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFnrlleLNEEARVEGEVRLFGRNIYSPDVdpiEVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 76 QNVGYLPSEVHFYDDMKVIDllkySAGFYKKFNQ--KRMKELAERLDLDLHK---------KIED----LSFGNRKKVGI 140
Cdd:PRK14267 85 REVGMVFQYPNPFPHLTIYD----NVAIGVKLNGlvKSKKELDERVEWALKKaalwdevkdRLNDypsnLSGGQRQRLVI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1021811607 141 VQALLHEPKLLILDEPTGGLDPLMQNTFFEILTEEREKgTTIIFSSHILSEVQKMCDRVAIIKEGELVKVETIENLTKN 219
Cdd:PRK14267 161 ARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFEN 238
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-210 |
7.27e-18 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 82.38 E-value: 7.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 1 MKIIDVKNLTKTYKKNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDI--VKQSKeirQNV 78
Cdd:PRK11000 1 MASVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMndVPPAE---RGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 79 GYLPSEVHFYDDMKVIDLLKYS---AGFYKKFNQKRMKELAERLDLD--LHKKIEDLSFGNRKKVGIVQALLHEPKLLIL 153
Cdd:PRK11000 78 GMVFQSYALYPHLSVAENMSFGlklAGAKKEEINQRVNQVAEVLQLAhlLDRKPKALSGGQRQRVAIGRTLVAEPSVFLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1021811607 154 DEPTGGLDP-LMQNTFFEILTEEREKGTTIIFSSHILSEVQKMCDRVAIIKEGELVKV 210
Cdd:PRK11000 158 DEPLSNLDAaLRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQV 215
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-209 |
7.52e-18 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 82.10 E-value: 7.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 1 MKIIDVKNLTKTYKKN----RGIVNLTFSVEEGEIFGFIGPNGAGKSTT---IRTLLNFLYPTSGSATIF-GKDIVKQS- 71
Cdd:PRK11022 1 MALLNVDKLSVHFGDEsapfRAVDRISYSVKQGEVVGIVGESGSGKSVSslaIMGLIDYPGRVMAEKLEFnGQDLQRISe 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 72 KEIRQNVGylpSEVH--FYDDM-----------KVIDLLKYSAGFYKKFNQKRMKEL---------AERLDLDLHKkied 129
Cdd:PRK11022 81 KERRNLVG---AEVAmiFQDPMtslnpcytvgfQIMEAIKVHQGGNKKTRRQRAIDLlnqvgipdpASRLDVYPHQ---- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 130 LSFGNRKKVGIVQALLHEPKLLILDEPTGGLDPLMQNTFFEILTE-EREKGTTIIFSSHILSEVQKMCDRVAIIKEGELV 208
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLElQQKENMALVLITHDLALVAEAAHKIIVMYAGQVV 233
|
.
gi 1021811607 209 K 209
Cdd:PRK11022 234 E 234
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-221 |
9.49e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 80.90 E-value: 9.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 3 IIDVKNLTKTYKK-----NRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQSKEIR-Q 76
Cdd:COG1101 1 MLELKNLSKTFNPgtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRaK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 77 NVGYLpsevhFYD-------DMKVID--LLKYSAGfyKKFN---------QKRMKELAERLDLDLHKKIED----LSFGN 134
Cdd:COG1101 81 YIGRV-----FQDpmmgtapSMTIEEnlALAYRRG--KRRGlrrgltkkrRELFRELLATLGLGLENRLDTkvglLSGGQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 135 RKKVGIVQALLHEPKLLILDEPTGGLDP-----LMQntffeiLTEE--REKGTTIIFSSHILSEVQKMCDRVAIIKEGEL 207
Cdd:COG1101 154 RQALSLLMATLTKPKLLLLDEHTAALDPktaalVLE------LTEKivEENNLTTLMVTHNMEQALDYGNRLIMMHEGRI 227
|
250
....*....|....*..
gi 1021811607 208 V---KVETIENLTKNNL 221
Cdd:COG1101 228 IldvSGEEKKKLTVEDL 244
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
3-205 |
9.50e-18 |
|
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: 80.17 E-value: 9.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 3 IIDVKNLTKTY-------KKNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLL-NFLyPTSGSATI---FGK-DIVKQ 70
Cdd:COG4778 4 LLEVENLSKTFtlhlqggKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYgNYL-PDSGSILVrhdGGWvDLAQA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 71 SK----EIRQN-VGY-------LP----SEVhfyddmkVIDLLkYSAGFYKKFNQKRMKELAERLDLDlhkkiEDL---- 130
Cdd:COG4778 83 SPreilALRRRtIGYvsqflrvIPrvsaLDV-------VAEPL-LERGVDREEARARARELLARLNLP-----ERLwdlp 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1021811607 131 ----SFGNRKKVGIVQALLHEPKLLILDEPTGGLDPLMQNTFFEILTEEREKGTTIIFSSHILSEVQKMCDRVAIIKEG 205
Cdd:COG4778 150 patfSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
3-217 |
1.07e-17 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 82.67 E-value: 1.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 3 IIDVKNLTKTYKKNRGIV---NLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNfLYPTSGSATIF--GK--DIVKQSKEIR 75
Cdd:PRK13549 259 ILEVRNLTAWDPVNPHIKrvdDVSFSLRRGEILGIAGLVGAGRTELVQCLFG-AYPGRWEGEIFidGKpvKIRNPQQAIA 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 76 QNVGYLPSEVHFYD---DMKVIDLLKYSAgfYKKF-NQKRMKELAE---------RLDL---DLHKKIEDLSFGNRKKVG 139
Cdd:PRK13549 338 QGIAMVPEDRKRDGivpVMGVGKNITLAA--LDRFtGGSRIDDAAElktilesiqRLKVktaSPELAIARLSGGNQQKAV 415
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1021811607 140 IVQALLHEPKLLILDEPTGGLDPLMQNTFFEILTEEREKGTTIIFSSHILSEVQKMCDRVAIIKEGELVKVETIENLT 217
Cdd:PRK13549 416 LAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKLKGDLINHNLT 493
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
4-216 |
1.63e-17 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 81.30 E-value: 1.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 4 IDVKNLTKTYKKNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQSKEIR------QN 77
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRdicmvfQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 78 VGYLPsevHfyddMKVIDLLKYS---AGFYKKFNQKRMKELAERLDLD--LHKKIEDLSFGNRKKVGIVQALLHEPKLLI 152
Cdd:PRK11432 87 YALFP---H----MSLGENVGYGlkmLGVPKEERKQRVKEALELVDLAgfEDRYVDQISGGQQQRVALARALILKPKVLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1021811607 153 LDEPTGGLDPLMQNTFFEILTEEREK-GTTIIFSSHILSEVQKMCDRVAIIKEGELVKVETIENL 216
Cdd:PRK11432 160 FDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
6-207 |
2.59e-17 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 79.34 E-value: 2.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 6 VKNLTKTYKKNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRtLLNFLYPTSGSATIFGKDIVKQSKE-IR---QNVGYL 81
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLR-LLAGLETPSAGELLAGTAPLAEAREdTRlmfQDARLL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 82 PSEvhfyddmKVIDllKYSAGFYKKFNQKRMKELAErldLDLHKKIED----LSFGNRKKVGIVQALLHEPKLLILDEPT 157
Cdd:PRK11247 94 PWK-------KVID--NVGLGLKGQWRDAALQALAA---VGLADRANEwpaaLSGGQKQRVALARALIHRPGLLLLDEPL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1021811607 158 GGLDPL----MQNtffeiLTEE--REKGTTIIFSSHILSEVQKMCDRVAIIKEGEL 207
Cdd:PRK11247 162 GALDALtrieMQD-----LIESlwQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
4-208 |
2.63e-17 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 79.43 E-value: 2.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 4 IDVKNLTKTYKKNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVK-QSKEIRQNVGYLP 82
Cdd:PRK13548 3 LEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADwSPAELARRRAVLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 83 --SEVHFydDMKVID-----LLKYSAGfykkfnQKRMKELA----ERLDLD--LHKKIEDLSFGNRKKVGIVQALL---- 145
Cdd:PRK13548 83 qhSSLSF--PFTVEEvvamgRAPHGLS------RAEDDALVaaalAQVDLAhlAGRDYPQLSGGEQQRVQLARVLAqlwe 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1021811607 146 --HEPKLLILDEPTGGLDPLMQNTFFEILTE-EREKGTTIIFSSHILSEVQKMCDRVAIIKEGELV 208
Cdd:PRK13548 155 pdGPPRWLLLDEPTSALDLAHQHHVLRLARQlAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLV 220
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-209 |
3.14e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 79.32 E-value: 3.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 5 DVKNLTKTYK--KNRGIV-NLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFL------YPTSGSATIFGKDIVK-QSKEI 74
Cdd:PRK14246 9 DVFNISRLYLyiNDKAILkDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIeiydskIKVDGKVLYFGKDIFQiDAIKL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 75 RQNVGYLPSEVHFYDDMKVIDLLKY---SAGFYKKFNQKRMKELAERlDLDLHKKIED--------LSFGNRKKVGIVQA 143
Cdd:PRK14246 89 RKEVGMVFQQPNPFPHLSIYDNIAYplkSHGIKEKREIKKIVEECLR-KVGLWKEVYDrlnspasqLSGGQQQRLTIARA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1021811607 144 LLHEPKLLILDEPTGGLDpLMQNTFFEILTEEREKGTTIIFSSHILSEVQKMCDRVAIIKEGELVK 209
Cdd:PRK14246 168 LALKPKVLLMDEPTSMID-IVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVE 232
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-208 |
3.47e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 81.41 E-value: 3.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 4 IDVKNLTKTYKKNRGIV--NLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQSKE-IRQNVGY 80
Cdd:PRK11160 339 LTLNNVSFTYPDQPQPVlkGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAaLRQAISV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 81 LPSEVH-FYDDMKviDLLKYSAgfyKKFNQKRMKELAERLDLDlhKKIED--------------LSFGNRKKVGIVQALL 145
Cdd:PRK11160 419 VSQRVHlFSATLR--DNLLLAA---PNASDEALIEVLQQVGLE--KLLEDdkglnawlgeggrqLSGGEQRRLGIARALL 491
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1021811607 146 HEPKLLILDEPTGGLDplmQNTFFEILTEERE--KGTTIIFSSHILSEVQKMcDRVAIIKEGELV 208
Cdd:PRK11160 492 HDAPLLLLDEPTEGLD---AETERQILELLAEhaQNKTVLMITHRLTGLEQF-DRICVMDNGQII 552
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
27-208 |
3.69e-17 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 81.25 E-value: 3.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 27 EEGEIFGFIGPNGAGKSTTIRTLLNFLYP---TSGSATIFGKDIvkQSKEIRQNVGYLPSEVHFYDDMKVIDLLKYSAGF 103
Cdd:TIGR00955 49 KPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPI--DAKEMRAISAYVQQDDLFIPTLTVREHLMFQAHL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 104 ------YKKFNQKRMKELAERLDL-----------DLHKkieDLSFGNRKKVGIVQALLHEPKLLILDEPTGGLDPLMQN 166
Cdd:TIGR00955 127 rmprrvTKKEKRERVDEVLQALGLrkcantrigvpGRVK---GLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAY 203
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1021811607 167 TFFEILTEEREKGTTIIFSSH-ILSEVQKMCDRVAIIKEGELV 208
Cdd:TIGR00955 204 SVVQVLKGLAQKGKTIICTIHqPSSELFELFDKIILMAEGRVA 246
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
3-208 |
4.61e-17 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 80.92 E-value: 4.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 3 IIDVKNLTKTYKKNRGIV----NLTFSVEEGEIFGFIGPNGAGKSttirTLLNFL----YPTSGSATIFGKDIVKQSKEI 74
Cdd:PRK10535 4 LLELKDIRRSYPSGEEQVevlkGISLDIYAGEMVAIVGASGSGKS----TLMNILgcldKPTSGTYRVAGQDVATLDADA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 75 -----RQNVGYLPSEVHFYDDMKV---IDLLKYSAGFYKKFNQKRMKELAERLDLD--LHKKIEDLSFGNRKKVGIVQAL 144
Cdd:PRK10535 80 laqlrREHFGFIFQRYHLLSHLTAaqnVEVPAVYAGLERKQRLLRAQELLQRLGLEdrVEYQPSQLSGGQQQRVSIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1021811607 145 LHEPKLLILDEPTGGLDPLMQNTFFEILTEEREKGTTIIFSSHIlSEVQKMCDRVAIIKEGELV 208
Cdd:PRK10535 160 MNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHD-PQVAAQAERVIEIRDGEIV 222
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
21-205 |
5.41e-17 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 78.49 E-value: 5.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 21 NLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQS--KEIRQNVGYLPSEVHFYDDMKVID--- 95
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPghQIARMGVVRTFQHVRLFREMTVIEnll 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 96 --------------LLKYSAgfYKKFNQKRMKELAERLD----LDL-HKKIEDLSFGNRKKVGIVQALLHEPKLLILDEP 156
Cdd:PRK11300 103 vaqhqqlktglfsgLLKTPA--FRRAESEALDRAATWLErvglLEHaNRQAGNLAYGQQRRLEIARCMVTQPEILMLDEP 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1021811607 157 TGGLDPLMQNTFFEILTEER-EKGTTIIFSSHILSEVQKMCDRVAIIKEG 205
Cdd:PRK11300 181 AAGLNPKETKELDELIAELRnEHNVTVLLIEHDMKLVMGISDRIYVVNQG 230
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-230 |
5.42e-17 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 80.64 E-value: 5.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 3 IIDVKNLTKTYKKNRGIV---NLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNfLYPTSGSATIF--GK--DIVKQSKEIR 75
Cdd:TIGR02633 257 ILEARNLTCWDVINPHRKrvdDVSFSLRRGEILGVAGLVGAGRTELVQALFG-AYPGKFEGNVFinGKpvDIRNPAQAIR 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 76 QNVGYLPSEVH---FYDDMKVIDLLKYSAgfYKKFNQK-RMKELAERLDLD-----LHKK-------IEDLSFGNRKKVG 139
Cdd:TIGR02633 336 AGIAMVPEDRKrhgIVPILGVGKNITLSV--LKSFCFKmRIDAAAELQIIGsaiqrLKVKtaspflpIGRLSGGNQQKAV 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 140 IVQALLHEPKLLILDEPTGGLDPLMQNTFFEILTEEREKGTTIIFSSHILSEVQKMCDRVAIIKEGELvkvetienltKN 219
Cdd:TIGR02633 414 LAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKL----------KG 483
|
250
....*....|.
gi 1021811607 220 NLKNITITFEQ 230
Cdd:TIGR02633 484 DFVNHALTQEQ 494
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
4-248 |
6.86e-17 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 78.20 E-value: 6.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 4 IDVKNLTKTYKKNRGIVNLTFSVEEGEIFGFIGPNGAGKSttirTLLNF----LYPTSGSATIFGKDIVKQ-SKEIRQNV 78
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKS----TLLSMisrlLPPDSGEVLVDGLDVATTpSRELAKRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 79 GYLPSEVHFYDDMKVIDLLK-----YSAGFYKKFNQKRMKELAERLDL-DL-HKKIEDLSFGNRKKVGIVQALLHEPKLL 151
Cdd:COG4604 78 AILRQENHINSRLTVRELVAfgrfpYSKGRLTAEDREIIDEAIAYLDLeDLaDRYLDELSGGQRQRAFIAMVLAQDTDYV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 152 ILDEPTGGLDP-----LMQNtfFEILTEEREKgTTII------FSSHilsevqkMCDRVAIIKEGELVKVETIEN-LTKN 219
Cdd:COG4604 158 LLDEPLNNLDMkhsvqMMKL--LRRLADELGK-TVVIvlhdinFASC-------YADHIVAMKDGRVVAQGTPEEiITPE 227
|
250 260
....*....|....*....|....*....
gi 1021811607 220 NLKNItitFEqtnaIDFDLEgivkkEING 248
Cdd:COG4604 228 VLSDI---YD----TDIEVE-----EIDG 244
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
3-227 |
7.32e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 78.49 E-value: 7.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 3 IIDVKNLTKTYKKNR-GIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQSK--EIRQNVG 79
Cdd:PRK13644 1 MIRLENVSYSYPDGTpALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKlqGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 80 --YLPSEVHFYDDMKVIDLlkysagfykKFNQKRM----KELAERLDLDL---------HKKIEDLSFGNRKKVGIVQAL 144
Cdd:PRK13644 81 ivFQNPETQFVGRTVEEDL---------AFGPENLclppIEIRKRVDRALaeiglekyrHRSPKTLSGGQGQCVALAGIL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 145 LHEPKLLILDEPTGGLDPLMQNTFFEILTEEREKGTTIIFSSHILSEVQkMCDRVAIIKEGELVKVETIEN-LTKNNLKN 223
Cdd:PRK13644 152 TMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELH-DADRIIVMDRGKIVLEGEPENvLSDVSLQT 230
|
....
gi 1021811607 224 ITIT 227
Cdd:PRK13644 231 LGLT 234
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
21-195 |
7.49e-17 |
|
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: 77.01 E-value: 7.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 21 NLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQSKEIRQNVGYLPSEVHFYDDMKVIDLLKYS 100
Cdd:TIGR01189 18 GLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPELSALENLHFW 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 101 AGFYKKfNQKRMKELAERLDLDLHKKI--EDLSFGNRKKVGIVQALLHEPKLLILDEPTGGLDPLMQNTFFEILTEEREK 178
Cdd:TIGR01189 98 AAIHGG-AQRTIEDALAAVGLTGFEDLpaAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGLLRAHLAR 176
|
170 180
....*....|....*....|
gi 1021811607 179 GTTIIFSSHI---LSEVQKM 195
Cdd:TIGR01189 177 GGIVLLTTHQdlgLVEAREL 196
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-210 |
9.18e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 78.03 E-value: 9.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 1 MKIIDVKNLTKTYKKNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTL--LNFLYP---TSGSATIFGKDIVKQS-KEI 74
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFnrLIELYPearVSGEVYLDGQDIFKMDvIEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 75 RQNVGYLPSEVHFYDDMKVIDllkySAGFYKKFNQ--KRMKELAERLDLDLHK-----KIED--------LSFGNRKKVG 139
Cdd:PRK14247 81 RRRVQMVFQIPNPIPNLSIFE----NVALGLKLNRlvKSKKELQERVRWALEKaqlwdEVKDrldapagkLSGGQQQRLC 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1021811607 140 IVQALLHEPKLLILDEPTGGLDPlmQNTF-FEILTEEREKGTTIIFSSHILSEVQKMCDRVAIIKEGELVKV 210
Cdd:PRK14247 157 IARALAFQPEVLLADEPTANLDP--ENTAkIESLFLELKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEW 226
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
24-216 |
1.22e-16 |
|
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: 78.99 E-value: 1.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 24 FSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQSKEI-----RQNVGYLPSEVHFYDDMKVIDLLK 98
Cdd:COG4148 20 FTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARGIflpphRRRIGYVFQEARLFPHLSVRGNLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 99 YSAGFYKKFNQK-RMKELAERLDLD--LHKKIEDLSFGNRKKVGIVQALLHEPKLLILDEPTGGLDplmQNTFFEILTE- 174
Cdd:COG4148 100 YGRKRAPRAERRiSFDEVVELLGIGhlLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALD---LARKAEILPYl 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1021811607 175 ER---EKGTTIIFSSHILSEVQKMCDRVAIIKEGELVKVETIENL 216
Cdd:COG4148 177 ERlrdELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEV 221
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-223 |
1.30e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 77.77 E-value: 1.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 4 IDVKNLTKTYKKNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTL-----LNFLYPTSGSATIFGKDIVKQS---KEIR 75
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLnrmneLESEVRVEGRVEFFNQNIYERRvnlNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 76 QNVGYLPSEVHFYDdMKVIDLLKYSA---GFYKKF-------NQKRMKELAERLDLDLHKKIEDLSFGNRKKVGIVQALL 145
Cdd:PRK14258 88 RQVSMVHPKPNLFP-MSVYDNVAYGVkivGWRPKLeiddiveSALKDADLWDEIKHKIHKSALDLSGGQQQRLCIARALA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1021811607 146 HEPKLLILDEPTGGLDPLMQNTFFEILTEEREKGT-TIIFSSHILSEVQKMCDRVAIIKEGELVKVETIENLTKNNLKN 223
Cdd:PRK14258 167 VKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSElTMVIVSHNLHQVSRLSDFTAFFKGNENRIGQLVEFGLTKKIFN 245
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
3-208 |
1.63e-16 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 79.36 E-value: 1.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 3 IIDVKNLTKTYKKNRGIV-----------NLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNfLYPTSGSATIFGKDI---- 67
Cdd:PRK15134 275 LLDVEQLQVAFPIRKGILkrtvdhnvvvkNISFTLRPGETLGLVGESGSGKSTTGLALLR-LINSQGEIWFDGQPLhnln 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 68 VKQSKEIRQNVgylpsEVHFYDD----------MKVID--LLKYSAGFYKKFNQKRMKELAERLDLD---LHKKIEDLSF 132
Cdd:PRK15134 354 RRQLLPVRHRI-----QVVFQDPnsslnprlnvLQIIEegLRVHQPTLSAAQREQQVIAVMEEVGLDpetRHRYPAEFSG 428
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1021811607 133 GNRKKVGIVQALLHEPKLLILDEPTGGLDPLMQNTFFEILTEEREK-GTTIIFSSHILSEVQKMCDRVAIIKEGELV 208
Cdd:PRK15134 429 GQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKhQLAYLFISHDLHVVRALCHQVIVLRQGEVV 505
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
3-223 |
1.66e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 77.12 E-value: 1.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 3 IIDVKNLTKTYKKNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTL--LNFLYP---TSGSATIFGKDIVK---QSKEI 74
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPevtITGSIVYNGHNIYSprtDTVDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 75 RQNVGYL-----PSEVHFYDDM-------KVIDLLKYSAGFYKKFNQKRM-KELAERLdldlHKKIEDLSFGNRKKVGIV 141
Cdd:PRK14239 85 RKEIGMVfqqpnPFPMSIYENVvyglrlkGIKDKQVLDEAVEKSLKGASIwDEVKDRL----HDSALGLSGGQQQRVCIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 142 QALLHEPKLLILDEPTGGLDPLMQNTFFEILTEEREKgTTIIFSSHILSEVQKMCDRVAIIKEGELVKVetieNLTKNNL 221
Cdd:PRK14239 161 RVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSMQQASRISDRTGFFLDGDLIEY----NDTKQMF 235
|
..
gi 1021811607 222 KN 223
Cdd:PRK14239 236 MN 237
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
3-221 |
1.69e-16 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 79.28 E-value: 1.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 3 IIDVKNLTKTYKKNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIV----KQSKE----- 73
Cdd:PRK10762 4 LLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfngpKSSQEagigi 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 74 IRQNVGYLPSEV---------HFYDDMKVIDllkysagfYKKFNQKRMKELAeRLDL--DLHKKIEDLSFGNRKKVGIVQ 142
Cdd:PRK10762 84 IHQELNLIPQLTiaeniflgrEFVNRFGRID--------WKKMYAEADKLLA-RLNLrfSSDKLVGELSIGEQQMVEIAK 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1021811607 143 ALLHEPKLLILDEPTGGLDPLMQNTFFEILTEEREKGTTIIFSSHILSEVQKMCDRVAIIKEGELVKVETIENLTKNNL 221
Cdd:PRK10762 155 VLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADLTEDSL 233
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
21-192 |
1.70e-16 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 75.73 E-value: 1.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 21 NLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDivkqskeirqNVGYLP--SEVhfyDD---MKVID 95
Cdd:NF040873 10 GVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGA----------RVAYVPqrSEV---PDslpLTVRD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 96 LLkySAGFYKKFNQKRMKELAERLDLD-----------LHKKIEDLSFGNRKKVGIVQALLHEPKLLILDEPTGGLDPLM 164
Cdd:NF040873 77 LV--AMGRWARRGLWRRLTRDDRAAVDdalervgladlAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAES 154
|
170 180
....*....|....*....|....*...
gi 1021811607 165 QNTFFEILTEEREKGTTIIFSSHILSEV 192
Cdd:NF040873 155 RERIIALLAEEHARGATVVVVTHDLELV 182
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
3-212 |
1.75e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 77.97 E-value: 1.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 3 IIDVKNLTKTYKKN-----RGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGsaTIFGKDI---------- 67
Cdd:PRK13631 21 ILRVKNLYCVFDEKqenelVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYG--TIQVGDIyigdkknnhe 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 68 ---------VKQSKEIRQNVGYL---PSEVHFYDDM-KVIDLLKYSAGFYKKFNQKRMKELAERLDLD---LHKKIEDLS 131
Cdd:PRK13631 99 litnpyskkIKNFKELRRRVSMVfqfPEYQLFKDTIeKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDdsyLERSPFGLS 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 132 FGNRKKVGIVQALLHEPKLLILDEPTGGLDPLMQNTFFEILTEEREKGTTIIFSSHILSEVQKMCDRVAIIKEGELVKVE 211
Cdd:PRK13631 179 GGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTG 258
|
.
gi 1021811607 212 T 212
Cdd:PRK13631 259 T 259
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-206 |
2.40e-16 |
|
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: 74.02 E-value: 2.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 4 IDVKNLTKTYKKNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGsatifgkdIVKQSKEIRqnVGYLPs 83
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEG--------IVTWGSTVK--IGYFE- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 84 evhfyddmkvidllkysagfykkfnQkrmkelaerldldlhkkiedLSFGNRKKVGIVQALLHEPKLLILDEPTGGLDPL 163
Cdd:cd03221 70 -------------------------Q--------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLE 104
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1021811607 164 MQntffEILTEE-REKGTTIIFSSHILSEVQKMCDRVAIIKEGE 206
Cdd:cd03221 105 SI----EALEEAlKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
3-218 |
2.61e-16 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 78.68 E-value: 2.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 3 IIDVKNLTKTYKKNRGIVNLTFSVEEGEIFGFIGPNGAGKSTtirtLLNFL---YPT-SGSATIFGKDIVKQSKEIRQnv 78
Cdd:NF040905 1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKST----LMKVLsgvYPHgSYEGEILFDGEVCRFKDIRD-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 79 gylpSE----VHFYDDMKVIDLLKYSAGFY-----KKF-------NQKRMKELAER--LDLDLHKKIEDLSFGNRKKVGI 140
Cdd:NF040905 75 ----SEalgiVIIHQELALIPYLSIAENIFlgnerAKRgvidwneTNRRARELLAKvgLDESPDTLVTDIGVGKQQLVEI 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1021811607 141 VQALLHEPKLLILDEPTGGLDPLMQNTFFEILTEEREKGTTIIFSSHILSEVQKMCDRVAIIKEGelvkvETIENLTK 218
Cdd:NF040905 151 AKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDG-----RTIETLDC 223
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-216 |
5.04e-16 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 77.82 E-value: 5.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 1 MKIIDVKNLTKTYKKN---RGIVN-LTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFL------YPtSGSATIFGKDIVKQ 70
Cdd:PRK15134 3 QPLLAIENLSVAFRQQqtvRTVVNdVSLQIEAGETLALVGESGSGKSVTALSILRLLpsppvvYP-SGDIRFHGESLLHA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 71 S-KEIRQNVGYLPSEVhFYDDM-----------KVIDLLKYSAGFYKKFNQKRMKELAERLDL-DLHKKIED----LSFG 133
Cdd:PRK15134 82 SeQTLRGVRGNKIAMI-FQEPMvslnplhtlekQLYEVLSLHRGMRREAARGEILNCLDRVGIrQAAKRLTDyphqLSGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 134 NRKKVGIVQALLHEPKLLILDEPTGGLDPLMQNTFFEILTE-EREKGTTIIFSSHILSEVQKMCDRVAIIKEGELVKVET 212
Cdd:PRK15134 161 ERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRElQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNR 240
|
....
gi 1021811607 213 IENL 216
Cdd:PRK15134 241 AATL 244
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
21-188 |
5.48e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 74.91 E-value: 5.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 21 NLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVkqskeirqnVGYLPSEVHFY---DDMK----V 93
Cdd:PRK13539 20 GLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDID---------DPDVAEACHYLghrNAMKpaltV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 94 IDLLKYSAGFYkkfNQKRMK--ELAERLDLD--LHKKIEDLSFGNRKKVGIVQALLHEPKLLILDEPTGGLDPLMQNTFF 169
Cdd:PRK13539 91 AENLEFWAAFL---GGEELDiaAALEAVGLAplAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFA 167
|
170
....*....|....*....
gi 1021811607 170 EILTEEREKGTTIIFSSHI 188
Cdd:PRK13539 168 ELIRAHLAQGGIVIAATHI 186
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
23-208 |
1.03e-15 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 74.62 E-value: 1.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 23 TFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQSKEIRQnVGYLPSEVHFYDDMKV---IDL--- 96
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRP-VSMLFQENNLFSHLTVaqnIGLgln 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 97 --LKYSAGfykkfNQKRMKELAERLDLD--LHKKIEDLSFGNRKKVGIVQALLHEPKLLILDEPTGGLDPLMQNTFFEIL 172
Cdd:PRK10771 98 pgLKLNAA-----QREKLHAIARQMGIEdlLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLV 172
|
170 180 190
....*....|....*....|....*....|....*..
gi 1021811607 173 TEE-REKGTTIIFSSHILSEVQKMCDRVAIIKEGELV 208
Cdd:PRK10771 173 SQVcQERQLTLLMVSHSLEDAARIAPRSLVVADGRIA 209
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
6-168 |
1.06e-15 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 74.06 E-value: 1.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 6 VKNLTKTYKKNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYP---TSGSATIFGKDIVKQSKEIRQnVGYLP 82
Cdd:COG4136 4 LENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAEQRR-IGILF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 83 SEVHFYDDMKVIDLLKYS--AGFYKKFNQKRMKELAERLDLD--LHKKIEDLSFGNRKKVGIVQALLHEPKLLILDEPTG 158
Cdd:COG4136 83 QDDLLFPHLSVGENLAFAlpPTIGRAQRRARVEQALEEAGLAgfADRDPATLSGGQRARVALLRALLAEPRALLLDEPFS 162
|
170
....*....|
gi 1021811607 159 GLDPLMQNTF 168
Cdd:COG4136 163 KLDAALRAQF 172
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
4-210 |
1.76e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 75.04 E-value: 1.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 4 IDVKNLTKTYKKN-----RGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRtLLNFLYPTSGSATIFGK-------DIVKQS 71
Cdd:PRK13645 7 IILDNVSYTYAKKtpfefKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQ-LTNGLIISETGQTIVGDyaipanlKKIKEV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 72 KEIRQNVGYL---PSEVHFYDDM-KVIDLLKYSAGFYKKFNQKRMKELAERLDL--DLHKKIE-DLSFGNRKKVGIVQAL 144
Cdd:PRK13645 86 KRLRKEIGLVfqfPEYQLFQETIeKDIAFGPVNLGENKQEAYKKVPELLKLVQLpeDYVKRSPfELSGGQKRRVALAGII 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1021811607 145 LHEPKLLILDEPTGGLDPLMQNTFFEILTE-EREKGTTIIFSSHILSEVQKMCDRVAIIKEGELVKV 210
Cdd:PRK13645 166 AMDGNTLVLDEPTGGLDPKGEEDFINLFERlNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISI 232
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
20-208 |
2.00e-15 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 74.44 E-value: 2.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 20 VNLTFSVeeGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVK-QSKEIRQNVGYLPSEVHFYDDMKVIDLL- 97
Cdd:PRK10575 30 LSLTFPA--GKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESwSSKAFARKVAYLPQQLPAAEGMTVRELVa 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 98 --KY----SAGFYKKFNQKRMKELAERLDLD--LHKKIEDLSFGNRKKVGIVQALLHEPKLLILDEPTGGLDPLMQ-NTF 168
Cdd:PRK10575 108 igRYpwhgALGRFGAADREKVEEAISLVGLKplAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQvDVL 187
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1021811607 169 FEILTEEREKGTTIIFSSHILSEVQKMCDRVAIIKEGELV 208
Cdd:PRK10575 188 ALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMI 227
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
3-208 |
2.11e-15 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 73.37 E-value: 2.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 3 IIDVKNLTKTYKKNR-GIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVK-QSKEI---RQN 77
Cdd:PRK10908 1 MIRFEHVSKAYLGGRqALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRlKNREVpflRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 78 VGYLPSEVHFYDDMKVIDLLKYS---AGFYKKFNQKRMKELAERLDL-DLHKKIE-DLSFGNRKKVGIVQALLHEPKLLI 152
Cdd:PRK10908 81 IGMIFQDHHLLMDRTVYDNVAIPliiAGASGDDIRRRVSAALDKVGLlDKAKNFPiQLSGGEQQRVGIARAVVNKPAVLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1021811607 153 LDEPTGGLDPLMQNTFFEILTEEREKGTTIIFSSHILSEVQKMCDRVAIIKEGELV 208
Cdd:PRK10908 161 ADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
21-199 |
2.55e-15 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 73.21 E-value: 2.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 21 NLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQSKEI-RQNVGYLPSEVHFYDDmKVIDLLKY 99
Cdd:PRK10247 25 NISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIyRQQVSYCAQTPTLFGD-TVYDNLIF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 100 SAGFYKKFNQ-KRMKELAERLDLDLH---KKIEDLSFGNRKKVGIVQALLHEPKLLILDEPTGGLDPLMQNTFFEILTE- 174
Cdd:PRK10247 104 PWQIRNQQPDpAIFLDDLERFALPDTiltKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRy 183
|
170 180
....*....|....*....|....*
gi 1021811607 175 EREKGTTIIFSSHILSEVQKmCDRV 199
Cdd:PRK10247 184 VREQNIAVLWVTHDKDEINH-ADKV 207
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
15-220 |
2.82e-15 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 75.77 E-value: 2.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 15 KNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQSKE-IRQNVGylpseVHFYDDM-- 91
Cdd:PRK13657 347 SRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRAsLRRNIA-----VVFQDAGlf 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 92 -----KVIDLLKYSAgfykkfNQKRMKELAERLD-LDLHKKIED------------LSFGNRKKVGIVQALLHEPKLLIL 153
Cdd:PRK13657 422 nrsieDNIRVGRPDA------TDEEMRAAAERAQaHDFIERKPDgydtvvgergrqLSGGERQRLAIARALLKDPPILIL 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1021811607 154 DEPTGGLDPLMQNTFFEILTEEREKGTTIIFsSHILSEVQKmCDRVAIIKEGELVKVETIENLTKNN 220
Cdd:PRK13657 496 DEATSALDVETEAKVKAALDELMKGRTTFII-AHRLSTVRN-ADRILVFDNGRVVESGSFDELVARG 560
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
6-209 |
2.90e-15 |
|
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: 72.56 E-value: 2.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 6 VKNLTKTYKKNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLY--PTSGSATIFGKDIVKQSKEIRQNVG-YL- 81
Cdd:cd03217 3 IKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKyeVTEGEILFKGEDITDLPPEERARLGiFLa 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 82 ---PSEVHfydDMKVIDLLKY-SAGFykkfnqkrmkelaerldldlhkkiedlSFGNRKKVGIVQALLHEPKLLILDEPT 157
Cdd:cd03217 83 fqyPPEIP---GVKNADFLRYvNEGF---------------------------SGGEKKRNEILQLLLLEPDLAILDEPD 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1021811607 158 GGLDPLMQNTFFEILTEEREKGTTIIFSSH---ILSEVQKmcDRVAIIKEGELVK 209
Cdd:cd03217 133 SGLDIDALRLVAEVINKLREEGKSVLIITHyqrLLDYIKP--DRVHVLYDGRIVK 185
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
15-205 |
2.90e-15 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 75.69 E-value: 2.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 15 KNRGIVN-LTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDiVKQSKEIRQNVGYLPSEVHFYDDMKV 93
Cdd:PLN03211 79 QERTILNgVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNFTGTILANN-RKPTKQILKRTGFVTQDDILYPHLTV 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 94 IDLLKYSA--GFYKKFNQKRMKELAERL--DLDLHKK---------IEDLSFGNRKKVGIVQALLHEPKLLILDEPTGGL 160
Cdd:PLN03211 158 RETLVFCSllRLPKSLTKQEKILVAESVisELGLTKCentiignsfIRGISGGERKRVSIAHEMLINPSLLILDEPTSGL 237
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1021811607 161 DPLMQNTFFEILTEEREKGTTIIFSSH-ILSEVQKMCDRVAIIKEG 205
Cdd:PLN03211 238 DATAAYRLVLTLGSLAQKGKTIVTSMHqPSSRVYQMFDSVLVLSEG 283
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
3-210 |
3.63e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 75.28 E-value: 3.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 3 IIDVKNLTKTYKKNRGIVN-----------LTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGK--DIVK 69
Cdd:PRK10261 313 ILQVRNLVTRFPLRSGLLNrvtrevhavekVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQriDTLS 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 70 QSK-------------------EIRQNVGYlpsevHFYDDMKVIDLLKYSAGfykkfnQKRMKELAERLDLDLH---KKI 127
Cdd:PRK10261 393 PGKlqalrrdiqfifqdpyaslDPRQTVGD-----SIMEPLRVHGLLPGKAA------AARVAWLLERVGLLPEhawRYP 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 128 EDLSFGNRKKVGIVQALLHEPKLLILDEPTGGLDPLMQNTFFEILTE-EREKGTTIIFSSHILSEVQKMCDRVAIIKEGE 206
Cdd:PRK10261 462 HEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDlQRDFGIAYLFISHDMAVVERISHRVAVMYLGQ 541
|
....
gi 1021811607 207 LVKV 210
Cdd:PRK10261 542 IVEI 545
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
2-251 |
4.33e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 73.58 E-value: 4.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 2 KIIDVKNLTKTYKKNR------GIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQSK--E 73
Cdd:PRK13633 3 EMIKCKNVSYKYESNEesteklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENlwD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 74 IRQNVGYL---PsevhfyDDMKVIDLLKYSAGF-------YKKFNQKRMKELAERLDLDLHKKIED--LSFGNRKKVGIV 141
Cdd:PRK13633 83 IRNKAGMVfqnP------DNQIVATIVEEDVAFgpenlgiPPEEIRERVDESLKKVGMYEYRRHAPhlLSGGQKQRVAIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 142 QALLHEPKLLILDEPTGGLDPL----MQNTFFEIlteEREKGTTIIFSSHILSEVQKmCDRVAIIKEGELVKVETIENLT 217
Cdd:PRK13633 157 GILAMRPECIIFDEPTAMLDPSgrreVVNTIKEL---NKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIF 232
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1021811607 218 KN--NLKNITITFEQTNAIDFDL--EGI-VKKEI-NGSEM 251
Cdd:PRK13633 233 KEveMMKKIGLDVPQVTELAYELkkEGVdIPSDIlTIDEM 272
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
3-191 |
5.40e-15 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 72.81 E-value: 5.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 3 IIDVKNLTKTYKKNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQSKE---IRQNVG 79
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAErgvVFQNEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 80 YLPSEvhfyddmKVIDLLKYS---AGFYKKFNQKRMKELAERLDLD--LHKKIEDLSFGNRKKVGIVQALLHEPKLLILD 154
Cdd:PRK11248 81 LLPWR-------NVQDNVAFGlqlAGVEKMQRLEIAHQMLKKVGLEgaEKRYIWQLSGGQRQRVGIARALAANPQLLLLD 153
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1021811607 155 EPTGGLDPL----MQNTffeILTEEREKGTTIIFSSHILSE 191
Cdd:PRK11248 154 EPFGALDAFtreqMQTL---LLKLWQETGKQVLLITHDIEE 191
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
4-208 |
6.11e-15 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 74.67 E-value: 6.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 4 IDVKNLTKTY--KKNRGIVNLTFSVEEGEIFGFIGPNGAGKSTtIRTLLNFLYP-TSGSATIFGKDIVKQS-KEIRQNVG 79
Cdd:PRK11176 342 IEFRNVTFTYpgKEVPALRNINFKIPAGKTVALVGRSGSGKST-IANLLTRFYDiDEGEILLDGHDLRDYTlASLRNQVA 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 80 YLPSEVHFYDDmKVIDLLKYSA-GFYKKFNQKRMKELA------ERLDLDLHKKIED----LSFGNRKKVGIVQALLHEP 148
Cdd:PRK11176 421 LVSQNVHLFND-TIANNIAYARtEQYSREQIEEAARMAyamdfiNKMDNGLDTVIGEngvlLSGGQRQRIAIARALLRDS 499
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 149 KLLILDEPTGGLDPLMQNTFFEILtEEREKGTTIIFSSHILSEVQKmCDRVAIIKEGELV 208
Cdd:PRK11176 500 PILILDEATSALDTESERAIQAAL-DELQKNRTSLVIAHRLSTIEK-ADEILVVEDGEIV 557
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-208 |
6.94e-15 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 74.54 E-value: 6.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 4 IDVKNLTKTYKKNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSatifgkdiVKQSKEIrqNVGYLP- 82
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGT--------VKWSENA--NIGYYAq 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 83 -SEVHFYDDMKVIDLLkysagfyKKFNQKRMKELAERLDL--------DLHKKIEDLSFGNRKKVGIVQALLHEPKLLIL 153
Cdd:PRK15064 390 dHAYDFENDLTLFDWM-------SQWRQEGDDEQAVRGTLgrllfsqdDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVM 462
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1021811607 154 DEPTGGLDplMQNtfFEILTEEREKGT-TIIFSSHILSEVQKMCDRVAIIKEGELV 208
Cdd:PRK15064 463 DEPTNHMD--MES--IESLNMALEKYEgTLIFVSHDREFVSSLATRIIEITPDGVV 514
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
3-161 |
8.03e-15 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 74.46 E-value: 8.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 3 IIDVKNLTKTYKknrgivNLTFSVEEGEIF-----GFIGPNGAGKSTTIRTLLNFLYPTSGSAtifgkdivkqSKEIRqn 77
Cdd:PRK13409 340 LVEYPDLTKKLG------DFSLEVEGGEIYegeviGIVGPNGIGKTTFAKLLAGVLKPDEGEV----------DPELK-- 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 78 VGYLPSEVHFYDDMKVIDLL-----KYSAGFYKkfnqkrmKELAERLDLD--LHKKIEDLSFGNRKKVGIVQALLHEPKL 150
Cdd:PRK13409 402 ISYKPQYIKPDYDGTVEDLLrsitdDLGSSYYK-------SEIIKPLQLErlLDKNVKDLSGGELQRVAIAACLSRDADL 474
|
170
....*....|.
gi 1021811607 151 LILDEPTGGLD 161
Cdd:PRK13409 475 YLLDEPSAHLD 485
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-161 |
8.54e-15 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 74.20 E-value: 8.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 2 KIIDVKNLTKTYKKNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIfGKDI----VKQSKEI--- 74
Cdd:TIGR03719 321 KVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVklayVDQSRDAldp 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 75 RQNVGYLPSevhfyDDMKVIDLLKY---SAGFYKKFNQKrmkelaerlDLDLHKKIEDLSFGNRKKVGIVQALLHEPKLL 151
Cdd:TIGR03719 400 NKTVWEEIS-----GGLDIIKLGKReipSRAYVGRFNFK---------GSDQQKKVGQLSGGERNRVHLAKTLKSGGNVL 465
|
170
....*....|
gi 1021811607 152 ILDEPTGGLD 161
Cdd:TIGR03719 466 LLDEPTNDLD 475
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
22-188 |
1.29e-14 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 70.98 E-value: 1.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 22 LTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQSKEIRQNVGYLPSEVHFYDDMKVIDLLKysa 101
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENLR--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 102 gFYKKFNQKRMKELA-ERLDLD--LHKKIEDLSFGNRKKVGIVQALLHEPKLLILDEPTGGLDPLMQNTFFEILTEEREK 178
Cdd:cd03231 96 -FWHADHSDEQVEEAlARVGLNgfEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGHCAR 174
|
170
....*....|
gi 1021811607 179 GTTIIFSSHI 188
Cdd:cd03231 175 GGMVVLTTHQ 184
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
20-162 |
1.34e-14 |
|
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: 73.55 E-value: 1.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 20 VNLTfsVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQSK-EIRQNVGYLPSEVHFYDdMKVIDLLK 98
Cdd:TIGR02868 354 VSLD--LPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQdEVRRRVSVCAQDAHLFD-TTVRENLR 430
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1021811607 99 YSAG------FYKKFNQKRMKELAERLDLDLHKKI-ED---LSFGNRKKVGIVQALLHEPKLLILDEPTGGLDP 162
Cdd:TIGR02868 431 LARPdatdeeLWAALERVGLADWLRALPDGLDTVLgEGgarLSGGERQRLALARALLADAPILLLDEPTEHLDA 504
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
22-220 |
1.55e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 73.86 E-value: 1.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 22 LTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQS-KEIRQNVGYLPSEVHFYDDMKVIDLLKYS 100
Cdd:PLN03232 1255 LSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGlTDLRRVLSIIPQSPVLFSGTVRFNIDPFS 1334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 101 ----AGFYKKFNQKRMKELAER----LDLDLHKKIEDLSFGNRKKVGIVQALLHEPKLLILDEPTGGL----DPLMQNTF 168
Cdd:PLN03232 1335 ehndADLWEALERAHIKDVIDRnpfgLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVdvrtDSLIQRTI 1414
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1021811607 169 feiltEEREKGTTIIFSSHILSEVQKmCDRVAIIKEGELVKVETIENLTKNN 220
Cdd:PLN03232 1415 -----REEFKSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSRD 1460
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
22-219 |
3.60e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 72.85 E-value: 3.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 22 LTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQS-KEIRQNVGYLP-SEVHFYDDMKvIDLLKY 99
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGlMDLRKVLGIIPqAPVLFSGTVR-FNLDPF 1336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 100 S----AGFYKKFNQKRMKELAER----LDLDLHKKIEDLSFGNRKKVGIVQALLHEPKLLILDEPTG----GLDPLMQNT 167
Cdd:PLN03130 1337 NehndADLWESLERAHLKDVIRRnslgLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAavdvRTDALIQKT 1416
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1021811607 168 FfeiltEEREKGTTIIFSSHILSEVQKmCDRVAIIKEGELVKVETIENLTKN 219
Cdd:PLN03130 1417 I-----REEFKSCTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPENLLSN 1462
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
2-209 |
4.74e-14 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 70.59 E-value: 4.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 2 KIIDVKNLTKTYKKNRG---------IVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATI------FGkD 66
Cdd:PRK15112 3 TLLEVRNLSKTFRYRTGwfrrqtveaVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIddhplhFG-D 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 67 IVKQSKEI-------------RQNVGYL--------------PSEVHFYDDMKVIDLLKYSAGFYKKFnqkrmkelaerl 119
Cdd:PRK15112 82 YSYRSQRIrmifqdpstslnpRQRISQIldfplrlntdlepeQREKQIIETLRQVGLLPDHASYYPHM------------ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 120 dldlhkkiedLSFGNRKKVGIVQALLHEPKLLILDEPTGGLDPLMQNTFFEILTEEREK-GTTIIFSSHILSEVQKMCDR 198
Cdd:PRK15112 150 ----------LAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKqGISYIYVTQHLGMMKHISDQ 219
|
250
....*....|.
gi 1021811607 199 VAIIKEGELVK 209
Cdd:PRK15112 220 VLVMHQGEVVE 230
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
4-212 |
4.75e-14 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 71.27 E-value: 4.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 4 IDVKNLTKTYKKNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQSKEIRQnVGYLPS 83
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRK-VGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 84 EVHFYDDMKVIDLLKY------------SAGFYKKFNQ----KRMKELAERLDldlhkkiEDLSFGNRKKVGIVQALLHE 147
Cdd:PRK10851 82 HYALFRHMTVFDNIAFgltvlprrerpnAAAIKAKVTQllemVQLAHLADRYP-------AQLSGGQKQRVALARALAVE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1021811607 148 PKLLILDEPTGGLDPLMQNTFFEILTE-EREKGTTIIFSSHILSEVQKMCDRVAIIKEGELVKVET 212
Cdd:PRK10851 155 PQILLLDEPFGALDAQVRKELRRWLRQlHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGT 220
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
4-207 |
6.87e-14 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 70.00 E-value: 6.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 4 IDVKNLTKTYKKNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLlNFL-YPTSGSATIFGKDIV-------------- 68
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCI-NFLeKPSEGSIVVNGQTINlvrdkdgqlkvadk 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 69 KQSKEIRQNVGYLPSEVHFYDDMKVIDLLKYSA----GFYKKFNQKRMKELAERLDLDLHKKIE---DLSFGNRKKVGIV 141
Cdd:PRK10619 85 NQLRLLRTRLTMVFQHFNLWSHMTVLENVMEAPiqvlGLSKQEARERAVKYLAKVGIDERAQGKypvHLSGGQQQRVSIA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1021811607 142 QALLHEPKLLILDEPTGGLDPLMQNTFFEILTEEREKGTTIIFSSHILSEVQKMCDRVAIIKEGEL 207
Cdd:PRK10619 165 RALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKI 230
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
21-220 |
9.53e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 71.03 E-value: 9.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 21 NLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLyPTSGSATIFG---KDIVKQS----------------KEIRQNVgyL 81
Cdd:PRK11174 368 PLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGielRELDPESwrkhlswvgqnpqlphGTLRDNV--L 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 82 PSEVHfYDDMKVIDLLKysagfykkfnQKRMKELAERLDLDLHKKIED----LSFGNRKKVGIVQALLHEPKLLILDEPT 157
Cdd:PRK11174 445 LGNPD-ASDEQLQQALE----------NAWVSEFLPLLPQGLDTPIGDqaagLSVGQAQRLALARALLQPCQLLLLDEPT 513
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1021811607 158 GGLDPLMQNTFFEILTEEREKGTTIIFsSHILSEVQKMcDRVAIIKEGELVKVETIENLTKNN 220
Cdd:PRK11174 514 ASLDAHSEQLVMQALNAASRRQTTLMV-THQLEDLAQW-DQIWVMQDGQIVQQGDYAELSQAG 574
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
25-228 |
3.75e-13 |
|
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: 67.43 E-value: 3.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 25 SVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDivkqskeirqnVGYLPSEVHFYDDMKVIDLL------K 98
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDT-----------VSYKPQYIKADYEGTVRDLLssitkdF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 99 YSAGFYKkfnqkrmKELAERLDLD--LHKKIEDLSFGNRKKVGIVQALLHEPKLLILDEPTGGLDP---LMQNTFFEILT 173
Cdd:cd03237 90 YTHPYFK-------TEIAKPLQIEqiLDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVeqrLMASKVIRRFA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1021811607 174 EEREKGTTIIfsSHILSEVQKMCDRVaIIKEGElVKVETIENLTKNN-------LKNITITF 228
Cdd:cd03237 163 ENNEKTAFVV--EHDIIMIDYLADRL-IVFEGE-PSVNGVANPPQSLrsgmnrfLKNLDITF 220
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
25-161 |
3.80e-13 |
|
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: 69.43 E-value: 3.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 25 SVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSAtifgkdivkqSKEIRqnVGYLPSEVHFYDDMKVIDLL------K 98
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV----------DEDLK--ISYKPQYISPDYDGTVEEFLrsantdD 429
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1021811607 99 YSAGFYKkfnqkrmKELAERLDLD--LHKKIEDLSFGNRKKVGIVQALLHEPKLLILDEPTGGLD 161
Cdd:COG1245 430 FGSSYYK-------TEIIKPLGLEklLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 487
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-160 |
3.88e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 67.45 E-value: 3.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 3 IIDVKNLTKTYKKNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTI-----RTLlnflyPTSGSATIFGKDIVKQSK-EI-R 75
Cdd:COG4674 10 ILYVEDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMdvitgKTR-----PDSGSVLFGGTDLTGLDEhEIaR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 76 QNVG---YLPSeVhfYDDMKVIDLLKYSAGFYK--------KFNQK---RMKELAERLDLD--LHKKIEDLSFGNRKKVG 139
Cdd:COG4674 85 LGIGrkfQKPT-V--FEELTVFENLELALKGDRgvfaslfaRLTAEerdRIEEVLETIGLTdkADRLAGLLSHGQKQWLE 161
|
170 180
....*....|....*....|.
gi 1021811607 140 IVQALLHEPKLLILDEPTGGL 160
Cdd:COG4674 162 IGMLLAQDPKLLLLDEPVAGM 182
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
3-216 |
6.45e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 68.73 E-value: 6.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 3 IIDVKNLTKTYKKNRGIV----NLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGK----------DIV 68
Cdd:PRK10261 12 VLAVENLNIAFMQEQQKIaavrNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMllrrrsrqviELS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 69 KQSKEIRQNVGYLPSEVHFYDDMK-------VIDLLKYSAGFYKKFNQKRMKELAERLdLD----------LHKKIEDLS 131
Cdd:PRK10261 92 EQSAAQMRHVRGADMAMIFQEPMTslnpvftVGEQIAESIRLHQGASREEAMVEAKRM-LDqvripeaqtiLSRYPHQLS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 132 FGNRKKVGIVQALLHEPKLLILDEPTGGLDPLMQNTFFE---ILTEEREKGttIIFSSHILSEVQKMCDRVAIIKEGELV 208
Cdd:PRK10261 171 GGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQlikVLQKEMSMG--VIFITHDMGVVAEIADRVLVMYQGEAV 248
|
....*...
gi 1021811607 209 KVETIENL 216
Cdd:PRK10261 249 ETGSVEQI 256
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
3-219 |
6.77e-13 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 67.11 E-value: 6.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 3 IIDVKNLTKTYKKNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTL--LNFLYPT---SGSATIFGKDIVKQS---KEI 74
Cdd:PRK14243 10 VLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFnrLNDLIPGfrvEGKVTFHGKNLYAPDvdpVEV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 75 RQNVGYL-----PSEVHFYDDMkvidllkysaGFYKKFN--QKRMKELAER------LDLDLHKKIED----LSFGNRKK 137
Cdd:PRK14243 90 RRRIGMVfqkpnPFPKSIYDNI----------AYGARINgyKGDMDELVERslrqaaLWDEVKDKLKQsglsLSGGQQQR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 138 VGIVQALLHEPKLLILDEPTGGLDPLMQNTFFEILTEEREKgTTIIFSSHILSEVQKMCDRVAI---------IKEGELV 208
Cdd:PRK14243 160 LCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHNMQQAARVSDMTAFfnvelteggGRYGYLV 238
|
250
....*....|.
gi 1021811607 209 KVETIENLTKN 219
Cdd:PRK14243 239 EFDRTEKIFNS 249
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
3-170 |
9.22e-13 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 68.23 E-value: 9.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 3 IIDVKNLTKTYKKNRGIVNLTFSVEEGEIFGFIGPNGAGKSTtirtLLNFL----YPTSGSATIFGKDIvkQSKEIRQNV 78
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSS----LLSLIagarKIQQGRVEVLGGDM--ADARHRRAV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 79 G----YLPSEV--HFYDDMKV---IDLlkysagFYKKFNQKRmkelAERldldlHKKIEDL-------SFGNR------- 135
Cdd:NF033858 75 CpriaYMPQGLgkNLYPTLSVfenLDF------FGRLFGQDA----AER-----RRRIDELlratglaPFADRpagklsg 139
|
170 180 190
....*....|....*....|....*....|....*...
gi 1021811607 136 ---KKVGIVQALLHEPKLLILDEPTGGLDPLMQNTFFE 170
Cdd:NF033858 140 gmkQKLGLCCALIHDPDLLILDEPTTGVDPLSRRQFWE 177
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
2-209 |
9.24e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 67.04 E-value: 9.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 2 KIIDVKNLTKTYKKNRGIVNL---TFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQSK-EIRQN 77
Cdd:PRK13642 3 KILEVENLVFKYEKESDVNQLngvSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVwNLRRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 78 VGYLPSEVhfyDDMKVIDLLKYSAGFYKKFNQKRMKELAERLD--------LDLH-KKIEDLSFGNRKKVGIVQALLHEP 148
Cdd:PRK13642 83 IGMVFQNP---DNQFVGATVEDDVAFGMENQGIPREEMIKRVDeallavnmLDFKtREPARLSGGQKQRVAVAGIIALRP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1021811607 149 KLLILDEPTGGLDPLMQNTFFEILTEEREK-GTTIIFSSHILSEVQKmCDRVAIIKEGELVK 209
Cdd:PRK13642 160 EIIILDESTSMLDPTGRQEIMRVIHEIKEKyQLTVLSITHDLDEAAS-SDRILVMKAGEIIK 220
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2-207 |
2.09e-12 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 66.92 E-value: 2.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 2 KIIDVKNLTKTYKKNR---GIVNLTfsVEEGEIFGFIGPNGAGKSTTIRtLLNFLY-PTSGSATIFGKDI-VKQSKEIRQ 76
Cdd:PRK10522 321 QTLELRNVTFAYQDNGfsvGPINLT--IKRGELLFLIGGNGSGKSTLAM-LLTGLYqPQSGEILLDGKPVtAEQPEDYRK 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 77 NVGYLPSEVHFYDDmkvidLLKySAGFYKkfNQKRMKELAERLDLDlHK-KIED-------LSFGNRKKVGIVQALLHEP 148
Cdd:PRK10522 398 LFSAVFTDFHLFDQ-----LLG-PEGKPA--NPALVEKWLERLKMA-HKlELEDgrisnlkLSKGQKKRLALLLALAEER 468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 149 KLLILDEPTGGLDPLMQNTFF-EILTEEREKGTTIIFSSHILSEVQkMCDRVAIIKEGEL 207
Cdd:PRK10522 469 DILLLDEWAADQDPHFRREFYqVLLPLLQEMGKTIFAISHDDHYFI-HADRLLEMRNGQL 527
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
4-216 |
2.18e-12 |
|
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: 65.65 E-value: 2.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 4 IDVKNLTKTYKKNRGIV--NLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYpTSGSATIFGKDIVKQS-KEIRQNVGY 80
Cdd:cd03289 3 MTVKDLTAKYTEGGNAVleNISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPlQKWRKAFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 81 LPSEVHFYDDMKVIDLLKYSA----GFYKKFNQKRMKELAERLDLDLHKKIED----LSFGNRKKVGIVQALLHEPKLLI 152
Cdd:cd03289 82 IPQKVFIFSGTFRKNLDPYGKwsdeEIWKVAEEVGLKSVIEQFPGQLDFVLVDggcvLSHGHKQLMCLARSVLSKAKILL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1021811607 153 LDEPTGGLDPLMQNTFFEILtEEREKGTTIIFSSHILsEVQKMCDRVAIIKEGELVKVETIENL 216
Cdd:cd03289 162 LDEPSAHLDPITYQVIRKTL-KQAFADCTVILSEHRI-EAMLECQRFLVIEENKVRQYDSIQKL 223
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
3-219 |
2.21e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 67.06 E-value: 2.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 3 IIDVKNLTKtyKKNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQS----------- 71
Cdd:PRK10982 250 ILEVRNLTS--LRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNaneainhgfal 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 72 -KEIRQNVG-YLPSEVHFYDDMKVIDLLKYSAGFykkFNQKRMKE------LAERLDLDLHK-KIEDLSFGNRKKVGIVQ 142
Cdd:PRK10982 328 vTEERRSTGiYAYLDIGFNSLISNIRNYKNKVGL---LDNSRMKSdtqwviDSMRVKTPGHRtQIGSLSGGNQQKVIIGR 404
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1021811607 143 ALLHEPKLLILDEPTGGLDPLMQNTFFEILTEEREKGTTIIFSSHILSEVQKMCDRVAIIKEGELVKVETIENLTKN 219
Cdd:PRK10982 405 WLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLVAGIVDTKTTTQN 481
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
2-207 |
2.86e-12 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 64.80 E-value: 2.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 2 KIIDVKNLTKTYKKNRGIVNLTFSVE----EGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQSKEIR-- 75
Cdd:PRK10584 5 NIVEVHHLKKSVGQGEHELSILTGVElvvkRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARak 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 76 ---QNVGY------LPSEVHFYDDMKVIDLLKysaGFYKKFNQKRMKELAERLDLD--LHKKIEDLSFGNRKKVGIVQAL 144
Cdd:PRK10584 85 lraKHVGFvfqsfmLIPTLNALENVELPALLR---GESSRQSRNGAKALLEQLGLGkrLDHLPAQLSGGEQQRVALARAF 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1021811607 145 LHEPKLLILDEPTGGLDPLMQNTFFEILTE-EREKGTTIIFSSHIlSEVQKMCDRVAIIKEGEL 207
Cdd:PRK10584 162 NGRPDVLFADEPTGNLDRQTGDKIADLLFSlNREHGTTLILVTHD-LQLAARCDRRLRLVNGQL 224
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
21-187 |
2.96e-12 |
|
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: 63.33 E-value: 2.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 21 NLTFSVEEGEIFGFIGPNGAGKSTTIRTLlNFLYPtSGSATIfgkdivkqSKEIRQNVGYLPSEVHFYDdmkvidllkys 100
Cdd:cd03223 19 DLSFEIKPGDRLLITGPSGTGKSSLFRAL-AGLWP-WGSGRI--------GMPEGEDLLFLPQRPYLPL----------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 101 aGfykkfnqkrmkELAERLDLDLHKKiedLSFGNRKKVGIVQALLHEPKLLILDEPTGGLDPLMQNTFFEILteeREKGT 180
Cdd:cd03223 78 -G-----------TLREQLIYPWDDV---LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLL---KELGI 139
|
....*..
gi 1021811607 181 TIIFSSH 187
Cdd:cd03223 140 TVISVGH 146
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
19-187 |
4.90e-12 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 63.82 E-value: 4.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 19 IVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIfgkdivkqskEIRQNvgylpsevHFYDDMKVIDllk 98
Cdd:COG2401 46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCV----------DVPDN--------QFGREASLID--- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 99 ysaGFYKKFNQKRMKELAERLDLD----LHKKIEDLSFGNRKKVGIVQALLHEPKLLILDEPTGGLDPLM-QNTFFEILT 173
Cdd:COG2401 105 ---AIGRKGDFKDAVELLNAVGLSdavlWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTaKRVARNLQK 181
|
170
....*....|....
gi 1021811607 174 EEREKGTTIIFSSH 187
Cdd:COG2401 182 LARRAGITLVVATH 195
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
3-187 |
5.25e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 63.43 E-value: 5.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 3 IIDVKNLTKTYKKNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQSKEIRQNVGYL- 81
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 82 ------PS----EVHFYDdmkvidlLKYSAGFYKKFNQKRMKELAERLDLDLHKkiedLSFGNRKKVGIVQALLHEPKLL 151
Cdd:PRK13540 81 hrsginPYltlrENCLYD-------IHFSPGAVGITELCRLFSLEHLIDYPCGL----LSSGQKRQVALLRLWMSKAKLW 149
|
170 180 190
....*....|....*....|....*....|....*.
gi 1021811607 152 ILDEPTGGLDPLMQNTFFEILTEEREKGTTIIFSSH 187
Cdd:PRK13540 150 LLDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSH 185
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
4-209 |
5.45e-12 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 64.20 E-value: 5.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 4 IDVKNLTKTYKKNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNflYP----TSGSATIFGKDIVKQSKEIRQNVG 79
Cdd:TIGR01978 1 LKIKDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAG--HPsyevTSGTILFKGQDLLELEPDERARAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 80 -YL----PSEV----------------HFYDDMKVIDLLKYsagfykkfnQKRMKELAERLDLD---LHKKI-EDLSFGN 134
Cdd:TIGR01978 79 lFLafqyPEEIpgvsnleflrsalnarRSARGEEPLDLLDF---------EKLLKEKLALLDMDeefLNRSVnEGFSGGE 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1021811607 135 RKKVGIVQALLHEPKLLILDEPTGGLDPLMQNTFFEILTEEREKGTTIIFSSH---ILSEVQKmcDRVAIIKEGELVK 209
Cdd:TIGR01978 150 KKRNEILQMALLEPKLAILDEIDSGLDIDALKIVAEGINRLREPDRSFLIITHyqrLLNYIKP--DYVHVLLDGRIVK 225
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
2-214 |
6.20e-12 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 64.28 E-value: 6.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 2 KIIDVKNLTKTYKKNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNflYP----TSGSATIFGKDIVKQSKEIRQN 77
Cdd:CHL00131 6 PILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPaykiLEGDILFKGESILDLEPEERAH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 78 VGYL-----PSEVHFYDDMkviDLLKYSAGFYKKFNQKRMKE-------LAERLDLD------LHKKI-EDLSFGNRKKV 138
Cdd:CHL00131 84 LGIFlafqyPIEIPGVSNA---DFLRLAYNSKRKFQGLPELDplefleiINEKLKLVgmdpsfLSRNVnEGFSGGEKKRN 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1021811607 139 GIVQALLHEPKLLILDEPTGGLDPLMQNTFFEILTEEREKGTTIIFSSH---ILSEVQKmcDRVAIIKEGELVKVETIE 214
Cdd:CHL00131 161 EILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHyqrLLDYIKP--DYVHVMQNGKIIKTGDAE 237
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-161 |
1.06e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 64.75 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 2 KIIDVKNLTKTYKKNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIfGkDIVK-----QS----- 71
Cdd:PRK11819 323 KVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-G-ETVKlayvdQSrdald 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 72 --KEIRQNVGylpsevhfyDDMKVIDLLKY---SAGFYKKFNQKrmkelaerlDLDLHKKIEDLSFGNRKKVGIVQALLH 146
Cdd:PRK11819 401 pnKTVWEEIS---------GGLDIIKVGNReipSRAYVGRFNFK---------GGDQQKKVGVLSGGERNRLHLAKTLKQ 462
|
170
....*....|....*
gi 1021811607 147 EPKLLILDEPTGGLD 161
Cdd:PRK11819 463 GGNVLLLDEPTNDLD 477
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
4-237 |
1.17e-11 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 64.37 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 4 IDVKNLTKTYKKNRGIVNLTFSVEEGEIFGFIGPNGAGKSttiRTLL--NFLYPTSGSATIFGKDIVKQSKEIRQNVGY- 80
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**---RGALpaHV*GPDAGRRPWRF*TWCANRRALRRTIG*h 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 81 ----------LPSEVHFYDDMKVIDLLKYSAgfykkfnQKRMKELAERLDLD--LHKKIEDLSFGNRKKVGIVQALLHEP 148
Cdd:NF000106 91 rpvr*grresFSGRENLYMIGR*LDLSRKDA-------RARADELLERFSLTeaAGRAAAKYSGGMRRRLDLAASMIGRP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 149 KLLILDEPTGGLDPLMQNTFFEILTEEREKGTTIIFSSHILSEVQKMCDRVAIIKEGELVKVETIENLtKNNLKNITITF 228
Cdd:NF000106 164 AVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL-KTKVGGRTLQI 242
|
....*....
gi 1021811607 229 EQTNAIDFD 237
Cdd:NF000106 243 RPAHAAELD 251
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
13-208 |
1.54e-11 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 64.46 E-value: 1.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 13 YKKNRGIV-NLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDI--VKQSkEIRQNVGYLPSE-VHFY 88
Cdd:COG5265 367 YDPERPILkGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIrdVTQA-SLRAAIGIVPQDtVLFN 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 89 DDmkvidlLKY-------SAGfykkfnqkrMKELAERLDL-DLHKKIED---------------LSFGNRKKVGIVQALL 145
Cdd:COG5265 446 DT------IAYniaygrpDAS---------EEEVEAAARAaQIHDFIESlpdgydtrvgerglkLSGGEKQRVAIARTLL 510
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1021811607 146 HEPKLLILDEPTGGLDplmQNTFFEILTEERE--KGTTIIFSSHILSEVQKmCDRVAIIKEGELV 208
Cdd:COG5265 511 KNPPILIFDEATSALD---SRTERAIQAALREvaRGRTTLVIAHRLSTIVD-ADEILVLEAGRIV 571
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
3-268 |
1.57e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 63.28 E-value: 1.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 3 IIDVKNLTKTYKKN-RGIVN-LTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQSK----EIRQ 76
Cdd:PRK13640 5 IVEFKHVSFTYPDSkKPALNdISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVDGITLTAktvwDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 77 NVGYLPSEVhfyDDMKVIDLLKYSAGF---YKKFNQKRMKELAERL--DLDLHKKIE----DLSFGNRKKVGIVQALLHE 147
Cdd:PRK13640 85 KVGIVFQNP---DNQFVGATVGDDVAFgleNRAVPRPEMIKIVRDVlaDVGMLDYIDsepaNLSGGQKQRVAIAGILAVE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 148 PKLLILDEPTGGLDPLMQNTFFEILTE-EREKGTTIIFSSHILSEVQkMCDRVAIIKEGELVKVETIENLTKNN--LKNI 224
Cdd:PRK13640 162 PKIIILDESTSMLDPAGKEQILKLIRKlKKKNNLTVISITHDIDEAN-MADQVLVLDDGKLLAQGSPVEIFSKVemLKEI 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1021811607 225 --TITFEQTNAIDFDLEGI-VKKEINGSEMMLLYsgdiktlLNQLNT 268
Cdd:PRK13640 241 glDIPFVYKLKNKLKEKGIsVPQEINTEEKLVQY-------LCQLNS 280
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
3-220 |
1.83e-11 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 63.25 E-value: 1.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 3 IIDVKNLTKTyKKNRGIV-NLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQSK----EIRQN 77
Cdd:PRK11831 7 LVDMRGVSFT-RGNRCIFdNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRsrlyTVRKR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 78 VGYLPSEVHFYDDMKVIDLLKYSAGFYKKFNQK------RMKELAERLDLDLHKKIEDLSFGNRKKVGIVQALLHEPKLL 151
Cdd:PRK11831 86 MSMLFQSGALFTDMNVFDNVAYPLREHTQLPAPllhstvMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLI 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 152 ILDEPTGGLDPLMQNTFFEILTE-EREKGTTIIFSSHILSEVQKMCDRVAIIKEGELVKVETIENLTKNN 220
Cdd:PRK11831 166 MFDEPFVGQDPITMGVLVKLISElNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANP 235
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
21-208 |
2.41e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 63.82 E-value: 2.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 21 NLTFSVEEGEIFGFIGPNGAGKSTTIRTLL--------NFLY-------------PTSGSATIFG---------KDIVKQ 70
Cdd:PRK11147 21 NAELHIEDNERVCLVGRNGAGKSTLMKILNgevllddgRIIYeqdlivarlqqdpPRNVEGTVYDfvaegieeqAEYLKR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 71 SKEIRQNVGYLPSEVHFYDDMKVIDLLKYSAGFykKFnQKRMKELAERLDLDLHKKIEDLSFGNRKKVGIVQALLHEPKL 150
Cdd:PRK11147 101 YHDISHLVETDPSEKNLNELAKLQEQLDHHNLW--QL-ENRINEVLAQLGLDPDAALSSLSGGWLRKAALGRALVSNPDV 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1021811607 151 LILDEPTGGLDplmqntffeILTEE------REKGTTIIFSSHILSEVQKMCDRVAIIKEGELV 208
Cdd:PRK11147 178 LLLDEPTNHLD---------IETIEwlegflKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLV 232
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
8-216 |
2.46e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 62.81 E-value: 2.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 8 NLTKTYKKNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLlNFL------YPTSGSATIFGKDIV--KQSKEIRQNVG 79
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTL-NRMndkvsgYRYSGDVLLGGRSIFnyRDVLEFRRRVG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 80 YLPSEVHFYDdMKVIDLLKYSAGFYKKFNQKRMKELAE-RL-DLDLHKKIED--------LSFGNRKKVGIVQALLHEPK 149
Cdd:PRK14271 105 MLFQRPNPFP-MSIMDNVLAGVRAHKLVPRKEFRGVAQaRLtEVGLWDAVKDrlsdspfrLSGGQQQLLCLARTLAVNPE 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1021811607 150 LLILDEPTGGLDPLMQNTFFEILTEEREKgTTIIFSSHILSEVQKMCDRVAIIKEGELVKVETIENL 216
Cdd:PRK14271 184 VLLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQL 249
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
4-216 |
2.52e-11 |
|
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: 64.16 E-value: 2.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 4 IDVKNLTKTYKKN-RGIV-NLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLyPTSGSATIFGKDIVKQS-KEIRQNVGY 80
Cdd:TIGR01271 1218 MDVQGLTAKYTEAgRAVLqDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLL-STEGEIQIDGVSWNSVTlQTWRKAFGV 1296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 81 LPSEVHFYDDMKVIDLLKYS----AGFYKKFNQKRMKELAERLDLDLHKKIED----LSFGNRKKVGIVQALLHEPKLLI 152
Cdd:TIGR01271 1297 IPQKVFIFSGTFRKNLDPYEqwsdEEIWKVAEEVGLKSVIEQFPDKLDFVLVDggyvLSNGHKQLMCLARSILSKAKILL 1376
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1021811607 153 LDEPTGGLDPLMqntfFEILTEEREKG---TTIIFSSHILsEVQKMCDRVAIIKEGELVKVETIENL 216
Cdd:TIGR01271 1377 LDEPSAHLDPVT----LQIIRKTLKQSfsnCTVILSEHRV-EALLECQQFLVIEGSSVKQYDSIQKL 1438
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
4-187 |
3.81e-11 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 63.28 E-value: 3.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 4 IDVKNLTKTYKKNRGI-------VNLTFsvEEGEIFGFIGPNGAGKSTTIRTLLNfLY-PTSGSATIFGKDIVKQSKEI- 74
Cdd:COG4615 328 LELRGVTYRYPGEDGDegftlgpIDLTI--RRGELVFIVGGNGSGKSTLAKLLTG-LYrPESGEILLDGQPVTADNREAy 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 75 RQNVGYLPSEVHFYDDMkvidllkysAGFYKKFNQKRMKELAERLDLDlHK-KIED-------LSFGNRKKVGIVQALLH 146
Cdd:COG4615 405 RQLFSAVFSDFHLFDRL---------LGLDGEADPARARELLERLELD-HKvSVEDgrfsttdLSQGQRKRLALLVALLE 474
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1021811607 147 EPKLLILDEPTGGLDPLMQNTFF-EILTEEREKGTTIIFSSH 187
Cdd:COG4615 475 DRPILVFDEWAADQDPEFRRVFYtELLPELKARGKTVIAISH 516
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
3-199 |
4.08e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 62.67 E-value: 4.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 3 IIDVKNLTKTYKKNRGI---------VN-LTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQSK 72
Cdd:PRK11308 5 LLQAIDLKKHYPVKRGLfkperlvkaLDgVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 73 E----IRQNVgylpsEVHFYDDmkvidllkysagfYKKFN--QKRMKELAERLDL--DLHK-----KIEDL--------- 130
Cdd:PRK11308 85 EaqklLRQKI-----QIVFQNP-------------YGSLNprKKVGQILEEPLLIntSLSAaerreKALAMmakvglrpe 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 131 ---------SFGNRKKVGIVQALLHEPKLLILDEPTGGLDPLMQ----NTFFEIlteEREKGTTIIFSSHILSEVQKMCD 197
Cdd:PRK11308 147 hydryphmfSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQaqvlNLMMDL---QQELGLSYVFISHDLSVVEHIAD 223
|
..
gi 1021811607 198 RV 199
Cdd:PRK11308 224 EV 225
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
26-161 |
6.14e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 62.52 E-value: 6.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 26 VEEGEIFGFIGPNGAGKSTTIRTLLNFLYP----TSGSATIfgKDIVKQ--------------SKEIR-----QNVGYLP 82
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPnlgdYEEEPSW--DEVLKRfrgtelqnyfkklyNGEIKvvhkpQYVDLIP 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 83 SEVhfydDMKVIDLLKysagfyKKFNQKRMKELAERLDLD--LHKKIEDLSFGNRKKVGIVQALLHEPKLLILDEPTGGL 160
Cdd:PRK13409 174 KVF----KGKVRELLK------KVDERGKLDEVVERLGLEniLDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYL 243
|
.
gi 1021811607 161 D 161
Cdd:PRK13409 244 D 244
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-213 |
6.76e-11 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 62.17 E-value: 6.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 1 MKIIDVKNLTKTYK-KNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQSKEIR---- 75
Cdd:PRK11650 1 MAGLKLQAVRKSYDgKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRdiam 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 76 --QNVGYLPsevHfyddMKVIDLLKYS---AGFYKKFNQKRMKELAERLDLD--LHKKIEDLSFGNRKKVGIVQALLHEP 148
Cdd:PRK11650 81 vfQNYALYP---H----MSVRENMAYGlkiRGMPKAEIEERVAEAARILELEplLDRKPRELSGGQRQRVAMGRAIVREP 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1021811607 149 KLLILDEPTGGLDP-L---MQntfFEILTEEREKGTTIIFSSHILSEVQKMCDRVAIIKEGElvkVETI 213
Cdd:PRK11650 154 AVFLFDEPLSNLDAkLrvqMR---LEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGV---AEQI 216
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
3-208 |
6.92e-11 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 61.10 E-value: 6.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 3 IIDVKNLTKTYKKNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIV----------KQSK 72
Cdd:PRK11701 6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQlrdlyalseaERRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 73 EIRQNVGYlpseVHFYD----DMKVidllkySAG-------------FYKKFNQKRMKELaERLDLDLhKKIEDL----S 131
Cdd:PRK11701 86 LLRTEWGF----VHQHPrdglRMQV------SAGgnigerlmavgarHYGDIRATAGDWL-ERVEIDA-ARIDDLpttfS 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1021811607 132 FGNRKKVGIVQALLHEPKLLILDEPTGGLDPLMQNTFFEIL-TEEREKGTTIIFSSHILSEVQKMCDRVAIIKEGELV 208
Cdd:PRK11701 154 GGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLrGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVV 231
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
21-187 |
7.14e-11 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 62.52 E-value: 7.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 21 NLTFSVEEGE---IfgfIGPNGAGKSTTIRTLlNFLYPtSGSATIfgkdIVKQSKEI--------------RQNVGYlPS 83
Cdd:COG4178 381 DLSLSLKPGErllI---TGPSGSGKSTLLRAI-AGLWP-YGSGRI----ARPAGARVlflpqrpylplgtlREALLY-PA 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 84 EVHFYDDMKVIDLLKysagfykkfnQKRMKELAERLDLDLH-KKIedLSFGNRKKVGIVQALLHEPKLLILDEPTGGLDP 162
Cdd:COG4178 451 TAEAFSDAELREALE----------AVGLGHLAERLDEEADwDQV--LSLGEQQRLAFARLLLHKPDWLFLDEATSALDE 518
|
170 180
....*....|....*....|....*
gi 1021811607 163 LMQNTFFEILTEEReKGTTIIFSSH 187
Cdd:COG4178 519 ENEAALYQLLREEL-PGTTVISVGH 542
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-161 |
8.30e-11 |
|
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: 62.26 E-value: 8.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 3 IIDVKNLTKTYKKNRGIV-NLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSAtIFGKDIvkqskeirqNVGYL 81
Cdd:TIGR03719 4 IYTMNRVSKVVPPKKEILkDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEA-RPQPGI---------KVGYL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 82 PSEVHFyDDMK-----VIDLLKYSAGFYKKFNQ----------------KRMKELAERLD-LDLHK-------------- 125
Cdd:TIGR03719 74 PQEPQL-DPTKtvrenVEEGVAEIKDALDRFNEisakyaepdadfdklaAEQAELQEIIDaADAWDldsqleiamdalrc 152
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1021811607 126 -----KIEDLSFGNRKKVGIVQALLHEPKLLILDEPTGGLD 161
Cdd:TIGR03719 153 ppwdaDVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD 193
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
27-161 |
1.14e-10 |
|
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: 61.72 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 27 EEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSG---------------SATIFG---KDIVKqsKEIR-----QNVGYLPS 83
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPNLGdydeepswdevlkrfRGTELQdyfKKLAN--GEIKvahkpQYVDLIPK 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 84 EVhfydDMKVIDLLkysagfyKKFNQK-RMKELAERLDLD--LHKKIEDLSFGNRKKVGIVQALLHEPKLLILDEPTGGL 160
Cdd:COG1245 175 VF----KGTVRELL-------EKVDERgKLDELAEKLGLEniLDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYL 243
|
.
gi 1021811607 161 D 161
Cdd:COG1245 244 D 244
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
21-187 |
1.20e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 59.82 E-value: 1.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 21 NLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQSKEIRQNVGYL-----------PSE-VHFY 88
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLLYLghqpgikteltALEnLRFY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 89 -------DDMKVIDLLkysagfyKKFNqkrmkeLAERLDLDLHKkiedLSFGNRKKVGIVQALLHEPKLLILDEPTGGLD 161
Cdd:PRK13538 99 qrlhgpgDDEALWEAL-------AQVG------LAGFEDVPVRQ----LSAGQQRRVALARLWLTRAPLWILDEPFTAID 161
|
170 180
....*....|....*....|....*.
gi 1021811607 162 PLMQNTFFEILTEEREKGTTIIFSSH 187
Cdd:PRK13538 162 KQGVARLEALLAQHAEQGGMVILTTH 187
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
4-206 |
3.33e-10 |
|
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: 58.63 E-value: 3.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 4 IDVKNLTKTYKKNRGIVNLT-----FSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKD-IVKQ-----SK 72
Cdd:cd03250 1 ISVEDASFTWDSGEQETSFTlkdinLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIaYVSQepwiqNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 73 EIRQNVgyLpsevhfyddmkvidllkysagFYKKFNQKRMKELAER--LDLDLhKKIED------------LSFGNRKKV 138
Cdd:cd03250 81 TIRENI--L---------------------FGKPFDEERYEKVIKAcaLEPDL-EILPDgdlteigekginLSGGQKQRI 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1021811607 139 GIVQALLHEPKLLILDEPTGGLDP-----LMQNTFFEILTEERekgtTIIFSSHILSEVQKmCDRVAIIKEGE 206
Cdd:cd03250 137 SLARAVYSDADIYLLDDPLSAVDAhvgrhIFENCILGLLLNNK----TRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
21-207 |
5.00e-10 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 58.67 E-value: 5.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 21 NLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVkqskeIRQNVGyLPSEVhfyDDMKVIDLLKYS 100
Cdd:PRK13546 42 DISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSV-----IAISAG-LSGQL---TGIENIEFKMLC 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 101 AGFYKKFNQKRMKELAERLDLD--LHKKIEDLSFGNRKKVGIVQALLHEPKLLILDEPTGGLDPLMQNTFFEILTEEREK 178
Cdd:PRK13546 113 MGFKRKEIKAMTPKIIEFSELGefIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEFKEQ 192
|
170 180
....*....|....*....|....*....
gi 1021811607 179 GTTIIFSSHILSEVQKMCDRVAIIKEGEL 207
Cdd:PRK13546 193 NKTIFFVSHNLGQVRQFCTKIAWIEGGKL 221
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
25-161 |
5.72e-10 |
|
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: 58.53 E-value: 5.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 25 SVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSAT-------------------IFGKDIVKQSKEIR--QNVGYLPS 83
Cdd:cd03236 22 VPREGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDdppdwdeildefrgselqnYFTKLLEGDVKVIVkpQYVDLIPK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 84 EVhfydDMKVIDLLKysagfyKKFNQKRMKELAERLDLD--LHKKIEDLSFGNRKKVGIVQALLHEPKLLILDEPTGGLD 161
Cdd:cd03236 102 AV----KGKVGELLK------KKDERGKLDELVDQLELRhvLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLD 171
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
24-208 |
6.32e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 59.64 E-value: 6.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 24 FSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQSKE----------IRQNVGYL-PSEvhfyDDM- 91
Cdd:PRK10938 24 LTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEqlqklvsdewQRNNTDMLsPGE----DDTg 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 92 ----KVIDLlkysagfYKKFNQkRMKELAERLDLD--LHKKIEDLSFGNRKKVGIVQALLHEPKLLILDEPTGGLDPLMQ 165
Cdd:PRK10938 100 rttaEIIQD-------EVKDPA-RCEQLAQQFGITalLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASR 171
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1021811607 166 NTFFEILTEEREKGTTIIFSSHILSEVQKMCDRVAIIKEGELV 208
Cdd:PRK10938 172 QQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLA 214
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
31-215 |
8.84e-10 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 58.73 E-value: 8.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 31 IFGFigpNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQSKEI-----RQNVGYLPSEVHFYDDMKVIDLLKYSagfYK 105
Cdd:PRK11144 29 IFGR---SGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGIclppeKRRIGYVFQDARLFPHYKVRGNLRYG---MA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 106 KFNQKRMKELAERLDLD--LHKKIEDLSFGNRKKVGIVQALLHEPKLLILDEPTGGLD-P----LMQntFFEILTEEREk 178
Cdd:PRK11144 103 KSMVAQFDKIVALLGIEplLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDlPrkreLLP--YLERLAREIN- 179
|
170 180 190
....*....|....*....|....*....|....*..
gi 1021811607 179 gTTIIFSSHILSEVQKMCDRVAIIKEGELVKVETIEN 215
Cdd:PRK11144 180 -IPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEE 215
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
3-209 |
1.49e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 57.45 E-value: 1.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 3 IIDVKNLTKTYKKNRGIV--NLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQS-KEIRQNVG 79
Cdd:PRK13648 7 IIVFKNVSFQYQSDASFTlkDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNfEKLRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 80 YLpseVHFYDDMKVIDLLKYSAGF--------YKKFnQKRMKELAERLDLDLHKKIE--DLSFGNRKKVGIVQALLHEPK 149
Cdd:PRK13648 87 IV---FQNPDNQFVGSIVKYDVAFglenhavpYDEM-HRRVSEALKQVDMLERADYEpnALSGGQKQRVAIAGVLALNPS 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1021811607 150 LLILDEPTGGLDPLMQNTFFEILTE-EREKGTTIIFSSHILSEVQKmCDRVAIIKEGELVK 209
Cdd:PRK13648 163 VIILDEATSMLDPDARQNLLDLVRKvKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYK 222
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
21-207 |
2.58e-09 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 57.59 E-value: 2.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 21 NLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKD--IVKQSKEIRQNVGylpsevhfyddMKVIDLLK 98
Cdd:PRK13545 42 NISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAalIAISSGLNGQLTG-----------IENIELKG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 99 YSAGFYKKFNQKRMKELAERLDLD--LHKKIEDLSFGNRKKVGIVQALLHEPKLLILDEPTGGLDPLMQNTFFEILTEER 176
Cdd:PRK13545 111 LMMGLTKEKIKEIIPEIIEFADIGkfIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNEFK 190
|
170 180 190
....*....|....*....|....*....|.
gi 1021811607 177 EKGTTIIFSSHILSEVQKMCDRVAIIKEGEL 207
Cdd:PRK13545 191 EQGKTIFFISHSLSQVKSFCTKALWLHYGQV 221
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
4-162 |
8.67e-09 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 55.19 E-value: 8.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 4 IDVKNLTKTYKKN---RGIvnlTFSVEEGEIFGFIGPNGAGKSTTIRTLlNFL-YPTSGSATIFGKDI-VKQSKEIRQNV 78
Cdd:COG4598 9 LEVRDLHKSFGDLevlKGV---SLTARKGDVISIIGSSGSGKSTFLRCI-NLLeTPDSGEIRVGGEEIrLKPDRDGELVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 79 GylpsevhfydDMKVIDLLKYSAGF-YKKFN------------------QKRMK----ELAERLdldLHK-KIED----- 129
Cdd:COG4598 85 A----------DRRQLQRIRTRLGMvFQSFNlwshmtvlenvieapvhvLGRPKaeaiERAEAL---LAKvGLADkrday 151
|
170 180 190
....*....|....*....|....*....|....*.
gi 1021811607 130 ---LSFGNRKKVGIVQALLHEPKLLILDEPTGGLDP 162
Cdd:COG4598 152 pahLSGGQQQRAAIARALAMEPEVMLFDEPTSALDP 187
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
22-162 |
1.44e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 54.08 E-value: 1.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 22 LTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIvkQSKEIRQNVGYLPSEVHFYDDMKVIDLLKYSA 101
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTA--TRGDRSRFMAYLGHLPGLKADLSTLENLHFLC 107
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1021811607 102 GFYKKFNQKRMKELAERLDLDLHKK--IEDLSFGNRKKVGIVQALLHEPKLLILDEPTGGLDP 162
Cdd:PRK13543 108 GLHGRRAKQMPGSALAIVGLAGYEDtlVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1-208 |
2.64e-08 |
|
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: 53.04 E-value: 2.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 1 MKIIDVKNLTKTYKKNRGIV----NLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFL---YPTSGSATIFGKDIVKQSKE 73
Cdd:cd03233 1 ASTLSWRNISFTTGKGRSKIpilkDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTegnVSVEGDIHYNGIPYKEFAEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 74 IRQNVGYLPSEVHFYDDMKVIDLLKYSAgfykkfnqkRMKElaerldldlHKKIEDLSFGNRKKVGIVQALLHEPKLLIL 153
Cdd:cd03233 81 YPGEIIYVSEEDVHFPTLTVRETLDFAL---------RCKG---------NEFVRGISGGERKRVSIAEALVSRASVLCW 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 154 DEPTGGLDplmQNTFFEILTEERE-----KGTTIIFSSHILSEVQKMCDRVAIIKEGELV 208
Cdd:cd03233 143 DNSTRGLD---SSTALEILKCIRTmadvlKTTTFVSLYQASDEIYDLFDKVLVLYEGRQI 199
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
7-161 |
3.40e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 54.35 E-value: 3.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 7 KNLTKTYKKNRGIV-NLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIfgkdivkqSKEIRqnVGYLPSEV 85
Cdd:PRK11819 10 NRVSKVVPPKKQILkDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARP--------APGIK--VGYLPQEP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 86 HFyDDMK-----VIDLLKYSAGFYKKFNQ----------------KRMKELAERLD-LDLH------------------- 124
Cdd:PRK11819 80 QL-DPEKtvrenVEEGVAEVKAALDRFNEiyaayaepdadfdalaAEQGELQEIIDaADAWdldsqleiamdalrcppwd 158
|
170 180 190
....*....|....*....|....*....|....*..
gi 1021811607 125 KKIEDLSFGNRKKVGIVQALLHEPKLLILDEPTGGLD 161
Cdd:PRK11819 159 AKVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD 195
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
3-209 |
3.57e-08 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 53.26 E-value: 3.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 3 IIDVKNLTKTYKKNRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNF--LYPTSGSATIFGKDIVKQSKEIRQNVGY 80
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSPEDRAGEGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 81 L-----PSEV-----HFYDDMKVIDLLKYSAGF------YKKFNQKRMKELAERLDLDLHKKIEDLSFGNRKKVGIVQAL 144
Cdd:PRK09580 81 FmafqyPVEIpgvsnQFFLQTALNAVRSYRGQEpldrfdFQDLMEEKIALLKMPEDLLTRSVNVGFSGGEKKRNDILQMA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1021811607 145 LHEPKLLILDEPTGGLDPLMQNTFFEILTEEREKGTTIIFSSH---ILSEVQKmcDRVAIIKEGELVK 209
Cdd:PRK09580 161 VLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHyqrILDYIKP--DYVHVLYQGRIVK 226
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
3-161 |
5.07e-08 |
|
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: 51.86 E-value: 5.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 3 IIDVKNLTKTYKKNRG----IVNLTFSVEEGEIFGFIGPNGAGKSTtirtLLNFLYP------TSGSATIFGKdivKQSK 72
Cdd:cd03232 3 VLTWKNLNYTVPVKGGkrqlLNNISGYVKPGTLTALMGESGAGKTT----LLDVLAGrktagvITGEILINGR---PLDK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 73 EIRQNVGYLPSE-VHFyDDMKVIDLLKYSAgfykkfnqkrmkelaerldldlhkKIEDLSFGNRKKVGIVQALLHEPKLL 151
Cdd:cd03232 76 NFQRSTGYVEQQdVHS-PNLTVREALRFSA------------------------LLRGLSVEQRKRLTIGVELAAKPSIL 130
|
170
....*....|
gi 1021811607 152 ILDEPTGGLD 161
Cdd:cd03232 131 FLDEPTSGLD 140
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
4-216 |
6.33e-08 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 53.80 E-value: 6.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 4 IDVKNLTKTYKKNRGIV--NLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQS-KEIRQNVGY 80
Cdd:TIGR00957 1285 VEFRNYCLRYREDLDLVlrHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGlHDLRFKITI 1364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 81 LPSE-VHF-------------YDDMKVIDLLKYSagFYKKFnqkrMKELAERLDLDLHKKIEDLSFGNRKKVGIVQALLH 146
Cdd:TIGR00957 1365 IPQDpVLFsgslrmnldpfsqYSDEEVWWALELA--HLKTF----VSALPDKLDHECAEGGENLSVGQRQLVCLARALLR 1438
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1021811607 147 EPKLLILDEPTGGL----DPLMQNTffeILTEEREkgTTIIFSSHILSEVQKMCdRVAIIKEGELVKVETIENL 216
Cdd:TIGR00957 1439 KTKILVLDEATAAVdletDNLIQST---IRTQFED--CTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNL 1506
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
21-208 |
9.05e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 52.87 E-value: 9.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 21 NLTFSVEEGEIFGFIGPNGAGksttiRTLL-------NFLYPTSGSATIFGKDIVKQ--SKEIRQNVGYLpSE------V 85
Cdd:NF040905 278 DVSLNVRRGEIVGIAGLMGAG-----RTELamsvfgrSYGRNISGTVFKDGKEVDVStvSDAIDAGLAYV-TEdrkgygL 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 86 HFYDDMK---------------VIDL---LKYSAGFYKKFNQKRMkelaerldlDLHKKIEDLSFGNRKKVGIVQALLHE 147
Cdd:NF040905 352 NLIDDIKrnitlanlgkvsrrgVIDEneeIKVAEEYRKKMNIKTP---------SVFQKVGNLSGGNQQKVVLSKWLFTD 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1021811607 148 PKLLILDEPTGGLDPLMQNTFFEILTEEREKGTTIIFSSHILSEVQKMCDRVAIIKEGELV 208
Cdd:NF040905 423 PDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMNEGRIT 483
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
4-220 |
1.83e-07 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 52.26 E-value: 1.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 4 IDVKNLTKTYKKNR--GIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGkdivkqskeirqNVGYL 81
Cdd:TIGR00957 637 ITVHNATFTWARDLppTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG------------SVAYV 704
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 82 PSEVHFYDDMkvidlLKYSAGFYKKFNQKRMKELAERLDL--DLH-----------KKIEDLSFGNRKKVGIVQALLHEP 148
Cdd:TIGR00957 705 PQQAWIQNDS-----LRENILFGKALNEKYYQQVLEACALlpDLEilpsgdrteigEKGVNLSGGQKQRVSLARAVYSNA 779
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1021811607 149 KLLILDEPTGGLDPLMQNTFFE--ILTEEREKGTTIIFSSHILSEVQKMcDRVAIIKEGELVKVETIENLTKNN 220
Cdd:TIGR00957 780 DIYLFDDPLSAVDAHVGKHIFEhvIGPEGVLKNKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLQRD 852
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
21-216 |
2.05e-07 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 50.85 E-value: 2.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 21 NLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYP----TSGSATIFGKDIVKQS------KEIRQNVGYLPSEVHFYDD 90
Cdd:PRK10418 21 GVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVAPCAlrgrkiATIMQNPRSAFNPLHTMHT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 91 MKVIDLLkySAGfyKKFNQKRMKELAERLDLDLHKKIEDL-----SFGNRKKVGIVQALLHEPKLLILDEPTGGLDPLMQ 165
Cdd:PRK10418 101 HARETCL--ALG--KPADDATLTAALEAVGLENAARVLKLypfemSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQ 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1021811607 166 NTFFEILTE-EREKGTTIIFSSHILSEVQKMCDRVAIIKEGELVKVETIENL 216
Cdd:PRK10418 177 ARILDLLESiVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETL 228
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
21-219 |
2.81e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 51.66 E-value: 2.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 21 NLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIfgkdivkqskeIRQNVGYLPsEVHFYDDMKVIDLLKYS 100
Cdd:PLN03130 635 NINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVV-----------IRGTVAYVP-QVSWIFNATVRDNILFG 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 101 AGF-YKKFNQK-RMKELAERLDL----DLHKKIE---DLSFGNRKKVGIVQALLHEPKLLILDEPTGGLDP-LMQNTFFE 170
Cdd:PLN03130 703 SPFdPERYERAiDVTALQHDLDLlpggDLTEIGErgvNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAhVGRQVFDK 782
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1021811607 171 ILTEEREKGTTIIFSS--HILSEVqkmcDRVAIIKEGELVKVETIENLTKN 219
Cdd:PLN03130 783 CIKDELRGKTRVLVTNqlHFLSQV----DRIILVHEGMIKEEGTYEELSNN 829
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
29-198 |
2.86e-07 |
|
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: 48.91 E-value: 2.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 29 GEIFGFIGPNGAGKSTTIRTLLNFLYPTSGsatifgkdivkqskeirqnvgylpsevhfydDMKVIDLlkysagfykkfN 108
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGG-------------------------------GVIYIDG-----------E 39
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 109 QKRMKELAERLDLDLHKKIEDLSFGNRKKVGIVQALLHEPKLLILDEPTGGLDPLMQNTFFEILT------EEREKGTTI 182
Cdd:smart00382 40 DILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrllllLKSEKNLTV 119
|
170
....*....|....*.
gi 1021811607 183 IFSSHILSEVQKMCDR 198
Cdd:smart00382 120 ILTTNDEKDLGPALLR 135
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
4-216 |
5.80e-07 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 50.49 E-value: 5.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 4 IDVKNLTKTYKKNRGIV-NLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQSKEI-RQNVGYL 81
Cdd:PRK10790 341 IDIDNVSFAYRDDNLVLqNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVlRQGVAMV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 82 PSEV-----HFYDDMKV---IDllkySAGFYKKFNQKRMKELAERLDLDLHKKI----EDLSFGNRKKVGIVQALLHEPK 149
Cdd:PRK10790 421 QQDPvvladTFLANVTLgrdIS----EEQVWQALETVQLAELARSLPDGLYTPLgeqgNNLSVGQKQLLALARVLVQTPQ 496
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1021811607 150 LLILDEPTGGLDPLMQNTFFEILTEEREKgTTIIFSSHILSEVQKmCDRVAIIKEGELVKVETIENL 216
Cdd:PRK10790 497 ILILDEATANIDSGTEQAIQQALAAVREH-TTLVVIAHRLSTIVE-ADTILVLHRGQAVEQGTHQQL 561
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
16-193 |
1.47e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 47.94 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 16 NRGIVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQSKEIrqnVGYLPSEVHFYDDMKVID 95
Cdd:PRK13541 13 QKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPY---CTYIGHNLGLKLEMTVFE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 96 LLKYSAGFYKKFNQKRMKELAERLDLDLHKKIEDLSFGNRKKVGIVQALLHEPKLLILDEPTGGLDPLMQNTFFEILTEE 175
Cdd:PRK13541 90 NLKFWSEIYNSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVMK 169
|
170
....*....|....*...
gi 1021811607 176 REKGTTIIFSSHILSEVQ 193
Cdd:PRK13541 170 ANSGGIVLLSSHLESSIK 187
|
|
| COG4938 |
COG4938 |
Predicted ATPase [General function prediction only]; |
1-209 |
1.69e-06 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443965 [Multi-domain] Cd Length: 277 Bit Score: 48.43 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 1 MKIIDVKNLtKTYKKnrgivnltFSVEEGEIFGFIGPNGAGKSTTIRTLL-----NFLYPTSG--SATIFGKDIVKQSKE 73
Cdd:COG4938 1 IKSISIKNF-GPFKE--------AELELKPLTLLIGPNGSGKSTLIQALLlllqsNFIYLPAErsGPARLYPSLVRELSD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 74 IRQNVGYLpseVHFYDDMKVIDLLKYSAGFYKKFNQKRMKEL-AERLDLDLHKKIEDLSF---GNRKKVGIVQ------- 142
Cdd:COG4938 72 LGSRGEYT---ADFLAELENLEILDDKSKELLEQVEEWLEKIfPGKVEVDASSDLVRLVFrpsGNGKRIPLSNvgsgvse 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1021811607 143 ------ALLHEPK---LLILDEPTGGLDPLMQNTFFEILTEEREKGTTIIF---SSHILSEVQKMcdrvaiIKEGELVK 209
Cdd:COG4938 149 llpillALLSAAKpgsLLIIEEPEAHLHPKAQSALAELLAELANSGVQVIIethSDYILNGLRNL------IKEGKLLD 221
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
35-203 |
2.53e-06 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 46.58 E-value: 2.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 35 IGPNGAGKSTTIR-TLLNFLYptSGSATIFGKDIvkqskEIRQNVGYlpSEVHFYddmkvIDLLKYSAGfykkfnQKRMK 113
Cdd:cd03227 27 TGPNGSGKSTILDaIGLALGG--AQSATRRRSGV-----KAGCIVAA--VSAELI-----FTRLQLSGG------EKELS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 114 ELAERLDLdlhkkiedlsfgnrkkvgivqALLHEPKLLILDEPTGGLDPLMQNTFFEILTEEREKGTTIIFSSHiLSEVQ 193
Cdd:cd03227 87 ALALILAL---------------------ASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITH-LPELA 144
|
170
....*....|
gi 1021811607 194 KMCDRVAIIK 203
Cdd:cd03227 145 ELADKLIHIK 154
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
127-187 |
6.43e-06 |
|
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: 46.61 E-value: 6.43e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1021811607 127 IEDLSFGNRKKVGIVQALL---HEPKLLILDEPTGGLDPLMQNTFFEILTEEREKGTTIIFSSH 187
Cdd:pfam13304 234 AFELSDGTKRLLALLAALLsalPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTH 297
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
1-224 |
1.05e-05 |
|
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: 46.15 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 1 MKI--IDVKNLtktykknRGIVNLTFSVEEGeIFGFIGPNGAGKSTTIRtLLNFLYPTSGSATIFGKDIVKQSKEIRQNV 78
Cdd:COG3593 1 MKLekIKIKNF-------RSIKDLSIELSDD-LTVLVGENNSGKSSILE-ALRLLLGPSSSRKFDEEDFYLGDDPDLPEI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 79 ---GYLPSEV-----HFYDDMKVIDLLKYSAGFYKKFNQ----------KRMKELAERLDLDLHKKIED---------LS 131
Cdd:COG3593 72 eieLTFGSLLsrllrLLLKEEDKEELEEALEELNEELKEalkalnellsEYLKELLDGLDLELELSLDEledllkslsLR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 132 FGNRKKV-------GIVQALL-------------HEPKLLILDEPTGGLDPLMQNTFFEILTEEREKGTTIIFSSH---I 188
Cdd:COG3593 152 IEDGKELpldrlgsGFQRLILlallsalaelkraPANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTHsphL 231
|
250 260 270
....*....|....*....|....*....|....*..
gi 1021811607 189 LSEVQKmcDRVAII-KEGELVKVETIENLTKNNLKNI 224
Cdd:COG3593 232 LSEVPL--ENIRRLrRDSGGTTSTKLIDLDDEDLRKL 266
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
4-161 |
1.98e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 45.71 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 4 IDVKNLTKtykknrgivNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGK----------DIVKQSKE 73
Cdd:PRK11147 329 IDGKQLVK---------DFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKlevayfdqhrAELDPEKT 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 74 IRQNVGYLPSEV-------HfyddmkvidLLKYSAGFYkkFNQKRMKelaerldldlhKKIEDLSFGNRKKVGIVQALLH 146
Cdd:PRK11147 400 VMDNLAEGKQEVmvngrprH---------VLGYLQDFL--FHPKRAM-----------TPVKALSGGERNRLLLARLFLK 457
|
170
....*....|....*
gi 1021811607 147 EPKLLILDEPTGGLD 161
Cdd:PRK11147 458 PSNLLILDEPTNDLD 472
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
1-201 |
5.53e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 44.63 E-value: 5.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 1 MKIIDVkNLTKTYKKNRGIV-NLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNF--------------------------- 52
Cdd:PTZ00265 1166 IEIMDV-NFRYISRPNVPIYkDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFydlkndhhivfknehtndmtneqdyqg 1244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 53 ---------------------------LYPTSGSATIFGKDIVKQSKEIRQNVGYLPSEVHFYDDMKVIDLLKYSAGFYK 105
Cdd:PTZ00265 1245 deeqnvgmknvnefsltkeggsgedstVFKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDAT 1324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 106 KFNQKR----------MKELAERLDLDLHKKIEDLSFGNRKKVGIVQALLHEPKLLILDEPTGGLDPLMQNTFFEILTEE 175
Cdd:PTZ00265 1325 REDVKRackfaaidefIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDI 1404
|
250 260
....*....|....*....|....*..
gi 1021811607 176 REKG-TTIIFSSHILSEVqKMCDRVAI 201
Cdd:PTZ00265 1405 KDKAdKTIITIAHRIASI-KRSDKIVV 1430
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
28-207 |
1.57e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 42.96 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 28 EGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSAtifgkdivkqSKEIRQNVGYLPSEVHFYDDMKVIDLLKYSAGFYKKF 107
Cdd:PRK15064 26 GGNRYGLIGANGCGKSTFMKILGGDLEPSAGNV----------SLDPNERLGKLRQDQFAFEEFTVLDTVIMGHTELWEV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 108 NQKR--------------MK------ELAER-----------------LDLDLHK-KIEDLSFGNRKKVGIVQALLHEPK 149
Cdd:PRK15064 96 KQERdriyalpemseedgMKvadlevKFAEMdgytaearagelllgvgIPEEQHYgLMSEVAPGWKLRVLLAQALFSNPD 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1021811607 150 LLILDEPTGGLDplmQNT--FFEILTEEReKGTTIIFS--SHILSEVqkmCDRVAIIKEGEL 207
Cdd:PRK15064 176 ILLLDEPTNNLD---INTirWLEDVLNER-NSTMIIIShdRHFLNSV---CTHMADLDYGEL 230
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
1-193 |
1.86e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 43.09 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 1 MKIIDVKNLTKTYKKNRGI---VNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFG----KDI------ 67
Cdd:PTZ00265 380 IKKIQFKNVRFHYDTRKDVeiyKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDshnlKDInlkwwr 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 68 -----VKQ-----SKEIRQNVGYlpsEVHFYDDMKVIDLLKYSAGFYKKFNQKRMKELAERLDLDL-------------- 123
Cdd:PTZ00265 460 skigvVSQdpllfSNSIKNNIKY---SLYSLKDLEALSNYYNEDGNDSQENKNKRNSCRAKCAGDLndmsnttdsnelie 536
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 124 ----HKKIED---------------------------------LSFGNRKKVGIVQALLHEPKLLILDEPTGGLDP---- 162
Cdd:PTZ00265 537 mrknYQTIKDsevvdvskkvlihdfvsalpdkyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNksey 616
|
250 260 270
....*....|....*....|....*....|.
gi 1021811607 163 LMQNTFFEIltEEREKGTTIIFsSHILSEVQ 193
Cdd:PTZ00265 617 LVQKTINNL--KGNENRITIII-AHRLSTIR 644
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
7-161 |
2.43e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 42.79 E-value: 2.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 7 KNLTKTYK----KNRGIVNLTFSVEEGEIFGFIGPNGAGKSTtirtLLNFL-------YPTSGSATIFGKDI-------- 67
Cdd:TIGR00956 763 RNLTYEVKikkeKRVILNNVDGWVKPGTLTALMGASGAGKTT----LLNVLaervttgVITGGDRLVNGRPLdssfqrsi 838
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 68 --VKQS---------KEIRQNVGYL--PSEVHFYDDM----KVIDLLKysagfykkfnqkrMKELAERLdldLHKKIEDL 130
Cdd:TIGR00956 839 gyVQQQdlhlptstvRESLRFSAYLrqPKSVSKSEKMeyveEVIKLLE-------------MESYADAV---VGVPGEGL 902
|
170 180 190
....*....|....*....|....*....|..
gi 1021811607 131 SFGNRKKVGIVQALLHEPKLLI-LDEPTGGLD 161
Cdd:TIGR00956 903 NVEQRKRLTIGVELVAKPKLLLfLDEPTSGLD 934
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
21-209 |
8.37e-04 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 40.85 E-value: 8.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 21 NLTFSVEEGEIFGFIGPNGAGKSTTIRTLLN-----------------------------------FLYPTSGSATI-FG 64
Cdd:PRK10789 333 NVNFTLKPGQMLGICGPTGSGKSTLLSLIQRhfdvsegdirfhdipltklqldswrsrlavvsqtpFLFSDTVANNIaLG 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 65 KDIVKQSkEIRQnVGYLPSeVHfyddmkvIDLLKYSAGFykkfnqkrMKELAERLDLdlhkkiedLSFGNRKKVGIVQAL 144
Cdd:PRK10789 413 RPDATQQ-EIEH-VARLAS-VH-------DDILRLPQGY--------DTEVGERGVM--------LSGGQKQRISIARAL 466
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1021811607 145 LHEPKLLILDEPTGGLDplmQNTFFEILTEERE--KGTTIIFSSHILSEVQKmCDRVAIIKEGELVK 209
Cdd:PRK10789 467 LLNAEILILDDALSAVD---GRTEHQILHNLRQwgEGRTVIISAHRLSALTE-ASEILVMQHGHIAQ 529
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
26-206 |
8.62e-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: 39.48 E-value: 8.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 26 VEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVkqskeirqnvgYLPSEVhfyddmkvidllkysagfyk 105
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPV-----------YKPQYI-------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 106 kfnqkrmkelaerldldlhkkieDLSFGNRKKVGIVQALLHEPKLLILDEPTGGLDP---LMQNTFFEILTEEREKgtTI 182
Cdd:cd03222 71 -----------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIeqrLNAARAIRRLSEEGKK--TA 125
|
170 180
....*....|....*....|....
gi 1021811607 183 IFSSHILSEVQKMCDRVaIIKEGE 206
Cdd:cd03222 126 LVVEHDLAVLDYLSDRI-HVFEGE 148
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
21-189 |
1.02e-03 |
|
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: 39.62 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 21 NLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSATIFGKDIVKQSKEI-----RQNVGYLPSEVHFYDDMkvid 95
Cdd:cd03290 19 NINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEAtrsrnRYSVAYAAQKPWLLNAT---- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 96 lLKYSAGFYKKFNQKRMKELAE----RLDLDL---------HKKIEDLSFGNRKKVGIVQALLHEPKLLILDEPTGGL-- 160
Cdd:cd03290 95 -VEENITFGSPFNKQRYKAVTDacslQPDIDLlpfgdqteiGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALdi 173
|
170 180 190
....*....|....*....|....*....|..
gi 1021811607 161 ---DPLMQNTFFEILTEEREkgtTIIFSSHIL 189
Cdd:cd03290 174 hlsDHLMQEGILKFLQDDKR---TLVLVTHKL 202
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
19-161 |
1.32e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 40.23 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 19 IVNLTFSVEEGEIFGFIGPNGAGKSTTIRTLLNFL---YPTSGSATIFGKDIVKQSKEIRQNV--------GYLPSEVHF 87
Cdd:PLN03073 193 IVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAMHAidgIPKNCQILHVEQEVVGDDTTALQCVlntdiertQLLEEEAQL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 88 YDDMKVIDL--------LKYSAGFYKKFNQKRMKELAERLDL---------------------DL-HKKIEDLSFGNRKK 137
Cdd:PLN03073 273 VAQQRELEFetetgkgkGANKDGVDKDAVSQRLEEIYKRLELidaytaearaasilaglsftpEMqVKATKTFSGGWRMR 352
|
170 180
....*....|....*....|....
gi 1021811607 138 VGIVQALLHEPKLLILDEPTGGLD 161
Cdd:PLN03073 353 IALARALFIEPDLLLLDEPTNHLD 376
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
26-161 |
3.69e-03 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 38.94 E-value: 3.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 26 VEEGEIFGFIGPNGAGKSTTIRTLLNFLYPTSGSAT-------IFGKDIVKQskeIRQNVGYLP-SEVHFyDDMKVIDLL 97
Cdd:TIGR00956 84 IKPGELTVVLGRPGSGCSTLLKTIASNTDGFHIGVEgvitydgITPEEIKKH---YRGDVVYNAeTDVHF-PHLTVGETL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 98 KYSA----------GFYKKFNQKRMKELAER-LDLDlHKK--------IEDLSFGNRKKVGIVQALLHEPKLLILDEPTG 158
Cdd:TIGR00956 160 DFAArcktpqnrpdGVSREEYAKHIADVYMAtYGLS-HTRntkvgndfVRGVSGGERKRVSIAEASLGGAKIQCWDNATR 238
|
...
gi 1021811607 159 GLD 161
Cdd:TIGR00956 239 GLD 241
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
112-216 |
4.10e-03 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 37.97 E-value: 4.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021811607 112 MKELAERLDLDLHKKIEDLSFGNRKKVGIVQALLHEPKLLILDEPTGGLDPLMQNTFFEILTEEREKGTTIIFS---SHI 188
Cdd:cd03288 139 VKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAhrvSTI 218
|
90 100
....*....|....*....|....*...
gi 1021811607 189 LSevqkmCDRVAIIKEGELVKVETIENL 216
Cdd:cd03288 219 LD-----ADLVLVLSRGILVECDTPENL 241
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
121-187 |
5.74e-03 |
|
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: 36.92 E-value: 5.74e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1021811607 121 LDLHKKIEDLSFGNRKKVGIVQALLHEPK--LLILDEPTGGLDPLMQNTFFEILTEEREKGTTIIFSSH 187
Cdd:cd03238 79 LTLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEH 147
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