|
Name |
Accession |
Description |
Interval |
E-value |
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1-248 |
0e+00 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 505.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 1 MLSIQDLHVAVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEVTGGRVEFKGKNLLELAAEDRAGEGI 80
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEVTGGTVEFKGKDLLELSPEDRAGEGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 81 FMAFQYPVEIPGVSNQFFLQTALNAVRNYRGQEALDRFDFQDLMEEKIKLLQMPEDLLTRSVNVGFSGGEKKRNDILQMA 160
Cdd:PRK09580 81 FMAFQYPVEIPGVSNQFFLQTALNAVRSYRGQEPLDRFDFQDLMEEKIALLKMPEDLLTRSVNVGFSGGEKKRNDILQMA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 161 VLEPELCILDESDSGLDIDALKIVSQGVNALRDGKRAFIIVTHYQRILDYIKPDYVHVLYQGRIVKSGDFSLVKQLEEQG 240
Cdd:PRK09580 161 VLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYQRILDYIKPDYVHVLYQGRIVKSGDFTLVKQLEEQG 240
|
....*...
gi 488998194 241 YGWLTEQQ 248
Cdd:PRK09580 241 YGWLTEQQ 248
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
2-247 |
4.43e-162 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 448.36 E-value: 4.43e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 2 LSIQDLHVAVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEVTGGRVEFKGKNLLELAAEDRAGEGIF 81
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKYEVTSGSILLDGEDILELSPDERARAGIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 82 MAFQYPVEIPGVSNQFFLQTALNAVRnyrgQEALDRFDFQDLMEEKIKLLQMPEDLLTRSVNVGFSGGEKKRNDILQMAV 161
Cdd:COG0396 81 LAFQYPVEIPGVSVSNFLRTALNARR----GEELSAREFLKLLKEKMKELGLDEDFLDRYVNEGFSGGEKKRNEILQMLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 162 LEPELCILDESDSGLDIDALKIVSQGVNALRDGKRAFIIVTHYQRILDYIKPDYVHVLYQGRIVKSGDFSLVKQLEEQGY 241
Cdd:COG0396 157 LEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITHYQRILDYIKPDFVHVLVDGRIVKSGGKELALELEEEGY 236
|
....*.
gi 488998194 242 GWLTEQ 247
Cdd:COG0396 237 DWLKEE 242
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
2-244 |
2.81e-155 |
|
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: 430.91 E-value: 2.81e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 2 LSIQDLHVAVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEVTGGRVEFKGKNLLELAAEDRAGEGIF 81
Cdd:TIGR01978 1 LKIKDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGHPSYEVTSGTILFKGQDLLELEPDERARAGLF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 82 MAFQYPVEIPGVSNQFFLQTALNAVRNYRGQEALDRFDFQDLMEEKIKLLQMPEDLLTRSVNVGFSGGEKKRNDILQMAV 161
Cdd:TIGR01978 81 LAFQYPEEIPGVSNLEFLRSALNARRSARGEEPLDLLDFEKLLKEKLALLDMDEEFLNRSVNEGFSGGEKKRNEILQMAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 162 LEPELCILDESDSGLDIDALKIVSQGVNALRDGKRAFIIVTHYQRILDYIKPDYVHVLYQGRIVKSGDFSLVKQLEEQGY 241
Cdd:TIGR01978 161 LEPKLAILDEIDSGLDIDALKIVAEGINRLREPDRSFLIITHYQRLLNYIKPDYVHVLLDGRIVKSGDVELAKELEAKGY 240
|
...
gi 488998194 242 GWL 244
Cdd:TIGR01978 241 DWV 243
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-246 |
2.71e-131 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 370.90 E-value: 2.71e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 1 MLSIQDLHVAVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEVTGGRVEFKGKNLLELAAEDRAGEGI 80
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKILEGDILFKGESILDLEPEERAHLGI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 81 FMAFQYPVEIPGVSNQFFLQTALNAVRNYRGQEALDRFDFQDLMEEKIKLLQMPEDLLTRSVNVGFSGGEKKRNDILQMA 160
Cdd:CHL00131 87 FLAFQYPIEIPGVSNADFLRLAYNSKRKFQGLPELDPLEFLEIINEKLKLVGMDPSFLSRNVNEGFSGGEKKRNEILQMA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 161 VLEPELCILDESDSGLDIDALKIVSQGVNALRDGKRAFIIVTHYQRILDYIKPDYVHVLYQGRIVKSGDFSLVKQLEEQG 240
Cdd:CHL00131 167 LLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHYQRLLDYIKPDYVHVMQNGKIIKTGDAELAKELEKKG 246
|
....*.
gi 488998194 241 YGWLTE 246
Cdd:CHL00131 247 YDWLKQ 252
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
2-241 |
1.66e-117 |
|
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: 333.72 E-value: 1.66e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 2 LSIQDLHVAVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEVTGGRVEFKGKNLLELAAEDRAGEGIF 81
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEVTEGEILFKGEDITDLPPEERARLGIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 82 MAFQYPVEIPGVSNQFFLqtalnavrnyrgqealdrfdfqdlmeekikllqmpedlltRSVNVGFSGGEKKRNDILQMAV 161
Cdd:cd03217 81 LAFQYPPEIPGVKNADFL----------------------------------------RYVNEGFSGGEKKRNEILQLLL 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 162 LEPELCILDESDSGLDIDALKIVSQGVNALRDGKRAFIIVTHYQRILDYIKPDYVHVLYQGRIVKSGDFSLVKQLEEQGY 241
Cdd:cd03217 121 LEPDLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHYQRLLDYIKPDRVHVLYDGRIVKSGDKELALEIEKKGY 200
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
13-223 |
7.64e-32 |
|
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: 116.03 E-value: 7.64e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 13 DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGRVEFKGKNLLELAAEDRAGEgIFMAFQYPveipg 92
Cdd:cd03225 13 ARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLL--GPTSGEVLVDGKDLTKLSLKELRRK-VGLVFQNP----- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 93 vSNQFFLQTALN----AVRNY---------RGQEALDRFDFQDLMEEKIKLLqmpedlltrsvnvgfSGGEKKRNDILQM 159
Cdd:cd03225 85 -DDQFFGPTVEEevafGLENLglpeeeieeRVEEALELVGLEGLRDRSPFTL---------------SGGQKQRVAIAGV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488998194 160 AVLEPELCILDESDSGLDIDALKIVSQGVNALRDGKRAFIIVTHYqriLDYIKP--DYVHVLYQGR 223
Cdd:cd03225 149 LAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHD---LDLLLElaDRVIVLEDGK 211
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-238 |
7.31e-31 |
|
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: 113.97 E-value: 7.31e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 2 LSIQDLHVAVED-KAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGRVEFKGKNLLELAAED---RAG 77
Cdd:COG1122 1 IELENLSFSYPGgTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGL--LKPTSGEVLVDGKDITKKNLRElrrKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 78 egifMAFQYPveipgvSNQFFLQTALNAV----RNY---------RGQEALDRFDFQDLMEEKIKLLqmpedlltrsvnv 144
Cdd:COG1122 79 ----LVFQNP------DDQLFAPTVEEDVafgpENLglpreeireRVEEALELVGLEHLADRPPHEL------------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 145 gfSGGEKKRndiLQMA---VLEPELCILDESDSGLDIDALKIVSQGVNALRDGKRAFIIVTHYqriLDYIKP--DYVHVL 219
Cdd:COG1122 136 --SGGQKQR---VAIAgvlAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHD---LDLVAElaDRVIVL 207
|
250 260
....*....|....*....|...
gi 488998194 220 YQGRIVKSGD----FSLVKQLEE 238
Cdd:COG1122 208 DDGRIVADGTprevFSDYELLEE 230
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-223 |
7.79e-29 |
|
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: 106.56 E-value: 7.79e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 3 SIQDLHVAVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGRVEFKGKNLLELAAEdRAGEGIFM 82
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGL--LKPTSGEILIDGKDIAKLPLE-ELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 83 AFQypveipgvsnqfflqtalnavrnyrgqealdrfdfqdlmeekikllqmpedlltrsvnvgFSGGEKKRNDILQMAVL 162
Cdd:cd00267 78 VPQ------------------------------------------------------------LSGGQRQRVALARALLL 97
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488998194 163 EPELCILDESDSGLDIDALKIVSQGVNALRDGKRAFIIVTHYQRILDYIkPDYVHVLYQGR 223
Cdd:cd00267 98 NPDLLLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELA-ADRVIVLKDGK 157
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-228 |
1.32e-28 |
|
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: 107.98 E-value: 1.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 1 MLSIQDLHVAVEDKA----ILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGRVEFKGKNLLELAAEDRA 76
Cdd:cd03257 1 LLEVKNLSVSFPTGGgsvkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLL--KPTSGSIIFDGKDLLKLSRRLRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 77 --GEGIFMAFQYPveipgvsnqfflQTALNAVRNYRGQ--EAL-------DRFDFQDLMEEKIKLLQMPEDLLTRSVNvG 145
Cdd:cd03257 79 irRKEIQMVFQDP------------MSSLNPRMTIGEQiaEPLrihgklsKKEARKEAVLLLLVGVGLPEEVLNRYPH-E 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 146 FSGGEKKRNDIlQMA-VLEPELCILDESDSGLDIDalkIVSQGVNALRDGKR----AFIIVTHYQRILDYIKpDYVHVLY 220
Cdd:cd03257 146 LSGGQRQRVAI-ARAlALNPKLLIADEPTSALDVS---VQAQILDLLKKLQEelglTLLFITHDLGVVAKIA-DRVAVMY 220
|
....*...
gi 488998194 221 QGRIVKSG 228
Cdd:cd03257 221 AGKIVEEG 228
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-203 |
5.38e-28 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 106.05 E-value: 5.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 2 LSIQDLHVAVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYevTGGRVEFKGKNLLELAAED-RAgeGI 80
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPP--TSGEIYLDGKPLSAMPPPEwRR--QV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 81 FMAFQYPVEIPGVsnqffLQTALNAVRNYRgQEALDRFDFQDLMEEkiklLQMPEDLLTRSVNvGFSGGEKKRNDILQMA 160
Cdd:COG4619 77 AYVPQEPALWGGT-----VRDNLPFPFQLR-ERKFDRERALELLER----LGLPPDILDKPVE-RLSGGERQRLALIRAL 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488998194 161 VLEPELCILDESDSGLDIDALKIVSQGVNALRDGK-RAFIIVTH 203
Cdd:COG4619 146 LLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEgRAVLWVSH 189
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-239 |
7.40e-28 |
|
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: 106.48 E-value: 7.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 1 MLSIQDLHVAVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYevTGGRVEFKGKNLLELAAEDRAGEGI 80
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKP--DSGSILIDGEDVRKEPREARRQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 81 FmafqyPVEIPGVSNqfflQTALNAVRNYRGQEALDRFDFQDLMEEKIKLLQMpEDLLTRSVNvGFSGGEKKRNDILQMA 160
Cdd:COG4555 79 L-----PDERGLYDR----LTVRENIRYFAELYGLFDEELKKRIEELIELLGL-EEFLDRRVG-ELSTGMKKKVALARAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 161 VLEPELCILDESDSGLDIDALKIVSQGVNALRDGKRAFIIVTHyqrILDYIKP--DYVHVLYQGRIVKSGDFSLVKQLEE 238
Cdd:COG4555 148 VHDPKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSH---IMQEVEAlcDRVVILHKGKVVAQGSLDELREEIG 224
|
.
gi 488998194 239 Q 239
Cdd:COG4555 225 E 225
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-229 |
4.30e-27 |
|
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: 108.45 E-value: 4.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 1 MLSIQDLHVAV--EDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEVT-GGRVEFKGKNLLELAAEDRAG 77
Cdd:COG1123 4 LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGRiSGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 78 EgIFMAFQYPveipgvSNQFFLQTALNAVRNYRGQEALDRFDFQDLMEEKIKLLQMpEDLLTRSVNVgFSGGEKKRNDIL 157
Cdd:COG1123 84 R-IGMVFQDP------MTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGL-ERRLDRYPHQ-LSGGQRQRVAIA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488998194 158 QMAVLEPELCILDESDSGLDIDALKIVSQGVNAL-RDGKRAFIIVTHYQRILDYIkPDYVHVLYQGRIVKSGD 229
Cdd:COG1123 155 MALALDPDLLIADEPTTALDVTTQAEILDLLRELqRERGTTVLLITHDLGVVAEI-ADRVVVMDDGRIVEDGP 226
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-228 |
4.40e-27 |
|
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: 104.12 E-value: 4.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 2 LSIQDLHVAVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGRVEFKGKNLLELAAED--RAGEG 79
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGL--LRPDSGEVLIDGEDISGLSEAElyRLRRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 80 IFMAFQypveipgvSNQFFlqTALNAVRN----YRGQEALDRFDFQDLMEEKIKLL-------QMPEDLltrsvnvgfSG 148
Cdd:cd03261 79 MGMLFQ--------SGALF--DSLTVFENvafpLREHTRLSEEEIREIVLEKLEAVglrgaedLYPAEL---------SG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 149 GEKKRNDILQMAVLEPELCILDESDSGLDidalKIVSQGVNAL-RDGKRAF----IIVTHYQRILDYIkPDYVHVLYQGR 223
Cdd:cd03261 140 GMKKRVALARALALDPELLLYDEPTAGLD----PIASGVIDDLiRSLKKELgltsIMVTHDLDTAFAI-ADRIAVLYDGK 214
|
....*
gi 488998194 224 IVKSG 228
Cdd:cd03261 215 IVAEG 219
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-238 |
1.01e-26 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 103.22 E-value: 1.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 2 LSIQDLHVAVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGRVEFKGKNLLELAAEDRAgeGIF 81
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGL--LRPTSGEVRVLGEDVARDPAEVRR--RIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 82 MAFQYPVEIPGVsnqfflqTALNAVRNYRGQEALDRFDFQDLMEEKIKLLQMpEDLLTRSVNvGFSGGEKKRNDILQMAV 161
Cdd:COG1131 77 YVPQEPALYPDL-------TVRENLRFFARLYGLPRKEARERIDELLELFGL-TDAADRKVG-TLSGGMKQRLGLALALL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 162 LEPELCILDESDSGLDIDALKIVSQGVNALRDGKRAFIIVTHY----QRILdyikpDYVHVLYQGRIVKSGDFSLVKQ-- 235
Cdd:COG1131 148 HDPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYleeaERLC-----DRVAIIDKGRIVADGTPDELKArl 222
|
...
gi 488998194 236 LEE 238
Cdd:COG1131 223 LED 225
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-229 |
1.49e-26 |
|
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: 103.20 E-value: 1.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 1 MLSIQDLHVAVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGRVEFKGKNLLELAAEDRAGEgi 80
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAG--LLKPSSGEVLLDGRDLASLSRRELARR-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 81 fMAF--QYPVEIPGVsnqfflqTALNAVRNYR--GQEALDRFDFQD--LMEEKIKLLQMpEDLLTRSVNvGFSGGEKkrn 154
Cdd:COG1120 77 -IAYvpQEPPAPFGL-------TVRELVALGRypHLGLFGRPSAEDreAVEEALERTGL-EHLADRPVD-ELSGGER--- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 155 dilQMAVL------EPELCILDESDSGLDI----DALKIVSQGVnalRDGKRAFIIVTHYqriLD----YIkpDYVHVLY 220
Cdd:COG1120 144 ---QRVLIaralaqEPPLLLLDEPTSHLDLahqlEVLELLRRLA---RERGRTVVMVLHD---LNlaarYA--DRLVLLK 212
|
....*....
gi 488998194 221 QGRIVKSGD 229
Cdd:COG1120 213 DGRIVAQGP 221
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
2-229 |
1.60e-26 |
|
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: 102.90 E-value: 1.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 2 LSIQDLHVAVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGRVEFKGKNLLELAAEDRAGEGIF 81
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGF--LRPTSGSVLFDGEDITGLPPHEIARLGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 82 MAFQYPVEIPG--------VSNQFFLQTALNAVRNYRGQ--------EALDRFDFQDLMEEKIKLLqmpedlltrsvnvg 145
Cdd:cd03219 79 RTFQIPRLFPEltvlenvmVAAQARTGSGLLLARARREEreareraeELLERVGLADLADRPAGEL-------------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 146 fSGGEKKRndiLQMA---VLEPELCILDESDSGLDIDALKIVSQGVNALRDGKRAFIIVTHyqrILDYIKP--DYVHVLY 220
Cdd:cd03219 145 -SYGQQRR---LEIAralATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEH---DMDVVMSlaDRVTVLD 217
|
....*....
gi 488998194 221 QGRIVKSGD 229
Cdd:cd03219 218 QGRVIAEGT 226
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-229 |
1.66e-26 |
|
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: 106.91 E-value: 1.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 1 MLSIQDLHV-----AVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGRVEFKGKNLLELAAEDR 75
Cdd:COG1123 260 LLEVRNLSKrypvrGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLL--RPTSGSILFDGKDLTKLSRRSL 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 76 A--GEGIFMAFQYPveipgvsnqfflQTALN-----------AVRNYRGqeaLDRFDFQDLMEEKIKLLQMPEDLLTRSV 142
Cdd:COG1123 338 RelRRRVQMVFQDP------------YSSLNprmtvgdiiaePLRLHGL---LSRAERRERVAELLERVGLPPDLADRYP 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 143 NvGFSGGEKKRNDILQMAVLEPELCILDESDSGLDidaLKIVSQGVNALRDGKR----AFIIVTHYQRILDYIKpDYVHV 218
Cdd:COG1123 403 H-ELSGGQRQRVAIARALALEPKLLILDEPTSALD---VSVQAQILNLLRDLQRelglTYLFISHDLAVVRYIA-DRVAV 477
|
250
....*....|.
gi 488998194 219 LYQGRIVKSGD 229
Cdd:COG1123 478 MYDGRIVEDGP 488
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-229 |
1.71e-25 |
|
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: 99.95 E-value: 1.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 2 LSIQDLHVAVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRED---YEVTGGRVEFKGKNLLELAA---EDR 75
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipGAPDEGEVLLDGKDIYDLDVdvlELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 76 AGEGifMAFQYPVEIPGvsnqfflqTALNAV------RNYRGQEALDrfdfqDLMEEKIKLLQMPEDLLTRSVNVGFSGG 149
Cdd:cd03260 81 RRVG--MVFQKPNPFPG--------SIYDNVayglrlHGIKLKEELD-----ERVEEALRKAALWDEVKDRLHALGLSGG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 150 EKKRNDILQMAVLEPELCILDESDSGLDIDALKIVSQGVNALRDgKRAFIIVTH----YQRIldyikPDYVHVLYQGRIV 225
Cdd:cd03260 146 QQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKK-EYTIVIVTHnmqqAARV-----ADRTAFLLNGRLV 219
|
....
gi 488998194 226 KSGD 229
Cdd:cd03260 220 EFGP 223
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-225 |
7.21e-25 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 98.72 E-value: 7.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 1 MLSIQDLHVA----VEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDyeVTGGRVEFKGKNLLELAAEDRA 76
Cdd:COG1124 1 MLEVRNLSVSygqgGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLER--PWSGEVTFDGRPVTRRRRKAFR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 77 GEgIFMAFQYPveipgvsnqfflQTALNAVRNYRGQ--EALDRFDFQDLMEEKIKLLQ---MPEDLLTRSVNvGFSGGEK 151
Cdd:COG1124 79 RR-VQMVFQDP------------YASLHPRHTVDRIlaEPLRIHGLPDREERIAELLEqvgLPPSFLDRYPH-QLSGGQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 152 KRNDILQMAVLEPELCILDESDSGLDidalkIVSQG--VNALRDGKR----AFIIVTHYQRILDYIkPDYVHVLYQGRIV 225
Cdd:COG1124 145 QRVAIARALILEPELLLLDEPTSALD-----VSVQAeiLNLLKDLREerglTYLFVSHDLAVVAHL-CDRVAVMQNGRIV 218
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-203 |
1.72e-24 |
|
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: 96.78 E-value: 1.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 1 MLSIQDLHVAVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGRVEFKGKNLLElaAEDRAGEGI 80
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLL--PPSAGEVLWNGEPIRD--AREDYRRRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 81 FMAFQYpveiPGVSNQFFLQTALNAVRNYRG--------QEALDRFDFQDLMEEKIKLLqmpedlltrsvnvgfSGGEKK 152
Cdd:COG4133 78 AYLGHA----DGLKPELTVRENLRFWAALYGlradreaiDEALEAVGLAGLADLPVRQL---------------SAGQKR 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488998194 153 RNDILQMAVLEPELCILDESDSGLDIDALKIVSQGVNALRDGKRAFIIVTH 203
Cdd:COG4133 139 RVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTH 189
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-230 |
5.14e-24 |
|
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: 96.20 E-value: 5.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 1 MLSIQDLHVAVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGRVEFKGKNLLELAAEDRAG--E 78
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGL--LRPDSGEILVDGQDITGLSEKELYElrR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 79 GIFMAFQypveipgvSNQFFlqTALNAVRN----YRGQEALDRFDFQDLMEEKIKLL-------QMPEDLltrsvnvgfS 147
Cdd:COG1127 83 RIGMLFQ--------GGALF--DSLTVFENvafpLREHTDLSEAEIRELVLEKLELVglpgaadKMPSEL---------S 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 148 GGEKKRndilqmA------VLEPELCILDESDSGLDIDALKIVSQGVNALRDGKRA-FIIVTHyqrILDYIK--PDYVHV 218
Cdd:COG1127 144 GGMRKR------ValaralALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLtSVVVTH---DLDSAFaiADRVAV 214
|
250
....*....|..
gi 488998194 219 LYQGRIVKSGDF 230
Cdd:COG1127 215 LADGKIIAEGTP 226
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-228 |
2.46e-23 |
|
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: 94.77 E-value: 2.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 1 MLSIQDLHVAVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLsATLAGREDYEVTGGRVEFKGknllelaaEDRAGEGI 80
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTL-LSLITGDLPPTYGNDVRLFG--------ERRGGEDV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 81 F------------MAFQYPVEIpgvsnqfflqTALNAV-----------RNY------RGQEALDRFDFQDLMEEKIKLL 131
Cdd:COG1119 74 WelrkriglvspaLQLRFPRDE----------TVLDVVlsgffdsiglyREPtdeqreRARELLELLGLAHLADRPFGTL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 132 qmpedlltrsvnvgfSGGEKKRndiLQMA---VLEPELCILDESDSGLDIDALKIVSQGVNAL-RDGKRAFIIVTHYqri 207
Cdd:COG1119 144 ---------------SQGEQRR---VLIAralVKDPELLILDEPTAGLDLGARELLLALLDKLaAEGAPTLVLVTHH--- 202
|
250 260
....*....|....*....|...
gi 488998194 208 LDYIKPDYVHVLY--QGRIVKSG 228
Cdd:COG1119 203 VEEIPPGITHVLLlkDGRVVAAG 225
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
17-171 |
8.50e-23 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 90.78 E-value: 8.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 17 LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGRVEFKGKNLLELAAEDRAGEgIFMAFQYPVEIPGVsnq 96
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGL--LSPTEGTILLDGQDLTDDERKSLRKE-IGYVFQDPQLFPRL--- 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488998194 97 fflqTALNAVRNYRGQEALDRFDFQDLMEEKIKLLQMPEDLLTRSVNVG--FSGGEKKRNDILQMAVLEPELCILDE 171
Cdd:pfam00005 75 ----TVRENLRLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVGERPgtLSGGQRQRVAIARALLTKPKLLLLDE 147
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-228 |
1.20e-22 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 92.87 E-value: 1.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 1 MLSIQDLHVAVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGRVEFKGKNLLELAAEDRAGE-G 79
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTG--ELTPSSGEVRLNGRPLAAWSPWELARRrA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 80 IF-----MAFQYPVE-------IPGVSNQFFLQTALnavrnyrgQEALDRFDFQDLMEekikllqmpedlltRSVNvGFS 147
Cdd:COG4559 79 VLpqhssLAFPFTVEevvalgrAPHGSSAAQDRQIV--------REALALVGLAHLAG--------------RSYQ-TLS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 148 GGEKKRndiLQMA-VL---------EPELCILDESDSGLDI----DALKIVSQgvnaLRDGKRAFIIVTH-------Y-Q 205
Cdd:COG4559 136 GGEQQR---VQLArVLaqlwepvdgGPRWLFLDEPTSALDLahqhAVLRLARQ----LARRGGGVVAVLHdlnlaaqYaD 208
|
250 260
....*....|....*....|...
gi 488998194 206 RILdyikpdyvhVLYQGRIVKSG 228
Cdd:COG4559 209 RIL---------LLHQGRLVAQG 222
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-224 |
1.51e-22 |
|
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: 90.53 E-value: 1.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 2 LSIQDLHVAVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGRVEFKGKNLLELAAEDRagEGIF 81
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGL--LKPDSGEIKVLGKDIKKEPEEVK--RRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 82 MAFQYPVEIPgvsnqfflqtalnavrNYRGQEALDrfdfqdlmeekikllqmpedlltrsvnvgFSGGEKKRNDILQMAV 161
Cdd:cd03230 77 YLPEEPSLYE----------------NLTVRENLK-----------------------------LSGGMKQRLALAQALL 111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488998194 162 LEPELCILDESDSGLDIDALKIVSQGVNALRDGKRAFIIVTHYQRILDYIKpDYVHVLYQGRI 224
Cdd:cd03230 112 HDPELLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLC-DRVAILNNGRI 173
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
2-229 |
4.45e-22 |
|
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: 90.57 E-value: 4.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 2 LSIQDLHVAVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDyeVTGGRVEFKGKNLLELAAEDRAGEGIF 81
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLP--PRSGSIRFDGRDITGLPPHERARAGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 82 MAFQypveipgvSNQFF--------LQTALNAVRNYRGQEALDR-FD-FQDLMEekiKLLQMPEDLltrsvnvgfSGGEK 151
Cdd:cd03224 79 YVPE--------GRRIFpeltveenLLLGAYARRRAKRKARLERvYElFPRLKE---RRKQLAGTL---------SGGEQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 152 KrndILQMA---VLEPELCILDESDSGLdidALKIVSQ---GVNALRDGKRAFIIVTHY-QRILDYIkpDYVHVLYQGRI 224
Cdd:cd03224 139 Q---MLAIAralMSRPKLLLLDEPSEGL---APKIVEEifeAIRELRDEGVTILLVEQNaRFALEIA--DRAYVLERGRV 210
|
....*
gi 488998194 225 VKSGD 229
Cdd:cd03224 211 VLEGT 215
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-229 |
1.07e-21 |
|
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: 91.65 E-value: 1.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 1 MLSIQDLHV--AVEDKAI--LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAG-REDYEVTGGRVEFKGKNLLELAAEDR 75
Cdd:COG0444 1 LLEVRNLKVyfPTRRGVVkaVDGVSFDVRRGETLGLVGESGSGKSTLARAILGlLPPPGITSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 76 A---GEGIFMAFQYPveipgvsnqfflQTALNAVRNYRGQ--EAL---DRFDFQDLMEEKIKLLQM-----PEDLLTRsv 142
Cdd:COG0444 81 RkirGREIQMIFQDP------------MTSLNPVMTVGDQiaEPLrihGGLSKAEARERAIELLERvglpdPERRLDRyp 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 143 nvgFSGGEKKRNDILqMA-VLEPELCILDESDSGLDIDalkIVSQGVNALRDGKR----AFIIVTHyqrilD-----YIK 212
Cdd:COG0444 149 -heLSGGMRQRVMIA-RAlALEPKLLIADEPTTALDVT---IQAQILNLLKDLQRelglAILFITH-----DlgvvaEIA 218
|
250
....*....|....*..
gi 488998194 213 pDYVHVLYQGRIVKSGD 229
Cdd:COG0444 219 -DRVAVMYAGRIVEEGP 234
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
3-228 |
1.70e-21 |
|
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: 87.88 E-value: 1.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 3 SIQDLHVAVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGRVEFKGKNLLELAAEDRAGEgifM 82
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGL--LKPSSGEILLDGKDLASLSPKELARK---I 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 83 AfqypveipgvsnqfFLQTALNAVrnyrgqealdrfdfqDLmeekikllqmpEDLLTRSVNVgFSGGEKKRNDILQMAVL 162
Cdd:cd03214 76 A--------------YVPQALELL---------------GL-----------AHLADRPFNE-LSGGERQRVLLARALAQ 114
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488998194 163 EPELCILDESDSGLDI----DALKIVSQGVnalRDGKRAFIIVTHYqriLD--YIKPDYVHVLYQGRIVKSG 228
Cdd:cd03214 115 EPPILLLDEPTSHLDIahqiELLELLRRLA---RERGKTVVMVLHD---LNlaARYADRVILLKDGRIVAQG 180
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-228 |
2.82e-21 |
|
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: 88.35 E-value: 2.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 2 LSIQDLHVAVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGRVEFKGKNLLELAAEDRageGIF 81
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLE--RPDSGEILIDGRDVTGVPPERR---NIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 82 MAFQypveipgvsnQFFLQTALNAVRNYR---GQEALDRFDFQDLMEEKIKLLQMpEDLLTRSVNvGFSGGEKKRNDILQ 158
Cdd:cd03259 76 MVFQ----------DYALFPHLTVAENIAfglKLRGVPKAEIRARVRELLELVGL-EGLLNRYPH-ELSGGQQQRVALAR 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488998194 159 MAVLEPELCILDESDSGLDID-ALKIVSQGVNALRDGKRAFIIVTHYQ----RILDYIKpdyvhVLYQGRIVKSG 228
Cdd:cd03259 144 ALAREPSLLLLDEPLSALDAKlREELREELKELQRELGITTIYVTHDQeealALADRIA-----VMNEGRIVQVG 213
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-228 |
5.02e-21 |
|
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: 87.81 E-value: 5.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 1 MLSIQDLHVAVEDKA----ILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGRVEFKGKNLLELAAEDRA 76
Cdd:cd03266 1 MITADALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGL--LEPDAGFATVDGFDVVKEPAEARR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 77 GEGIFmafqypveiPGVSNQFFLQTALNAVRNYRGQEALDRFDFQDLMEEKIKLLQMpEDLLTRSVNvGFSGGEKKRNDI 156
Cdd:cd03266 79 RLGFV---------SDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGM-EELLDRRVG-GFSTGMRQKVAI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488998194 157 LQMAVLEPELCILDESDSGLDIDALKIVSQGVNALRDGKRAFIIVTHyqrILDYIKP--DYVHVLYQGRIVKSG 228
Cdd:cd03266 148 ARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTH---IMQEVERlcDRVVVLHRGRVVYEG 218
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-229 |
8.73e-21 |
|
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: 87.79 E-value: 8.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 1 MLSIQDLH------VAVEDkailrgLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGRVEFKGKNLLELAAED 74
Cdd:COG0411 4 LLEVRGLTkrfgglVAVDD------VSLEVERGEIVGLIGPNGAGKTTLFNLITGF--YRPTSGRILFDGRDITGLPPHR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 75 RAGEGIFMAFQYPVEIPGVS-------------NQFFLQTALNAVRNYRG--------QEALDRFDFQDLMEEKIKLLqm 133
Cdd:COG0411 76 IARLGIARTFQNPRLFPELTvlenvlvaaharlGRGLLAALLRLPRARREereareraEELLERVGLADRADEPAGNL-- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 134 pedlltrsvnvgfSGGEKKRndiLQMA---VLEPELCILDESDSGLDIDALKIVSQGVNALRDG-KRAFIIVTHyqrILD 209
Cdd:COG0411 154 -------------SYGQQRR---LEIAralATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErGITILLIEH---DMD 214
|
250 260
....*....|....*....|..
gi 488998194 210 YIKP--DYVHVLYQGRIVKSGD 229
Cdd:COG0411 215 LVMGlaDRIVVLDFGRVIAEGT 236
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
3-203 |
9.31e-21 |
|
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: 86.54 E-value: 9.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 3 SIQDLHVAVEDKA-ILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGRVEFKGKNlleLAAEDRAgEGIF 81
Cdd:cd03226 1 RIENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGL--IKESSGSILLNGKP---IKAKERR-KSIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 82 MAFQypveipGVSNQFFLQTALNAVR---------NYRGQEALDRFDFQDLMEekikllQMPEDLltrsvnvgfSGGEKK 152
Cdd:cd03226 75 YVMQ------DVDYQLFTDSVREELLlglkeldagNEQAETVLKDLDLYALKE------RHPLSL---------SGGQKQ 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488998194 153 RNDILQMAVLEPELCILDESDSGLDIDALKIVSQGVNALRDGKRAFIIVTH 203
Cdd:cd03226 134 RLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITH 184
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-229 |
1.23e-20 |
|
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: 86.96 E-value: 1.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 1 MLSIQDLHVAVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGRVEFKGKNLLELAAEDRAGEGI 80
Cdd:COG0410 3 MLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISG--LLPPRSGSIRFDGEDITGLPPHRIARLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 81 FMA------FqypveiPGVS---NqffLQTALNAVRNYRG-QEALDR-FD-FQDLmEEKIKllQMPEDLltrsvnvgfSG 148
Cdd:COG0410 81 GYVpegrriF------PSLTveeN---LLLGAYARRDRAEvRADLERvYElFPRL-KERRR--QRAGTL---------SG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 149 GEKkrndilQM-A-----VLEPELCILDESDSGLdidALKIVSQ---GVNALRDGKRAFIIVTHY-QRILDYIkpDYVHV 218
Cdd:COG0410 140 GEQ------QMlAigralMSRPKLLLLDEPSLGL---APLIVEEifeIIRRLNREGVTILLVEQNaRFALEIA--DRAYV 208
|
250
....*....|.
gi 488998194 219 LYQGRIVKSGD 229
Cdd:COG0410 209 LERGRIVLEGT 219
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-231 |
4.52e-20 |
|
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: 88.67 E-value: 4.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 2 LSIQDLHVA--VEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGRVEFKGKNLLELAAEDRAgeg 79
Cdd:COG4987 334 LELEDVSFRypGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLR--FLDPQSGSITLGGVDLRDLDEDDLR--- 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 80 ifmafqypvEIPGVSNQ---FFLQTALNAVRNYRGQ-------EALDRFDFQDLmeekikLLQMPEDLLTRsvnVG---- 145
Cdd:COG4987 409 ---------RRIAVVPQrphLFDTTLRENLRLARPDatdeelwAALERVGLGDW------LAALPDGLDTW---LGeggr 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 146 -FSGGEKKRndiLQMA-VL--EPELCILDESDSGLDIDALKIVSQGVNALRDGkRAFIIVTHYQRILDYIkpDYVHVLYQ 221
Cdd:COG4987 471 rLSGGERRR---LALArALlrDAPILLLDEPTEGLDAATEQALLADLLEALAG-RTVLLITHRLAGLERM--DRILVLED 544
|
250
....*....|
gi 488998194 222 GRIVKSGDFS 231
Cdd:COG4987 545 GRIVEQGTHE 554
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
16-224 |
4.56e-20 |
|
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: 85.23 E-value: 4.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 16 ILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDyeVTGGRVEFKGKNLLELAAEDRA---GEGIFMAFQYP----- 87
Cdd:cd03255 19 ALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDR--PTSGEVRVDGTDISKLSEKELAafrRRHIGFVFQSFnllpd 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 88 ------VEIPgvsnqFFLQTALNAVRNYRGQEALDRFDFQDLMEekikllQMPEDLltrsvnvgfSGGEKKRNDILQMAV 161
Cdd:cd03255 97 ltalenVELP-----LLLAGVPKKERRERAEELLERVGLGDRLN------HYPSEL---------SGGQQQRVAIARALA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488998194 162 LEPELCILDESDSGLDIDALKIVsqgVNALRD-----GKrAFIIVTHYQRILDYIkpDYVHVLYQGRI 224
Cdd:cd03255 157 NDPKIILADEPTGNLDSETGKEV---MELLRElnkeaGT-TIVVVTHDPELAEYA--DRIIELRDGKI 218
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-229 |
4.92e-20 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 85.53 E-value: 4.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 1 MLSIQDLHVAVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGRVEFKGKNLlelaaeDRAGEGI 80
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILG--LLPPTSGTVRLFGKPP------RRARRRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 81 -----FMAF--QYPVeipgvsnqfflqTALNAVR----NYRG-------------QEALDRFDFQDLMEEKIKLLqmped 136
Cdd:COG1121 78 gyvpqRAEVdwDFPI------------TVRDVVLmgryGRRGlfrrpsradreavDEALERVGLEDLADRPIGEL----- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 137 lltrsvnvgfSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVSQGVNALRDGKRAFIIVTH-YQRILDYIKpdy 215
Cdd:COG1121 141 ----------SGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHdLGAVREYFD--- 207
|
250
....*....|....*
gi 488998194 216 vHVLY-QGRIVKSGD 229
Cdd:COG1121 208 -RVLLlNRGLVAHGP 221
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-228 |
1.02e-19 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 85.21 E-value: 1.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 1 MLSIQDLHVAVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGRVEFKGKNLLELAAEDRAG--- 77
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSG--ELSPDSGEVRLNGRPLADWSPAELARrra 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 78 ---EGIFMAFQYPVE-------IPGVSNQFFLQTALnavrnyrgQEALDRFDFQDLMEEKIKLLqmpedlltrsvnvgfS 147
Cdd:PRK13548 80 vlpQHSSLSFPFTVEevvamgrAPHGLSRAEDDALV--------AAALAQVDLAHLAGRDYPQL---------------S 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 148 GGEKKRndiLQMA-VL--------EPELCILDESDSGLDI----DALKIVSQgvNALRDGkRAFIIVTH-------YQri 207
Cdd:PRK13548 137 GGEQQR---VQLArVLaqlwepdgPPRWLLLDEPTSALDLahqhHVLRLARQ--LAHERG-LAVIVVLHdlnlaarYA-- 208
|
250 260
....*....|....*....|.
gi 488998194 208 ldyikpDYVHVLYQGRIVKSG 228
Cdd:PRK13548 209 ------DRIVLLHQGRLVADG 223
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-203 |
1.04e-19 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 84.07 E-value: 1.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 1 MLSIQDLHVAVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEVTG-GRVEFKGKNLLELAAEDRageG 79
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAFSAsGEVLLNGRRLTALPAEQR---R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 80 IFMAFQYPVEIPGVS---N-QFFLQTALN-AVRNYRGQEALDRFDFQDLMEekikllQMPEDLltrsvnvgfSGGEKKRN 154
Cdd:COG4136 78 IGILFQDDLLFPHLSvgeNlAFALPPTIGrAQRRARVEQALEEAGLAGFAD------RDPATL---------SGGQRARV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488998194 155 DILQMAVLEPELCILDESDSGLDidalkivsqgvNALRDGKRAF------------IIVTH 203
Cdd:COG4136 143 ALLRALLAEPRALLLDEPFSKLD-----------AALRAQFREFvfeqirqrgipaLLVTH 192
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
12-203 |
1.31e-19 |
|
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: 83.24 E-value: 1.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 12 EDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGRVEFKGKNLlelaAEDRAG-----EGIFMAFQY 86
Cdd:TIGR01166 3 GGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGL--LRPQSGAVLIDGEPL----DYSRKGllerrQRVGLVFQD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 87 PveipgvSNQFFLQTALNAV----RNY---------RGQEALDRFDFQDLMEEKIKLLqmpedlltrsvnvgfSGGEKKR 153
Cdd:TIGR01166 77 P------DDQLFAADVDQDVafgpLNLglseaeverRVREALTAVGASGLRERPTHCL---------------SGGEKKR 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488998194 154 NDILQMAVLEPELCILDESDSGLDIDALKIVSQGVNALRDGKRAFIIVTH 203
Cdd:TIGR01166 136 VAIAGAVAMRPDVLLLDEPTAGLDPAGREQMLAILRRLRAEGMTVVISTH 185
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-230 |
6.47e-19 |
|
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: 85.19 E-value: 6.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 2 LSIQDLHVA-VEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGRVEFKGKNLLELAAEDRAgEGI 80
Cdd:COG4988 337 IELEDVSFSyPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGF--LPPYSGSILINGVDLSDLDPASWR-RQI 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 81 FMAFQYPVEIPGvsnqfflqTALNAVRNYRG-------QEALDRFDFQDLMEekikllQMPEDLLTR--SVNVGFSGGEK 151
Cdd:COG4988 414 AWVPQNPYLFAG--------TIRENLRLGRPdasdeelEAALEAAGLDEFVA------ALPDGLDTPlgEGGRGLSGGQA 479
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488998194 152 KRNDILQMAVLEPELCILDESDSGLDIDALKIVSQGVNALRDGkRAFIIVTHyqRILDYIKPDYVHVLYQGRIVKSGDF 230
Cdd:COG4988 480 QRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKG-RTVILITH--RLALLAQADRILVLDDGRIVEQGTH 555
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-228 |
6.87e-19 |
|
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: 81.88 E-value: 6.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 2 LSIQDLHVAVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGRVEFKGKNLLELA-AEDRAGEGI 80
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLI--KPDSGEITFDGKSYQKNIeALRRIGALI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 81 fmafQYPVEIPGVSNQFFLQTALNA--VRNYRGQEALDRFDFQDLMEEKIKllqmpedlltrsvnvGFSGGEKKRNDILQ 158
Cdd:cd03268 79 ----EAPGFYPNLTARENLRLLARLlgIRKKRIDEVLDVVGLKDSAKKKVK---------------GFSLGMKQRLGIAL 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 159 MAVLEPELCILDESDSGLDIDALKIVSQGVNALRDGKRAFIIVTHYQRILDYIKPDYVhVLYQGRIVKSG 228
Cdd:cd03268 140 ALLGNPDLLILDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIG-IINKGKLIEEG 208
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-226 |
1.11e-18 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 81.63 E-value: 1.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 1 MLSIQDLH----VAVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDyeVTGGRVEFKGKNLLELAAEDRA 76
Cdd:COG1136 4 LLELRNLTksygTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDR--PTSGEVLIDGQDISSLSERELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 77 ---GEGIFMAFQypveipgvsnQFFLQTALNAVRN------YRG----------QEALDRFDFQDLMEekikllQMPEDL 137
Cdd:COG1136 82 rlrRRHIGFVFQ----------FFNLLPELTALENvalpllLAGvsrkerreraRELLERVGLGDRLD------HRPSQL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 138 ltrsvnvgfSGGEKKRndilqMA-----VLEPELCILDE------SDSGLDI-DALkivsQGVNalRDGKRAFIIVTHYQ 205
Cdd:COG1136 146 ---------SGGQQQR-----VAiaralVNRPKLILADEptgnldSKTGEEVlELL----RELN--RELGTTIVMVTHDP 205
|
250 260
....*....|....*....|.
gi 488998194 206 RILDYIkpDYVHVLYQGRIVK 226
Cdd:COG1136 206 ELAARA--DRVIRLRDGRIVS 224
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
12-223 |
1.62e-18 |
|
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: 79.73 E-value: 1.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 12 EDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGRVEFKGKNLLELAAEDragegifmafqypveip 91
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLR--LYDPTSGEILIDGVDLRDLDLES----------------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 92 gvsnqffLQTALNAVrnyrGQEALdrfdfqdlmeekikllqmpedLLTRSV--NVgFSGGEKKRNDILQMAVLEPELCIL 169
Cdd:cd03228 74 -------LRKNIAYV----PQDPF---------------------LFSGTIreNI-LSGGQRQRIAIARALLRDPPILIL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488998194 170 DESDSGLDIDALKIVSQGVNALRDGkRAFIIVTHyqRILDYIKPDYVHVLYQGR 223
Cdd:cd03228 121 DEATSALDPETEALILEALRALAKG-KTVIVIAH--RLSTIRDADRIIVLDDGR 171
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-229 |
1.72e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 81.96 E-value: 1.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 1 MLSIQDLHVA--VEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGRVEFKGK-----NLLELaae 73
Cdd:PRK13632 7 MIKVENVSFSypNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGL--LKPQSGEIKIDGItiskeNLKEI--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 74 dRAGEGIFmaFQYPveipgvSNQFFLQTALNAV----RNYRgqeaLDRFDFQDLMEEKIKLLQMpEDLLTRSVNvGFSGG 149
Cdd:PRK13632 82 -RKKIGII--FQNP------DNQFIGATVEDDIafglENKK----VPPKKMKDIIDDLAKKVGM-EDYLDKEPQ-NLSGG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 150 EKKRNDILQMAVLEPELCILDESDSGLDIDALKIVSQGVNALRD-GKRAFIIVTHyqRILDYIKPDYVHVLYQGRIVKSG 228
Cdd:PRK13632 147 QKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKtRKKTLISITH--DMDEAILADKVIVFSEGKLIAQG 224
|
.
gi 488998194 229 D 229
Cdd:PRK13632 225 K 225
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
17-228 |
3.43e-18 |
|
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: 80.11 E-value: 3.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 17 LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGRVEFKGKNLLELAAEDRAGEGIfmAFQYPV---EIPGV 93
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTL--LKPTSGRATVAGHDVVREPREVRRRIGI--VFQDLSvddELTGW 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 94 SNqFFLQTALNAVRNYRGQEALDR-FDFQDLMEEKIKLLQMpedlltrsvnvgFSGGEKKRNDILQMAVLEPELCILDES 172
Cdd:cd03265 92 EN-LYIHARLYGVPGAERRERIDElLDFVGLLEAADRLVKT------------YSGGMRRRLEIARSLVHRPEVLFLDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 173 DSGLDIDALKIVSQGVNALrdgKRAF----IIVTHYQRILDYIKpDYVHVLYQGRIVKSG 228
Cdd:cd03265 159 TIGLDPQTRAHVWEYIEKL---KEEFgmtiLLTTHYMEEAEQLC-DRVAIIDHGRIIAEG 214
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
12-248 |
3.75e-18 |
|
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: 83.34 E-value: 3.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 12 EDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGRVEFKGKNLLELAAEDRAgEGIFMAFQypveip 91
Cdd:COG2274 486 DSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLG--LYEPTSGRILIDGIDLRQIDPASLR-RQIGVVLQ------ 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 92 gvSNQFFLQTALNavrNYRGqeALDRFDFQDLME--------EKIKllQMPEDLLTRsvnVG-----FSGGEKKRndiLQ 158
Cdd:COG2274 557 --DVFLFSGTIRE---NITL--GDPDATDEEIIEaarlaglhDFIE--ALPMGYDTV---VGeggsnLSGGQRQR---LA 621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 159 MA---VLEPELCILDESDSGLDIDALKIVSQGVNALRDGkRAFIIVTHYQRILDYIkpDYVHVLYQGRIVKSGDFSLVkq 235
Cdd:COG2274 622 IAralLRNPRILILDEATSALDAETEAIILENLRRLLKG-RTVIIIAHRLSTIRLA--DRIIVLDKGRIVEDGTHEEL-- 696
|
250
....*....|....
gi 488998194 236 LEEQG-YGWLTEQQ 248
Cdd:COG2274 697 LARKGlYAELVQQQ 710
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
17-228 |
1.29e-17 |
|
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: 80.13 E-value: 1.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 17 LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGRVEFKGKNLLELAAEDRagEGIFMAFQYPV---EIPGV 93
Cdd:TIGR01188 9 VDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTL--LRPTSGTARVAGYDVVREPRKVR--RSIGIVPQYASvdeDLTGR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 94 SNQFF---LQTALNAVRNYRGQEALDRFDFQDLMEEKIKllqmpedlltrsvnvGFSGGEKKRNDILQMAVLEPELCILD 170
Cdd:TIGR01188 85 ENLEMmgrLYGLPKDEAEERAEELLELFELGEAADRPVG---------------TYSGGMRRRLDIAASLIHQPDVLFLD 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488998194 171 ESDSGLDIDALKIVSQGVNALRDGKRAFIIVTHYQRILDYIKpDYVHVLYQGRIVKSG 228
Cdd:TIGR01188 150 EPTTGLDPRTRRAIWDYIRALKEEGVTILLTTHYMEEADKLC-DRIAIIDHGRIIAEG 206
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-228 |
1.45e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 79.19 E-value: 1.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 2 LSIQDLHVAVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagredyevtggrvefkgKNLLELAAEDRA----- 76
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVF-----------------NRLIELYPEARVsgevy 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 77 --GEGIF------------MAFQYPVEIPGVSnqFFLQTALNAVRNyrgQEALDRFDFQDLMEEKIKLLQMPEDLLTR-- 140
Cdd:PRK14247 67 ldGQDIFkmdvielrrrvqMVFQIPNPIPNLS--IFENVALGLKLN---RLVKSKKELQERVRWALEKAQLWDEVKDRld 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 141 SVNVGFSGGEKKRNDILQMAVLEPELCILDESDSGLD-IDALKIVSQGVNALRDgkRAFIIVTHYQRILDYIKpDYVHVL 219
Cdd:PRK14247 142 APAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDpENTAKIESLFLELKKD--MTIVLVTHFPQQAARIS-DYVAFL 218
|
....*....
gi 488998194 220 YQGRIVKSG 228
Cdd:PRK14247 219 YKGQIVEWG 227
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-203 |
1.56e-17 |
|
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: 78.34 E-value: 1.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 2 LSIQDLHVAVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGRVEFKGKNL-LELAAEDRAGEGI 80
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLE--EPDSGTIIIDGLKLtDDKKNINELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 81 FMAFQypveipgvsnQFFLQTALNAVRNyrgqealdrfdfqdLMEEKIKLLQMP--------EDLLTRsvnVG------- 145
Cdd:cd03262 79 GMVFQ----------QFNLFPHLTVLEN--------------ITLAPIKVKGMSkaeaeeraLELLEK---VGladkada 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488998194 146 ----FSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVSQGVNALRDGKRAFIIVTH 203
Cdd:cd03262 132 ypaqLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTH 193
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-203 |
1.81e-17 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 79.05 E-value: 1.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 1 MLSIQDLHVAVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDY--EVT-GGRVEFKGKNL-------LEL 70
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLnpEVTiTGSIVYNGHNIysprtdtVDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 71 AAEdragegIFMAFQYPveipgvsNQFFLQTALNAVRNYRGQEALDRFDFQDLMEEKIKLLQMPEDLLTR--SVNVGFSG 148
Cdd:PRK14239 85 RKE------IGMVFQQP-------NPFPMSIYENVVYGLRLKGIKDKQVLDEAVEKSLKGASIWDEVKDRlhDSALGLSG 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488998194 149 GEKKRNDILQMAVLEPELCILDESDSGLD-IDALKIvSQGVNALRDgKRAFIIVTH 203
Cdd:PRK14239 152 GQQQRVCIARVLATSPKIILLDEPTSALDpISAGKI-EETLLGLKD-DYTMLLVTR 205
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
3-203 |
1.91e-17 |
|
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: 77.96 E-value: 1.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 3 SIQDLHVAVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGRVEFKGKNllelAAEDRAGEGiFM 82
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILG--LLKPTSGSIRVFGKP----LEKERKRIG-YV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 83 A------FQYPVEIPGVsnqfflqTALNAVRNYRGQEALDRFDFQDLmEEKIKLLQMpEDLLTRsvNVG-FSGGEKKRND 155
Cdd:cd03235 74 PqrrsidRDFPISVRDV-------VLMGLYGHKGLFRRLSKADKAKV-DEALERVGL-SELADR--QIGeLSGGQQQRVL 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488998194 156 ILQMAVLEPELCILDESDSGLDIDALKIVSQGVNALRDGKRAFIIVTH 203
Cdd:cd03235 143 LARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTH 190
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-229 |
1.93e-17 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 80.14 E-value: 1.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 1 MLSIQDLHVAVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGRVEFKGKNLLELAAEDRageGI 80
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFE--TPDSGRILLDGRDVTGLPPEKR---NV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 81 FMAFQ---------------YPVEIPGVSnqfflqtalNAVRNYRGQEALDRFDFQDLmEEKikllqMPEDLltrsvnvg 145
Cdd:COG3842 80 GMVFQdyalfphltvaenvaFGLRMRGVP---------KAEIRARVAELLELVGLEGL-ADR-----YPHQL-------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 146 fSGGEKKRndilqMA-----VLEPELCILDESDSGLD-------IDALKivsqgvNALRDGKRAFIIVTHYQ-------- 205
Cdd:COG3842 137 -SGGQQQR-----VAlaralAPEPRVLLLDEPLSALDaklreemREELR------RLQRELGITFIYVTHDQeealalad 204
|
250 260
....*....|....*....|....
gi 488998194 206 RILdyikpdyvhVLYQGRIVKSGD 229
Cdd:COG3842 205 RIA---------VMNDGRIEQVGT 219
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
14-228 |
3.55e-17 |
|
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: 76.82 E-value: 3.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 14 KAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEVTGGRVEFKGKNLLELAAEDRAG----EGIFMAFqypve 89
Cdd:cd03213 22 KQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGVSGEVLINGRPLDKRSFRKIIGyvpqDDILHPT----- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 90 ipgvsnqfflQTAlnavrnyrgQEALDrfdfqdlMEEKIKllqmpedlltrsvnvGFSGGEKKRNDI-LQMaVLEPELCI 168
Cdd:cd03213 97 ----------LTV---------RETLM-------FAAKLR---------------GLSGGERKRVSIaLEL-VSNPSLLF 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488998194 169 LDESDSGLD-IDALKIVSQgVNALRDGKRAFIIVTHYQRILDYIKPDYVHVLYQGRIVKSG 228
Cdd:cd03213 135 LDEPTSGLDsSSALQVMSL-LRRLADTGRTIICSIHQPSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
12-240 |
4.24e-17 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 78.24 E-value: 4.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 12 EDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGRVEFKG------KNLLELaaEDRAGegifMAFQ 85
Cdd:TIGR04520 13 SEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGL--LLPTSGKVTVDGldtldeENLWEI--RKKVG----MVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 86 YPveipgvSNQFFLQTALNAV----RNyRGqeaLDRFDFQDLMEEKIKLLQMpEDLLTRSVNVgFSGGEKKRNDILQMAV 161
Cdd:TIGR04520 85 NP------DNQFVGATVEDDVafglEN-LG---VPREEMRKRVDEALKLVGM-EDFRDREPHL-LSGGQKQRVAIAGVLA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 162 LEPELCILDESDSGLDIDALKIVSQGVNAL-RDGKRAFIIVTHYqrILDYIKPDYVHVLYQGRIVKSGD----FSLVKQL 236
Cdd:TIGR04520 153 MRPDIIILDEATSMLDPKGRKEVLETIRKLnKEEGITVISITHD--MEEAVLADRVIVMNKGKIVAEGTpreiFSQVELL 230
|
....
gi 488998194 237 EEQG 240
Cdd:TIGR04520 231 KEIG 234
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-228 |
9.40e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 77.01 E-value: 9.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 1 MLSIQDLHVAVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGR-EDYEV---TGGRVEFKGKNLLELAAEDRA 76
Cdd:PRK14246 10 VFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLiEIYDSkikVDGKVLYFGKDIFQIDAIKLR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 77 GEgIFMAFQYPVEIPGVSnqfflqTALNAVRNYRGQEALDRFDFQDLMEEKIKLLQMPEDLLTR--SVNVGFSGGEKKRN 154
Cdd:PRK14246 90 KE-VGMVFQQPNPFPHLS------IYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRlnSPASQLSGGQQQRL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488998194 155 DILQMAVLEPELCILDESDSGLDIDALKIVSQGVNALRDgKRAFIIVTHYQRILDYIKpDYVHVLYQGRIVKSG 228
Cdd:PRK14246 163 TIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKN-EIAIVIVSHNPQQVARVA-DYVAFLYNGELVEWG 234
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-203 |
1.34e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 78.57 E-value: 1.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 1 MLSIQDLHVAVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGRVEFkgknllelaaedraGEGI 80
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGEL--EPDSGTVKL--------------GETV 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 81 FMAF--QypveipgvsNQFFL---QTALNAVRNYR--GQEA-----LDRFDFQdlmeekikllqmPEDLLTRsVNVgFSG 148
Cdd:COG0488 379 KIGYfdQ---------HQEELdpdKTVLDELRDGApgGTEQevrgyLGRFLFS------------GDDAFKP-VGV-LSG 435
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488998194 149 GEKKRndiLQMAVL---EPELCILDESDSGLDIDALKIVsqgVNALRDGKRAFIIVTH 203
Cdd:COG0488 436 GEKAR---LALAKLllsPPNVLLLDEPTNHLDIETLEAL---EEALDDFPGTVLLVSH 487
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
17-227 |
2.66e-16 |
|
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: 73.62 E-value: 2.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 17 LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGRVEFKGKNLLELAAEDRAGEGIFMAFQYPVeipgvsnq 96
Cdd:cd03216 16 LDGVSLSVRRGEVHALLGENGAGKSTLMKILSG--LYKPDSGEILVDGKEVSFASPRDARRAGIAMVYQLSV-------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 97 fflqtalnavrnyrgqealdrfdfqdlmeekikllqmpedlltrsvnvgfsgGEKKRNDILQMAVLEPELCILDESDSGL 176
Cdd:cd03216 86 ----------------------------------------------------GERQMVEIARALARNARLLILDEPTAAL 113
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488998194 177 DIDALKIVSQGVNALRDGKRAFIIVTHYqriLDYIKP--DYVHVLYQGRIVKS 227
Cdd:cd03216 114 TPAEVERLFKVIRRLRAQGVAVIFISHR---LDEVFEiaDRVTVLRDGRVVGT 163
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
16-248 |
2.72e-16 |
|
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: 75.27 E-value: 2.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 16 ILRGLNLEVRPGEVHAIMGPNGSGKSTLsATLAGREdYEVTGGRVEFKGKNLLELAAEDRAGEgIFMAFQYPVeipgvsn 95
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTV-VSLLERF-YDPTSGEILLDGVDIRDLNLRWLRSQ-IGLVSQEPV------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 96 qFFLQTALNAVRnyrgqeaLDRFDFQDLMEEKIKLL--------QMPEDLLTRSVNVGF--SGGEKKRNDILQMAVLEPE 165
Cdd:cd03249 88 -LFDGTIAENIR-------YGKPDATDEEVEEAAKKanihdfimSLPDGYDTLVGERGSqlSGGQKQRIAIARALLRNPK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 166 LCILDESDSGLDIDALKIVSQGVNALRDGkRAFIIVTHyqRILDYIKPDYVHVLYQGRIVKSGDFS-LVKQleEQGYGWL 244
Cdd:cd03249 160 ILLLDEATSALDAESEKLVQEALDRAMKG-RTTIVIAH--RLSTIRNADLIAVLQNGQVVEQGTHDeLMAQ--KGVYAKL 234
|
....
gi 488998194 245 TEQQ 248
Cdd:cd03249 235 VKAQ 238
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-203 |
3.83e-16 |
|
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: 77.33 E-value: 3.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 2 LSIQDLHVAVEDK-AILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGRVEFKGKNLLELAAEDRaGEGI 80
Cdd:TIGR02857 322 LEFSGVSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGF--VDPTEGSIAVNGVPLADADADSW-RDQI 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 81 FMAFQYPveipgvsnQFFLQTALNAVRNYRG-------QEALDRFDFQDLMEEkikllqMPEDLLTR--SVNVGFSGGEK 151
Cdd:TIGR02857 399 AWVPQHP--------FLFAGTIAENIRLARPdasdaeiREALERAGLDEFVAA------LPQGLDTPigEGGAGLSGGQA 464
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488998194 152 KRNDILQMAVLEPELCILDESDSGLDIDALKIVSQGVNALRDGkRAFIIVTH 203
Cdd:TIGR02857 465 QRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQG-RTVLLVTH 515
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-228 |
6.45e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 75.11 E-value: 6.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 1 MLSIQDLHVAVED-KAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGRVEFKG-------KNLLELaa 72
Cdd:PRK13639 1 ILETRDLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGI--LKPTSGEVLIKGepikydkKSLLEV-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 73 edRAGEGIfmAFQYPveipgvSNQFFLQTALNAVRNYRGQEALDRFDFQDLMEEKIKLLQMPEdlLTRSVNVGFSGGEKK 152
Cdd:PRK13639 77 --RKTVGI--VFQNP------DDQLFAPTVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEG--FENKPPHHLSGGQKK 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488998194 153 RNDILQMAVLEPELCILDESDSGLDIDALKIVSQGVNALRDGKRAFIIVTHyQRILDYIKPDYVHVLYQGRIVKSG 228
Cdd:PRK13639 145 RVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTH-DVDLVPVYADKVYVMSDGKIIKEG 219
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
16-228 |
7.93e-16 |
|
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: 74.06 E-value: 7.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 16 ILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGRVEFKGKNLLELAAED-RAGEGIFMAfqypveipgvS 94
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRF--YVPENGRVLVDGHDLALADPAWlRRQVGVVLQ----------E 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 95 NQFFLQTALNAVRnyRGQEALDRfdfqDLMEEKIKL-------LQMPE--DLLTRSVNVGFSGGEKKRNDILQMAVLEPE 165
Cdd:cd03252 85 NVLFNRSIRDNIA--LADPGMSM----ERVIEAAKLagahdfiSELPEgyDTIVGEQGAGLSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488998194 166 LCILDESDSGLDIDALKIVSQGVNALRDGkRAFIIVTHyqRILDYIKPDYVHVLYQGRIVKSG 228
Cdd:cd03252 159 ILIFDEATSALDYESEHAIMRNMHDICAG-RTVIIIAH--RLSTVKNADRIIVMEKGRIVEQG 218
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-228 |
1.70e-15 |
|
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: 72.67 E-value: 1.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 2 LSIQDLHVAVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGRVEFKGKNLLELAAEDRageGIF 81
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLE--EPTSGRIYIGGRDVTDLPPKDR---DIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 82 MAFQypveipgvsnQFFLQTALNAVRNYRGQEALDRFDfQDLMEEKI----KLLQMpEDLLTRSVNvGFSGGEKKRNDIL 157
Cdd:cd03301 76 MVFQ----------NYALYPHMTVYDNIAFGLKLRKVP-KDEIDERVrevaELLQI-EHLLDRKPK-QLSGGQRQRVALG 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488998194 158 QMAVLEPELCILDESDSGLDIDA-LKIVSQGVNALRDGKRAFIIVTHyqrilDYIKP----DYVHVLYQGRIVKSG 228
Cdd:cd03301 143 RAIVREPKVFLMDEPLSNLDAKLrVQMRAELKRLQQRLGTTTIYVTH-----DQVEAmtmaDRIAVMNDGQIQQIG 213
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
14-226 |
2.03e-15 |
|
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: 73.30 E-value: 2.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 14 KAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGRVEFKGKNLLELAAEDRAgegifmAFQYPVeipgv 93
Cdd:TIGR02769 24 APVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLE--KPAQGTVSFRGQDLYQLDRKQRR------AFRRDV----- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 94 snQFFLQTALNAV--------------RNYrgqEALDRFDFQDLMEEKIKLLQMPEDLLTRsVNVGFSGGEKKRNDILQM 159
Cdd:TIGR02769 91 --QLVFQDSPSAVnprmtvrqiigeplRHL---TSLDESEQKARIAELLDMVGLRSEDADK-LPRQLSGGQLQRINIARA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488998194 160 AVLEPELCILDESDSGLDIDALKIVSQGVNALR-DGKRAFIIVTHYQRILDYIKpDYVHVLYQGRIVK 226
Cdd:TIGR02769 165 LAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQqAFGTAYLFITHDLRLVQSFC-QRVAVMDKGQIVE 231
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-177 |
2.13e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 73.20 E-value: 2.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 1 MLSIQDLHVA-----VEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGRVEFKGKNLLELAAEDR 75
Cdd:COG1101 1 MLELKNLSKTfnpgtVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAG--SLPPDSGSILIDGKDVTKLPEYKR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 76 AGegiFMA--FQYPVeipgvsnqffLQTALN-------AVRNYRGQE-----ALDRfDFQDLMEEKIKLLQMP-EDLLTr 140
Cdd:COG1101 79 AK---YIGrvFQDPM----------MGTAPSmtieenlALAYRRGKRrglrrGLTK-KRRELFRELLATLGLGlENRLD- 143
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 488998194 141 sVNVGF-SGGEkkRNDI-LQMAVL-EPELCILDESDSGLD 177
Cdd:COG1101 144 -TKVGLlSGGQ--RQALsLLMATLtKPKLLLLDEHTAALD 180
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-229 |
2.20e-15 |
|
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: 73.00 E-value: 2.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 1 MLSIQDLHVAVEDKA----ILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYevTGGRVEFKGKNLLELAAEDR- 75
Cdd:cd03258 1 MIELKNVSKVFGDTGgkvtALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERP--TSGSVLVDGTDLTLLSGKELr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 76 -AGEGIFMAFQ---------------YPVEIPGVSnqfflqtalnavRNYRGQEALDRFDFQDLmEEKIKllQMPEDLlt 139
Cdd:cd03258 79 kARRRIGMIFQhfnllssrtvfenvaLPLEIAGVP------------KAEIEERVLELLELVGL-EDKAD--AYPAQL-- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 140 rsvnvgfSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVsqgVNALRDGKRAF----IIVTHYqriLDYIKP-- 213
Cdd:cd03258 142 -------SGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSI---LALLRDINRELgltiVLITHE---MEVVKRic 208
|
250
....*....|....*.
gi 488998194 214 DYVHVLYQGRIVKSGD 229
Cdd:cd03258 209 DRVAVMEKGEVVEEGT 224
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
12-228 |
2.45e-15 |
|
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: 72.64 E-value: 2.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 12 EDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGRVEFKGKNLLELAaEDRAGEGIFMAFQYPVEIP 91
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRF--YDPQKGQILIDGIDIRDIS-RKSLRSMIGVVLQDTFLFS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 92 GvsnqfflqTALNAVRnYRGQEALDrfdfqDLMEEKIKLLQM-------PEDLLTRSVNVG--FSGGEKKRNDILQMAVL 162
Cdd:cd03254 91 G--------TIMENIR-LGRPNATD-----EEVIEAAKEAGAhdfimklPNGYDTVLGENGgnLSQGERQLLAIARAMLR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488998194 163 EPELCILDESDSGLDIDALKIVSQGVNALRDGKRAFIIVTHYQRILDyikPDYVHVLYQGRIVKSG 228
Cdd:cd03254 157 DPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKN---ADKILVLDDGKIIEEG 219
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
13-240 |
2.72e-15 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 74.76 E-value: 2.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 13 DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGRVEFKGKNLLELaaedragegifmafqypveipg 92
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALL--QNLYQPTGGQVLLDGVPLVQY---------------------- 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 93 vsNQFFLQTALNAVrnyrGQE--------------ALDRFDFQDLMEEKIK------LLQMPEDLLTrsvNVG-----FS 147
Cdd:TIGR00958 549 --DHHYLHRQVALV----GQEpvlfsgsvreniayGLTDTPDEEIMAAAKAanahdfIMEFPNGYDT---EVGekgsqLS 619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 148 GGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVSQGVNAlrdGKRAFIIVTHYQRILDyiKPDYVHVLYQGRIVKS 227
Cdd:TIGR00958 620 GGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSR---ASRTVLLIAHRLSTVE--RADQILVLKKGSVVEM 694
|
250
....*....|...
gi 488998194 228 GDFslvKQLEEQG 240
Cdd:TIGR00958 695 GTH---KQLMEDQ 704
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
14-225 |
3.02e-15 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 73.18 E-value: 3.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 14 KAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGRVEFKGKNLLELAAEDRAgegifmAFQYPVeipgv 93
Cdd:PRK10419 25 QTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLE--SPSQGNVSWRGEPLAKLNRAQRK------AFRRDI----- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 94 snQFFLQTALNAV-----------RNYRGQEALDRFDFQDLMEEKIKLLQMPEDLLTRsVNVGFSGGEKKRNDILQMAVL 162
Cdd:PRK10419 92 --QMVFQDSISAVnprktvreiirEPLRHLLSLDKAERLARASEMLRAVDLDDSVLDK-RPPQLSGGQLQRVCLARALAV 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 163 EPELCILDESDSGLD-------IDALKIVSQgvnalRDGKrAFIIVTHYQRILDYIkPDYVHVLYQGRIV 225
Cdd:PRK10419 169 EPKLLILDEAVSNLDlvlqagvIRLLKKLQQ-----QFGT-ACLFITHDLRLVERF-CQRVMVMDNGQIV 231
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
14-230 |
3.85e-15 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 73.59 E-value: 3.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 14 KAIlRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGRVEFKGKNLLELAAEDR--AGEGIFMAFQYPVeip 91
Cdd:PRK15079 35 KAV-DGVTLRLYEGETLGVVGESGCGKSTFARAIIGL--VKATDGEVAWLGKDLLGMKDDEWraVRSDIQMIFQDPL--- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 92 gvsnqfflqTALNAvRNYRGQ---EALDRFD---FQDLMEEKIKLLQMPEDLLTRSVNV---GFSGGEKKRNDILQMAVL 162
Cdd:PRK15079 109 ---------ASLNP-RMTIGEiiaEPLRTYHpklSRQEVKDRVKAMMLKVGLLPNLINRyphEFSGGQCQRIGIARALIL 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488998194 163 EPELCILDESDSGLDIdalKIVSQGVNALRDGKR----AFIIVTHYQRILDYIKpDYVHVLYQGRIVKSGDF 230
Cdd:PRK15079 179 EPKLIICDEPVSALDV---SIQAQVVNLLQQLQRemglSLIFIAHDLAVVKHIS-DRVLVMYLGHAVELGTY 246
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
13-228 |
5.88e-15 |
|
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: 71.50 E-value: 5.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 13 DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGRVEFKGKNLLELAAEDRageGIFMAFQYPVEIPG 92
Cdd:cd03300 12 GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFE--TPTSGEILLDGKDITNLPPHKR---PVNTVFQNYALFPH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 93 VS---N-QFFLQTAlnavrnyrgqeALDRFDFQDLMEEKIKLLQMpEDLLTRSVNvGFSGGEKKRNDILQMAVLEPELCI 168
Cdd:cd03300 87 LTvfeNiAFGLRLK-----------KLPKAEIKERVAEALDLVQL-EGYANRKPS-QLSGGQQQRVAIARALVNEPKVLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488998194 169 LDESDSGLDidaLKIVSQGVNALRDGKR----AFIIVTHYQRILDYIKpDYVHVLYQGRIVKSG 228
Cdd:cd03300 154 LDEPLGALD---LKLRKDMQLELKRLQKelgiTFVFVTHDQEEALTMS-DRIAVMNKGKIQQIG 213
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
12-228 |
6.93e-15 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 73.66 E-value: 6.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 12 EDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGRVEFKGKNLLELAAED-RagEGIFMAFQypvei 90
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRF--YDPTSGRILIDGVDIRDLTLESlR--RQIGVVPQ----- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 91 pgvsnQFFL--QTALNAVRnYRGQEALDrfdfqDLMEEKIKLLQ-------MPEDLLT----RSVNvgFSGGEKKRNDIL 157
Cdd:COG1132 422 -----DTFLfsGTIRENIR-YGRPDATD-----EEVEEAAKAAQahefieaLPDGYDTvvgeRGVN--LSGGQRQRIAIA 488
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488998194 158 QMAVLEPELCILDESDSGLDIDALKIVSQGVNALRDGKRAFII------VTHYQRILdyikpdyvhVLYQGRIVKSG 228
Cdd:COG1132 489 RALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIahrlstIRNADRIL---------VLDDGRIVEQG 556
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-85 |
7.07e-15 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 71.31 E-value: 7.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 1 MLSIQDLHVAVEDKA----ILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDyeVTGGRVEFKGKNLLELAAEDRA 76
Cdd:COG4181 8 IIELRGLTKTVGTGAgeltILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDR--PTSGTVRLAGQDLFALDEDARA 85
|
90
....*....|....*
gi 488998194 77 ---GEGI---FMAFQ 85
Cdd:COG4181 86 rlrARHVgfvFQSFQ 100
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
13-228 |
1.17e-14 |
|
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: 70.61 E-value: 1.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 13 DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGRVEFKGKNLLELAaeDRAGEGIFMAFQYPVEIPG 92
Cdd:cd03263 14 TKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGEL--RPTSGTAYINGYSIRTDR--KAARQSLGYCPQFDALFDE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 93 VSN----QFFLQtalnaVRNYRGQEAldrfdfQDLMEEKIKLLQMPEDLLTRSVNvgFSGGEKKRndiLQ--MAVL-EPE 165
Cdd:cd03263 90 LTVrehlRFYAR-----LKGLPKSEI------KEEVELLLRVLGLTDKANKRART--LSGGMKRK---LSlaIALIgGPS 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488998194 166 LCILDESDSGLDIDALKIVSQGVNALRDGkRAFIIVTHYQRILDYIKpDYVHVLYQGRIVKSG 228
Cdd:cd03263 154 VLLLDEPTSGLDPASRRAIWDLILEVRKG-RSIILTTHSMDEAEALC-DRIAIMSDGKLRCIG 214
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
14-225 |
1.21e-14 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 70.76 E-value: 1.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 14 KAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEVTGGRVEfkgknllelaaedragegiFMAFQYPVEIPGV 93
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD-------------------VPDNQFGREASLI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 94 SNQFFLQTALNAVrnyrgqEALDRFDFQD--LMEEKIKLLqmpedlltrsvnvgfSGGEKKRNDILQMAVLEPELCILDE 171
Cdd:COG2401 104 DAIGRKGDFKDAV------ELLNAVGLSDavLWLRRFKEL---------------STGQKFRFRLALLLAERPKLLVIDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488998194 172 SDSGLDIDALKIVSQGV-NALRDGKRAFIIVTHYQRILDYIKPD-YVHVLYQGRIV 225
Cdd:COG2401 163 FCSHLDRQTAKRVARNLqKLARRAGITLVVATHHYDVIDDLQPDlLIFVGYGGVPE 218
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-229 |
1.59e-14 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 71.68 E-value: 1.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 1 MLSIQDLHV----------AVEDkailrgLNLEVRPGEVHAIMGPNGSGKS----TLSATLA--GRedyevTGGRVEFKG 64
Cdd:PRK09473 12 LLDVKDLRVtfstpdgdvtAVND------LNFSLRAGETLGIVGESGSGKSqtafALMGLLAanGR-----IGGSATFNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 65 KNLLELAAED----RAgEGIFMAFQYPVeipgvsnqfflqTALNAVRNYRGQ--EAL---DRFDFQDLMEEKIKLL---Q 132
Cdd:PRK09473 81 REILNLPEKElnklRA-EQISMIFQDPM------------TSLNPYMRVGEQlmEVLmlhKGMSKAEAFEESVRMLdavK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 133 MPEdlLTRSVNV---GFSGGEKKRNDIlQMAVL-EPELCILDESDSGLDIdalKIVSQGVNALRDGKRAF----IIVTHY 204
Cdd:PRK09473 148 MPE--ARKRMKMyphEFSGGMRQRVMI-AMALLcRPKLLIADEPTTALDV---TVQAQIMTLLNELKREFntaiIMITHD 221
|
250 260
....*....|....*....|....*
gi 488998194 205 QRILDYIkPDYVHVLYQGRIVKSGD 229
Cdd:PRK09473 222 LGVVAGI-CDKVLVMYAGRTMEYGN 245
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-203 |
1.65e-14 |
|
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: 70.00 E-value: 1.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 2 LSIQDLHVAVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGRVEFKGKNlLELAAEDRAG---- 77
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGI--ILPDSGEVLFDGKP-LDIAARNRIGylpe 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 78 -EGIFMAFQ------YPVEIPGVSnqffLQTALNAVRNYrgqeaLDRFDFQDLMEEKIKLLqmpedlltrsvnvgfSGGE 150
Cdd:cd03269 78 eRGLYPKMKvidqlvYLAQLKGLK----KEEARRRIDEW-----LERLELSEYANKRVEEL---------------SKGN 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488998194 151 KKRNDILQMAVLEPELCILDESDSGLDIDALKIVSQGVNALRDGKRAFIIVTH 203
Cdd:cd03269 134 QQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTH 186
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-203 |
1.68e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 72.40 E-value: 1.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 4 IQDLHVAVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYevTGGRVEF-KGKNLLELAAEDRAGEG--- 79
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEP--DSGEVSIpKGLRIGYLPQEPPLDDDltv 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 80 ---IFMAFQYPVEIPGVSNQFFLQTALNAVRNYRGQEALDRFDFQDL--MEEKIK--L--LQMPEDLLTRSVNVgFSGGE 150
Cdd:COG0488 79 ldtVLDGDAELRALEAELEELEAKLAEPDEDLERLAELQEEFEALGGweAEARAEeiLsgLGFPEEDLDRPVSE-LSGGW 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488998194 151 KKRNDILQMAVLEPELCILDESDSGLDIDA---LkivsqgVNALRDGKRAFIIVTH 203
Cdd:COG0488 158 RRRVALARALLSEPDLLLLDEPTNHLDLESiewL------EEFLKNYPGTVLVVSH 207
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
13-228 |
1.92e-14 |
|
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: 69.99 E-value: 1.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 13 DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGR-EDYEVTGGRVEFKGKNLlelaaeDRAgegifmafQYPVEIP 91
Cdd:cd03234 19 YARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRvEGGGTTSGQILFNGQPR------KPD--------QFQKCVA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 92 GVSNQFFLQTALnAVRNY-------RGQEALDrfDFQDLMEEKIKLLQMPEDLLTRSVNV-GFSGGEKKRNDILQMAVLE 163
Cdd:cd03234 85 YVRQDDILLPGL-TVRETltytailRLPRKSS--DAIRKKRVEDVLLRDLALTRIGGNLVkGISGGERRRVSIAVQLLWD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488998194 164 PELCILDESDSGLD-IDALKIVSQGVNALRDGKraFIIVTHYQ------RILDYIKpdyvhVLYQGRIVKSG 228
Cdd:cd03234 162 PKVLILDEPTSGLDsFTALNLVSTLSQLARRNR--IVILTIHQprsdlfRLFDRIL-----LLSSGEIVYSG 226
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-223 |
2.24e-14 |
|
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: 68.75 E-value: 2.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 2 LSIQDLHVAVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGRVEFKGKNLLELAAEDRAGEG-I 80
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLE--EPDSGSILIDGEDLTDLEDELPPLRRrI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 81 FMAFQYPVEIPGvsnqfflqtalnavrnyrgqealdrfdfqdlmeekikllqmpedlLTRSVNVGF--SGGEKKRNDILQ 158
Cdd:cd03229 79 GMVFQDFALFPH---------------------------------------------LTVLENIALglSGGQQQRVALAR 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488998194 159 MAVLEPELCILDESDSGLDIDALKIVSQGVNALRDG-KRAFIIVTHYQRILDYIKpDYVHVLYQGR 223
Cdd:cd03229 114 ALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLA-DRVVVLRDGK 178
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-229 |
2.25e-14 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 72.02 E-value: 2.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 1 MLSIQDLHVAV----EDKAILRGLNLEVRPGEVHAIMGPNGSGKS--TLSAT--LAgrEDYEVTGGRVEFKGKNLLELAA 72
Cdd:COG4172 6 LLSVEDLSVAFgqggGTVEAVKGVSFDIAAGETLALVGESGSGKSvtALSILrlLP--DPAAHPSGSILFDGQDLLGLSE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 73 ED-RA--GEGIFMAFQYPveipgvsnqfflQTALNAV--------------RNYRGQEALDRFdfqdlmeekIKLLQM-- 133
Cdd:COG4172 84 RElRRirGNRIAMIFQEP------------MTSLNPLhtigkqiaevlrlhRGLSGAAARARA---------LELLERvg 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 134 ---PEDLLTRsvnvgF----SGGEKKRNDIlQMAVL-EPELCILDESDSGLDIdalKIVSQGVNALRDGKR----AFIIV 201
Cdd:COG4172 143 ipdPERRLDA-----YphqlSGGQRQRVMI-AMALAnEPDLLIADEPTTALDV---TVQAQILDLLKDLQRelgmALLLI 213
|
250 260 270
....*....|....*....|....*....|..
gi 488998194 202 TH----YQRIldyikPDYVHVLYQGRIVKSGD 229
Cdd:COG4172 214 THdlgvVRRF-----ADRVAVMRQGEIVEQGP 240
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
13-224 |
2.45e-14 |
|
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: 69.81 E-value: 2.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 13 DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGRVEFKGKNlLELAAEDRAGEGIFMAFQYPVEIPG 92
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALL--ENFYQPQGGQVLLDGKP-ISQYEHKYLHSKVSLVGQEPVLFAR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 93 vSNQFFLQTALNAVRNYRGQEALDRFDFQDLMEEkikllqMPEDLLTRSVNVG--FSGGEKKRNDILQMAVLEPELCILD 170
Cdd:cd03248 103 -SLQDNIAYGLQSCSFECVKEAAQKAHAHSFISE------LASGYDTEVGEKGsqLSGGQKQRVAIARALIRNPQVLILD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488998194 171 ESDSGLDIDALKIVSQgvnALRDG--KRAFIIVTHyqRILDYIKPDYVHVLYQGRI 224
Cdd:cd03248 176 EATSALDAESEQQVQQ---ALYDWpeRRTVLVIAH--RLSTVERADQILVLDGGRI 226
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
13-228 |
2.77e-14 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 71.67 E-value: 2.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 13 DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGRVEFKGKNLLELAAED-RAgegifmafqypvEIP 91
Cdd:TIGR02203 344 DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIP--RFYEPDSGQILLDGHDLADYTLASlRR------------QVA 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 92 GVSNQFFL--QTALNAVRNYRG--------QEALDRFDFQDLMEekikllQMPEDLLTrsvNVG-----FSGGEKKRNDI 156
Cdd:TIGR02203 410 LVSQDVVLfnDTIANNIAYGRTeqadraeiERALAAAYAQDFVD------KLPLGLDT---PIGengvlLSGGQRQRLAI 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488998194 157 LQMAVLEPELCILDESDSGLDIDALKIVSQGVNALRDGkRAFIIVTHyqRILDYIKPDYVHVLYQGRIVKSG 228
Cdd:TIGR02203 481 ARALLKDAPILILDEATSALDNESERLVQAALERLMQG-RTTLVIAH--RLSTIEKADRIVVMDDGRIVERG 549
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
17-240 |
2.85e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 70.43 E-value: 2.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 17 LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEvtGGRVEFKGKNLLELAAED-RAGEGifMAFQYPveipgvSN 95
Cdd:PRK13635 23 LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPE--AGTITVGGMVLSEETVWDvRRQVG--MVFQNP------DN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 96 QFFLQTALNAVRNYRGQEALDRFDFQDLMEEKIKLLQMpEDLLTRSVNvGFSGGEKKRNDILQMAVLEPELCILDESDSG 175
Cdd:PRK13635 93 QFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGM-EDFLNREPH-RLSGGQKQRVAIAGVLALQPDIIILDEATSM 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 176 LDIDALKIVSQGVNALRDGKRAFII-VTHyqRILDYIKPDYVHVLYQGRIVKSGD----FSLVKQLEEQG 240
Cdd:PRK13635 171 LDPRGRREVLETVRQLKEQKGITVLsITH--DLDEAAQADRVIVMNKGEILEEGTpeeiFKSGHMLQEIG 238
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-203 |
6.05e-14 |
|
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: 67.09 E-value: 6.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 2 LSIQDLHVAVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGRVEFkgknllelaaedragegif 81
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGEL--EPDEGIVTW------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 82 mafqypveIPGVSNQFFLQtalnavrnyrgqealdrfdfqdlmeekikllqmpedlltrsvnvgFSGGEKKRNDILQMAV 161
Cdd:cd03221 60 --------GSTVKIGYFEQ---------------------------------------------LSGGEKMRLALAKLLL 86
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488998194 162 LEPELCILDESDSGLDIDALKIVsqgVNALRDGKRAFIIVTH 203
Cdd:cd03221 87 ENPNLLLLDEPTNHLDLESIEAL---EEALKEYPGTVILVSH 125
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-228 |
7.03e-14 |
|
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: 67.72 E-value: 7.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 2 LSIQDLHVAV--EDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGRVEFKGKNLLELaaedrageg 79
Cdd:cd03247 1 LSINNVSFSYpeQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTG--DLKPQQGEITLDGVPVSDL--------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 80 ifmafqypveipgvsnqfflqtalnavrnyrgqealdrfdfQDLMEEKIKLLQMPEDLLTRSV--NVG--FSGGEKKRND 155
Cdd:cd03247 70 -----------------------------------------EKALSSLISVLNQRPYLFDTTLrnNLGrrFSGGERQRLA 108
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488998194 156 ILQMAVLEPELCILDESDSGLD-IDALKIVSQGVNALRDgkRAFIIVTHYQRILDYIkpDYVHVLYQGRIVKSG 228
Cdd:cd03247 109 LARILLQDAPIVLLDEPTVGLDpITERQLLSLIFEVLKD--KTLIWITHHLTGIEHM--DKILFLENGKIIMQG 178
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-228 |
8.20e-14 |
|
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: 67.99 E-value: 8.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 2 LSIQDLHVAVEDKAILRGLNLEVRPGeVHAIMGPNGSGKSTLSATLAGRedYEVTGGRVEFKGKNLLELAAEDRAGEGiF 81
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATL--TPPSSGTIRIDGQDVLKQPQKLRRRIG-Y 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 82 MAFQYPVeIPGVSNQFFL--QTALNAVRNYRGQEALDRfdfqdlMEEKIKLlqmpEDLLTRSVNvGFSGGEKKRNDILQM 159
Cdd:cd03264 77 LPQEFGV-YPNFTVREFLdyIAWLKGIPSKEVKARVDE------VLELVNL----GDRAKKKIG-SLSGGMRRRVGIAQA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488998194 160 AVLEPELCILDESDSGLDIdALKI------VSQGVNalrdgkRAFIIVTHyqrILDYIKP--DYVHVLYQGRIVKSG 228
Cdd:cd03264 145 LVGDPSILIVDEPTAGLDP-EERIrfrnllSELGED------RIVILSTH---IVEDVESlcNQVAVLNKGKLVFEG 211
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
13-225 |
1.16e-13 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 67.77 E-value: 1.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 13 DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGRVEFKGKNLLELAAEDRA------GegifMAFQ- 85
Cdd:COG2884 14 GREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYG--EERPTSGQVLVNGQDLSRLKRREIPylrrriG----VVFQd 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 86 --------------YPVEIPGVSnqfflqtalNAVRNYRGQEALDRFDfqdlMEEKIKllQMPEDLltrsvnvgfSGGEK 151
Cdd:COG2884 88 frllpdrtvyenvaLPLRVTGKS---------RKEIRRRVREVLDLVG----LSDKAK--ALPHEL---------SGGEQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488998194 152 KRNDILQMAVLEPELCILDESDSGLDID-ALKIVS--QGVNALrdGKrAFIIVTHYQRILDYIkPDYVHVLYQGRIV 225
Cdd:COG2884 144 QRVAIARALVNRPELLLADEPTGNLDPEtSWEIMEllEEINRR--GT-TVLIATHDLELVDRM-PKRVLELEDGRLV 216
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-203 |
1.19e-13 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 67.82 E-value: 1.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 1 MLSIQDLHVAVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGRVEFKGKNLLELAAEdRAGEGI 80
Cdd:PRK10247 7 LLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASL--ISPTSGTLLFEGEDISTLKPE-IYRQQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 81 FMAFQYPVeipgvsnqFFLQTALN------AVRNYRGQEA-----LDRFDfqdlmeekikllqMPEDLLTRSVNvGFSGG 149
Cdd:PRK10247 84 SYCAQTPT--------LFGDTVYDnlifpwQIRNQQPDPAiflddLERFA-------------LPDTILTKNIA-ELSGG 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488998194 150 EKKRNDILQMAVLEPELCILDESDSGLDIDALKIVSQGVNAL-RDGKRAFIIVTH 203
Cdd:PRK10247 142 EKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYvREQNIAVLWVTH 196
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
26-228 |
1.35e-13 |
|
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: 67.71 E-value: 1.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 26 PGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGRVEFKGKNLLE------LAAEDRageGIFMAFQypveipgvsnQFFL 99
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLE--KPDGGTIVLNGTVLFDsrkkinLPPQQR---KIGLVFQ----------QYAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 100 QTALNAVRNYR-GQEALDRFDFQDLMEEKIKLLQMpEDLLTRSVNvGFSGGEKKRNDILQMAVLEPELCILDESDSGLDi 178
Cdd:cd03297 87 FPHLNVRENLAfGLKRKRNREDRISVDELLDLLGL-DHLLNRYPA-QLSGGEKQRVALARALAAQPELLLLDEPFSALD- 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488998194 179 DALKivSQGVNALRDGKRAF----IIVTHYQRILDYIKPDYVhVLYQGRIVKSG 228
Cdd:cd03297 164 RALR--LQLLPELKQIKKNLnipvIFVTHDLSEAEYLADRIV-VMEDGRLQYIG 214
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
13-228 |
1.54e-13 |
|
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: 67.64 E-value: 1.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 13 DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGRVEFKGKNLLELAAED-RAGEGIFmafqyPVEIP 91
Cdd:cd03253 13 GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLF--RFYDVSSGSILIDGQDIREVTLDSlRRAIGVV-----PQDTV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 92 gvsnqFFLQTALNAVRnYRGQEALDrfdfqdlmEEKI----------KLLQMPEDLLTRsvnVG-----FSGGEKKRNDI 156
Cdd:cd03253 86 -----LFNDTIGYNIR-YGRPDATD--------EEVIeaakaaqihdKIMRFPDGYDTI---VGerglkLSGGEKQRVAI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488998194 157 LQMAVLEPELCILDESDSGLDIDALKIVSQGVNALRDGkRAFIIVTHyqRILDYIKPDYVHVLYQGRIVKSG 228
Cdd:cd03253 149 ARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKG-RTTIVIAH--RLSTIVNADKIIVLKDGRIVERG 217
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
20-235 |
1.86e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 68.22 E-value: 1.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 20 LNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGRVEFkGKNLLELAAEDR----AGEGIFMAFQYPveipgvSN 95
Cdd:PRK13643 25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGL--LQPTEGKVTV-GDIVVSSTSKQKeikpVRKKVGVVFQFP------ES 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 96 QFFLQTALNAVRNYRGQEALDRFDFQDLMEEKIKLLQMPEDLLTRSvNVGFSGGEKKRNDILQMAVLEPELCILDESDSG 175
Cdd:PRK13643 96 QLFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFWEKS-PFELSGGQMRRVAIAGILAMEPEVLVLDEPTAG 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488998194 176 LDIDALKIVSQGVNALRDGKRAFIIVTH-YQRILDYikPDYVHVLYQGRIVKSGDFSLVKQ 235
Cdd:PRK13643 175 LDPKARIEMMQLFESIHQSGQTVVLVTHlMDDVADY--ADYVYLLEKGHIISCGTPSDVFQ 233
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-246 |
2.21e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 67.72 E-value: 2.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 1 MLSIQDLHVAVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGRVEFKGKNLlelaaeDRAGEGI 80
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGL--LRPQKGAVLWQGKPL------DYSKRGL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 81 FMAFQYPVEIPGVSNQFFLQTALN-----AVRNY---------RGQEALDRFDFQDLMEEKIKLLqmpedlltrsvnvgf 146
Cdd:PRK13638 73 LALRQQVATVFQDPEQQIFYTDIDsdiafSLRNLgvpeaeitrRVDEALTLVDAQHFRHQPIQCL--------------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 147 SGGEKKRNDILQMAVLEPELCILDESDSGLD-------IDALK-IVSQGVNalrdgkrafIIVTHYQRILDYIKPDYVHV 218
Cdd:PRK13638 138 SHGQKKRVAIAGALVLQARYLLLDEPTAGLDpagrtqmIAIIRrIVAQGNH---------VIISSHDIDLIYEISDAVYV 208
|
250 260 270
....*....|....*....|....*....|....
gi 488998194 219 LYQGRIVKSGD----FSLVKQLEEQGYG--WLTE 246
Cdd:PRK13638 209 LRQGQILTHGApgevFACTEAMEQAGLTqpWLVK 242
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
8-178 |
3.33e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 66.88 E-value: 3.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 8 HVAVEDKaiLRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEvtgGRVEFKGKNLLELAAEDRAGEGIFMA---- 83
Cdd:PRK03695 5 DVAVSTR--LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGS---GSIQFAGQPLEAWSAAELARHRAYLSqqqt 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 84 --FQYPVeipgvsnqF-FLQTALNAVRNYRgqealdrfDFQDLMEEKIKLLQMpEDLLTRSVNvGFSGGEKKR----NDI 156
Cdd:PRK03695 80 ppFAMPV--------FqYLTLHQPDKTRTE--------AVASALNEVAEALGL-DDKLGRSVN-QLSGGEWQRvrlaAVV 141
|
170 180
....*....|....*....|....*
gi 488998194 157 LQMA-VLEPE--LCILDESDSGLDI 178
Cdd:PRK03695 142 LQVWpDINPAgqLLLLDEPMNSLDV 166
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
12-229 |
3.90e-13 |
|
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: 66.49 E-value: 3.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 12 EDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLsATLAGREdYEVTGGRVEFKGKNLLELAAED-RAGEGIfmafqypvei 90
Cdd:cd03251 13 DGPPVLRDISLDIPAGETVALVGPSGSGKSTL-VNLIPRF-YDVDSGRILIDGHDVRDYTLASlRRQIGL---------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 91 pgVSNQFFL--QTALNAVRNYRGQEALDRFDF-------QDLMEEkikllqMPEDLLT----RSVNVgfSGGEKKRNDIL 157
Cdd:cd03251 81 --VSQDVFLfnDTVAENIAYGRPGATREEVEEaaraanaHEFIME------LPEGYDTvigeRGVKL--SGGQRQRIAIA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488998194 158 QMAVLEPELCILDESDSGLDIDALKIVSQGVNALRDGKRAFIIVTHYQRILDyikPDYVHVLYQGRIVKSGD 229
Cdd:cd03251 151 RALLKDPPILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIEN---ADRIVVLEDGKIVERGT 219
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
16-228 |
4.26e-13 |
|
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: 66.13 E-value: 4.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 16 ILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGR-EDYEVTGGRVEFKGKNLLElaaedragegifMAFQYPVEIpgvs 94
Cdd:cd03233 22 ILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRtEGNVSVEGDIHYNGIPYKE------------FAEKYPGEI---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 95 nqfflqtalnavrNYRGQEalDRFDFQDLMEEKIKL-LQMPEDLLTRsvnvGFSGGEKKRNDILQMAVLEPELCILDESD 173
Cdd:cd03233 86 -------------IYVSEE--DVHFPTLTVRETLDFaLRCKGNEFVR----GISGGERKRVSIAEALVSRASVLCWDNST 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488998194 174 SGLD-IDALKIVsQGVNALRDGKRAFIIVTHYQ---RILDYIkpDYVHVLYQGRIVKSG 228
Cdd:cd03233 147 RGLDsSTALEIL-KCIRTMADVLKTTTFVSLYQasdEIYDLF--DKVLVLYEGRQIYYG 202
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
17-233 |
8.01e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 67.50 E-value: 8.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 17 LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGRVEFKGKNLLELAAEDRAGEGIFMAFQYPVEIPGVSNQ 96
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGI--HEPTKGTITINNINYNKLDHKLAAQLGIGIIYQELSVIDELTVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 97 FFLQTALNAVRNYRGQEALDRFDFQDLMEEKIKLLQMPEDLLTRSVNVGFSggEKKRNDILQMAVLEPELCILDESDSGL 176
Cdd:PRK09700 99 ENLYIGRHLTKKVCGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSIS--HKQMLEIAKTLMLDAKVIIMDEPTSSL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 177 ---DIDALKIVsqgVNALRDGKRAFIIVTHYQRILDYIKpDYVHVLYQGRIVKSGDFSLV 233
Cdd:PRK09700 177 tnkEVDYLFLI---MNQLRKEGTAIVYISHKLAEIRRIC-DRYTVMKDGSSVCSGMVSDV 232
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
17-203 |
1.16e-12 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 64.56 E-value: 1.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 17 LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGRVEFKGKNLLELA----AEDRAgegifmafqYPVeipg 92
Cdd:NF040873 8 LHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVL--RPTSGTVRRAGGARVAYVpqrsEVPDS---------LPL---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 93 vsnqfflqTALNAV--------RNYRGQEALDRFDFQDLMEEkiklLQMpEDLLTRSVNvGFSGGEKKRNDILQMAVLEP 164
Cdd:NF040873 73 --------TVRDLVamgrwarrGLWRRLTRDDRAAVDDALER----VGL-ADLAGRQLG-ELSGGQRQRALLAQGLAQEA 138
|
170 180 190
....*....|....*....|....*....|....*....
gi 488998194 165 ELCILDESDSGLDIDALKIVSQGVNALRDGKRAFIIVTH 203
Cdd:NF040873 139 DLLLLDEPTTGLDAESRERIIALLAEEHARGATVVVVTH 177
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
3-223 |
1.20e-12 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 66.83 E-value: 1.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 3 SIQDLHVAVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEVTGGRVEFKGKNLLELAAEdRAGegiFM 82
Cdd:PLN03211 70 KISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNFTGTILANNRKPTKQILK-RTG---FV 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 83 AfQYPVEIPGVSnqffLQTALNAVRNYRGQEALDRFDFQDLMEEKIKLLQMPE---DLLTRSVNVGFSGGEKKRNDILQM 159
Cdd:PLN03211 146 T-QDDILYPHLT----VRETLVFCSLLRLPKSLTKQEKILVAESVISELGLTKcenTIIGNSFIRGISGGERKRVSIAHE 220
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488998194 160 AVLEPELCILDESDSGLD-IDALKIVSQGVNALRDGKrafIIVT--HYQRILDYIKPDYVHVLYQGR 223
Cdd:PLN03211 221 MLINPSLLILDEPTSGLDaTAAYRLVLTLGSLAQKGK---TIVTsmHQPSSRVYQMFDSVLVLSEGR 284
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
17-242 |
1.25e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 65.92 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 17 LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGRVEFKGKnllELAAEDRAGE------GIFMAFQYPvei 90
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGL--HVPTQGSVRVDDT---LITSTSKNKDikqirkKVGLVFQFP--- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 91 pgvSNQFFLQTALNAVRNYRGQEALDRFDFQDLMEEKIKLLQMPEDLLTRSvNVGFSGGEKKRNDILQMAVLEPELCILD 170
Cdd:PRK13649 95 ---ESQLFEETVLKDVAFGPQNFGVSQEEAEALAREKLALVGISESLFEKN-PFELSGGQMRRVAIAGILAMEPKILVLD 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488998194 171 ESDSGLDIDALKIVSQGVNALRDGKRAFIIVTH-YQRILDYikPDYVHVLYQGRIVKSGD----FSLVKQLEEQGYG 242
Cdd:PRK13649 171 EPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHlMDDVANY--ADFVYVLEKGKLVLSGKpkdiFQDVDFLEEKQLG 245
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
17-229 |
1.96e-12 |
|
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: 64.66 E-value: 1.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 17 LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGRVEFKGKNLLELAAEDRageGIFMAFQYPVEIPGVSNQ 96
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGF--IKPDSGKILLNGKDITNLPPEKR---DISYVPQNYALFPHMTVY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 97 FFLQTALNAVRNYRgqealdrfdfqdlMEEKIKLLQMPEDL-----LTRSVNVgFSGGEKKRNDILQMAVLEPELCILDE 171
Cdd:cd03299 90 KNIAYGLKKRKVDK-------------KEIERKVLEIAEMLgidhlLNRKPET-LSGGEQQRVAIARALVVNPKILLLDE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488998194 172 SDSGLDIdalKIVSQGVNALRDGKRAF----IIVTHYQ---RILDyikpDYVHVLYQGRIVKSGD 229
Cdd:cd03299 156 PFSALDV---RTKEKLREELKKIRKEFgvtvLHVTHDFeeaWALA----DKVAIMLNGKLIQVGK 213
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-229 |
2.20e-12 |
|
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: 64.49 E-value: 2.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 2 LSIQDLHVAVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGRVEFKGKNLLELAAEDRAGEGIf 81
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLV--KPDSGKILLDGQDITKLPMHKRARLGI- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 82 mafQY-PVEiPGVSNQFFLQTALNAVRNYRGqeaLDRFDFQDLMEEKIKLLQMPEdlLTRSVNVGFSGGEKKRNDILQMA 160
Cdd:cd03218 78 ---GYlPQE-ASIFRKLTVEENILAVLEIRG---LSKKEREEKLEELLEEFHITH--LRKSKASSLSGGERRRVEIARAL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 161 VLEPELCILDESDSGLDIDALKIVSQGVNALRDGKRAFIIVTHYQR-ILDYIkpDYVHVLYQGRIVKSGD 229
Cdd:cd03218 149 ATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVReTLSIT--DRAYIIYEGKVLAEGT 216
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-229 |
2.25e-12 |
|
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: 65.98 E-value: 2.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 2 LSIQDLHVAVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEVTGGRV----------------EFKGK 65
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEPTSGRIiyhvalcekcgyverpSKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 66 NLL----ELAAED------------RAGEGIFMAFQYPVEIPGvsNQFFLQTALNAVRN--YRGQEALDR-FDFQDLMEE 126
Cdd:TIGR03269 81 PCPvcggTLEPEEvdfwnlsdklrrRIRKRIAIMLQRTFALYG--DDTVLDNVLEALEEigYEGKEAVGRaVDLIEMVQL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 127 KIKLLQMPEDLltrsvnvgfSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVSQGV-NALRDGKRAFIIVTHYQ 205
Cdd:TIGR03269 159 SHRITHIARDL---------SGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALeEAVKASGISMVLTSHWP 229
|
250 260
....*....|....*....|....
gi 488998194 206 RILDYIKpDYVHVLYQGRIVKSGD 229
Cdd:TIGR03269 230 EVIEDLS-DKAIWLENGEIKEEGT 252
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-228 |
3.03e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 64.82 E-value: 3.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 1 MLSIQDL-HVAVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGRVEFKGKNLL-ELAAEDRAGE 78
Cdd:PRK13652 3 LIETRDLcYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGI--LKPTSGSVLIRGEPITkENIREVRKFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 79 GIfmAFQYPveipgvSNQFFLQTALNAVRNYRGQEALDRFDFQDLMEEKIKLLQMpEDLLTRsVNVGFSGGEKKRNDILQ 158
Cdd:PRK13652 81 GL--VFQNP------DDQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHMLGL-EELRDR-VPHHLSGGEKKRVAIAG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 159 MAVLEPELCILDESDSGLDIDALKIVSQGVNALRDGKRAFIIVTHYQRILDYIKPDYVHVLYQGRIVKSG 228
Cdd:PRK13652 151 VIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYG 220
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-203 |
3.21e-12 |
|
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: 63.64 E-value: 3.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 2 LSIQDLHVAVEDKA----ILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYevTGGRVEFKGKNLlelaaeDRAG 77
Cdd:cd03293 1 LEVRNVSKTYGGGGgavtALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERP--TSGEVLVDGEPV------TGPG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 78 EGIFMAFQ---------------YPVEIPGVSnqfflqtalNAVRNYRGQEALDRFDFQDLmEEKikllqMPEDLltrsv 142
Cdd:cd03293 73 PDRGYVFQqdallpwltvldnvaLGLELQGVP---------KAEARERAEELLELVGLSGF-ENA-----YPHQL----- 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488998194 143 nvgfSGGEKKRNDILQMAVLEPELCILDESDSGLD-IDALKIVSQGVNALRDGKRAFIIVTH 203
Cdd:cd03293 133 ----SGGMRQRVALARALAVDPDVLLLDEPFSALDaLTREQLQEELLDIWRETGKTVLLVTH 190
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
17-228 |
3.55e-12 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 64.18 E-value: 3.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 17 LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGRVEF--KGKNLLELAAEDRAGEGIFM----AF--QYPV 88
Cdd:PRK11701 22 CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSAR--LAPDAGEVHYrmRDGQLRDLYALSEAERRRLLrtewGFvhQHPR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 89 E--IPGVSNQFFLQTALNAV--RNYRG--QEALDRFDFQDLMEEKIkllqmpeDLLTRSvnvgFSGGEKKRndiLQMA-- 160
Cdd:PRK11701 100 DglRMQVSAGGNIGERLMAVgaRHYGDirATAGDWLERVEIDAARI-------DDLPTT----FSGGMQQR---LQIArn 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 161 -VLEPELCILDESDSGLDidalkiVSqgVNA---------LRDGKRAFIIVTH---YQRILdyikPDYVHVLYQGRIVKS 227
Cdd:PRK11701 166 lVTHPRLVFMDEPTGGLD------VS--VQArlldllrglVRELGLAVVIVTHdlaVARLL----AHRLLVMKQGRVVES 233
|
.
gi 488998194 228 G 228
Cdd:PRK11701 234 G 234
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-229 |
3.97e-12 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 63.90 E-value: 3.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 2 LSIQDLHVAVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLaGR-----EDYEVTgGRVEFKGKNLL-------E 69
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCL-NRmndliPGARVE-GEILLDGEDIYdpdvdvvE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 70 LAAedRAGegifMAFQYPveipgvsNQFFLQTALNAVRNYRGQEALDRFDFQDLMEEKIKLLQMPE---DLLTRSVnVGF 146
Cdd:COG1117 90 LRR--RVG----MVFQKP-------NPFPKSIYDNVAYGLRLHGIKSKSELDEIVEESLRKAALWDevkDRLKKSA-LGL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 147 SGGEKKRndiLQMA---VLEPELCILDESDSGLD-IDALKIvSQGVNALRDgKRAFIIVTH--YQ--RIldyikPDYVHV 218
Cdd:COG1117 156 SGGQQQR---LCIAralAVEPEVLLMDEPTSALDpISTAKI-EELILELKK-DYTIVIVTHnmQQaaRV-----SDYTAF 225
|
250
....*....|.
gi 488998194 219 LYQGRIVKSGD 229
Cdd:COG1117 226 FYLGELVEFGP 236
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
17-228 |
4.53e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 64.27 E-value: 4.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 17 LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGR----------EDYEVTGGRvefKGKNLLELaaedRAGEGIfmAFQY 86
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLlqptsgtvtiGERVITAGK---KNKKLKPL----RKKVGI--VFQF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 87 PveipgvSNQFFLQTALNAV----RNYRGQEAldrfDFQDLMEEKIKLLQMPEDLLTRSvNVGFSGGEKKRNDILQMAVL 162
Cdd:PRK13634 94 P------EHQLFEETVEKDIcfgpMNFGVSEE----DAKQKAREMIELVGLPEELLARS-PFELSGGQMRRVAIAGVLAM 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488998194 163 EPELCILDESDSGLDIDALKIVSQGVNAL-RDGKRAFIIVTH-YQRILDYikPDYVHVLYQGRIVKSG 228
Cdd:PRK13634 163 EPEVLVLDEPTAGLDPKGRKEMMEMFYKLhKEKGLTTVLVTHsMEDAARY--ADQIVVMHKGTVFLQG 228
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-229 |
4.59e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 64.36 E-value: 4.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 1 MLSIQDLHVAVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYevTGGRVEFKGKnllELAAEDRAGEGi 80
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAP--DSGEVLWDGE---PLDPEDRRRIG- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 81 FMafqyPVEiPG------VSNQ--FFLQ----TALNAVRnyRGQEALDRFDFQDLMEEKIkllqmpEDLltrsvnvgfSG 148
Cdd:COG4152 75 YL----PEE-RGlypkmkVGEQlvYLARlkglSKAEAKR--RADEWLERLGLGDRANKKV------EEL---------SK 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 149 GEKKRndiLQM--AVL-EPELCILDESDSGLDIDALKIVSQGVNALRDGKRAFIIVTHyqrILDYIKP--DYVHVLYQGR 223
Cdd:COG4152 133 GNQQK---VQLiaALLhDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSH---QMELVEElcDRIVIINKGR 206
|
....*.
gi 488998194 224 IVKSGD 229
Cdd:COG4152 207 KVLSGS 212
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
17-231 |
5.62e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 64.65 E-value: 5.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 17 LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGRVEFKGKNLLELAAEDRAGEGIFMAFQYPVEIPGVS-- 94
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSG--VYQPDSGEILLDGEPVRFRSPRDAQAAGIAIIHQELNLVPNLSva 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 95 -NQFFLQTALNA-VRNYRGQEAldrfDFQDLMEEkiklLQMPEDLLTRsvnVG-FSGGEKkrndilQM-----AV-LEPE 165
Cdd:COG1129 98 eNIFLGREPRRGgLIDWRAMRR----RARELLAR----LGLDIDPDTP---VGdLSVAQQ------QLveiarALsRDAR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488998194 166 LCILDESDSGL---DIDAL-KIVSQgvnaLRDGKRAFIIVTHYqriLDYIKP--DYVHVLYQGRIVKSGDFS 231
Cdd:COG1129 161 VLILDEPTASLterEVERLfRIIRR----LKAQGVAIIYISHR---LDEVFEiaDRVTVLRDGRLVGTGPVA 225
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
9-177 |
8.70e-12 |
|
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: 63.43 E-value: 8.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 9 VAVEDkailrgLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGRVEFKGKNLLELAAED-RA--GEGIFMAFQ 85
Cdd:cd03294 38 VGVND------VSLDVREGEIFVIMGLSGSGKSTLLRCINRL--IEPTSGKVLIDGQDIAAMSRKElRElrRKKISMVFQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 86 ---------------YPVEIPGVSNQfflqtalnaVRNYRGQEALDRFDFQDLMEEKIKLLqmpedlltrsvnvgfSGGE 150
Cdd:cd03294 110 sfallphrtvlenvaFGLEVQGVPRA---------EREERAAEALELVGLEGWEHKYPDEL---------------SGGM 165
|
170 180
....*....|....*....|....*..
gi 488998194 151 KKRNDILQMAVLEPELCILDESDSGLD 177
Cdd:cd03294 166 QQRVGLARALAVDPDILLMDEAFSALD 192
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-236 |
8.78e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 63.13 E-value: 8.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 2 LSIQDLHVAVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEV---TGGRVEFKGKNLLELAAE-DRAG 77
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrVEGRVEFFNQNIYERRVNlNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 78 EGIFMAFQYPveipgvsNQFFLQTALNAVRNYRGQEALDRFDFQDLMEEKIKLLQMPEDL---LTRSVnVGFSGGEKKRN 154
Cdd:PRK14258 88 RQVSMVHPKP-------NLFPMSVYDNVAYGVKIVGWRPKLEIDDIVESALKDADLWDEIkhkIHKSA-LDLSGGQQQRL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 155 DILQMAVLEPELCILDESDSGLD-IDALKIVSQGVNALRDGKRAFIIVTH----YQRILDYIKpdYVHVlYQGRIVKSGD 229
Cdd:PRK14258 160 CIARALAVKPKVLLMDEPCFGLDpIASMKVESLIQSLRLRSELTMVIVSHnlhqVSRLSDFTA--FFKG-NENRIGQLVE 236
|
....*..
gi 488998194 230 FSLVKQL 236
Cdd:PRK14258 237 FGLTKKI 243
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
12-228 |
9.14e-12 |
|
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: 62.61 E-value: 9.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 12 EDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGRVEFKGKNLLEL-AAEDRAGEGIFMafQYPVEI 90
Cdd:cd03245 15 QEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGL--YKPTSGSVLLDGTDIRQLdPADLRRNIGYVP--QDVTLF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 91 PGvsnqfflqtalnAVR---NYRGQEALDrfdfQDLME--------EKIKLLQMPEDLLTRSVNVGFSGGEKKRNDILQM 159
Cdd:cd03245 91 YG------------TLRdniTLGAPLADD----ERILRaaelagvtDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488998194 160 AVLEPELCILDESDSGLDIDALKIVSQGVNALRDGKrAFIIVTHYQRILDYIkpDYVHVLYQGRIVKSG 228
Cdd:cd03245 155 LLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDK-TLIIITHRPSLLDLV--DRIIVMDSGRIVADG 220
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
17-231 |
1.13e-11 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 63.83 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 17 LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGRVEFKGKNL--LELAAEDRAgegIFMAFQYP------- 87
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLL--QRVFDPQSGRILIDGTDIrtVTRASLRRN---IAVVFQDAglfnrsi 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 88 -----VEIPGVSNQFFLqtalnavrnyrgqEALDRFDFQDLMEEKikllqmPEDLLTrsvNVG-----FSGGEKKRNDIL 157
Cdd:PRK13657 426 ednirVGRPDATDEEMR-------------AAAERAQAHDFIERK------PDGYDT---VVGergrqLSGGERQRLAIA 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 158 QmAVL-EPELCILDESDSGLDIDALKIVSQGVNALRDGKRAFII------VTHYQRILdyikpdyvhVLYQGRIVKSGDF 230
Cdd:PRK13657 484 R-ALLkDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIahrlstVRNADRIL---------VFDNGRVVESGSF 553
|
.
gi 488998194 231 S 231
Cdd:PRK13657 554 D 554
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-229 |
1.25e-11 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 62.46 E-value: 1.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 1 MLSIQDLHVAVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATL-------AGR---EDYEVTGGRVEFKGKNLLEl 70
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCInlleqpeAGTirvGDITIDTARSLSQQKGLIR- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 71 aaEDRAGEG-IFMAFqypveipgvsNQFFLQTALNAVrnYRGQEALDRFDFQDLMEEKIKLLQM-----PEDLLTRSVnv 144
Cdd:PRK11264 82 --QLRQHVGfVFQNF----------NLFPHRTVLENI--IEGPVIVKGEPKEEATARARELLAKvglagKETSYPRRL-- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 145 gfSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVSQGVNALRDGKRAFIIVTHYQRILDYIKpDYVHVLYQGRI 224
Cdd:PRK11264 146 --SGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVA-DRAIFMDQGRI 222
|
....*
gi 488998194 225 VKSGD 229
Cdd:PRK11264 223 VEQGP 227
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
2-229 |
1.32e-11 |
|
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: 63.61 E-value: 1.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 2 LSIQDLHVAV--EDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGRVEFKGKNLlELAAEDRAGEG 79
Cdd:COG4618 331 LSVENLTVVPpgSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGV--WPPTAGSVRLDGADL-SQWDREELGRH 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 80 IfmafQY-PVEIpgvsnQFFLQT-ALNAVRnyrgqealdrfdFQDLMEEKI----KL-------LQMPEDLLTRsvnVG- 145
Cdd:COG4618 408 I----GYlPQDV-----ELFDGTiAENIAR------------FGDADPEKVvaaaKLagvhemiLRLPDGYDTR---IGe 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 146 ----FSGGEKKRndI-LQMAVL-EPELCILDESDSGLDIDALKIVSQGVNALRDGKRAFIIVTHYQRILDYIkpDYVHVL 219
Cdd:COG4618 464 ggarLSGGQRQR--IgLARALYgDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPSLLAAV--DKLLVL 539
|
250
....*....|
gi 488998194 220 YQGRIVKSGD 229
Cdd:COG4618 540 RDGRVQAFGP 549
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-233 |
1.70e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 62.56 E-value: 1.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 1 MLSIQDLHVAVEDKA-ILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGRVEFKG-------KNLLELAa 72
Cdd:PRK13636 5 ILKVEELNYNYSDGThALKGININIKKGEVTAILGGNGAGKSTLFQNLNGI--LKPSSGRILFDGkpidysrKGLMKLR- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 73 edragEGIFMAFQYPveipgvSNQFFLQTAlnavrnyrgqealdrfdFQDLMEEKIKlLQMPEDLLTRSVNVG------- 145
Cdd:PRK13636 82 -----ESVGMVFQDP------DNQLFSASV-----------------YQDVSFGAVN-LKLPEDEVRKRVDNAlkrtgie 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 146 ---------FSGGEKKRNDILQMAVLEPELCILDESDSGLD-IDALKIVSQGVNALRDGKRAFIIVTHYQRILDyIKPDY 215
Cdd:PRK13636 133 hlkdkpthcLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDpMGVSEIMKLLVEMQKELGLTIIIATHDIDIVP-LYCDN 211
|
250
....*....|....*...
gi 488998194 216 VHVLYQGRIVKSGDFSLV 233
Cdd:PRK13636 212 VFVMKEGRVILQGNPKEV 229
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
24-220 |
1.79e-11 |
|
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: 62.38 E-value: 1.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 24 VRPGEVHAIMGPNGSGKSTLSATLA-------GREDYEVTGGRV--EFKGKNLLELAAEDRAGE-GIFMAFQYPVEIPgv 93
Cdd:cd03236 23 PREGQVLGLVGPNGIGKSTALKILAgklkpnlGKFDDPPDWDEIldEFRGSELQNYFTKLLEGDvKVIVKPQYVDLIP-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 94 snqfflqtalNAVRNYRGqEALDRFDFQDLMEEKIKLLQMpEDLLTRSVNvGFSGGEKKRNDILQMAVLEPELCILDESD 173
Cdd:cd03236 101 ----------KAVKGKVG-ELLKKKDERGKLDELVDQLEL-RHVLDRNID-QLSGGELQRVAIAAALARDADFYFFDEPS 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488998194 174 SGLDIDALKIVSQGVNALRDGKRAFIIVTHYQRILDYIKpDYVHVLY 220
Cdd:cd03236 168 SYLDIKQRLNAARLIRELAEDDNYVLVVEHDLAVLDYLS-DYIHCLY 213
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-203 |
1.84e-11 |
|
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: 63.15 E-value: 1.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 2 LSIQDLHVAVEDKAI-LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDyeVTGGRVEFKGKNLLELAAEDRAgegi 80
Cdd:TIGR02868 335 LELRDLSAGYPGAPPvLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLD--PLQGEVTLDGVPVSSLDQDEVR---- 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 81 fmafqypvEIPGVSNQ---FFLQTALNAVRNYRGQ-------EALDRFDFQDLMEEkikllqMPEDLLTRSVNVG--FSG 148
Cdd:TIGR02868 409 --------RRVSVCAQdahLFDTTVRENLRLARPDatdeelwAALERVGLADWLRA------LPDGLDTVLGEGGarLSG 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488998194 149 GEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVSQGVNALRDGkRAFIIVTH 203
Cdd:TIGR02868 475 GERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSG-RTVVLITH 528
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-228 |
1.88e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 62.17 E-value: 1.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 6 DLHVAVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSAT----LAGREDYEVTgGRVEFKGKNLLEL---AAEDRAGE 78
Cdd:PRK14267 9 NLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTfnrlLELNEEARVE-GEVRLFGRNIYSPdvdPIEVRREV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 79 GifMAFQYPVEIPGVS--NQFFLQTALNAVrnYRGQEALDR-----FDFQDLMEE-KIKLLQMPEDLltrsvnvgfSGGE 150
Cdd:PRK14267 88 G--MVFQYPNPFPHLTiyDNVAIGVKLNGL--VKSKKELDErvewaLKKAALWDEvKDRLNDYPSNL---------SGGQ 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488998194 151 KKRNDILQMAVLEPELCILDESDSGLDIDALKIVSQGVNALRDgKRAFIIVTHYQRILDYIKpDYVHVLYQGRIVKSG 228
Cdd:PRK14267 155 RQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKK-EYTIVLVTHSPAQAARVS-DYVAFLYLGKLIEVG 230
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
12-72 |
2.16e-11 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 62.02 E-value: 2.16e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488998194 12 EDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGRVEFKGK--NLLELAA 72
Cdd:COG1134 37 EEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAG--ILEPTSGRVEVNGRvsALLELGA 97
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1-58 |
2.60e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 62.15 E-value: 2.60e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 488998194 1 MLSIQDLHVAVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGredyEVTGG 58
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG----DLTGG 54
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
12-184 |
3.31e-11 |
|
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: 61.43 E-value: 3.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 12 EDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGRVEFKGKNLLEL--AAEDRAGEGIFMAFQypvE 89
Cdd:cd03256 12 NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLV--EPTSGSVLIDGTDINKLkgKALRQLRRQIGMIFQ---Q 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 90 IPGVSNQFFLQTALNAVRNYRG--QEALDRFDFQDLmEEKIKLLQ---MPEDLLTRSVNVgfSGGEKKRNDILQMAVLEP 164
Cdd:cd03256 87 FNLIERLSVLENVLSGRLGRRStwRSLFGLFPKEEK-QRALAALErvgLLDKAYQRADQL--SGGQQQRVAIARALMQQP 163
|
170 180
....*....|....*....|
gi 488998194 165 ELCILDESDSGLDIDALKIV 184
Cdd:cd03256 164 KLILADEPVASLDPASSRQV 183
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
13-205 |
3.46e-11 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 62.35 E-value: 3.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 13 DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDyeVTGGRVEFKGKNLLELAAEDRageGIFMAFQYPVEIPG 92
Cdd:PRK11000 15 DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLED--ITSGDLFIGEKRMNDVPPAER---GVGMVFQSYALYPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 93 VS---NQFF---LQTALNAVRNYRGQEALDRFDFQDLMEEKikllqmPEDLltrsvnvgfSGGEKKRNDILQMAVLEPEL 166
Cdd:PRK11000 90 LSvaeNMSFglkLAGAKKEEINQRVNQVAEVLQLAHLLDRK------PKAL---------SGGQRQRVAIGRTLVAEPSV 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488998194 167 CILDESDSGLDIdALKiVSQGVNALRDGKR---AFIIVTHYQ 205
Cdd:PRK11000 155 FLLDEPLSNLDA-ALR-VQMRIEISRLHKRlgrTMIYVTHDQ 194
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
15-203 |
4.56e-11 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 60.56 E-value: 4.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 15 AILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDyeVTGGRVEFKGKNLLELAAEDRA---GEGIFMAFQypveip 91
Cdd:PRK10584 24 SILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDD--GSSGEVSLVGQPLHQMDEEARAklrAKHVGFVFQ------ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 92 gvsnQFFLQTALNAVRN------YRGQ-EALDRFDFQDLMEE---KIKLLQMPEDLltrsvnvgfSGGEKKRNDILQMAV 161
Cdd:PRK10584 96 ----SFMLIPTLNALENvelpalLRGEsSRQSRNGAKALLEQlglGKRLDHLPAQL---------SGGEQQRVALARAFN 162
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488998194 162 LEPELCILDESDSGLDID-ALKIVSQGVNALRDGKRAFIIVTH 203
Cdd:PRK10584 163 GRPDVLFADEPTGNLDRQtGDKIADLLFSLNREHGTTLILVTH 205
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
3-243 |
4.61e-11 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 62.04 E-value: 4.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 3 SIQDLHVAVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGRVEFKGKNLLELAAEDRAGEgifM 82
Cdd:PRK10789 317 NIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLI--QRHFDVSEGDIRFHDIPLTKLQLDSWRSR---L 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 83 AfqypveipgVSNQ---FFLQTALNAVrnyrgqeALDRFD-FQDLMEEKIKLLQMPEDLLT----RSVNVG-----FSGG 149
Cdd:PRK10789 392 A---------VVSQtpfLFSDTVANNI-------ALGRPDaTQQEIEHVARLASVHDDILRlpqgYDTEVGergvmLSGG 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 150 EKKRNDILQMAVLEPELCILDESDSGLDIDALKIVSQGVNALRDGkRAFIIVTHyqRILDYIKPDYVHVLYQGRIVKSGD 229
Cdd:PRK10789 456 QKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEG-RTVIISAH--RLSALTEASEILVMQHGHIAQRGN 532
|
250
....*....|....
gi 488998194 230 fslVKQLEEQGyGW 243
Cdd:PRK10789 533 ---HDQLAQQS-GW 542
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-205 |
5.03e-11 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 61.89 E-value: 5.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 2 LSIQDLHVAVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGRVEFKGKNLLELAAEDRAgegIF 81
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFE--TPDSGRIMLDGQDITHVPAENRH---VN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 82 MAFQYPVEIPGVS---NQFF---LQTALNAVRNYRGQEALDRFDFQDLMEEKIKLLqmpedlltrsvnvgfSGGEKKRND 155
Cdd:PRK09452 90 TVFQSYALFPHMTvfeNVAFglrMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQL---------------SGGQQQRVA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488998194 156 ILQMAVLEPELCILDESDSGLDidaLKIVSQGVNALRDGKR----AFIIVTHYQ 205
Cdd:PRK09452 155 IARAVVNKPKVLLLDESLSALD---YKLRKQMQNELKALQRklgiTFVFVTHDQ 205
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-229 |
5.68e-11 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 61.25 E-value: 5.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 1 MLSIQDLHV--AVEDKAI--LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGRVEFKGKNLLELAAEDRA 76
Cdd:COG1135 1 MIELENLSKtfPTKGGPVtaLDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLE--RPTSGSVLVDGVDLTALSERELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 77 GE--GIFMAFQ---------------YPVEIPGVSnqfflqtalNAVRNYRGQEALDRFDfqdlMEEKIKllQMPEDLlt 139
Cdd:COG1135 79 AArrKIGMIFQhfnllssrtvaenvaLPLEIAGVP---------KAEIRKRVAELLELVG----LSDKAD--AYPSQL-- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 140 rsvnvgfSGGEKKRNDILQMAVLEPELCILDESDSGLD------IDALkivsqgvnaLRDGKRAF----IIVTH----YQ 205
Cdd:COG1135 142 -------SGGQKQRVGIARALANNPKVLLCDEATSALDpettrsILDL---------LKDINRELgltiVLITHemdvVR 205
|
250 260
....*....|....*....|....
gi 488998194 206 RILdyikpDYVHVLYQGRIVKSGD 229
Cdd:COG1135 206 RIC-----DRVAVLENGRIVEQGP 224
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
4-229 |
5.88e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 61.26 E-value: 5.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 4 IQDLHVAVEDKAiLRGLNLEVRPGEVHAIMGPNGSGKST----LSATLAGredyevTGGRVEF---------KGKNLLEL 70
Cdd:PRK13651 11 IFNKKLPTELKA-LDNVSVEINQGEFIAIIGQTGSGKTTfiehLNALLLP------DTGTIEWifkdeknkkKTKEKEKV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 71 AAEDRAGEGIFMAFQYPVEIP---GVSNQF-----FLQTALNAV----RNY--RGQEALDRfdfqdlMEEKIKLLQMPED 136
Cdd:PRK13651 84 LEKLVIQKTRFKKIKKIKEIRrrvGVVFQFaeyqlFEQTIEKDIifgpVSMgvSKEEAKKR------AAKYIELVGLDES 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 137 LLTRSvNVGFSGGEKKRNDILQMAVLEPELCILDESDSGLD----IDALKIvsqgVNALRDGKRAFIIVTH-YQRILDYI 211
Cdd:PRK13651 158 YLQRS-PFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDpqgvKEILEI----FDNLNKQGKTIILVTHdLDNVLEWT 232
|
250
....*....|....*...
gi 488998194 212 KpdYVHVLYQGRIVKSGD 229
Cdd:PRK13651 233 K--RTIFFKDGKIIKDGD 248
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
16-203 |
6.16e-11 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 60.49 E-value: 6.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 16 ILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGRVEFKGKNLLELAAEDR-----AGegifMAFQypvei 90
Cdd:PRK09493 16 VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLE--EITSGDLIVDGLKVNDPKVDERlirqeAG----MVFQ----- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 91 pgvsnQFFL---QTALNAV----RNYRGQEaldRFDFQDLMEE---KIKLLQ----MPEDLltrsvnvgfSGGEKKRNDI 156
Cdd:PRK09493 85 -----QFYLfphLTALENVmfgpLRVRGAS---KEEAEKQAREllaKVGLAErahhYPSEL---------SGGQQQRVAI 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488998194 157 LQMAVLEPELCILDESDSGLDIDALKIVSQGVNALRDGKRAFIIVTH 203
Cdd:PRK09493 148 ARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTH 194
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
4-239 |
8.03e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 60.52 E-value: 8.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 4 IQDLHVAVED--KAiLRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGRVEFKGKNLLElAAEDRAGEGIF 81
Cdd:PRK13647 7 VEDLHFRYKDgtKA-LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGI--YLPQRGRVKVMGREVNA-ENEKWVRSKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 82 MAFQYPveipgvSNQFFLQTALNAVRNYRGQEALDRFDFQDLMEEKIKLLQMpEDLLTRSVNvGFSGGEKKRNDILQMAV 161
Cdd:PRK13647 83 LVFQDP------DDQVFSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRM-WDFRDKPPY-HLSYGQKKRVAIAGVLA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 162 LEPELCILDESDSGLDIDALKIVSQGVNALRDGKRAFIIVTHYqriLDYIK--PDYVHVLYQGRIVKSGDFSLV--KQLE 237
Cdd:PRK13647 155 MDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHD---VDLAAewADQVIVLKEGRVLAEGDKSLLtdEDIV 231
|
..
gi 488998194 238 EQ 239
Cdd:PRK13647 232 EQ 233
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
2-233 |
8.27e-11 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 60.24 E-value: 8.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 2 LSIQDLHVAVEdkaiLRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEvtgGRVEFKGKNLLELAAED----RA- 76
Cdd:COG4138 1 LQLNDVAVAGR----LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPGQ---GEILLNGRPLSDWSAAElarhRAy 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 77 -----GEGIFMA-FQYpveipgvsnqffLQTALNAVRNYRGQEALdrfdfqdLME--EKIKLlqmpEDLLTRSVNvGFSG 148
Cdd:COG4138 74 lsqqqSPPFAMPvFQY------------LALHQPAGASSEAVEQL-------LAQlaEALGL----EDKLSRPLT-QLSG 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 149 GEKKRndILQMAVL---------EPELCILDESDSGLDIDALKIVSQGVNALRDGKRAFIIVTHyqrilD----YIKPDY 215
Cdd:COG4138 130 GEWQR--VRLAAVLlqvwptinpEGQLLLLDEPMNSLDVAQQAALDRLLRELCQQGITVVMSSH-----DlnhtLRHADR 202
|
250
....*....|....*...
gi 488998194 216 VHVLYQGRIVKSGDFSLV 233
Cdd:COG4138 203 VWLLKQGKLVASGETAEV 220
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-241 |
8.71e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 60.49 E-value: 8.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 6 DLHVAVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRED----YEVT-----GGRVEFKGKNLLELaaEDRA 76
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDkvsgYRYSgdvllGGRSIFNYRDVLEF--RRRV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 77 GegifMAFQYPveipgvsNQFFLQTALNAVRNYRGQEALDRFDFQDLMEEKIKLLQMPEDLLTRSVNVGF--SGGEKKRN 154
Cdd:PRK14271 104 G----MLFQRP-------NPFPMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFrlSGGQQQLL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 155 DILQMAVLEPELCILDESDSGLDIDALKIVSQGVNALRDgKRAFIIVTHYQRILDYIKpDYVHVLYQGRIVKSGD----F 230
Cdd:PRK14271 173 CLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLAD-RLTVIIVTHNLAQAARIS-DRAALFFDGRLVEEGPteqlF 250
|
250
....*....|.
gi 488998194 231 SLVKQLEEQGY 241
Cdd:PRK14271 251 SSPKHAETARY 261
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-203 |
9.40e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 59.50 E-value: 9.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 1 MLSIQDLHVAVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGRVEFKGKNllelAAEDRAGEgi 80
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGL--LPPAAGTIKLDGGD----IDDPDVAE-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 81 fmAFQYpveipgVSNQFFLQTALNAV------RNYRGQ------EALDRFDFQDLMEEKIKLLqmpedlltrsvnvgfSG 148
Cdd:PRK13539 74 --ACHY------LGHRNAMKPALTVAenlefwAAFLGGeeldiaAALEAVGLAPLAHLPFGYL---------------SA 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488998194 149 GEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVSQGVNALRDGKRAFIIVTH 203
Cdd:PRK13539 131 GQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELIRAHLAQGGIVIAATH 185
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
14-241 |
1.17e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 61.28 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 14 KAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRED-YEVT-GGRVEFKGKNLLELAAEDRaGEGIFMAfQYPVEIP 91
Cdd:TIGR00956 74 FDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDgFHIGvEGVITYDGITPEEIKKHYR-GDVVYNA-ETDVHFP 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 92 GVSNQFFLQTA--LNAVRNyRGqEALDRFDFQdlmeEKIKLLQMPEDLL--TRSVNV------GFSGGEKKRNDILQMAV 161
Cdd:TIGR00956 152 HLTVGETLDFAarCKTPQN-RP-DGVSREEYA----KHIADVYMATYGLshTRNTKVgndfvrGVSGGERKRVSIAEASL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 162 LEPELCILDESDSGLD-IDALKIvsqgVNALRDGKR---AFIIVTHYQRILD-YIKPDYVHVLYQGRIVKSGDFSLVKQ- 235
Cdd:TIGR00956 226 GGAKIQCWDNATRGLDsATALEF----IRALKTSANildTTPLVAIYQCSQDaYELFDKVIVLYEGYQIYFGPADKAKQy 301
|
....*.
gi 488998194 236 LEEQGY 241
Cdd:TIGR00956 302 FEKMGF 307
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-229 |
1.50e-10 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 59.38 E-value: 1.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 1 MLSIQDLHVAVEDKAiLRgLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGRVEFKGKNLLELAAEDRageGI 80
Cdd:COG3840 1 MLRLDDLTYRYGDFP-LR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFL--PPDSGRILWNGQDLTALPPAER---PV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 81 FMAFQypveipgvSNQFF--LQTA------------LNAVRNYRGQEALDRFDFQDLMEEKikllqmPEDLltrsvnvgf 146
Cdd:COG3840 74 SMLFQ--------ENNLFphLTVAqniglglrpglkLTAEQRAQVEQALERVGLAGLLDRL------PGQL--------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 147 SGGEKKRNDILQMAVLEPELCILDESDSGLDIdALK-----IVSQgVNALRdgKRAFIIVTHY----QRIldyikPDYVH 217
Cdd:COG3840 131 SGGQRQRVALARCLVRKRPILLLDEPFSALDP-ALRqemldLVDE-LCRER--GLTVLMVTHDpedaARI-----ADRVL 201
|
250
....*....|..
gi 488998194 218 VLYQGRIVKSGD 229
Cdd:COG3840 202 LVADGRIAADGP 213
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-224 |
2.03e-10 |
|
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: 58.00 E-value: 2.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 2 LSIQDLHVAVED--KAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGRVEFKGknlLELAAEDRAGEG 79
Cdd:cd03246 1 LEVENVSFRYPGaePPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLL--RPTSGRVRLDG---ADISQWDPNELG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 80 IFMAFqypveipgvsnqfflqtalnavrnyrgqealdrfdfqdLMEEKIkllqmpedLLTRSV--NVgFSGGEKKRndIL 157
Cdd:cd03246 76 DHVGY--------------------------------------LPQDDE--------LFSGSIaeNI-LSGGQRQR--LG 106
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488998194 158 QMAVL--EPELCILDESDSGLDIDALKIVSQGVNALRDGKRAFIIVTHYQRILDYIkpDYVHVLYQGRI 224
Cdd:cd03246 107 LARALygNPRILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLASA--DRILVLEDGRV 173
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
13-228 |
2.10e-10 |
|
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: 60.22 E-value: 2.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 13 DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGRVEFKGKNLLELAAED-RAGEGIFmafqyPVEI- 90
Cdd:COG5265 370 ERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRF--YDVTSGRILIDGQDIRDVTQASlRAAIGIV-----PQDTv 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 91 --------------PGVSNQFFLQTALNAvrnyrgqeALDRFdfqdlmeekIKLLqmPEDLLTRsvnVG-----FSGGEK 151
Cdd:COG5265 443 lfndtiayniaygrPDASEEEVEAAARAA--------QIHDF---------IESL--PDGYDTR---VGerglkLSGGEK 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 152 KRNDILQMAVLEPELCILDESDSGLD------I-DALKIVSQGVNALrdgkrafII------VTHYQRILdyikpdyvhV 218
Cdd:COG5265 501 QRVAIARTLLKNPPILIFDEATSALDsrteraIqAALREVARGRTTL-------VIahrlstIVDADEIL---------V 564
|
250
....*....|
gi 488998194 219 LYQGRIVKSG 228
Cdd:COG5265 565 LEAGRIVERG 574
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-243 |
2.16e-10 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 60.12 E-value: 2.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 2 LSIQDLHVAV-EDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGRVEFKGKNLLELA-AEDRagEG 79
Cdd:PRK10790 341 IDIDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGY--YPLTEGEIRLDGRPLSSLShSVLR--QG 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 80 IFMAFQYPVEIpgvSNQFFLQTALNavRNYRGQ---EALDRFDFQDLMEEkikllqMPEDLLTRSVNVG--FSGGEKKrn 154
Cdd:PRK10790 417 VAMVQQDPVVL---ADTFLANVTLG--RDISEEqvwQALETVQLAELARS------LPDGLYTPLGEQGnnLSVGQKQ-- 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 155 dILQMA---VLEPELCILDESDSGLDIDALKIVSQGVNALRDgKRAFIIVTHyqRILDYIKPDYVHVLYQGRIVKSGDFS 231
Cdd:PRK10790 484 -LLALArvlVQTPQILILDEATANIDSGTEQAIQQALAAVRE-HTTLVVIAH--RLSTIVEADTILVLHRGQAVEQGTHQ 559
|
250
....*....|..
gi 488998194 232 lvKQLEEQGYGW 243
Cdd:PRK10790 560 --QLLAAQGRYW 569
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
24-220 |
2.72e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 59.82 E-value: 2.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 24 VRPGEVHAIMGPNGSGKST----LSATLA---GREDYEVTGGRV--EFKGKNLLELAAEDRAGEgIFMAF--QYPVEIPG 92
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTavkiLSGELIpnlGDYEEEPSWDEVlkRFRGTELQNYFKKLYNGE-IKVVHkpQYVDLIPK 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 93 VsnqfflqtalnavrnYRGQ--EALDRFDFQDLMEEKIKLLQMpEDLLTRSVNVgFSGGEKKRNDILQMAVLEPELCILD 170
Cdd:PRK13409 175 V---------------FKGKvrELLKKVDERGKLDEVVERLGL-ENILDRDISE-LSGGELQRVAIAAALLRDADFYFFD 237
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488998194 171 ESDSGLDIDALKIVSQGVNALRDGKrAFIIVTHYQRILDYIKpDYVHVLY 220
Cdd:PRK13409 238 EPTSYLDIRQRLNVARLIRELAEGK-YVLVVEHDLAVLDYLA-DNVHIAY 285
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
17-229 |
2.84e-10 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 59.66 E-value: 2.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 17 LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGRVEFKGKNL--------LELaaedrageGIFMAFQYPV 88
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGL--YQPDSGEILIDGKPVrirsprdaIAL--------GIGMVHQHFM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 89 EIP----------GVSNQFFLQTALNAVRNyRGQEALDRFDFqdlmeeKIKLLQMPEDLltrSVnvgfsgGEKKRNDILQ 158
Cdd:COG3845 91 LVPnltvaenivlGLEPTKGGRLDRKAARA-RIRELSERYGL------DVDPDAKVEDL---SV------GEQQRVEILK 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488998194 159 MAVLEPELCILDESDSGL---DIDALKIVsqgVNALRDGKRAFIIVTHYqriLDYIKP--DYVHVLYQGRIVKSGD 229
Cdd:COG3845 155 ALYRGARILILDEPTAVLtpqEADELFEI---LRRLAAEGKSIIFITHK---LREVMAiaDRVTVLRRGKVVGTVD 224
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
12-228 |
4.50e-10 |
|
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: 58.11 E-value: 4.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 12 EDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGRVEFKGKNLLELAAEDRAGEGIFMA--FQYPVE 89
Cdd:cd03267 32 REVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGL--LQPTSGEVRVAGLVPWKRRKKFLRRIGVVFGqkTQLWWD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 90 IPGVSNQFFLQtalnavRNYRgqeaLDRFDFQDLMEEKIKLLQMpEDLLTRSVNvGFSGGEKKRNDILQMAVLEPELCIL 169
Cdd:cd03267 110 LPVIDSFYLLA------AIYD----LPPARFKKRLDELSELLDL-EELLDTPVR-QLSLGQRMRAEIAAALLHEPEILFL 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 170 DESDSGLDIDALKIVSQGVNAL-RDGKRAFIIVTHYQRILDYIkPDYVHVLYQGRIVKSG 228
Cdd:cd03267 178 DEPTIGLDVVAQENIRNFLKEYnRERGTTVLLTSHYMKDIEAL-ARRVLVIDKGRLLYDG 236
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
16-241 |
5.43e-10 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 58.98 E-value: 5.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 16 ILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGRVEFKGKNLLELaaeDRAGEGIFMAF--QYPVEIPGV 93
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGF--FQARSGEILLNGFSLKDI---DRHTLRQFINYlpQEPYIFSGS 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 94 snqfFLQTALNAVRNYRGQEALDRFdfQDLMEEKIKLLQMPEDLLTR--SVNVGFSGGEKKRNDILQMAVLEPELCILDE 171
Cdd:TIGR01193 564 ----ILENLLLGAKENVSQDEIWAA--CEIAEIKDDIENMPLGYQTElsEEGSSISGGQKQRIALARALLTDSKVLILDE 637
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488998194 172 SDSGLD-IDALKIVSQGVNaLRDgkRAFIIVTHyqRILDYIKPDYVHVLYQGRIVKSGdfSLVKQLEEQGY 241
Cdd:TIGR01193 638 STSNLDtITEKKIVNNLLN-LQD--KTIIFVAH--RLSVAKQSDKIIVLDHGKIIEQG--SHDELLDRNGF 701
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
1-203 |
5.48e-10 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 57.55 E-value: 5.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 1 MLSIQDLHVAVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGRVEFKGKNllelaaEDRAGEGI 80
Cdd:PRK13543 11 LLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGL--LHVESGQIQIDGKT------ATRGDRSR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 81 FMAfqYPVEIPGvsnqffLQTALNAVRNYRGQEALDRFDFQDLMEEKIKLLQMP--EDLLTRSVnvgfSGGEKKRNDILQ 158
Cdd:PRK13543 83 FMA--YLGHLPG------LKADLSTLENLHFLCGLHGRRAKQMPGSALAIVGLAgyEDTLVRQL----SAGQKKRLALAR 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488998194 159 MAVLEPELCILDESDSGLDIDALKIVSQGVNALRDGKRAFIIVTH 203
Cdd:PRK13543 151 LWLSPAPLWLLDEPYANLDLEGITLVNRMISAHLRGGGAALVTTH 195
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
25-220 |
5.66e-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: 59.03 E-value: 5.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 25 RPGEVHAIMGPNGSGKST----LSATLA---GREDYEVTGGRV--EFKGKNLLELAAEDRAGEgIFMAF--QYPVEIPGV 93
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTalkiLSGELKpnlGDYDEEPSWDEVlkRFRGTELQDYFKKLANGE-IKVAHkpQYVDLIPKV 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 94 snqfflqtalnavrnYRG--QEALDRFDFQDLMEEKIKLLQMpEDLLTRSVNVgFSGGEKKRNDILQMAVLEPELCILDE 171
Cdd:COG1245 176 ---------------FKGtvRELLEKVDERGKLDELAEKLGL-ENILDRDISE-LSGGELQRVAIAAALLRDADFYFFDE 238
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488998194 172 SDSGLDIDALKIVSQGVNALRDGKRAFIIVTHYQRILDYIKpDYVHVLY 220
Cdd:COG1245 239 PSSYLDIYQRLNVARLIRELAEEGKYVLVVEHDLAILDYLA-DYVHILY 286
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
2-229 |
6.45e-10 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 58.54 E-value: 6.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 2 LSIQDLHVA-----------VEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDyevTGGRVEFKGKNLLEL 70
Cdd:COG4172 276 LEARDLKVWfpikrglfrrtVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP---SEGEIRFDGQDLDGL 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 71 AAED----RAgeGIFMAFQYPV----------EI---------PGVSnqfflqtalnavrnyrGQEALDRfdFQDLMEEk 127
Cdd:COG4172 353 SRRAlrplRR--RMQVVFQDPFgslsprmtvgQIiaeglrvhgPGLS----------------AAERRAR--VAEALEE- 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 128 iklLQMPEDLLTRSVNvGFSGGEKKRNDILQMAVLEPELCILDESDSGLDidalkiVS---QGVNALRDGKR----AFII 200
Cdd:COG4172 412 ---VGLDPAARHRYPH-EFSGGQRQRIAIARALILEPKLLVLDEPTSALD------VSvqaQILDLLRDLQRehglAYLF 481
|
250 260
....*....|....*....|....*....
gi 488998194 201 VTHYQRILDYIKpDYVHVLYQGRIVKSGD 229
Cdd:COG4172 482 ISHDLAVVRALA-HRVMVMKDGKVVEQGP 509
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
19-193 |
6.90e-10 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 57.69 E-value: 6.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 19 GLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGRVEFKGKNLLELAAEDRAGEGIFMAFQY--------PVEI 90
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGF--YKPTGGTILLRGQHIEGLPGHQIARMGVVRTFQHvrlfremtVIEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 91 PGVSNQFFLQT----ALNAVRNYR--GQEALDRFDFqdlMEEKIKLLqmpeDLLTRSV-NVGFsgGEKKRNDILQMAVLE 163
Cdd:PRK11300 101 LLVAQHQQLKTglfsGLLKTPAFRraESEALDRAAT---WLERVGLL----EHANRQAgNLAY--GQQRRLEIARCMVTQ 171
|
170 180 190
....*....|....*....|....*....|
gi 488998194 164 PELCILDESDSGLDIDALKIVSQGVNALRD 193
Cdd:PRK11300 172 PEILMLDEPAAGLNPKETKELDELIAELRN 201
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
11-228 |
7.33e-10 |
|
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: 57.16 E-value: 7.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 11 VEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGRVEFKGK--NLLELAAedragegifmAFQYpv 88
Cdd:cd03220 32 VGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGI--YPPDSGTVTVRGRvsSLLGLGG----------GFNP-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 89 EIPGVSNQFFLQTALNAVRNYRGQEALDRFDFQDL---MEEKIKllqmpedlltrsvnvGFSGGEKKRndiLQMAV---L 162
Cdd:cd03220 98 ELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELgdfIDLPVK---------------TYSSGMKAR---LAFAIataL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488998194 163 EPELCILDESDSGLDIDALKIVSQGVNALRDGKRAFIIVTHYqriLDYIKP--DYVHVLYQGRIVKSG 228
Cdd:cd03220 160 EPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHD---PSSIKRlcDRALVLEKGKIRFDG 224
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
27-228 |
1.05e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 57.45 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 27 GEVHAIMGPNGSGKSTLSATLAGREdyEVTGGRVEFKG-----KNLLELaaedRAGEGIfmAFQYPveipgvSNQFflqt 101
Cdd:PRK13648 35 GQWTSIVGHNGSGKSTIAKLMIGIE--KVKSGEIFYNNqaitdDNFEKL----RKHIGI--VFQNP------DNQF---- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 102 aLNAVRNYRGQEALDRFDF-QDLMEEKIKLLQMPEDLLTR--SVNVGFSGGEKKRNDILQMAVLEPELCILDESDSGLDI 178
Cdd:PRK13648 97 -VGSIVKYDVAFGLENHAVpYDEMHRRVSEALKQVDMLERadYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDP 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488998194 179 DALKIVSQGVNALRDGKRAFII-VTHyqRILDYIKPDYVHVLYQGRIVKSG 228
Cdd:PRK13648 176 DARQNLLDLVRKVKSEHNITIIsITH--DLSEAMEADHVIVMNKGTVYKEG 224
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
17-226 |
1.25e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 57.15 E-value: 1.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 17 LRGLNLEVRPGEVHAIMGPNGSGKSTL-------------SATLAGredYEVTggrVEFKGKNLLELAAEdragegIFMA 83
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLmqhfnallkpssgTITIAG---YHIT---PETGNKNLKKLRKK------VSLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 84 FQYPveipgvSNQFFLQTALNAV----RNYRGQEaldrfdfQDLMEEKIKLLQ---MPEDLLTRSvNVGFSGGEKKRNDI 156
Cdd:PRK13641 91 FQFP------EAQLFENTVLKDVefgpKNFGFSE-------DEAKEKALKWLKkvgLSEDLISKS-PFELSGGQMRRVAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488998194 157 LQMAVLEPELCILDESDSGLDIDALKivsQGVNALRDGKRA---FIIVTH-YQRILDYikPDYVHVLYQGRIVK 226
Cdd:PRK13641 157 AGVMAYEPEILCLDEPAAGLDPEGRK---EMMQLFKDYQKAghtVILVTHnMDDVAEY--ADDVLVLEHGKLIK 225
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-225 |
1.42e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 57.79 E-value: 1.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 1 MLSIQDLHVAV----EDKAILRGLNLEVRPGEVHAIMGPNGSGKS--TLSAT-LAGREDYEVTGGRVEFKGKNLLElAAE 73
Cdd:PRK15134 5 LLAIENLSVAFrqqqTVRTVVNDVSLQIEAGETLALVGESGSGKSvtALSILrLLPSPPVVYPSGDIRFHGESLLH-ASE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 74 DR----AGEGIFMAFQYPV----EIPGVSNQffLQTALNAVRNYRGQ----EALDRFDFQDLMEEKIKLLQMPEDLltrs 141
Cdd:PRK15134 84 QTlrgvRGNKIAMIFQEPMvslnPLHTLEKQ--LYEVLSLHRGMRREaargEILNCLDRVGIRQAAKRLTDYPHQL---- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 142 vnvgfSGGEKKRNDIlQMAVL-EPELCILDESDSGLDIdalKIVSQGVNALRDGKR----AFIIVTHYQRILDYIKpDYV 216
Cdd:PRK15134 158 -----SGGERQRVMI-AMALLtRPELLIADEPTTALDV---SVQAQILQLLRELQQelnmGLLFITHNLSIVRKLA-DRV 227
|
....*....
gi 488998194 217 HVLYQGRIV 225
Cdd:PRK15134 228 AVMQNGRCV 236
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-228 |
1.86e-09 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 56.56 E-value: 1.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 1 MLSIQDLHVAVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAgREDYEVTgGRVEFKGKNLLELAAEDRAGEGI 80
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFA-RLLTPQS-GTVFLGDKPISMLSSRQLARRLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 81 FMAFQYPVeiP-GVSNQFFLQTALNAVRNYRGQ-EALDRFDFQDLMeEKIKLLQMPEDLLTRsvnvgFSGGEKKRNDILQ 158
Cdd:PRK11231 80 LLPQHHLT--PeGITVRELVAYGRSPWLSLWGRlSAEDNARVNQAM-EQTRINHLADRRLTD-----LSGGQRQRAFLAM 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488998194 159 MAVLEPELCILDESDSGLDI----DALKIVSQgvnaLRDGKRAFIIVTH-YQRILDYIkpDYVHVLYQGRIVKSG 228
Cdd:PRK11231 152 VLAQDTPVVLLDEPTTYLDInhqvELMRLMRE----LNTQGKTVVTVLHdLNQASRYC--DHLVVLANGHVMAQG 220
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
2-203 |
1.93e-09 |
|
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: 55.83 E-value: 1.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 2 LSIQDLHVAVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGRVEFKGKNLLELAaeDRAGEGIF 81
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLL--RPDSGEVRWNGTPLAEQR--DEPHENIL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 82 mafqYPVEIPGVSN--------QF---FLQTALNAVrnyrgQEALDRFDFQDLmeekikllqmpEDLLTRSVnvgfSGGE 150
Cdd:TIGR01189 77 ----YLGHLPGLKPelsalenlHFwaaIHGGAQRTI-----EDALAAVGLTGF-----------EDLPAAQL----SAGQ 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488998194 151 KKRNDILQMAVLEPELCILDESDSGLDIDALKIVSQGVNALRDGKRAFIIVTH 203
Cdd:TIGR01189 133 QRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGLLRAHLARGGIVLLTTH 185
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
16-228 |
2.05e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 57.37 E-value: 2.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 16 ILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEvtGGRVEFKGKNLLELAAEDRAGEGIFMAFQYPVEIPgvsN 95
Cdd:PRK15439 26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPD--SGTLEIGGNPCARLTPAKAHQLGIYLVPQEPLLFP---N 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 96 QFFLQTALnaVRNYRGQEALDRfdfqdlMEEKIKLL--QMPEDLLTRSVNVgfsgGEKKRNDILQMAVLEPELCILDESD 173
Cdd:PRK15439 101 LSVKENIL--FGLPKRQASMQK------MKQLLAALgcQLDLDSSAGSLEV----ADRQIVEILRGLMRDSRILILDEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488998194 174 SGLDIDALKIVSQGVNALRDGKRAFIIVTHYQRILDYIKpDYVHVLYQGRIVKSG 228
Cdd:PRK15439 169 ASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLA-DRISVMRDGTIALSG 222
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1-84 |
2.15e-09 |
|
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: 55.13 E-value: 2.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 1 MLSIQDLHVavedKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGRVEFKGKNL------------L 68
Cdd:cd03215 4 VLEVRGLSV----KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFG--LRPPASGEITLDGKPVtrrsprdairagI 77
|
90
....*....|....*.
gi 488998194 69 ELAAEDRAGEGIFMAF 84
Cdd:cd03215 78 AYVPEDRKREGLVLDL 93
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-228 |
2.73e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 56.29 E-value: 2.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 1 MLSIQDLHVAVED-----KAILRgLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDY--EVTGGRVEFKGKNLLELAAE 73
Cdd:PRK11022 3 LLNVDKLSVHFGDesapfRAVDR-ISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYpgRVMAEKLEFNGQDLQRISEK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 74 DR---AGEGIFMAFQYPVEI--PGVSNQFFLQTALNA----VRNYRGQEALDRFDFQDLMEEKIKLLQMPEDLltrsvnv 144
Cdd:PRK11022 82 ERrnlVGAEVAMIFQDPMTSlnPCYTVGFQIMEAIKVhqggNKKTRRQRAIDLLNQVGIPDPASRLDVYPHQL------- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 145 gfSGGEKKRNDILQMAVLEPELCILDESDSGLDIdalKIVSQGVNALRDGKR----AFIIVTH--------YQRILdyik 212
Cdd:PRK11022 155 --SGGMSQRVMIAMAIACRPKLLIADEPTTALDV---TIQAQIIELLLELQQkenmALVLITHdlalvaeaAHKII---- 225
|
250
....*....|....*.
gi 488998194 213 pdyvhVLYQGRIVKSG 228
Cdd:PRK11022 226 -----VMYAGQVVETG 236
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
17-228 |
2.88e-09 |
|
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: 55.81 E-value: 2.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 17 LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDyeVTGGRVEFKGKNLLELAAEDRageGIFMAFQYPVEIPGVS-- 94
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLER--PDSGTILFGGEDATDVPVQER---NVGFVFQHYALFRHMTvf 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 95 -NQFFlqtalnAVRNYRGQEALDRFDFQDLMEEKIKLLQMpeDLLTRSVNVGFSGGEKKRNDILQMAVLEPELCILDESD 173
Cdd:cd03296 93 dNVAF------GLRVKPRSERPPEAEIRAKVHELLKLVQL--DWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPF 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488998194 174 SGLDIDALKIVSQGVNALRDGKR-AFIIVTHYQ-RILDYikPDYVHVLYQGRIVKSG 228
Cdd:cd03296 165 GALDAKVRKELRRWLRRLHDELHvTTVFVTHDQeEALEV--ADRVVVMNKGRIEQVG 219
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
17-226 |
3.22e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 55.87 E-value: 3.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 17 LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGR-EDYEvtgGRVEFKGKnllELAAED--RAGEGIFMAFQYPveipgv 93
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLfEEFE---GKVKIDGE---LLTAENvwNLRRKIGMVFQNP------ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 94 SNQFFLQTALNAVRNYRGQEALDRFDFQDLMEEKIKLLQMPeDLLTRSvNVGFSGGEKKRNDILQMAVLEPELCILDESD 173
Cdd:PRK13642 91 DNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNML-DFKTRE-PARLSGGQKQRVAVAGIIALRPEIIILDEST 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488998194 174 SGLDIDALKIVSQGVNALRDgKRAFIIVTHYQRILDYIKPDYVHVLYQGRIVK 226
Cdd:PRK13642 169 SMLDPTGRQEIMRVIHEIKE-KYQLTVLSITHDLDEAASSDRILVMKAGEIIK 220
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
17-224 |
3.43e-09 |
|
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: 55.11 E-value: 3.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 17 LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGRVEFKGKNLLELaaEDRA----GEGIFMAFQ------- 85
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEE--LPTSGTIRVNGQDVSDL--RGRAipylRRKIGVVFQdfrllpd 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 86 --------YPVEIPGVSNQfflqtalnaVRNYRGQEALDRFDFQDlmeekiKLLQMPEDLltrsvnvgfSGGEKKRNDIL 157
Cdd:cd03292 93 rnvyenvaFALEVTGVPPR---------EIRKRVPAALELVGLSH------KHRALPAEL---------SGGEQQRVAIA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488998194 158 QMAVLEPELCILDESDSGLDIDALKIVSQGVNALRDGKRAFIIVTHYQRILDYIKPDyVHVLYQGRI 224
Cdd:cd03292 149 RAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHR-VIALERGKL 214
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
14-240 |
3.55e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 55.96 E-value: 3.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 14 KAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAG------REDYEVTGGRVEFKGKNLLELaaEDRAGegifMAFQYP 87
Cdd:PRK13640 20 KPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGlllpddNPNSKITVDGITLTAKTVWDI--REKVG----IVFQNP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 88 veipgvSNQFFLQTALNAVRNYRGQEALDRFDFQDLMEEKIKLLQMPEDLLTRSVNVgfSGGEKKRNDILQMAVLEPELC 167
Cdd:PRK13640 94 ------DNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANL--SGGQKQRVAIAGILAVEPKII 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488998194 168 ILDESDSGLDIDALKIVSQGVNALRDGKRAFII-VTHyqRILDYIKPDYVHVLYQGRIVKSGD----FSLVKQLEEQG 240
Cdd:PRK13640 166 ILDESTSMLDPAGKEQILKLIRKLKKKNNLTVIsITH--DIDEANMADQVLVLDDGKLLAQGSpveiFSKVEMLKEIG 241
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-225 |
3.74e-09 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 56.19 E-value: 3.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 2 LSIQDLHVAVEDKAI-LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAG-RedyEVTGGRVEFKGKNLLELAA------- 72
Cdd:COG3845 258 LEVENLSVRDDRGVPaLKDVSLEVRAGEILGIAGVAGNGQSELAEALAGlR---PPASGSIRLDGEDITGLSPrerrrlg 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 73 -----EDRAGEGIFMAFqyPVEI---------PGVSNQFFLQTAlnAVRNYrGQEALDRFDfqdlmeekIKllqmpedll 138
Cdd:COG3845 335 vayipEDRLGRGLVPDM--SVAEnlilgryrrPPFSRGGFLDRK--AIRAF-AEELIEEFD--------VR--------- 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 139 TRSVNV---GFSGGekkrNdiLQMAVL------EPELCILDESDSGLDIDALKIVSQGVNALRDGKRAFIIVTHYqriLD 209
Cdd:COG3845 393 TPGPDTparSLSGG----N--QQKVILarelsrDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISED---LD 463
|
250
....*....|....*...
gi 488998194 210 YIK--PDYVHVLYQGRIV 225
Cdd:COG3845 464 EILalSDRIAVMYEGRIV 481
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
12-203 |
3.75e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 56.66 E-value: 3.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 12 EDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedyeVTGGRVEfKGKNLLElaaedraGEGIFMAFQypvEIP 91
Cdd:TIGR00956 774 EKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAER----VTTGVIT-GGDRLVN-------GRPLDSSFQ---RSI 838
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 92 GVSNQFFLQTALNAVRN-------YRGQEALDRFDFQDLMEEKIKLLQMPE--DLLTRSVNVGFSGGEKKRNDILQMAVL 162
Cdd:TIGR00956 839 GYVQQQDLHLPTSTVREslrfsayLRQPKSVSKSEKMEYVEEVIKLLEMESyaDAVVGVPGEGLNVEQRKRLTIGVELVA 918
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488998194 163 EPELCI-LDESDSGLDIDALKIVSQGVNALRDGKRAFIIVTH 203
Cdd:TIGR00956 919 KPKLLLfLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIH 960
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-75 |
4.00e-09 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 55.92 E-value: 4.00e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488998194 2 LSIQDLHVAVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGRVEFKGKNLL-ELAAEDR 75
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLE--TPDSGRIVLNGRDLFtNLPPRER 75
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
2-229 |
4.30e-09 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 55.36 E-value: 4.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 2 LSIQDLHVAVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTL-------------SATLAGREDYEV--TGGRVEFKGKN 66
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFlrcinflekpsegSIVVNGQTINLVrdKDGQLKVADKN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 67 LLELAAEDragegIFMAFQY----------------PVEIPGVSNQfflqtalnaVRNYRGQEALDRFDFQDLMEEKikl 130
Cdd:PRK10619 86 QLRLLRTR-----LTMVFQHfnlwshmtvlenvmeaPIQVLGLSKQ---------EARERAVKYLAKVGIDERAQGK--- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 131 lqMPEDLltrsvnvgfSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVSQGVNALRDGKRAFIIVTHYQRILDY 210
Cdd:PRK10619 149 --YPVHL---------SGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARH 217
|
250
....*....|....*....
gi 488998194 211 IKpDYVHVLYQGRIVKSGD 229
Cdd:PRK10619 218 VS-SHVIFLHQGKIEEEGA 235
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
14-241 |
4.53e-09 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 56.21 E-value: 4.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 14 KAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEVTG-GRVEFKGKNLleLAAEDRAGEGIFMafQYPVEIPG 92
Cdd:TIGR00955 38 KHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVKGsGSVLLNGMPI--DAKEMRAISAYVQ--QDDLFIPT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 93 --VSNQFFLQTALNAVRNY-------RGQEALDRFDFQDLMEEKIkllQMPEDLltrsvnVGFSGGEKKRNDILQMAVLE 163
Cdd:TIGR00955 114 ltVREHLMFQAHLRMPRRVtkkekreRVDEVLQALGLRKCANTRI---GVPGRV------KGLSGGERKRLAFASELLTD 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 164 PELCILDESDSGLD-------IDALKIVSQgvnalrdgKRAFIIVTHYQ---RILDYIkpDYVHVLYQGRIVKSGDFS-L 232
Cdd:TIGR00955 185 PPLLFCDEPTSGLDsfmaysvVQVLKGLAQ--------KGKTIICTIHQpssELFELF--DKIILMAEGRVAYLGSPDqA 254
|
....*....
gi 488998194 233 VKQLEEQGY 241
Cdd:TIGR00955 255 VPFFSDLGH 263
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
12-240 |
4.63e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 55.48 E-value: 4.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 12 EDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGRVEFKG------KNLLELaaEDRAGegifMAFQ 85
Cdd:PRK13633 21 TEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNAL--LIPSEGKVYVDGldtsdeENLWDI--RNKAG----MVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 86 YPveipgvSNQFF--------------LQTALNAVRNyRGQEALDRFDFQDLMEEKIKLLqmpedlltrsvnvgfSGGEK 151
Cdd:PRK13633 93 NP------DNQIVativeedvafgpenLGIPPEEIRE-RVDESLKKVGMYEYRRHAPHLL---------------SGGQK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 152 KRNDILQMAVLEPELCILDESDSGLDIDALKIVsqgVNALRDGKRAF----IIVTHYQRilDYIKPDYVHVLYQGRIVKS 227
Cdd:PRK13633 151 QRVAIAGILAMRPECIIFDEPTAMLDPSGRREV---VNTIKELNKKYgitiILITHYME--EAVEADRIIVMDSGKVVME 225
|
250
....*....|....*..
gi 488998194 228 GD----FSLVKQLEEQG 240
Cdd:PRK13633 226 GTpkeiFKEVEMMKKIG 242
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
16-231 |
4.79e-09 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 55.02 E-value: 4.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 16 ILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagredyevtggrvefkgkNLLELAaedRAGEgifmafqypVEIPGvsN 95
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVL------------------NLLEMP---RSGT---------LNIAG--N 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 96 QFFLQTALN--AVRNYRgQEALDRFD----------FQDLMEEKIKLLQMPED--------LLTRSVNVGF--------S 147
Cdd:PRK11124 65 HFDFSKTPSdkAIRELR-RNVGMVFQqynlwphltvQQNLIEAPCRVLGLSKDqalaraekLLERLRLKPYadrfplhlS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 148 GGEKKRNDILQMAVLEPELCILDESDSGLDIDalkIVSQGVNALRDGKRAFI---IVTHYqriLDYIKPDYVHVLY--QG 222
Cdd:PRK11124 144 GGQQQRVAIARALMMEPQVLLFDEPTAALDPE---ITAQIVSIIRELAETGItqvIVTHE---VEVARKTASRVVYmeNG 217
|
....*....
gi 488998194 223 RIVKSGDFS 231
Cdd:PRK11124 218 HIVEQGDAS 226
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
16-177 |
4.80e-09 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 55.86 E-value: 4.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 16 ILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYevTGGRVEFKGKNLLELAAEDRAGEGIFMAFQYPVEIPGVSN 95
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQ--TSGHIRFHGTDVSRLHARDRKVGFVFQHYALFRHMTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 96 QFFLQTALNavRNYRGQEALDRfdfQDLMeekiKLLQMPEdlLTRSVN---VGFSGGEKKRNDILQMAVLEPELCILDES 172
Cdd:PRK10851 95 IAFGLTVLP--RRERPNAAAIK---AKVT----QLLEMVQ--LAHLADrypAQLSGGQKQRVALARALAVEPQILLLDEP 163
|
....*
gi 488998194 173 DSGLD 177
Cdd:PRK10851 164 FGALD 168
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
2-230 |
5.68e-09 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 53.70 E-value: 5.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 2 LSIQDLHVAVED-KAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGRvefkgknllelaaedragegi 80
Cdd:cd03223 1 IELENLSLATPDgRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGL--WPWGSGR--------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 81 fmafqypVEIPGVSNQFFL-QTALNAVRNYRGQealdrfdfqdlmeekiklLQMP-EDLLtrsvnvgfSGGEKKRNDILQ 158
Cdd:cd03223 58 -------IGMPEGEDLLFLpQRPYLPLGTLREQ------------------LIYPwDDVL--------SGGEQQRLAFAR 104
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488998194 159 MAVLEPELCILDESDSGLDIDALKIVSQgvnALRDGKRAFIIVTHYQRILDYikpdYVHVLyqgRIVKSGDF 230
Cdd:cd03223 105 LLLHKPKFVFLDEATSALDEESEDRLYQ---LLKELGITVISVGHRPSLWKF----HDRVL---DLDGEGGW 166
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
2-228 |
6.63e-09 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 54.90 E-value: 6.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 2 LSIQDLHVAVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEvtGGRVEFKGKNLLELAAEDRAGEGIF 81
Cdd:PRK10895 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRD--AGNIIIDDEDISLLPLHARARRGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 82 MAFQYPVEIPGVSNQFFLQTALNAVRNYRGQEALDRFDfqDLMEEkikllqMPEDLLTRSVNVGFSGGEKKRNDILQMAV 161
Cdd:PRK10895 82 YLPQEASIFRRLSVYDNLMAVLQIRDDLSAEQREDRAN--ELMEE------FHIEHLRDSMGQSLSGGERRRVEIARALA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488998194 162 LEPELCILDESDSGLD----IDALKIVSQgvnaLRDGKRAFIIVTHYQR-ILDYIKPDYvhVLYQGRIVKSG 228
Cdd:PRK10895 154 ANPKFILLDEPFAGVDpisvIDIKRIIEH----LRDSGLGVLITDHNVReTLAVCERAY--IVSQGHLIAHG 219
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
3-178 |
7.96e-09 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 54.79 E-value: 7.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 3 SIQDLHVAVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLaGREdYEVTGGRVEFKGKNLLELAAEDRAGEGIFM 82
Cdd:PRK10575 13 ALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKML-GRH-QPPSEGEILLDAQPLESWSSKAFARKVAYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 83 AFQYPvEIPGVSNQfflqtALNAVRNYRGQEALDRFDFQDL--MEEKIKLLQMpEDLLTRSVNvGFSGGEKKRNDILQMA 160
Cdd:PRK10575 91 PQQLP-AAEGMTVR-----ELVAIGRYPWHGALGRFGAADRekVEEAISLVGL-KPLAHRLVD-SLSGGERQRAWIAMLV 162
|
170
....*....|....*...
gi 488998194 161 VLEPELCILDESDSGLDI 178
Cdd:PRK10575 163 AQDSRCLLLDEPTSALDI 180
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
12-242 |
8.46e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 54.67 E-value: 8.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 12 EDKAiLRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGRVEFKGKNLLELAA---EDRAGEGIfmAFQYPv 88
Cdd:PRK13637 19 EKKA-LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGL--LKPTSGKIIIDGVDITDKKVklsDIRKKVGL--VFQYP- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 89 eipgvSNQFFLQTALNAVRNYRGQEALDRFDFQDLMEEKIKLLQMP-EDLLTRSvNVGFSGGEKKRNDILQMAVLEPELC 167
Cdd:PRK13637 93 -----EYQLFEETIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDyEDYKDKS-PFELSGGQKRRVAIAGVVAMEPKIL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 168 ILDESDSGLDIDALKIVSQGVNALRDGKRAFII-VTHYQRilDYIK-PDYVHVLYQGRIVKSGD----FSLVKQLEEQGY 241
Cdd:PRK13637 167 ILDEPTAGLDPKGRDEILNKIKELHKEYNMTIIlVSHSME--DVAKlADRIIVMNKGKCELQGTprevFKEVETLESIGL 244
|
.
gi 488998194 242 G 242
Cdd:PRK13637 245 A 245
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-76 |
9.74e-09 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 54.32 E-value: 9.74e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488998194 1 MLSIQDLHVAVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLsATLAGREDyEVTGGRVEFKGKNLLELAAEDRA 76
Cdd:COG4604 1 MIEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTL-LSMISRLL-PPDSGEVLVDGLDVATTPSRELA 74
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
13-235 |
1.14e-08 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 54.84 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 13 DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEVtgGRVEFKGKNLLELAAEDRAGEGIFMAFQypveipG 92
Cdd:PRK13536 53 DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDA--GKITVLGVPVPARARLARARIGVVPQFD------N 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 93 VSNQFFLQTALNAVRNYRGQEALDrfdfqdlMEEKI-KLLQMPEdlLTRSVNV---GFSGGEKKRNDILQMAVLEPELCI 168
Cdd:PRK13536 125 LDLEFTVRENLLVFGRYFGMSTRE-------IEAVIpSLLEFAR--LESKADArvsDLSGGMKRRLTLARALINDPQLLI 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488998194 169 LDESDSGLDIDALKIVSQGVNALRDGKRAFIIVTHYQRILDYIkPDYVHVLYQGR-IVKSGDFSLVKQ 235
Cdd:PRK13536 196 LDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERL-CDRLCVLEAGRkIAEGRPHALIDE 262
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
19-229 |
1.42e-08 |
|
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: 54.81 E-value: 1.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 19 GLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGRVEFK-GKNLLELAAEDRAGEGifMAFQYpveIPGVSNQF 97
Cdd:TIGR03269 302 NVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGV--LEPTSGEVNVRvGDEWVDMTKPGPDGRG--RAKRY---IGILHQEY 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 98 FL---QTALNAVRNYRGQEALDRF------------DFQDLMEEKIkLLQMPEDLltrsvnvgfSGGEKKRNDILQMAVL 162
Cdd:TIGR03269 375 DLyphRTVLDNLTEAIGLELPDELarmkavitlkmvGFDEEKAEEI-LDKYPDEL---------SEGERHRVALAQVLIK 444
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 163 EPELCILDESDSGLD-IDALKIVSQGVNALRDGKRAFIIVTHYqriLDYIKP--DYVHVLYQGRIVKSGD 229
Cdd:TIGR03269 445 EPRIVILDEPTGTMDpITKVDVTHSILKAREEMEQTFIIVSHD---MDFVLDvcDRAALMRDGKIVKIGD 511
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1-73 |
1.69e-08 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 52.88 E-value: 1.69e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488998194 1 MLSIQDLHVAVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDyeVTGGRVEFKGKNLLELAAE 73
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLAR--PDAGEVLWQGEPIRRQRDE 71
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
16-203 |
1.82e-08 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 53.28 E-value: 1.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 16 ILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGRVEFKGKNLLELAAEDRAG-EGIFMAFQYpveipgvs 94
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLD--TPTSGDVIFNGQPMSKLSSAAKAElRNQKLGFIY-------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 95 nQF-FLQTALNAVRNYRgqealdrfdfQDLMEEKIKLLQMPEDLLTRSVNVG-----------FSGGEKKRNDILQMAVL 162
Cdd:PRK11629 94 -QFhHLLPDFTALENVA----------MPLLIGKKKPAEINSRALEMLAAVGlehranhrpseLSGGERQRVAIARALVN 162
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488998194 163 EPELCILDESDSGLDIDALKIVSQGVNAL--RDGKrAFIIVTH 203
Cdd:PRK11629 163 NPRLVLADEPTGNLDARNADSIFQLLGELnrLQGT-AFLVVTH 204
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
17-229 |
1.90e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 53.84 E-value: 1.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 17 LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEvtGGRVEFKGKNLLELAAEDRAGEGIFMAFQYPveipgvSNQ 96
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQ--KGKVLVSGIDTGDFSKLQGIRKLVGIVFQNP------ETQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 97 FFLQTALNAVRNYRGQEALDRFDFQDLMEEKIKLLQMpEDLLTRSVNVgFSGGEKKRNDILQMAVLEPELCILDESDSGL 176
Cdd:PRK13644 90 FVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGL-EKYRHRSPKT-LSGGQGQCVALAGILTMEPECLIFDEVTSML 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488998194 177 DIDALKIVSQGVNALRDGKRAFIIVTHYQRILDyiKPDYVHVLYQGRIVKSGD 229
Cdd:PRK13644 168 DPDSGIAVLERIKKLHEKGKTIVYITHNLEELH--DADRIIVMDRGKIVLEGE 218
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1-87 |
2.42e-08 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 53.76 E-value: 2.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 1 MLSIQDLHVAVED-----KAILRgLNLEVRPGEVHAIMGPNGSGKSTLSATLAG--REDYEVTGGRVEFKGKNLLELAAE 73
Cdd:COG4170 3 LLDIRNLTIEIDTpqgrvKAVDR-VSLTLNEGEIRGLVGESGSGKSLIAKAICGitKDNWHVTADRFRWNGIDLLKLSPR 81
|
90
....*....|....*..
gi 488998194 74 DR---AGEGIFMAFQYP 87
Cdd:COG4170 82 ERrkiIGREIAMIFQEP 98
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-177 |
2.57e-08 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 53.69 E-value: 2.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 1 MLSIQDLHVAVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGRVEFKGKNLLELAAEDRAgegI 80
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFE--QPTAGQIMLDGVDLSHVPPYQRP---I 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 81 FMAFQYPVEIPGVSNQFFLQTALNavrnyrgQEALDRFDFQDLMEEKIKLLQMPEdlLTRSVNVGFSGGEKKRNDILQMA 160
Cdd:PRK11607 94 NMMFQSYALFPHMTVEQNIAFGLK-------QDKLPKAEIASRVNEMLGLVHMQE--FAKRKPHQLSGGQRQRVALARSL 164
|
170
....*....|....*..
gi 488998194 161 VLEPELCILDESDSGLD 177
Cdd:PRK11607 165 AKRPKLLLLDEPMGALD 181
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
2-223 |
2.72e-08 |
|
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: 52.47 E-value: 2.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 2 LSIQDLHVAVEDKA-----ILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGRVEFKGKnllelaaedra 76
Cdd:cd03250 1 ISVEDASFTWDSGEqetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLG--ELEKLSGSVSVPGS----------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 77 gegifMAFqypveipgVSNQFFLQTAlnAVRN----------YRGQE-----ALDRfDFQdlmeekikllQMPEDLLT-- 139
Cdd:cd03250 68 -----IAY--------VSQEPWIQNG--TIREnilfgkpfdeERYEKvikacALEP-DLE----------ILPDGDLTei 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 140 --RSVNVgfSGGEKKRndI-LQMAVL-EPELCILDESDSGLDID-ALKIVSQGVNALRDGKRAFIIVTHYqriLDYIKP- 213
Cdd:cd03250 122 geKGINL--SGGQKQR--IsLARAVYsDADIYLLDDPLSAVDAHvGRHIFENCILGLLLNNKTRILVTHQ---LQLLPHa 194
|
250
....*....|
gi 488998194 214 DYVHVLYQGR 223
Cdd:cd03250 195 DQIVVLDNGR 204
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
14-229 |
3.03e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 53.43 E-value: 3.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 14 KAiLRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGRVEFKGKNLLELAAEDRAG--EGIFMAFQYP---- 87
Cdd:PRK11308 29 KA-LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIE--TPTGGELYYQGQDLLKADPEAQKLlrQKIQIVFQNPygsl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 88 ---------VEIPGVSNqfflqTALNAVrnyrgqealdrfdfqdlmEEKIKLLQMPEDLLTRSVNVG-----FSGGEKKR 153
Cdd:PRK11308 106 nprkkvgqiLEEPLLIN-----TSLSAA------------------ERREKALAMMAKVGLRPEHYDryphmFSGGQRQR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 154 NDILQMAVLEPELCILDESDSGLDIdalKIVSQGVNALRDGKR----AFIIVTHYQRILDYIKPDyVHVLYQGRIVKSGD 229
Cdd:PRK11308 163 IAIARALMLDPDVVVADEPVSALDV---SVQAQVLNLMMDLQQelglSYVFISHDLSVVEHIADE-VMVMYLGRCVEKGT 238
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
20-228 |
3.47e-08 |
|
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: 52.11 E-value: 3.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 20 LNLEVRPGEVHAIMGPNGSGKSTLSATLAGredYEV-TGGRVEFKGknlLELAAEDRAGEGIFMAFQypveipgvSNQFF 98
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAG---FETpQSGRVLING---VDVTAAPPADRPVSMLFQ--------ENNLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 99 LQTA--------------LNAVRNYRGQEALDRFDFQDLMeekiklLQMPEDLltrsvnvgfSGGEKKRNDILQMAVLEP 164
Cdd:cd03298 83 AHLTveqnvglglspglkLTAEDRQAIEVALARVGLAGLE------KRLPGEL---------SGGERQRVALARVLVRDK 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488998194 165 ELCILDESDSGLDIDALKIVSQGVNAL-RDGKRAFIIVTHYQRILDYIKPDYVHvLYQGRIVKSG 228
Cdd:cd03298 148 PVLLLDEPFAALDPALRAEMLDLVLDLhAETKMTVLMVTHQPEDAKRLAQRVVF-LDNGRIAAQG 211
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
17-65 |
4.83e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 52.99 E-value: 4.83e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 488998194 17 LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGRVEFKGK 65
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSG--NYQPDAGSILIDGQ 66
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
28-229 |
5.22e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 52.55 E-value: 5.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 28 EVHAIMGPNGSGKSTLSATLAGR----------EDYeVTGGRVEFKGKNLLELAAE----DRAGEGIFMAFQYPveipgv 93
Cdd:PRK13631 53 KIYFIIGNSGSGKSTLVTHFNGLikskygtiqvGDI-YIGDKKNNHELITNPYSKKiknfKELRRRVSMVFQFP------ 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 94 SNQFFLQTALNAVrnYRGQEAL--DRFDFQDLMEEKIKLLQMPEDLLTRSvNVGFSGGEKKRNDILQMAVLEPELCILDE 171
Cdd:PRK13631 126 EYQLFKDTIEKDI--MFGPVALgvKKSEAKKLAKFYLNKMGLDDSYLERS-PFGLSGGQKRRVAIAGILAIQPEILIFDE 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488998194 172 SDSGLDIDALKIVSQGV-NALRDGKRAFIIVTHYQRILDYikPDYVHVLYQGRIVKSGD 229
Cdd:PRK13631 203 PTAGLDPKGEHEMMQLIlDAKANNKTVFVITHTMEHVLEV--ADEVIVMDKGKILKTGT 259
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-248 |
6.05e-08 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 52.92 E-value: 6.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 2 LSIQDLHV-AVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEvtgGRVEFKGKNLLELAAEdragegi 80
Cdd:PRK11174 350 IEAEDLEIlSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ---GSLKINGIELRELDPE------- 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 81 fmafQYPVEIPGVSN--QFFLQTALNAVRnyRGQEALDRFDFQDLME-----EKIKLLQMPEDLLTRSVNVGFSGGEKKR 153
Cdd:PRK11174 420 ----SWRKHLSWVGQnpQLPHGTLRDNVL--LGNPDASDEQLQQALEnawvsEFLPLLPQGLDTPIGDQAAGLSVGQAQR 493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 154 ndI-LQMAVLEP-ELCILDESDSGLDIDALKIVSQGVNALRDGKRAfIIVTHyqRILDYIKPDYVHVLYQGRIVKSGDFS 231
Cdd:PRK11174 494 --LaLARALLQPcQLLLLDEPTASLDAHSEQLVMQALNAASRRQTT-LMVTH--QLEDLAQWDQIWVMQDGQIVQQGDYA 568
|
250 260
....*....|....*....|
gi 488998194 232 lvkQLEEQG---YGWLTEQQ 248
Cdd:PRK11174 569 ---ELSQAGglfATLLAHRQ 585
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
17-177 |
7.43e-08 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 51.70 E-value: 7.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 17 LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGRVEFKGKNLlelaaeDRAGEGIFMAFQYPVEIPGVSNQ 96
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLA--QPTSGGVILEGKQI------TEPGPDRMVVFQNYSLLPWLTVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 97 FFLQTALNAVRNYRGQEaldrfDFQDLMEEKIKLLQMPEDLLTRSVNVgfSGGEKKRNDILQMAVLEPELCILDESDSGL 176
Cdd:TIGR01184 73 ENIALAVDRVLPDLSKS-----ERRAIVEEHIALVGLTEAADKRPGQL--SGGMKQRVAIARALSIRPKVLLLDEPFGAL 145
|
.
gi 488998194 177 D 177
Cdd:TIGR01184 146 D 146
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
2-203 |
1.12e-07 |
|
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: 50.57 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 2 LSIQDLHVAVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGRVefkgknLLELAAEDRAGEGIF 81
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLS--PPLAGRV------LLNGGPLDFQRDSIA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 82 MAFQYPVEIPGVsnqfflQTALNAVRNYRG----------QEALDRFDFQDLmeekikllqmpEDLLTRSVnvgfSGGEK 151
Cdd:cd03231 73 RGLLYLGHAPGI------KTTLSVLENLRFwhadhsdeqvEEALARVGLNGF-----------EDRPVAQL----SAGQQ 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488998194 152 KRNDILQMAVLEPELCILDESDSGLDIDALKIVSQGVNALRDGKRAFIIVTH 203
Cdd:cd03231 132 RRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTH 183
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
12-224 |
1.22e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 51.27 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 12 EDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGRVEFKGKNLLELAAEDRAGEgIFMAFQYPveip 91
Cdd:PRK13650 18 QEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGL--LEAESGQIIIDGDLLTEENVWDIRHK-IGMVFQNP---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 92 gvSNQFFLQTALNAVRNYRGQEALDRFDFQDLMEEKIKLLQMpEDLLTRSvNVGFSGGEKKRNDILQMAVLEPELCILDE 171
Cdd:PRK13650 91 --DNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGM-QDFKERE-PARLSGGQKQRVAIAGAVAMRPKIIILDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488998194 172 SDSGLDIDALKIVSQGVNALRDGKRAFII-VTHYqriLDYIK-PDYVHVLYQGRI 224
Cdd:PRK13650 167 ATSMLDPEGRLELIKTIKGIRDDYQMTVIsITHD---LDEVAlSDRVLVMKNGQV 218
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-229 |
1.26e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 51.78 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 1 MLSIQDLHVAVEDK----AILRGLNLEVRPGEVHAIMGPNGSGKSTlsATLAGREDYEVTGGRVEF-------KGKNLLE 69
Cdd:PRK10261 12 VLAVENLNIAFMQEqqkiAAVRNLSFSLQRGETLAIVGESGSGKSV--TALALMRLLEQAGGLVQCdkmllrrRSRQVIE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 70 LAAEDRA------GEGIFMAFQYPVeipgvsnqfflqTALNAV--------RNYRGQEALDRfdfQDLMEEKIKLL---Q 132
Cdd:PRK10261 90 LSEQSAAqmrhvrGADMAMIFQEPM------------TSLNPVftvgeqiaESIRLHQGASR---EEAMVEAKRMLdqvR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 133 MPE--DLLTRSVNvGFSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVSQGVNAL-RDGKRAFIIVTHYQRILD 209
Cdd:PRK10261 155 IPEaqTILSRYPH-QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLqKEMSMGVIFITHDMGVVA 233
|
250 260
....*....|....*....|
gi 488998194 210 YIKpDYVHVLYQGRIVKSGD 229
Cdd:PRK10261 234 EIA-DRVLVMYQGEAVETGS 252
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
17-231 |
1.28e-07 |
|
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: 51.75 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 17 LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEVTGGRVEFKGKNLLELAAEDRAGEGIFMAFQYPVEIP--GVS 94
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTWDGEIYWSGSPLKASNIRDTERAGIVIIHQELTLVPelSVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 95 NQFFLQTALnAVRNYRGQEALDRFDFQDLMEEkiklLQMPEDLLTRSVNvGFSGGEKKRNDILQMAVLEPELCILDESDS 174
Cdd:TIGR02633 97 ENIFLGNEI-TLPGGRMAYNAMYLRAKNLLRE----LQLDADNVTRPVG-DYGGGQQQLVEIAKALNKQARLLILDEPSS 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488998194 175 GLDIDALKIVsqgVNALRDGKRAFIIVTHYQRILDYIKP--DYVHVLYQGRIVKSGDFS 231
Cdd:TIGR02633 171 SLTEKETEIL---LDIIRDLKAHGVACVYISHKLNEVKAvcDTICVIRDGQHVATKDMS 226
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
26-228 |
1.35e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 51.78 E-value: 1.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 26 PGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGRVEFKGKNLLELAAEDRAG--EGIFMAFQYPVEI--PGVSNQFFLQT 101
Cdd:PRK10261 349 PGETLSLVGESGSGKSTTGRALL--RLVESQGGEIIFNGQRIDTLSPGKLQAlrRDIQFIFQDPYASldPRQTVGDSIME 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 102 ALNAVRNYRGQEALDRFDFqdlMEEKIKLLqmPEDLLTRSVNvgFSGGEKKRNDILQMAVLEPELCILDESDSGLDIdal 181
Cdd:PRK10261 427 PLRVHGLLPGKAAAARVAW---LLERVGLL--PEHAWRYPHE--FSGGQRQRICIARALALNPKVIIADEAVSALDV--- 496
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488998194 182 KIVSQGVNALRDGKR----AFIIVTHYQRILDYIKpDYVHVLYQGRIVKSG 228
Cdd:PRK10261 497 SIRGQIINLLLDLQRdfgiAYLFISHDMAVVERIS-HRVAVMYLGQIVEIG 546
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-87 |
2.00e-07 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 51.00 E-value: 2.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 1 MLSIQDLHVAVEDKA-ILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGRVEFKGKNLLELAAEDRageG 79
Cdd:PRK11650 3 GLKLQAVRKSYDGKTqVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLE--RITSGEIWIGGRVVNELEPADR---D 77
|
90
....*....|..
gi 488998194 80 IFMAFQ----YP 87
Cdd:PRK11650 78 IAMVFQnyalYP 89
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-229 |
2.04e-07 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 50.41 E-value: 2.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 1 MLSIQDLHVAVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGRVEFKGKNLLELAAEDRAGEGI 80
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLV--KPDSGRIFLDGEDITHLPMHKRARLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 81 ------------------FMAfqypveipgvsnqfFLQTalnavRNYRGQEALDRFDfqDLMEE-KI-KLLQMPEDLLtr 140
Cdd:COG1137 81 gylpqeasifrkltvednILA--------------VLEL-----RKLSKKEREERLE--ELLEEfGItHLRKSKAYSL-- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 141 svnvgfSGGEKKRNDILQMAVLEPELCILDESDSGLD----IDALKIVSQgvnaLRD---GkrafIIVT--HYQRILDYI 211
Cdd:COG1137 138 ------SGGERRRVEIARALATNPKFILLDEPFAGVDpiavADIQKIIRH----LKErgiG----VLITdhNVRETLGIC 203
|
250
....*....|....*...
gi 488998194 212 kpDYVHVLYQGRIVKSGD 229
Cdd:COG1137 204 --DRAYIISEGKVLAEGT 219
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1-49 |
2.13e-07 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 51.35 E-value: 2.13e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 488998194 1 MLSIQDLHVAVED-KAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAG 49
Cdd:COG4178 362 ALALEDLTLRTPDgRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAG 411
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
14-49 |
2.20e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 50.94 E-value: 2.20e-07
10 20 30
....*....|....*....|....*....|....*.
gi 488998194 14 KAiLRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAG 49
Cdd:NF040905 15 KA-LDDVNLSVREGEIHALCGENGAGKSTLMKVLSG 49
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
17-237 |
2.44e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 50.39 E-value: 2.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 17 LRGLNLEVRPGEVHAIMGPNGSGKSTL------------SATLAGreDYEVTGGRVefKGKNLLELAAEdragegIFMAF 84
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMiqltngliisetGQTIVG--DYAIPANLK--KIKEVKRLRKE------IGLVF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 85 QYPveipgvSNQFFLQTALNAVRNYRGQEALDRFDFQDLMEEKIKLLQMPEDLLTRSvNVGFSGGEKKRNDILQMAVLEP 164
Cdd:PRK13645 97 QFP------EYQLFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDYVKRS-PFELSGGQKRRVALAGIIAMDG 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488998194 165 ELCILDESDSGLDIDALK-IVSQGVNALRDGKRAFIIVTH-YQRILDYikPDYVHVLYQGRIVKSGD-FSLVKQLE 237
Cdd:PRK13645 170 NTLVLDEPTGGLDPKGEEdFINLFERLNKEYKKRIIMVTHnMDQVLRI--ADEVIVMHEGKVISIGSpFEIFSNQE 243
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-203 |
2.57e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 50.17 E-value: 2.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 2 LSIQDLHVAVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYeVTGGRVE----FKGKNLLEL---AAED 74
Cdd:PRK14243 11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDL-IPGFRVEgkvtFHGKNLYAPdvdPVEV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 75 RAGEGifMAFQYPVEIPgvsNQFFLQTALNA-VRNYRGqealdrfDFQDLMEEKIK---LLQMPEDLLTRSvNVGFSGGE 150
Cdd:PRK14243 90 RRRIG--MVFQKPNPFP---KSIYDNIAYGArINGYKG-------DMDELVERSLRqaaLWDEVKDKLKQS-GLSLSGGQ 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488998194 151 KKRNDILQMAVLEPELCILDESDSGLD-IDALKIvSQGVNALRDgKRAFIIVTH 203
Cdd:PRK14243 157 QQRLCIARAIAVQPEVILMDEPCSALDpISTLRI-EELMHELKE-QYTIIIVTH 208
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-243 |
2.72e-07 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 50.98 E-value: 2.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 2 LSIQDLHVAVEDKA--ILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAgREdYEVTGGRVEFKGKNLLELAAED-RAGe 78
Cdd:PRK11160 339 LTLNNVSFTYPDQPqpVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLT-RA-WDPQQGEILLNGQPIADYSEAAlRQA- 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 79 gifMAFqypveipgVSNQ--FF-------LQTALNAVRNYRGQEALDRFDFQdlmeekiKLLQMPEDLLT------RSVn 143
Cdd:PRK11160 416 ---ISV--------VSQRvhLFsatlrdnLLLAAPNASDEALIEVLQQVGLE-------KLLEDDKGLNAwlgeggRQL- 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 144 vgfSGGEKKRNDILQmAVLEP-ELCILDESDSGLDIDALKIVSQGVNALRDGKrAFIIVTHYQRILDYIkpDYVHVLYQG 222
Cdd:PRK11160 477 ---SGGEQRRLGIAR-ALLHDaPLLLLDEPTEGLDAETERQILELLAEHAQNK-TVLMITHRLTGLEQF--DRICVMDNG 549
|
250 260
....*....|....*....|.
gi 488998194 223 RIVKSGDFSLVkqLEEQGYGW 243
Cdd:PRK11160 550 QIIEQGTHQEL--LAQQGRYY 568
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
2-229 |
3.74e-07 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 49.70 E-value: 3.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 2 LSIQDLHVAVeDKAILRGLNLEVRPGEVHAIMGPNGSGKS-TLSATL----AGredYEVTGGRVEFKGKnllELAAEDRA 76
Cdd:PRK10418 5 IELRNIALQA-AQPLVHGVSLTLQRGRVLALVGGSGSGKSlTCAAALgilpAG---VRQTAGRVLLDGK---PVAPCALR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 77 GEGIFMAFQYPveipgvsnqfflQTALNAVRNYR--GQE---ALDRFDFQDLMEEKIKLLQMPEDL-LTRSVNVGFSGGE 150
Cdd:PRK10418 78 GRKIATIMQNP------------RSAFNPLHTMHthAREtclALGKPADDATLTAALEAVGLENAArVLKLYPFEMSGGM 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 151 KKRNDIlQMAVL-EPELCILDESDSGLDIDA-LKIVSQGVNALRDGKRAFIIVTHYQRILDYIKpDYVHVLYQGRIVKSG 228
Cdd:PRK10418 146 LQRMMI-ALALLcEAPFIIADEPTTDLDVVAqARILDLLESIVQKRALGMLLVTHDMGVVARLA-DDVAVMSHGRIVEQG 223
|
.
gi 488998194 229 D 229
Cdd:PRK10418 224 D 224
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
24-203 |
5.53e-07 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 50.40 E-value: 5.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 24 VRPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGRVEFKGKNLLELAAEDRAGEGIFMAFQYPVEIPGVSNQFFLQTAL 103
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTG--DTTVTSGDATVAGKSILTNISDVHQNMGYCPQFDAIDDLLTGREHLYLYARL 2039
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 104 NAVRNyRGQEALDRFDFQDLMeekiklLQMPEDLLTRSvnvgFSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKI 183
Cdd:TIGR01257 2040 RGVPA-EEIEKVANWSIQSLG------LSLYADRLAGT----YSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRM 2108
|
170 180
....*....|....*....|
gi 488998194 184 VSQGVNALRDGKRAFIIVTH 203
Cdd:TIGR01257 2109 LWNTIVSIIREGRAVVLTSH 2128
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
9-205 |
5.57e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 50.01 E-value: 5.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 9 VAVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGR--EDYevtggrvefkgKNLLELAAEDR-AGEGIFMAFQ 85
Cdd:PRK10938 268 VSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDhpQGY-----------SNDLTLFGRRRgSGETIWDIKK 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 86 YpveIPGVSNQFFLQTALNA-VRN------------YrgQEALDRfdFQDLMEEKIKLLQMPEDLLTRSVNvGFSGGEKK 152
Cdd:PRK10938 337 H---IGYVSSSLHLDYRVSTsVRNvilsgffdsigiY--QAVSDR--QQKLAQQWLDILGIDKRTADAPFH-SLSWGQQR 408
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488998194 153 RNDILQMAVLEPELCILDESDSGLDIDALKIVSQGVNAL-RDGKRAFIIVTHYQ 205
Cdd:PRK10938 409 LALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLiSEGETQLLFVSHHA 462
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
17-85 |
7.10e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 49.73 E-value: 7.10e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488998194 17 LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGRVEFKGKNLLELAAEDRAGEGIFMAFQ 85
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGI--YQKDSGSILFQGKEIDFKSSKEALENGISMVHQ 80
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-177 |
8.82e-07 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 48.54 E-value: 8.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 1 MLSIQDLHVAVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEvtGGRVEFKGKNLLELAAEdRAgegi 80
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQ--HGSITLDGKPVEGPGAE-RG---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 81 fMAFQYPVEIPGVSNQ----FFLQTA--LNAVRNYRGQEALDRFDFQDLMEEKIKLLqmpedlltrsvnvgfSGGEKKRN 154
Cdd:PRK11248 74 -VVFQNEGLLPWRNVQdnvaFGLQLAgvEKMQRLEIAHQMLKKVGLEGAEKRYIWQL---------------SGGQRQRV 137
|
170 180
....*....|....*....|...
gi 488998194 155 DILQMAVLEPELCILDESDSGLD 177
Cdd:PRK11248 138 GIARALAANPQLLLLDEPFGALD 160
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-211 |
1.01e-06 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 48.65 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 2 LSIQDLHVAVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEvtGGRVEFKGKNLLELAAEDRAGEGIF 81
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPD--AGSISLCGEPVPSRARHARQRVGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 82 MAFQypveipGVSNQFFLQTALNAVRNYRGQEALD-RFDFQDLMEekIKLLQMPEDLLTRSVnvgfSGGEKKRNDILQMA 160
Cdd:PRK13537 86 PQFD------NLDPDFTVRENLLVFGRYFGLSAAAaRALVPPLLE--FAKLENKADAKVGEL----SGGMKRRLTLARAL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488998194 161 VLEPELCILDESDSGLDIDALKIVSQGVNALRDGKRAFIIVTHY----QRILDYI 211
Cdd:PRK13537 154 VNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFmeeaERLCDRL 208
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
12-207 |
1.21e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 49.07 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 12 EDK-AILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyevTGGRVEfkgknllelaaedraGEGIFMAFQYPVE- 89
Cdd:PLN03140 890 EDRlQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRK----TGGYIE---------------GDIRISGFPKKQEt 950
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 90 ---IPGVSNQFFLQTALNAVRnyrgqEAL---------------DRFDFQDLMEEKIKLLQMPEDLLTRSVNVGFSGGEK 151
Cdd:PLN03140 951 farISGYCEQNDIHSPQVTVR-----ESLiysaflrlpkevskeEKMMFVDEVMELVELDNLKDAIVGLPGVTGLSTEQR 1025
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488998194 152 KRNDILQMAVLEPELCILDESDSGLDIDALKIVSQGVNALRDGKRAFIIVTHYQRI 207
Cdd:PLN03140 1026 KRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSI 1081
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-49 |
1.65e-06 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 48.30 E-value: 1.65e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 488998194 1 MLSIQDLHVAVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAG 49
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAING 51
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
9-205 |
1.68e-06 |
|
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: 47.24 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 9 VAVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyevTGGRVEfkGKNLLelaaedrAGEGIFMAFQypv 88
Cdd:cd03232 15 VKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRK----TAGVIT--GEILI-------NGRPLDKNFQ--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 89 EIPGVSNQFFLQTALNAVRnyrgqEALdRFdfqdlmeekikllqmpedlltrSVNV-GFSGGEKKRNDILQMAVLEPELC 167
Cdd:cd03232 79 RSTGYVEQQDVHSPNLTVR-----EAL-RF----------------------SALLrGLSVEQRKRLTIGVELAAKPSIL 130
|
170 180 190
....*....|....*....|....*....|....*...
gi 488998194 168 ILDESDSGLDIDALKIVSQGVNALRDGKRAfIIVTHYQ 205
Cdd:cd03232 131 FLDEPTSGLDSQAAYNIVRFLKKLADSGQA-ILCTIHQ 167
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-229 |
1.84e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 48.16 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 1 MLSIQDLHVA-----------VEDKAILRGLNLEVRPGEVHAIMGPNGSGKST----LSATLAGRedyevtgGRVEFKGK 65
Cdd:PRK15134 275 LLDVEQLQVAfpirkgilkrtVDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINSQ-------GEIWFDGQ 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 66 NLLELaaeDRAG-----EGIFMAFQYPveipgvsnqfflQTALNAvrnyrgqealdRFDFQDLMEEKIKLLQ-------- 132
Cdd:PRK15134 348 PLHNL---NRRQllpvrHRIQVVFQDP------------NSSLNP-----------RLNVLQIIEEGLRVHQptlsaaqr 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 133 -------MPE---DLLTRSVNVG-FSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVSQGVNALRDGKR-AFII 200
Cdd:PRK15134 402 eqqviavMEEvglDPETRHRYPAeFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQlAYLF 481
|
250 260
....*....|....*....|....*....
gi 488998194 201 VTHYQRILDYIkPDYVHVLYQGRIVKSGD 229
Cdd:PRK15134 482 ISHDLHVVRAL-CHQVIVLRQGEVVEQGD 509
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
17-210 |
1.99e-06 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 47.70 E-value: 1.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 17 LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAG--------REDYEVTGGRVEFKGKnLLELAAEDRAGEG-IFMAFQY- 86
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGlitgdksaGSHIELLGRTVQREGR-LARDIRKSRANTGyIFQQFNLv 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 87 -------PVEIPGVSNQFFLQTAL---NAVRNYRGQEALDRFDFQDLMEEKIKLLqmpedlltrsvnvgfSGGEKKRNDI 156
Cdd:PRK09984 99 nrlsvleNVLIGALGSTPFWRTCFswfTREQKQRALQALTRVGMVHFAHQRVSTL---------------SGGQQQRVAI 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488998194 157 LQMAVLEPELCILDESDSGLDIDALKIVSQGVNALRDGKRAFIIVTHYQriLDY 210
Cdd:PRK09984 164 ARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQ--VDY 215
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-60 |
2.33e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 47.96 E-value: 2.33e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 488998194 2 LSIQDLHVAVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGRV 60
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVG--ELEPDSGTV 376
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
23-216 |
2.43e-06 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 47.40 E-value: 2.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 23 EVRPGEVHAIMGPNGSGKSTLSATLAGR-----EDYEVTGGRVEFKGKnllELAAEDragEGIFMAFQYPVeIPGVSNQF 97
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVlkpdeGDIEIELDTVSYKPQ---YIKADY---EGTVRDLLSSI-TKDFYTHP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 98 FLQTalnavrnyrgqealdrfdfqdlmeEKIKLLQMpEDLLTRSVNvGFSGGEKKRNDILQMAVLEPELCILDESDSGLD 177
Cdd:cd03237 94 YFKT------------------------EIAKPLQI-EQILDREVP-ELSGGELQRVAIAACLSKDADIYLLDEPSAYLD 147
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488998194 178 IDALKIVSQGVN--ALRDGKRAFiIVTHyqrilDYIKPDYV 216
Cdd:cd03237 148 VEQRLMASKVIRrfAENNEKTAF-VVEH-----DIIMIDYL 182
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-82 |
2.95e-06 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 47.71 E-value: 2.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 1 MLSIQDLHVavedKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGRVEFKGKNL------------L 68
Cdd:COG1129 256 VLEVEGLSV----GGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGAD--PADSGEIRLDGKPVrirsprdairagI 329
|
90
....*....|....
gi 488998194 69 ELAAEDRAGEGIFM 82
Cdd:COG1129 330 AYVPEDRKGEGLVL 343
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
20-228 |
3.48e-06 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 47.09 E-value: 3.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 20 LNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGRVEFKGKNlLELAAEDRAGEGIFMAFQYPveipgvsnqffl 99
Cdd:PRK15112 32 LSFTLREGQTLAIIGENGSGKSTLAKMLAGM--IEPTSGELLIDDHP-LHFGDYSYRSQRIRMIFQDP------------ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 100 QTALNAvRNYRGQ------------EALDRfdfqdlmEEKIKLLQMPEDLLTRSVNV---GFSGGEKKRNDILQMAVLEP 164
Cdd:PRK15112 97 STSLNP-RQRISQildfplrlntdlEPEQR-------EKQIIETLRQVGLLPDHASYyphMLAPGQKQRLGLARALILRP 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488998194 165 ELCILDESDSGLDidaLKIVSQGVNALRDGKR----AFIIVTHYQRILDYIKpDYVHVLYQGRIVKSG 228
Cdd:PRK15112 169 KVIIADEALASLD---MSMRSQLINLMLELQEkqgiSYIYVTQHLGMMKHIS-DQVLVMHQGEVVERG 232
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
17-67 |
3.59e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 47.23 E-value: 3.59e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 488998194 17 LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEVTGGRVEFKGKNL 67
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTYEGEIIFEGEEL 71
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-85 |
4.69e-06 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 46.72 E-value: 4.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 1 MLSIQDLH--VAVEDKAI--LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGRVEFKGKNLLELAAED-- 74
Cdd:PRK11153 1 MIELKNISkvFPQGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLE--RPTSGRVLVDGQDLTALSEKElr 78
|
90
....*....|.
gi 488998194 75 RAGEGIFMAFQ 85
Cdd:PRK11153 79 KARRQIGMIFQ 89
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
5-186 |
6.27e-06 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 46.13 E-value: 6.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 5 QDLHVAVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGRVEFKGKNLLELAAEDRAGEGIFMAF 84
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLS--RLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 85 QypVEIPG-VSNQfflqtALNAVRNYRGQEALDRFDFQDlmEEKI-KLLQMP--EDLLTRSVNVgFSGGEKKRNDILQMA 160
Cdd:PRK10253 89 N--ATTPGdITVQ-----ELVARGRYPHQPLFTRWRKED--EEAVtKAMQATgiTHLADQSVDT-LSGGQRQRAWIAMVL 158
|
170 180 190
....*....|....*....|....*....|
gi 488998194 161 VLEPELCILDESDSGLD----IDALKIVSQ 186
Cdd:PRK10253 159 AQETAIMLLDEPTTWLDishqIDLLELLSE 188
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
13-209 |
7.49e-06 |
|
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: 46.47 E-value: 7.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 13 DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGReDYEVTGgrvefkgknllelaaEDRAGEGIFMAF--QYPvei 90
Cdd:TIGR03719 17 KKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV-DKDFNG---------------EARPQPGIKVGYlpQEP--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 91 pgvsnqfflqtALNAVRNYRG---------QEALDRF------------DFQDLMEEKIKL---------------LQMP 134
Cdd:TIGR03719 78 -----------QLDPTKTVREnveegvaeiKDALDRFneisakyaepdaDFDKLAAEQAELqeiidaadawdldsqLEIA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 135 EDLL-----TRSVNVgFSGGEKKRNDILQMAVLEPELCILDESDSGLDIDAlkiVSQGVNALRDGKRAFIIVTHYQRILD 209
Cdd:TIGR03719 147 MDALrcppwDADVTK-LSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES---VAWLERHLQEYPGTVVAVTHDRYFLD 222
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
12-203 |
7.56e-06 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 46.64 E-value: 7.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 12 EDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLaGREDyEVTGGRVEFKGKNLLELAAEDRAG---EGIFMAFQ--- 85
Cdd:PRK10535 19 EQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNIL-GCLD-KPTSGTYRVAGQDVATLDADALAQlrrEHFGFIFQryh 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 86 --------YPVEIPGVsnqfFLQTALNAvRNYRGQEALDRFDFQDLMEEKikllqmPEDLltrsvnvgfSGGEKKRNDIL 157
Cdd:PRK10535 97 llshltaaQNVEVPAV----YAGLERKQ-RLLRAQELLQRLGLEDRVEYQ------PSQL---------SGGQQQRVSIA 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488998194 158 QMAVLEPELCILDESDSGLDIDALKIVSQGVNALRDGKRAFIIVTH 203
Cdd:PRK10535 157 RALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTH 202
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
11-229 |
8.95e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 46.70 E-value: 8.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 11 VEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGRVefkgknlleLAAEdragegifmAFQYpvei 90
Cdd:PTZ00243 670 LEPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLS--QFEISEGRV---------WAER---------SIAY---- 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 91 pgVSNQFFLQTAlnAVRN----YRGQEALDRFDFQDLMEEKIKLLQMPEDLLT----RSVNVgfSGGEKKRNDILQMAVL 162
Cdd:PTZ00243 726 --VPQQAWIMNA--TVRGnilfFDEEDAARLADAVRVSQLEADLAQLGGGLETeigeKGVNL--SGGQKARVSLARAVYA 799
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488998194 163 EPELCILDESDSGLDIDALKIVSQGV--NALRDGKRafIIVTHYQRILDyiKPDYVHVLYQGRIVKSGD 229
Cdd:PTZ00243 800 NRDVYLLDDPLSALDAHVGERVVEECflGALAGKTR--VLATHQVHVVP--RADYVVALGDGRVEFSGS 864
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2-171 |
1.12e-05 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 46.12 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 2 LSIQDLHVAVEDKAILRG-LNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGRVEFKGKnllELAAEDRAgegi 80
Cdd:PRK10522 323 LELRNVTFAYQDNGFSVGpINLTIKRGELLFLIGGNGSGKSTLAMLLTGL--YQPQSGEILLDGK---PVTAEQPE---- 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 81 fmafQYPVEIPGVSNQFFLQTALnavRNYRGQEALDrfdfqDLMEEKIKLLQMPEDLLT---RSVNVGFSGGEKKRNDIL 157
Cdd:PRK10522 394 ----DYRKLFSAVFTDFHLFDQL---LGPEGKPANP-----ALVEKWLERLKMAHKLELedgRISNLKLSKGQKKRLALL 461
|
170
....*....|....*
gi 488998194 158 qMAVLEP-ELCILDE 171
Cdd:PRK10522 462 -LALAEErDILLLDE 475
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
23-211 |
1.22e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 45.96 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 23 EVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGRVEFKGKnllelaaedragegifMAF--QYPVEIPGVSNQFFLQ 100
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVL--KPDEGEVDPELK----------------ISYkpQYIKPDYDGTVEDLLR 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 101 TALNAVR-NYRGQEALDRFDFQDLMEEKIKLLqmpedlltrsvnvgfSGGEKKRNDILQMAVLEPELCILDESDSGLDid 179
Cdd:PRK13409 423 SITDDLGsSYYKSEIIKPLQLERLLDKNVKDL---------------SGGELQRVAIAACLSRDADLYLLDEPSAHLD-- 485
|
170 180 190
....*....|....*....|....*....|....*....
gi 488998194 180 alkiVSQGVNALRDGKR-------AFIIVTHYQRILDYI 211
Cdd:PRK13409 486 ----VEQRLAVAKAIRRiaeereaTALVVDHDIYMIDYI 520
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
13-248 |
1.55e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 45.55 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 13 DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGRVEF-KGKNLLELAAED----RAGEGifmAFQYP 87
Cdd:PRK10636 324 DRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAG--ELAPVSGEIGLaKGIKLGYFAQHQleflRADES---PLQHL 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 88 VEI-PGVSNQfflqtalnAVRNYRGQealdrFDFQDlmeekikllqmpeDLLTrSVNVGFSGGEKKRNDILQMAVLEPEL 166
Cdd:PRK10636 399 ARLaPQELEQ--------KLRDYLGG-----FGFQG-------------DKVT-EETRRFSGGEKARLVLALIVWQRPNL 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 167 CILDESDSGLDIDALKIVSQgvnALRDGKRAFIIVTHYQRILDYIKPDyVHVLYQGRI-VKSGDFSLVKQleeqgygWLT 245
Cdd:PRK10636 452 LLLDEPTNHLDLDMRQALTE---ALIDFEGALVVVSHDRHLLRSTTDD-LYLVHDGKVePFDGDLEDYQQ-------WLS 520
|
...
gi 488998194 246 EQQ 248
Cdd:PRK10636 521 DVQ 523
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
14-66 |
1.64e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 45.38 E-value: 1.64e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 488998194 14 KAiLRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGRVEFKGKN 66
Cdd:PRK10762 18 KA-LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGI--YTRDAGSILYLGKE 67
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
14-87 |
1.72e-05 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 45.18 E-value: 1.72e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488998194 14 KAILRgLNLEVRPGEVHAIMGPNGSGKSTLSATLAG--REDYEVTGGRVEFKGKNLLELAAEDR---AGEGIFMAFQYP 87
Cdd:PRK15093 21 KAVDR-VSMTLTEGEIRGLVGESGSGKSLIAKAICGvtKDNWRVTADRMRFDDIDLLRLSPRERrklVGHNVSMIFQEP 98
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
21-236 |
2.66e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 44.62 E-value: 2.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 21 NLEVRPGEVHAIMGPNGSGKSTLSATLAGrEDYEVTGGRV--------------------EFKGKNlLELAAEDRAGEGI 80
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAG-ELPLLSGERQsqfshitrlsfeqlqklvsdEWQRNN-TDMLSPGEDDTGR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 81 FMAfqypveipgvsnqfflQTALNAVR-NYRGQEALDRFDFQDLMEEKIKLLqmpedlltrsvnvgfSGGEKKRNDILQM 159
Cdd:PRK10938 101 TTA----------------EIIQDEVKdPARCEQLAQQFGITALLDRRFKYL---------------STGETRKTLLCQA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 160 AVLEPELCILDESDSGLDIDALKIVSQGVNALRDGKRAFI-IVTHYQRILDYIkpDYVHVLYQGRIVKSGDF------SL 232
Cdd:PRK10938 150 LMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVlVLNRFDEIPDFV--QFAGVLADCTLAETGEReeilqqAL 227
|
....
gi 488998194 233 VKQL 236
Cdd:PRK10938 228 VAQL 231
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
23-211 |
3.06e-05 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 44.78 E-value: 3.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 23 EVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGRVEFKGKnllelaaedragegifMAF--QYPVEIPGVSNQFFLQ 100
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVL--KPDEGEVDEDLK----------------ISYkpQYISPDYDGTVEEFLR 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 101 TALNavrnyrgqealDRFDFQDLMEEKIKLLQMpEDLLTRSVNvGFSGGEKKRNDILQMAVLEPELCILDESDSGLDida 180
Cdd:COG1245 424 SANT-----------DDFGSSYYKTEIIKPLGL-EKLLDKNVK-DLSGGELQRVAIAACLSRDADLYLLDEPSAHLD--- 487
|
170 180 190
....*....|....*....|....*....|....*...
gi 488998194 181 lkiVSQGVNA-------LRDGKRAFIIVTHYQRILDYI 211
Cdd:COG1245 488 ---VEQRLAVakairrfAENRGKTAMVVDHDIYLIDYI 522
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-225 |
6.06e-05 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 42.94 E-value: 6.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 1 MLSIQDLHVAVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGRVEFKGKNLLELAAEDRAGEGI 80
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCG--DPRATSGRIVFDGKDITDWQTAKIMREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 81 FMafqypveIPGVSNQFFLQTALNAVRnyRGQEALDRFDFQDLMEEKIKLLqmPEDLLTRSVNVG-FSGGEKKRNDILQM 159
Cdd:PRK11614 83 AI-------VPEGRRVFSRMTVEENLA--MGGFFAERDQFQERIKWVYELF--PRLHERRIQRAGtMSGGEQQMLAIGRA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488998194 160 AVLEPELCILDESDSGLDIDALKIVSQGVNALR-DGKRAFIIVTHYQRILDYikPDYVHVLYQGRIV 225
Cdd:PRK11614 152 LMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLReQGMTIFLVEQNANQALKL--ADRGYVLENGHVV 216
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-177 |
6.08e-05 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 43.22 E-value: 6.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 1 MLSIQDLHVAVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEvtGGRVEFKGKNLLELAAED--RAGE 78
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPD--HGEILFDGENIPAMSRSRlyTVRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 79 GIFMAFQypveipgvSNQFFlqTALNAVRNYRgqealdrfdfQDLMEEKikllQMPEDLLTRSV-----NVG-------- 145
Cdd:PRK11831 85 RMSMLFQ--------SGALF--TDMNVFDNVA----------YPLREHT----QLPAPLLHSTVmmkleAVGlrgaaklm 140
|
170 180 190
....*....|....*....|....*....|....*
gi 488998194 146 ---FSGGEKKRNDILQMAVLEPELCILDESDSGLD 177
Cdd:PRK11831 141 pseLSGGMARRAALARAIALEPDLIMFDEPFVGQD 175
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
20-228 |
7.93e-05 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 43.17 E-value: 7.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 20 LNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGRVEFKGKNLLELAAEDRageGIFMAFQYPVEIPGVS---NQ 96
Cdd:PRK11432 25 LNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLE--KPTEGQIFIDGEDVTHRSIQQR---DICMVFQSYALFPHMSlgeNV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 97 FF---LQTALNAVRNYRGQEALDRFD---FQDLMEEKIkllqmpedlltrsvnvgfSGGEKKRNDILQMAVLEPELCILD 170
Cdd:PRK11432 100 GYglkMLGVPKEERKQRVKEALELVDlagFEDRYVDQI------------------SGGQQQRVALARALILKPKVLLFD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488998194 171 ESDSGLDIDALKIVSQGVnalRDGKRAFII----VTHYQRiLDYIKPDYVHVLYQGRIVKSG 228
Cdd:PRK11432 162 EPLSNLDANLRRSMREKI---RELQQQFNItslyVTHDQS-EAFAVSDTVIVMNKGKIMQIG 219
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
14-228 |
1.18e-04 |
|
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: 42.29 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 14 KAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGRVEFKGKNLLElaaedragegifmafQYPVE---- 89
Cdd:cd03295 14 KKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMI--NRLIEPTSGEIFIDGEDIRE---------------QDPVElrrk 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 90 IPGVSNQFFLQTALNAVRN---------YRGQEALDRFDfqdlmeEKIKLLQMPEDLLTRSVNVGFSGGEKKRNDILQMA 160
Cdd:cd03295 77 IGYVIQQIGLFPHMTVEENialvpkllkWPKEKIRERAD------ELLALVGLDPAEFADRYPHELSGGQQQRVGVARAL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 161 VLEPELCILDESDSGLD-IDALKIVSQGVNALRDGKRAFIIVTHyqRILDYIK-PDYVHVLYQGRIVKSG 228
Cdd:cd03295 151 AADPPLLLMDEPFGALDpITRDQLQEEFKRLQQELGKTIVFVTH--DIDEAFRlADRIAIMKNGEIVQVG 218
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
20-76 |
1.71e-04 |
|
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: 42.48 E-value: 1.71e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 488998194 20 LNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGRVEFKGKnllELAAEDRA 76
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGL--YRPESGEILLDGQ---PVTADNRE 402
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
144-209 |
1.90e-04 |
|
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: 40.81 E-value: 1.90e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 144 VGFSGGEKKRND---ILQMAVLEPE-LCILDESDSGLDIDALKIVSQGVNALRDGKRAFIIVTHYQRILD 209
Cdd:cd03227 76 LQLSGGEKELSAlalILALASLKPRpLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPELAE 145
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-211 |
2.03e-04 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 42.23 E-value: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 2 LSIQDLHVAVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGRVEFkGKNlLELAAEDRAGEGIF 81
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQE--QPDSGTIEI-GET-VKLAYVDQSRDALD 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 82 MAFQYPVEIPGVSNQFFLQTALNAVRNYRGqealdRFDF--QDlMEEKIKLLqmpedlltrsvnvgfSGGEKKRndiLQM 159
Cdd:TIGR03719 399 PNKTVWEEISGGLDIIKLGKREIPSRAYVG-----RFNFkgSD-QQKKVGQL---------------SGGERNR---VHL 454
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488998194 160 AVLEPE---LCILDESDSGLDIDALKivsqgvnALRDGKRAF----IIVTHYQRILDYI 211
Cdd:TIGR03719 455 AKTLKSggnVLLLDEPTNDLDVETLR-------ALEEALLNFagcaVVISHDRWFLDRI 506
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
24-248 |
2.04e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 42.08 E-value: 2.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 24 VRPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGRVEFKGKNLL-----ELAAEDRA-------GEGIFMAFQYPVEIP 91
Cdd:PRK10636 24 INPGQKVGLVGKNGCGKSTLLALLKN--EISADGGSYTFPGNWQLawvnqETPALPQPaleyvidGDREYRQLEAQLHDA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 92 GVSNQFflqtalNAVRNYRGQ-EALDRFDFQDLMEEKIKLLQMPEDLLTRSVNvGFSGGEKKRNDILQMAVLEPELCILD 170
Cdd:PRK10636 102 NERNDG------HAIATIHGKlDAIDAWTIRSRAASLLHGLGFSNEQLERPVS-DFSGGWRMRLNLAQALICRSDLLLLD 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488998194 171 ESDSGLDIDALKIVSQGvnaLRDGKRAFIIVTHYQRILDYIKPDYVHVLYQGRIVKSGDFSlvkQLEEQGYGWLTEQQ 248
Cdd:PRK10636 175 EPTNHLDLDAVIWLEKW---LKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEYTGNYS---SFEVQRATRLAQQQ 246
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
14-228 |
2.22e-04 |
|
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: 41.33 E-value: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 14 KAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGRVEFKGKNLLELAAED-RAgegiFMAF--QYPVEI 90
Cdd:cd03244 17 PPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRL--VELSSGSILIDGVDISKIGLHDlRS----RISIipQDPVLF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 91 PGvsnqfflqtalnAVRnyrgqEALDRFD-FQD--LME--EKIKL----LQMPEDLLTRSVNVG--FSGGEK-------- 151
Cdd:cd03244 91 SG------------TIR-----SNLDPFGeYSDeeLWQalERVGLkefvESLPGGLDTVVEEGGenLSVGQRqllclara 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 152 --KRNDILqmavlepelcILDESDSGLDIDALKIVSQGV-NALRDgkRAFIIVTHyqR---ILDYikpDYVHVLYQGRIV 225
Cdd:cd03244 154 llRKSKIL----------VLDEATASVDPETDALIQKTIrEAFKD--CTVLTIAH--RldtIIDS---DRILVLDKGRVV 216
|
...
gi 488998194 226 KSG 228
Cdd:cd03244 217 EFD 219
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
17-188 |
2.38e-04 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 41.01 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 17 LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGRVEFKGKNLLELAAEDRA--GEGIFMAFQ--------- 85
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIE--RPSAGKIWFSGHDITRLKNREVPflRRQIGMIFQdhhllmdrt 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 86 ------YPVEIPGVSNQfflqtalnAVRNyRGQEALDrfdfqdlmeeKIKLLQMpedllTRSVNVGFSGGEKKRNDILQM 159
Cdd:PRK10908 96 vydnvaIPLIIAGASGD--------DIRR-RVSAALD----------KVGLLDK-----AKNFPIQLSGGEQQRVGIARA 151
|
170 180
....*....|....*....|....*....
gi 488998194 160 AVLEPELCILDESDSGLDiDALkivSQGV 188
Cdd:PRK10908 152 VVNKPAVLLADEPTGNLD-DAL---SEGI 176
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
21-49 |
2.65e-04 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 41.11 E-value: 2.65e-04
10 20
....*....|....*....|....*....
gi 488998194 21 NLEVRPGEVHAIMGPNGSGKSTLSATLAG 49
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAG 47
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
16-228 |
2.94e-04 |
|
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: 40.86 E-value: 2.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 16 ILRGLNLEVRPGEVHAIMGPNGSGKSTLsaTLAGREDYEVTGGRVEFKGKNLLELAAED-RAGEGIFMafQYPVEIPGvs 94
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTL--ILALFRFLEAEEGKIEIDGIDISTIPLEDlRSSLTIIP--QDPTLFSG-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 95 nqfflqtalnAVRNyrgqeALDRFDFQDlmEEKIKllqmpEDLLTRSVNVGFSGGEKKRNDILQMAVLEPELCILDESDS 174
Cdd:cd03369 97 ----------TIRS-----NLDPFDEYS--DEEIY-----GALRVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488998194 175 GLDIDALKIVSQGVNALRDGKRAFIIVTHYQRILDYikpDYVHVLYQGRIVKSG 228
Cdd:cd03369 155 SIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDY---DKILVMDAGEVKEYD 205
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
17-231 |
3.26e-04 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 41.23 E-value: 3.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 17 LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGredyeV---TGGRVEFKG----KNLLELAAEdragegIFMAFqypve 89
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTG-----IlvpTSGEVRVLGyvpfKRRKEFARR------IGVVF----- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 90 ipGVSNQ----------FFLQTALnavrnYRgqeaLDRFDFQDLMEEKIKLLQMpEDLLTRSVNVgFSGGEKKRNDILqM 159
Cdd:COG4586 102 --GQRSQlwwdlpaidsFRLLKAI-----YR----IPDAEYKKRLDELVELLDL-GELLDTPVRQ-LSLGQRMRCELA-A 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 160 AVL-EPELCILDESDSGLDidalkIVSQgvNALRD-------GKRAFIIVT-HY--------QRILdyikpdyvhVLYQG 222
Cdd:COG4586 168 ALLhRPKILFLDEPTIGLD-----VVSK--EAIREflkeynrERGTTILLTsHDmddiealcDRVI---------VIDHG 231
|
....*....
gi 488998194 223 RIVKSGDFS 231
Cdd:COG4586 232 RIIYDGSLE 240
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
136-216 |
3.38e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 41.55 E-value: 3.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 136 DLLTRSVNVGFSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVSQGVNALRDGK-RAFIIVTHYQRILDYIKPD 214
Cdd:PTZ00265 570 ETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNEnRITIIIAHRLSTIRYANTI 649
|
..
gi 488998194 215 YV 216
Cdd:PTZ00265 650 FV 651
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-43 |
3.53e-04 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 40.87 E-value: 3.53e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 488998194 1 MLSIQDLHVAVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTL 43
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTL 46
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
13-209 |
3.84e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 41.26 E-value: 3.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 13 DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDyevtggrvEFKGknllelaaEDRAGEGIFMAF--QYP--- 87
Cdd:PRK11819 19 KKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDK--------EFEG--------EARPAPGIKVGYlpQEPqld 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 88 --------VEiPGVSNQFFLQTALNAVRNyrgQEALDRFDFQDLMEEKIKL---------------LQMPEDLLtR---- 140
Cdd:PRK11819 83 pektvrenVE-EGVAEVKAALDRFNEIYA---AYAEPDADFDALAAEQGELqeiidaadawdldsqLEIAMDAL-Rcppw 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488998194 141 --SVNVgFSGGEKKRNDILQMAVLEPELCILDESDSGLDIDAlkiVSQGVNALRDGKRAFIIVTHYQRILD 209
Cdd:PRK11819 158 daKVTK-LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES---VAWLEQFLHDYPGTVVAVTHDRYFLD 224
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
143-219 |
4.35e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 41.17 E-value: 4.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 143 NVG-----FSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVSQGVNALRD-GKRAFIIVTHyqRILDYIKPDYV 216
Cdd:PTZ00265 1351 NVGpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkADKTIITIAH--RIASIKRSDKI 1428
|
...
gi 488998194 217 HVL 219
Cdd:PTZ00265 1429 VVF 1431
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
31-203 |
4.67e-04 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 40.33 E-value: 4.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 31 AIMGPNGSGKSTL--SATLA----GREDYEVTGGRVEFK-GKNLLELAAEDRAGEGIFMAFQYpveiPGVSNQFFLQTAL 103
Cdd:cd03279 32 LICGPTGAGKSTIldAITYAlygkTPRYGRQENLRSVFApGEDTAEVSFTFQLGGKKYRVERS----RGLDYDQFTRIVL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 104 NAvrnyrgQEALDRFdfqdlmeekikllqmpedlLTRSVNvGFSGGEKKRNDI-LQMAVLEP---------ELCILDESD 173
Cdd:cd03279 108 LP------QGEFDRF-------------------LARPVS-TLSGGETFLASLsLALALSEVlqnrggarlEALFIDEGF 161
|
170 180 190
....*....|....*....|....*....|
gi 488998194 174 SGLDIDALKIVSQGVNALRDGKRAFIIVTH 203
Cdd:cd03279 162 GTLDPEALEAVATALELIRTENRMVGVISH 191
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
2-85 |
8.47e-04 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 39.66 E-value: 8.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 2 LSIQDLHVAVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGRVeFKGKNLLELAAEDragegIF 81
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLE--TPSAGEL-LAGTAPLAEARED-----TR 84
|
....
gi 488998194 82 MAFQ 85
Cdd:PRK11247 85 LMFQ 88
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
18-180 |
1.05e-03 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 40.03 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 18 RGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGRVEFKGKNLLELAA------------EDRAGEGIFM--- 82
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLR--PARGGRIMLNGKEINALSTaqrlarglvylpEDRQSSGLYLdap 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 83 ----AFQYPVEIPGvsnqFFLQTALNAVRNYRGQEALDrfdfqdlmeekIKLLQMPEDLLTrsvnvgFSGGEKKRndILQ 158
Cdd:PRK15439 358 lawnVCALTHNRRG----FWIKPARENAVLERYRRALN-----------IKFNHAEQAART------LSGGNQQK--VLI 414
|
170 180
....*....|....*....|....
gi 488998194 159 MAVLE--PELCILDESDSGLDIDA 180
Cdd:PRK15439 415 AKCLEasPQLLIVDEPTRGVDVSA 438
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
17-231 |
1.55e-03 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 39.22 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 17 LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGRVEFKGKNLLE------LAA------EDRAGEGIFMAF 84
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYG--ALPRTSGYVTLDGHEVVTrspqdgLANgivyisEDRKRDGLVLGM 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 85 QypveipgVSNQFFLqTALNAVRNYRG-------QEALDrfDFQDL-------MEEKIKLLqmpedlltrsvnvgfSGGE 150
Cdd:PRK10762 346 S-------VKENMSL-TALRYFSRAGGslkhadeQQAVS--DFIRLfniktpsMEQAIGLL---------------SGGN 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 151 KKRNDILQMAVLEPELCILDESDSGLDIDALKIVSQGVNALRDGKRAFIIVTH--------YQRILdyikpdyvhVLYQG 222
Cdd:PRK10762 401 QQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSempevlgmSDRIL---------VMHEG 471
|
....*....
gi 488998194 223 RIvkSGDFS 231
Cdd:PRK10762 472 RI--SGEFT 478
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
24-230 |
1.73e-03 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 39.04 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 24 VRPGEVHAIMGPNGSGKSTLSATLAGRedYE-VTGGRVEFKGKNL------------LELAAEDRAGEGIfmafqypVEI 90
Cdd:TIGR02633 283 LRRGEILGVAGLVGAGRTELVQALFGA--YPgKFEGNVFINGKPVdirnpaqairagIAMVPEDRKRHGI-------VPI 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 91 PGVSNQFflqtALNAVRNYRGQEALDRFDFQDLMEEKIKLLQM----PEDLLTRsvnvgFSGGEKKRNDILQMAVLEPEL 166
Cdd:TIGR02633 354 LGVGKNI----TLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVktasPFLPIGR-----LSGGNQQKAVLAKMLLTNPRV 424
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488998194 167 CILDESDSGLDIDALKIVSQGVNAL-RDGKRAFIIVTHYQRILDYikPDYVHVLYQGRIvkSGDF 230
Cdd:TIGR02633 425 LILDEPTRGVDVGAKYEIYKLINQLaQEGVAIIVVSSELAEVLGL--SDRVLVIGEGKL--KGDF 485
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
4-71 |
2.18e-03 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 38.78 E-value: 2.18e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488998194 4 IQDLHVAVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGRVEFKGKnlLELA 71
Cdd:PRK11147 322 MENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLG--QLQADSGRIHCGTK--LEVA 385
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
110-177 |
2.22e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 38.95 E-value: 2.22e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488998194 110 RGQEALDRFDFQDLMEekikllQMPEDL-LtrsvnvgfsgGEKKRndiLQMAVL---EPELCILDESDSGLD 177
Cdd:NF033858 377 RVAEMLERFDLADVAD------ALPDSLpL----------GIRQR---LSLAVAvihKPELLILDEPTSGVD 429
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
5-51 |
3.36e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 38.18 E-value: 3.36e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 488998194 5 QDLHVAVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRE 51
Cdd:PRK11819 328 ENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQE 374
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
17-64 |
3.80e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 38.33 E-value: 3.80e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 488998194 17 LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGredyeVT---GGRVEFKG 64
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAG-----VTmpnKGTVDIKG 85
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
22-43 |
3.98e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 34.88 E-value: 3.98e-03
|
| NadR3 |
COG3172 |
Nicotinamide riboside kinase [Coenzyme transport and metabolism]; Nicotinamide riboside kinase ... |
22-81 |
5.04e-03 |
|
Nicotinamide riboside kinase [Coenzyme transport and metabolism]; Nicotinamide riboside kinase is part of the Pathway/BioSystem: NAD biosynthesis
Pssm-ID: 442405 [Multi-domain] Cd Length: 178 Bit Score: 36.72 E-value: 5.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 22 LEVRPGEVH--AIMGPNGSGKSTLSATLA-----------GREDYEVTGGRVEF-------KGKNLLELAAEDRAGEGIF 81
Cdd:COG3172 1 PEVRPSFVKkiVLLGAESTGKTTLARALAahyntpwvpeyGREYLEEKGRALTYddllaiaRGQLALEDAAAKRANKLLF 80
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
21-43 |
6.55e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 37.22 E-value: 6.55e-03
|
| PRK06547 |
PRK06547 |
hypothetical protein; Provisional |
32-55 |
6.75e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 235825 Cd Length: 172 Bit Score: 36.26 E-value: 6.75e-03
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
146-239 |
7.70e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 37.15 E-value: 7.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 146 FSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVSqgvNALRDGKRAFIIVTHYQRILDYIKPDYVHVLYQGRIV 225
Cdd:PLN03073 345 FSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLE---TYLLKWPKTFIVVSHAREFLNTVVTDILHLHGQKLVT 421
|
90
....*....|....
gi 488998194 226 KSGDFSLVKQLEEQ 239
Cdd:PLN03073 422 YKGDYDTFERTREE 435
|
|
| RepA |
COG3598 |
RecA-family ATPase [Replication, recombination and repair]; |
24-159 |
8.78e-03 |
|
RecA-family ATPase [Replication, recombination and repair];
Pssm-ID: 442817 [Multi-domain] Cd Length: 313 Bit Score: 36.80 E-value: 8.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488998194 24 VRPGEVHAIMGPNGSGKSTLSATLA-----GRE--DYEVTGGRVefkgknlLELAAEDRAGE------GIFMAFQYPVEI 90
Cdd:COG3598 10 LPEGGVTLLAGPPGTGKSFLALQLAaavaaGGPwlGRRVPPGKV-------LYLAAEDDRGElrrrlkALGADLGLPFAD 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488998194 91 pgVSNQFFLQTALNAVRNYRGQEALDRFdfqdLMEEKIKLLQMpeDLLTRSvnvgFSGGEKKRNDILQM 159
Cdd:COG3598 83 --LDGRLRLLSLAGDLDDTDDLEALERA----IEEEGPDLVVI--DPLARV----FGGDENDAEEMRAF 139
|
|
| |
