|
Name |
Accession |
Description |
Interval |
E-value |
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-246 |
1.25e-112 |
|
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: 323.92 E-value: 1.25e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 1 MFTLSGVEMVRGGRRILAIEQLNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLAKAVAFL 80
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 81 PQKLPASAGLTVRELVRLGRFPWRGALGFWRQQDADIIRAAMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLI 160
Cdd:COG1120 81 PQEPPAPFGLTVRELVALGRYPHLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 161 LDEPTSALDVQHQYQLMALLAELNQKQGCGIIVILHDLNLALRYATHIVALKQGRIAFDGPATTLADEQRLSDLYQTPIT 240
Cdd:COG1120 161 LDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLTPELLEEVYGVEAR 240
|
....*.
gi 992343279 241 LIDHPH 246
Cdd:COG1120 241 VIEDPV 246
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
2-245 |
2.09e-84 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 252.79 E-value: 2.09e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 2 FTLSGVEMVRGGRRILAIEQLNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLAKAVAFLP 81
Cdd:PRK10575 12 FALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 82 QKLPASAGLTVRELVRLGRFPWRGALGFWRQQDADIIRAAMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLIL 161
Cdd:PRK10575 92 QQLPAAEGMTVRELVAIGRYPWHGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 162 DEPTSALDVQHQYQLMALLAELNQKQGCGIIVILHDLNLALRYATHIVALKQGRIAFDGPATTLADEQRLSDLYQTPITL 241
Cdd:PRK10575 172 DEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETLEQIYGIPMGI 251
|
....
gi 992343279 242 IDHP 245
Cdd:PRK10575 252 LPHP 255
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-246 |
4.29e-80 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 241.56 E-value: 4.29e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 1 MFTLSGVEMVRGGRRILAIEQLNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLAKAVAFL 80
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 81 PQKLPASAGLTVRELVRLGRFPWRGAlgfwRQQDADIIRAAMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQ------ 154
Cdd:COG4559 81 PQHSSLAFPFTVEEVVALGRAPHGSS----AAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAQlwepvd 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 155 -ESPVLILDEPTSALDVQHQYQLMALLAELNQkQGCGIIVILHDLNLALRYATHIVALKQGRIAFDGPATTLADEQRLSD 233
Cdd:COG4559 157 gGPRWLFLDEPTSALDLAHQHAVLRLARQLAR-RGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLTDELLER 235
|
250
....*....|...
gi 992343279 234 LYQTPITLIDHPH 246
Cdd:COG4559 236 VYGADLRVLAHPE 248
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-245 |
5.37e-78 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 236.21 E-value: 5.37e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 1 MFTLSGVEMVRGGRRILAIEQLNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLAKAVAFL 80
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 81 PQKLPASAGLTVRELVRLGRFPWRGAlgfwRQQDADIIRAAMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQ------ 154
Cdd:PRK13548 82 PQHSSLSFPFTVEEVVAMGRAPHGLS----RAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQlwepdg 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 155 ESPVLILDEPTSALDVQHQYQLMALLAELNQKQGCGIIVILHDLNLALRYATHIVALKQGRIAFDGPATTLADEQRLSDL 234
Cdd:PRK13548 158 PPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVLTPETLRRV 237
|
250
....*....|.
gi 992343279 235 YQTPITLIDHP 245
Cdd:PRK13548 238 YGADVLVQPHP 248
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-246 |
2.87e-77 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 234.21 E-value: 2.87e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 1 MFTLSGVEMVRGGRRILAIEQLNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLAKAVAFL 80
Cdd:COG4604 1 MIEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 81 PQKLPASAGLTVRELVRLGRFPW-RGALGfwrQQDADIIRAAMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVL 159
Cdd:COG4604 81 RQENHINSRLTVRELVAFGRFPYsKGRLT---AEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 160 ILDEPTSALDVQHQYQLMALLAELNQKQGCGIIVILHDLNLALRYATHIVALKQGRIAFDGPATTLADEQRLSDLYQTPI 239
Cdd:COG4604 158 LLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEIITPEVLSDIYDTDI 237
|
....*..
gi 992343279 240 TLIDHPH 246
Cdd:COG4604 238 EVEEIDG 244
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
12-220 |
3.16e-75 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 229.13 E-value: 3.16e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 12 GGRRILAIEQLNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLAKAVAFLPQKLPASAGLT 91
Cdd:PRK11231 13 GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTPEGIT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 92 VRELVRLGRFPWrgaLGFW---RQQDADIIRAAMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSAL 168
Cdd:PRK11231 93 VRELVAYGRSPW---LSLWgrlSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 992343279 169 DVQHQYQLMALLAELNQkQGCGIIVILHDLNLALRYATHIVALKQGRIAFDG 220
Cdd:PRK11231 170 DINHQVELMRLMRELNT-QGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQG 220
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
3-220 |
4.14e-71 |
|
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: 216.15 E-value: 4.14e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 3 TLSGVEMVRGGRRILAIEQLNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLAKAVAFLPQ 82
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 83 klpasagltvrelvrlgrfpwrgalgfwrqqdadiiraAMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILD 162
Cdd:cd03214 81 --------------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLD 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 992343279 163 EPTSALDVQHQYQLMALLAELNQKQGCGIIVILHDLNLALRYATHIVALKQGRIAFDG 220
Cdd:cd03214 123 EPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-244 |
1.95e-69 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 214.18 E-value: 1.95e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 1 MFTLSGVEMVRGGRRILaiEQLN--IPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKslakaVA 78
Cdd:COG1121 6 AIELENLTVSYGGRPVL--EDVSltIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRR-----IG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 79 FLPQKLPASAG--LTVRELVRLGRFPWRGALGFWRQQDADIIRAAMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQES 156
Cdd:COG1121 79 YVPQRAEVDWDfpITVRDVVLMGRYGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 157 PVLILDEPTSALDVQHQYQLMALLAELNQkQGCGIIVILHDLNLALRYATHIVALKQGRIAFDGPATTLADEqRLSDLYQ 236
Cdd:COG1121 159 DLLLLDEPFAGVDAATEEALYELLRELRR-EGKTILVVTHDLGAVREYFDRVLLLNRGLVAHGPPEEVLTPE-NLSRAYG 236
|
....*...
gi 992343279 237 TPITLIDH 244
Cdd:COG1121 237 GPVALLAH 244
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
22-247 |
4.73e-67 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 208.69 E-value: 4.73e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 22 LNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLAKAVAFLPQKLPASAGLTVRELVRLGRF 101
Cdd:PRK10253 28 VEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDITVQELVARGRY 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 102 PWRGALGFWRQQDADIIRAAMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSALDVQHQYQLMALLA 181
Cdd:PRK10253 108 PHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLS 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 992343279 182 ELNQKQGCGIIVILHDLNLALRYATHIVALKQGRIAFDGPATTLADEQRLSDLYQTPITLIDHPHA 247
Cdd:PRK10253 188 ELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERIYGLRCMIIDDPVA 253
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
12-219 |
1.71e-57 |
|
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: 182.35 E-value: 1.71e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 12 GGRRILAIEQLNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKslakaVAFLPQKLPASAG-- 89
Cdd:cd03235 10 GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKR-----IGYVPQRRSIDRDfp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 90 LTVRELVRLGRFPWRGALGFWRQQDADIIRAAMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSALD 169
Cdd:cd03235 85 ISVRDVVLMGLYGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 992343279 170 VQHQYQLMALLAELNQKqGCGIIVILHDLNLALRYATHIVALKQGRIAFD 219
Cdd:cd03235 165 PKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLLNRTVVASG 213
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
12-235 |
3.87e-56 |
|
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: 180.07 E-value: 3.87e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 12 GGRRILAIEQLNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLAKA---VAFLPQKLPASA 88
Cdd:cd03256 12 NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLrrqIGMIFQQFNLIE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 89 GLTVRELVRLGRFP----WRGALGFWRQQDADIIRAAMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEP 164
Cdd:cd03256 92 RLSVLENVLSGRLGrrstWRSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQPKLILADEP 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 992343279 165 TSALDVQHQYQLMALLAELNQKQGCGIIVILHDLNLALRYATHIVALKQGRIAFDGPATTLaDEQRLSDLY 235
Cdd:cd03256 172 VASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL-TDEVLDEIY 241
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-221 |
4.26e-54 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 179.65 E-value: 4.26e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 1 MFTLSGVEMVRGGRRILAIEQLNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLAKAVAFL 80
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 81 PQKLPASAGLTVRELVRLGRFPWRGALGFWRQQDADIIRAAMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLI 160
Cdd:PRK09536 83 PQDTSLSFEFDVRQVVEMGRTPHRSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 992343279 161 LDEPTSALDVQHQYQLMALLAELNQkQGCGIIVILHDLNLALRYATHIVALKQGRIAFDGP 221
Cdd:PRK09536 163 LDEPTASLDINHQVRTLELVRRLVD-DGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGP 222
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
22-231 |
9.88e-51 |
|
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: 165.58 E-value: 9.88e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 22 LNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLAKAVAFLPQKlPAS--AGLTVRELVRLG 99
Cdd:COG1122 22 LSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLVFQN-PDDqlFAPTVEEDVAFG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 100 -RfpwrgALGFWRQQDADIIRAAMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSALDVQHQYQLMA 178
Cdd:COG1122 101 pE-----NLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 992343279 179 LLAELNQkQGCGIIVILHDLNLALRYATHIVALKQGRIAFDG-PATTLADEQRL 231
Cdd:COG1122 176 LLKRLNK-EGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGtPREVFSDYELL 228
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
22-215 |
1.10e-48 |
|
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: 159.94 E-value: 1.10e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 22 LNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLAKAVAFLPQKlPAS--AGLTVRELVRLG 99
Cdd:cd03225 22 LTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVFQN-PDDqfFGPTVEEEVAFG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 100 RfpwrGALGFWRQQDADIIRAAMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSALDVQHQYQLMAL 179
Cdd:cd03225 101 L----ENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLEL 176
|
170 180 190
....*....|....*....|....*....|....*.
gi 992343279 180 LAELNQkQGCGIIVILHDLNLALRYATHIVALKQGR 215
Cdd:cd03225 177 LKKLKA-EGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
10-222 |
1.39e-45 |
|
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: 159.68 E-value: 1.39e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 10 VRGGRRILAIEQ--LNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKS---LAKAVAFLPQKl 84
Cdd:COG1123 272 VRGKGGVRAVDDvsLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSlreLRRRVQMVFQD- 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 85 PASA---GLTVRELVRlgrFPWRGALGFWRQQDADIIRAAMDKTGVSA-FADTFVDELSGGERQRAWVAMLLAQESPVLI 160
Cdd:COG1123 351 PYSSlnpRMTVGDIIA---EPLRLHGLLSRAERRERVAELLERVGLPPdLADRYPHELSGGQRQRVAIARALALEPKLLI 427
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 992343279 161 LDEPTSALDVQHQYQLMALLAELNQKQGCGIIVILHDLNLALRYATHIVALKQGRIAFDGPA 222
Cdd:COG1123 428 LDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPT 489
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
3-235 |
1.49e-45 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 152.53 E-value: 1.49e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 3 TLSGVEMVRGGRRILAIEQLNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLAKaVAFLPQ 82
Cdd:COG1131 2 EVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRR-IGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 83 KLPASAGLTVRELVRLgrfpWRGALGFWRQQDADIIRAAMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILD 162
Cdd:COG1131 81 EPALYPDLTVRENLRF----FARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 992343279 163 EPTSALDVQHQYQLMALLAELNqKQGCGIIVILHDLNLALRYATHIVALKQGRIAFDGPATTLAdEQRLSDLY 235
Cdd:COG1131 157 EPTSGLDPEARRELWELLRELA-AEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELK-ARLLEDVF 227
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
22-216 |
1.52e-45 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 152.12 E-value: 1.52e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 22 LNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLAK----AVAFLPQK---LPasaGLTVRE 94
Cdd:COG1136 29 LSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELARlrrrHIGFVFQFfnlLP---ELTALE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 95 LVRLgrfPWRGAlGFWRQQDADIIRAAMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSALDVQHQY 174
Cdd:COG1136 106 NVAL---PLLLA-GVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGE 181
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 992343279 175 QLMALLAELNQKQGCGIIVILHDLNLAlRYATHIVALKQGRI 216
Cdd:COG1136 182 EVLELLRELNRELGTTIVMVTHDPELA-ARADRVIRLRDGRI 222
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
12-211 |
7.01e-43 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 144.30 E-value: 7.01e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 12 GGRRILAIEQLNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVwlndapltslsSKSLAKAVAFLPQK--LPASAG 89
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV-----------RRAGGARVAYVPQRseVPDSLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 90 LTVRELVRLGRFPWRGALGFWRQQDADIIRAAMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSALD 169
Cdd:NF040873 72 LTVRDLVAMGRWARRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLD 151
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 992343279 170 VQHQYQLMALLAELnQKQGCGIIVILHDLNLALRyATHIVAL 211
Cdd:NF040873 152 AESRERIIALLAEE-HARGATVVVVTHDLELVRR-ADPCVLL 191
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
11-216 |
5.49e-42 |
|
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: 143.01 E-value: 5.49e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 11 RGGRRILAIEQ--LNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLAKA----VAFLPQK- 83
Cdd:cd03255 12 GGGEKVQALKGvsLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFrrrhIGFVFQSf 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 84 --LPasaGLTVRELVRLGrFPWRGALGFWRQQDAdiiRAAMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLIL 161
Cdd:cd03255 92 nlLP---DLTALENVELP-LLLAGVPKKERRERA---EELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPKIILA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 992343279 162 DEPTSALDVQHQYQLMALLAELNQKQGCGIIVILHDLNLAlRYATHIVALKQGRI 216
Cdd:cd03255 165 DEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELA-EYADRIIELRDGKI 218
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1-248 |
6.07e-42 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 144.58 E-value: 6.07e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 1 MFTLSGVEMVRGGRRILAIEQLNIPTNELTVVLGHNGSGKSTLVSLLSGQ----QAPD----TGSVWLNDAPLTSLSSKS 72
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDltggGAPRgarvTGDVTLNGEPLAAIDAPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 73 LAKAVAFLPQKLPASAGLTVRELVRLGRFPWRGALGFWRQQDADIIRAAMDKTGVSAFADTFVDELSGGERQRAWVAMLL 152
Cdd:PRK13547 81 LARLRAVLPQAAQPAFAFSAREIVLLGRYPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 153 AQESP---------VLILDEPTSALDVQHQYQLMALLAELNQKQGCGIIVILHDLNLALRYATHIVALKQGRIAFDGPAT 223
Cdd:PRK13547 161 AQLWPphdaaqpprYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPA 240
|
250 260
....*....|....*....|....*
gi 992343279 224 TLADEQRLSDLYQTPITLIDHPHAV 248
Cdd:PRK13547 241 DVLTPAHIARCYGFAVRLVDAGDGV 265
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-242 |
2.36e-41 |
|
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: 141.92 E-value: 2.36e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 1 MFTLSGVEMVRGGRRILAIEQLNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLaKAVAFL 80
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREAR-RQIGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 81 PQKLPASAGLTVRELVR-LGRFpwrgaLGFWRQQDADIIRAAMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVL 159
Cdd:COG4555 80 PDERGLYDRLTVRENIRyFAEL-----YGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 160 ILDEPTSALDVQHQYQLMALLAELNqKQGCGIIVILHDLNLALRYATHIVALKQGRIAFDGPATTLADEQRLSDLYQTPI 239
Cdd:COG4555 155 LLDEPTNGLDVMARRLLREILRALK-KEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEENLEDAFV 233
|
...
gi 992343279 240 TLI 242
Cdd:COG4555 234 ALI 236
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
7-232 |
1.12e-40 |
|
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: 146.59 E-value: 1.12e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 7 VEMVRGGRRILAIEQLNIPTNELTVVLGHNGSGKSTLVSLLSG---QQAPDTGSVWLNDAPLTSLSSKSLAKAVAFLPQK 83
Cdd:COG1123 12 VRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGllpHGGRISGEVLLDGRDLLELSEALRGRRIGMVFQD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 84 lPASA--GLTVRELVRlgrFPWRgALGFWRQQDADIIRAAMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLIL 161
Cdd:COG1123 92 -PMTQlnPVTVGDQIA---EALE-NLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 992343279 162 DEPTSALDVQHQYQLMALLAELNQKQGCGIIVILHDLNLALRYATHIVALKQGRIAFDGPATT-LADEQRLS 232
Cdd:COG1123 167 DEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEiLAAPQALA 238
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-208 |
1.58e-40 |
|
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: 138.77 E-value: 1.58e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 1 MFTLSGVEMVRGGRRILAIEQLNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSkSLAKAVAFL 80
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARE-DYRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 81 PQKLPASAGLTVRELVRLgrfpWRGALGFwrQQDADIIRAAMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLI 160
Cdd:COG4133 81 GHADGLKPELTVRENLRF----WAALYGL--RADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 992343279 161 LDEPTSALDVQHQYQLMALLAELNQKQGCgIIVILHDLnLALRYATHI 208
Cdd:COG4133 155 LDEPFTALDAAGVALLAELIAAHLARGGA-VLLTTHQP-LELAAARVL 200
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
22-227 |
4.08e-40 |
|
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: 138.78 E-value: 4.08e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 22 LNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLAKAVAFLPQKLPASA--GLTVRELVRLg 99
Cdd:COG1124 26 LEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMVFQDPYASLhpRHTVDRILAE- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 100 rfPWRgALGfwRQQDADIIRAAMDKTGV-SAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSALDVQHQYQLMA 178
Cdd:COG1124 105 --PLR-IHG--LPDREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILEPELLLLDEPTSALDVSVQAEILN 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 992343279 179 LLAELNQKQGCGIIVILHDLNLALRYATHIVALKQGRIAFDGPATTLAD 227
Cdd:COG1124 180 LLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLA 228
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
22-229 |
6.82e-40 |
|
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: 137.95 E-value: 6.82e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 22 LNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLAK---AVAF-LPQKLPasaGLTVRELVR 97
Cdd:cd03219 21 FSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARlgiGRTFqIPRLFP---ELTVLENVM 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 98 LGRFPWRG---ALGFWRQQDADIIRAAM---DKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSALDVQ 171
Cdd:cd03219 98 VAAQARTGsglLLARARREEREARERAEellERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPE 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 992343279 172 HQYQLMALLAELNQkQGCGIIVILHDLNLALRYATHIVALKQGRIAFDG-PATTLADEQ 229
Cdd:cd03219 178 ETEELAELIRELRE-RGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGtPDEVRNNPR 235
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
3-229 |
1.27e-39 |
|
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: 144.13 E-value: 1.27e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 3 TLSGVEmVRGGRRILAIEQLN--IPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLAKAVAFL 80
Cdd:COG4988 338 ELEDVS-FSYPGGRPALDGLSltIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 81 PQK--LPASaglTVRELVRLGRfpwrgalgfwRQQDADIIRAAMDKTGVSAFA-------DTFVDE----LSGGERQRAW 147
Cdd:COG4988 417 PQNpyLFAG---TIRENLRLGR----------PDASDEELEAALEAAGLDEFVaalpdglDTPLGEggrgLSGGQAQRLA 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 148 VAMLLAQESPVLILDEPTSALDVQHQYQLMALLAELnqKQGCGIIVILHDLNLaLRYATHIVALKQGRIAFDGPATTLAD 227
Cdd:COG4988 484 LARALLRDAPLLLLDEPTAHLDAETEAEILQALRRL--AKGRTVILITHRLAL-LAQADRILVLDDGRIVEQGTHEELLA 560
|
..
gi 992343279 228 EQ 229
Cdd:COG4988 561 KN 562
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
22-216 |
2.18e-38 |
|
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: 133.79 E-value: 2.18e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 22 LNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLA---KAVAFLPQKlPASA---GLTVREL 95
Cdd:cd03257 26 FSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKirrKEIQMVFQD-PMSSlnpRMTIGEQ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 96 VRlgrFPWRGALGFWRQQDADIIRAAMDKtGV---SAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSALDVQH 172
Cdd:cd03257 105 IA---EPLRIHGKLSKKEARKEAVLLLLV-GVglpEEVLNRYPHELSGGQRQRVAIARALALNPKLLIADEPTSALDVSV 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 992343279 173 QYQLMALLAELNQKQGCGIIVILHDLNLALRYATHIVALKQGRI 216
Cdd:cd03257 181 QAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-217 |
3.87e-38 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 134.06 E-value: 3.87e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 1 MFTLSGVEMV--RGGRRILAIEQLN--IPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKslaka 76
Cdd:COG1116 7 ALELRGVSKRfpTGGGGVTALDDVSltVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 77 VAFLPQK---LPAsagLTVRELVRLGRfpwrGALGFWRQQDADIIRAAMDKTGVSAFADTFVDELSGGERQRAWVAMLLA 153
Cdd:COG1116 82 RGVVFQEpalLPW---LTVLDNVALGL----ELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 992343279 154 QESPVLILDEPTSALDVQHQYQLMALLAELNQKQGCGIIVILHDLNLALRYATHIVALKQ--GRIA 217
Cdd:COG1116 155 NDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSArpGRIV 220
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-242 |
4.38e-38 |
|
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: 133.67 E-value: 4.38e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 1 MFTLSGVEMVRGGRRILAIEQLNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTG-SVWLNDAPLTSLSSKSLAKAVAF 79
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWELRKRIGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 80 ----LPQKLPASagLTVRELVRLGRFpwrGALGFWRQ---QDADIIRAAMDKTGVSAFADTFVDELSGGERQRAWVAMLL 152
Cdd:COG1119 83 vspaLQLRFPRD--ETVLDVVLSGFF---DSIGLYREptdEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 153 AQESPVLILDEPTSALDVQHQYQLMALLAELNQKQGCGIIVILHDLNLALRYATHIVALKQGRIAFDGPATTLADEQRLS 232
Cdd:COG1119 158 VKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEVLTSENLS 237
|
250
....*....|
gi 992343279 233 DLYQTPITLI 242
Cdd:COG1119 238 EAFGLPVEVE 247
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
22-227 |
4.50e-38 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 133.34 E-value: 4.50e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 22 LNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSskslakavaflPQKLPAS---------AGLTV 92
Cdd:COG3840 20 LTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALP-----------PAERPVSmlfqennlfPHLTV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 93 RELVRLGRFPwrgALGFWRQQDADIIRAAmDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSALDVQH 172
Cdd:COG3840 89 AQNIGLGLRP---GLKLTAEQRAQVEQAL-ERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPAL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 992343279 173 QYQLMALLAELNQKQGCGIIVILHDLNLALRYATHIVALKQGRIAFDGPATTLAD 227
Cdd:COG3840 165 RQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLD 219
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-215 |
7.56e-38 |
|
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: 130.44 E-value: 7.56e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 3 TLSGVEMVRGGRRILAIEQLNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLAKAVAFLPQ 82
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 83 klpasagltvrelvrlgrfpwrgalgfwrqqdadiiraamdktgvsafadtfvdeLSGGERQRAWVAMLLAQESPVLILD 162
Cdd:cd00267 81 -------------------------------------------------------LSGGQRQRVALARALLLNPDLLLLD 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 992343279 163 EPTSALDVQHQYQLMALLAELNQkQGCGIIVILHDLNLALRYATHIVALKQGR 215
Cdd:cd00267 106 EPTSGLDPASRERLLELLRELAE-EGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
12-217 |
4.90e-36 |
|
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: 127.59 E-value: 4.90e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 12 GGRRILAIEQ--LNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSskslaKAVAFLPQK---LPA 86
Cdd:cd03293 13 GGGAVTALEDisLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG-----PDRGYVFQQdalLPW 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 87 sagLTVRELVRLGRfpwrGALGFWRQQDADIIRAAMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTS 166
Cdd:cd03293 88 ---LTVLDNVALGL----ELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 992343279 167 ALDVQHQYQLMALLAELNQKQGCGIIVILHDLNLALRYATHIVALKQ--GRIA 217
Cdd:cd03293 161 ALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIV 213
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
3-217 |
6.04e-36 |
|
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: 127.25 E-value: 6.04e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 3 TLSGVEMVRGGRRILAIEQLNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSlaKAVAFLPQ 82
Cdd:cd03259 2 ELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPER--RNIGMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 83 KLPASAGLTVRELVRlgrFPWRgALGFWRQQDADIIRAAMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILD 162
Cdd:cd03259 80 DYALFPHLTVAENIA---FGLK-LRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 992343279 163 EPTSALDVQHQYQLMALLAELNQKQGCGIIVILHDLNLALRYATHIVALKQGRIA 217
Cdd:cd03259 156 EPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIV 210
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-216 |
7.78e-36 |
|
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: 125.59 E-value: 7.78e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 4 LSGVEMVRGGRRILAIEQLNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSlSSKSLAKAVAFLPQK 83
Cdd:cd03230 3 VRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYLPEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 84 LPASAGLTVRELVRLgrfpwrgalgfwrqqdadiiraamdktgvsafadtfvdelSGGERQRAWVAMLLAQESPVLILDE 163
Cdd:cd03230 82 PSLYENLTVRENLKL----------------------------------------SGGMKQRLALAQALLHDPELLILDE 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 992343279 164 PTSALDVQHQYQLMALLAELNqKQGCGIIVILHDLNLALRYATHIVALKQGRI 216
Cdd:cd03230 122 PTSGLDPESRREFWELLRELK-KEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-216 |
1.46e-35 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 126.08 E-value: 1.46e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 2 FTLSGVEMVRGGRRILAIEQLNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLAKAVAFLP 81
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 82 QKlPASAGLTVRELVRlgrFPWRGALgfwRQQDADIIRAAMDKTGVSA-FADTFVDELSGGERQRAWVAMLLAQESPVLI 160
Cdd:COG4619 81 QE-PALWGGTVRDNLP---FPFQLRE---RKFDRERALELLERLGLPPdILDKPVERLSGGERQRLALIRALLLQPDVLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 992343279 161 LDEPTSALDVQHQYQLMALLAELNQKQGCGIIVILHDLNLALRYATHIVALKQGRI 216
Cdd:COG4619 154 LDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-229 |
2.15e-35 |
|
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: 126.46 E-value: 2.15e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 4 LSGVEMVRGGRRILAIEQLNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSK---SLAKAVAFL 80
Cdd:cd03261 3 LRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAelyRLRRRMGML 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 81 PQKlpaSA---GLTVRELVrlgRFPWRGALGFWRQQDADIIRAAMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESP 157
Cdd:cd03261 83 FQS---GAlfdSLTVFENV---AFPLREHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPE 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 992343279 158 VLILDEPTSALDVQHQYQLMALLAELNQKQGCGIIVILHDLNLALRYATHIVALKQGRIAFDGPATTLADEQ 229
Cdd:cd03261 157 LLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRASD 228
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-215 |
3.72e-35 |
|
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: 123.84 E-value: 3.72e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 2 FTLSGVEMVRGGRRILAIEQLNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLA--KAVAF 79
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPlrRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 80 LPQKLPASAGLTVRELVRLGrfpwrgalgfwrqqdadiiraamdktgvsafadtfvdeLSGGERQRAWVAMLLAQESPVL 159
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG--------------------------------------LSGGQQQRVALARALAMDPDVL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 992343279 160 ILDEPTSALDVQHQYQLMALLAELNQKQGCGIIVILHDLNLALRYATHIVALKQGR 215
Cdd:cd03229 123 LLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
22-166 |
1.15e-34 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 121.99 E-value: 1.15e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 22 LNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLAKAVAFLPQKLPASAGLTVRELVRLGRF 101
Cdd:pfam00005 6 LTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRLTVRENLRLGLL 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 992343279 102 PWrgalGFWRQQDADIIRAAMDKTGVSAFADTFVD----ELSGGERQRAWVAMLLAQESPVLILDEPTS 166
Cdd:pfam00005 86 LK----GLSKREKDARAEEALEKLGLGDLADRPVGerpgTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
4-227 |
1.65e-34 |
|
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: 124.32 E-value: 1.65e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 4 LSGVEMVRGGRRILaiEQLN--IPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLAKA---VA 78
Cdd:COG1127 8 VRNLTKSFGDRVVL--DGVSldVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELrrrIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 79 FLPQklpASA---GLTVRE-----LVRLGRFPwrgalgfwRQQDADIIRAAMDKTGVSAFADTFVDELSGGERQRAWVAM 150
Cdd:COG1127 86 MLFQ---GGAlfdSLTVFEnvafpLREHTDLS--------EAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALAR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 992343279 151 LLAQESPVLILDEPTSALDVQHQYQLMALLAELNQKQGCGIIVILHDLNLALRYATHIVALKQGRIAFDGPATTLAD 227
Cdd:COG1127 155 ALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLA 231
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
22-236 |
2.61e-34 |
|
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: 129.50 E-value: 2.61e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 22 LNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLAKAVAFLPQKLPASAGlTVRELVRLGRf 101
Cdd:COG4987 356 LTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDT-TLRENLRLAR- 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 102 pwrgalgfwrqQDADI--IRAAMDKTGVSAFA-------DTFVDE----LSGGERQRAWVAMLLAQESPVLILDEPTSAL 168
Cdd:COG4987 434 -----------PDATDeeLWAALERVGLGDWLaalpdglDTWLGEggrrLSGGERRRLALARALLRDAPILLLDEPTEGL 502
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 992343279 169 DVQHQYQLMALLAELNqkQGCGIIVILHDLnLALRYATHIVALKQGRIAFDG-PATTLADEQRLSDLYQ 236
Cdd:COG4987 503 DAATEQALLADLLEAL--AGRTVLLITHRL-AGLERMDRILVLEDGRIVEQGtHEELLAQNGRYRQLYQ 568
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-222 |
4.01e-34 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 122.47 E-value: 4.01e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 1 MFTLSGVEMV-RGGRRILAIEQLNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSskslAKAVAF 79
Cdd:COG2884 1 MIRFENVSKRyPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLK----RREIPY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 80 LPQK----------LPasaGLTVRELVrlgRFPWRgALGFWRQQDADIIRAAMDKTGVSAFADTFVDELSGGERQRAWVA 149
Cdd:COG2884 77 LRRRigvvfqdfrlLP---DRTVYENV---ALPLR-VTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 992343279 150 MLLAQESPVLILDEPTSALDVQHQYQLMALLAELNQkQGCGIIVILHDLNLALRYATHIVALKQGRIAFDGPA 222
Cdd:COG2884 150 RALVNRPELLLADEPTGNLDPETSWEIMELLEEINR-RGTTVLIATHDLELVDRMPKRVLELEDGRLVRDEAR 221
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
28-244 |
6.37e-34 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 123.03 E-value: 6.37e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 28 ELTVVLGHNGSGKSTLVSLLSGQqAPDTGSVWLNDAPLTSLSSKSLAKAVAFLPQKLPASAGLTVRELVRLGRfpwrgal 107
Cdd:COG4138 23 ELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDWSAAELARHRAYLSQQQSPPFAMPVFQYLALHQ------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 108 gfwrqqdADIIRAAMDKTGVSAFADTF---------VDELSGGERQRAWVAMLLAQESPV-------LILDEPTSALDVQ 171
Cdd:COG4138 95 -------PAGASSEAVEQLLAQLAEALgledklsrpLTQLSGGEWQRVRLAAVLLQVWPTinpegqlLLLDEPMNSLDVA 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 992343279 172 HQYQLMALLAELNQkQGCGIIVILHDLNLALRYATHIVALKQGRIAFDGPATTLADEQRLSDLYQTPITLIDH 244
Cdd:COG4138 168 QQAALDRLLRELCQ-QGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMTPENLSEVFGVKFRRLEV 239
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
22-221 |
2.62e-33 |
|
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: 127.64 E-value: 2.62e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 22 LNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLAKAVAFLPQKLPASAGlTVRELVRLGRf 101
Cdd:COG2274 496 LTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSG-TIRENITLGD- 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 102 PWRGalgfwrqqDADIIRAAMDkTGVSAFA-------DTFVDE----LSGGERQRAWVAMLLAQESPVLILDEPTSALDV 170
Cdd:COG2274 574 PDAT--------DEEIIEAARL-AGLHDFIealpmgyDTVVGEggsnLSGGQRQRLAIARALLRNPRILILDEATSALDA 644
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 992343279 171 QHQYQLMALLAELnqKQGCGIIVILHDLNLaLRYATHIVALKQGRIAFDGP 221
Cdd:COG2274 645 ETEAIILENLRRL--LKGRTVIIIAHRLST-IRLADRIIVLDKGRIVEDGT 692
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-216 |
4.76e-33 |
|
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: 119.92 E-value: 4.76e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 4 LSGVEMVRGGRRILAIEQL--NIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSlSSKSLAKAVAFLP 81
Cdd:cd03263 3 IRNLTKTYKKGTKPAVDDLslNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGYCP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 82 QKLPASAGLTVRELVRL-GRFpwRGalGFWRQQDADIIrAAMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLI 160
Cdd:cd03263 82 QFDALFDELTVREHLRFyARL--KG--LPKSEIKEEVE-LLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 992343279 161 LDEPTSALDVQHQYQLMALLAELnqKQGCGIIVILHDLNLALRYATHIVALKQGRI 216
Cdd:cd03263 157 LDEPTSGLDPASRRAIWDLILEV--RKGRSIILTTHSMDEAEALCDRIAIMSDGKL 210
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
22-220 |
5.46e-33 |
|
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: 119.52 E-value: 5.46e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 22 LNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKslAKAVAFLPQKLPASAGLTVRELVRLGRF 101
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVSMLFQENNLFAHLTVEQNVGLGLS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 102 PwRGALgfwRQQDADIIRAAMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSALDVQHQYQLMALLA 181
Cdd:cd03298 97 P-GLKL---TAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVL 172
|
170 180 190
....*....|....*....|....*....|....*....
gi 992343279 182 ELNQKQGCGIIVILHDLNLALRYATHIVALKQGRIAFDG 220
Cdd:cd03298 173 DLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
22-215 |
1.97e-32 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 116.71 E-value: 1.97e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 22 LNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLAKAVAFLPQKlpasagltvrelvrlgrf 101
Cdd:cd03228 23 LTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAYVPQD------------------ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 102 PWRgalgfwrqqdadiiraamdktgvsaFADTFVDE-LSGGERQRAWVAMLLAQESPVLILDEPTSALDVQHQYQLMALL 180
Cdd:cd03228 85 PFL-------------------------FSGTIRENiLSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEAL 139
|
170 180 190
....*....|....*....|....*....|....*
gi 992343279 181 AELnqKQGCGIIVILHDLNLaLRYATHIVALKQGR 215
Cdd:cd03228 140 RAL--AKGKTVIVIAHRLST-IRDADRIIVLDDGR 171
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
22-237 |
2.76e-31 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 116.27 E-value: 2.76e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 22 LNIPTNELTVVLGHNGSGKSTLV----SLLSGQQAPDT-----GSVWLNDAPLTSLSSKSLAKAvAFLPQKLPASAGLTV 92
Cdd:PRK09984 25 LNIHHGEMVALLGPSGSGKSTLLrhlsGLITGDKSAGShiellGRTVQREGRLARDIRKSRANT-GYIFQQFNLVNRLSV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 93 RELV---RLGRFP-WRGALGFWRQQDADIIRAAMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSAL 168
Cdd:PRK09984 104 LENVligALGSTPfWRTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEPIASL 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 992343279 169 DVQHQYQLMALLAELNQKQGCGIIVILHDLNLALRYATHIVALKQGRIAFDGPATTLaDEQRLSDLYQT 237
Cdd:PRK09984 184 DPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQF-DNERFDHLYRS 251
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
22-224 |
1.73e-30 |
|
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: 113.59 E-value: 1.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 22 LNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSlaKAVAFLPQKLPASAGLTVRELVRLGrf 101
Cdd:cd03296 23 LDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE--RNVGFVFQHYALFRHMTVFDNVAFG-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 102 pWRGALGFWRQQDADI---IRAAMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSALDVQHQYQLMA 178
Cdd:cd03296 99 -LRVKPRSERPPEAEIrakVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKELRR 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 992343279 179 LLAELNQKQGCGIIVILHDLNLALRYATHIVALKQGRI--------AFDGPATT 224
Cdd:cd03296 178 WLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIeqvgtpdeVYDHPASP 231
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
11-216 |
2.50e-30 |
|
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: 112.35 E-value: 2.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 11 RGGRRILAIEQLNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLtslSSKSLAKAVAFLPQKLPASA-G 89
Cdd:cd03226 10 KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI---KAKERRKSIGYVMQDVDYQLfT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 90 LTVRELVRLGRfpwrGALGfwrqQDADIIRAAMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSALD 169
Cdd:cd03226 87 DSVREELLLGL----KELD----AGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 992343279 170 VQHQYQLMALLAELnQKQGCGIIVILHDLNLALRYATHIVALKQGRI 216
Cdd:cd03226 159 YKNMERVGELIREL-AAQGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
28-231 |
3.47e-30 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 117.43 E-value: 3.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 28 ELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSK-SLAKAVAFLPQKLPASAGLTVRELVRLGRFPWRGa 106
Cdd:COG1129 31 EVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRdAQAAGIAIIHQELNLVPNLSVAENIFLGREPRRG- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 107 lGF--WRQQDADiIRAAMDKTGVSAFADTFVDELSGGERQ-----RAwvamlLAQESPVLILDEPTSALDVQHQYQLMAL 179
Cdd:COG1129 110 -GLidWRAMRRR-ARELLARLGLDIDPDTPVGDLSVAQQQlveiaRA-----LSRDARVLILDEPTASLTEREVERLFRI 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 992343279 180 LAELnQKQGCGIIVILHDLNLALRYATHIVALKQGRIAFDGPATTLaDEQRL 231
Cdd:COG1129 183 IRRL-KAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL-TEDEL 232
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
12-217 |
7.40e-30 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 112.65 E-value: 7.40e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 12 GGRRILAIEQLN--IPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKslaKAVAFlpQK---LPa 86
Cdd:COG4525 16 GGQPQPALQDVSltIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGAD---RGVVF--QKdalLP- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 87 saGLTVRELVRLG-RFPwrgalGFWRQQDADIIRAAMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPT 165
Cdd:COG4525 90 --WLNVLDNVAFGlRLR-----GVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPF 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 992343279 166 SALDVQHQYQLMALLAELNQKQGCGIIVILHDLNLALRYATHIVALK--QGRIA 217
Cdd:COG4525 163 GALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMSpgPGRIV 216
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-221 |
1.03e-29 |
|
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: 111.52 E-value: 1.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 1 MFTLSGVEMV--RGGRRILAIEQ--LNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLAKA 76
Cdd:cd03258 1 MIELKNVSKVfgDTGGKVTALKDvsLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 77 ---VAFLPQKLPASAGLTVRELVRLgrfpwrgALGFWRQQDADIIRAA---MDKTGVSAFADTFVDELSGGERQRAWVAM 150
Cdd:cd03258 81 rrrIGMIFQHFNLLSSRTVFENVAL-------PLEIAGVPKAEIEERVlelLELVGLEDKADAYPAQLSGGQKQRVGIAR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 992343279 151 LLAQESPVLILDEPTSALDVQHQYQLMALLAELNQKQGCGIIVILHDLNLALRYATHIVALKQGRIAFDGP 221
Cdd:cd03258 154 ALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGT 224
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
22-234 |
1.21e-29 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the 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: 112.14 E-value: 1.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 22 LNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDapLTSLSSKSL---AKAVAFLPQKlPAS--AGLTVRELV 96
Cdd:TIGR04520 23 LSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDG--LDTLDEENLweiRKKVGMVFQN-PDNqfVGATVEDDV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 97 rlgrfpwrgA-----LGFWRQQDADIIRAAMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSALDVQ 171
Cdd:TIGR04520 100 ---------AfglenLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDIIILDEATSMLDPK 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 992343279 172 HQYQLMALLAELNQKQGCGIIVILHDLNLALRyATHIVALKQGRIAFDG-PATTLADEQRLSDL 234
Cdd:TIGR04520 171 GRKEVLETIRKLNKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGtPREIFSQVELLKEI 233
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
3-211 |
5.70e-29 |
|
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: 114.31 E-value: 5.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 3 TLSGVEMVRGGRRIlAIEQLN--IPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLAKAVAFL 80
Cdd:TIGR02857 323 EFSGVSVAYPGRRP-ALRPVSftVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 81 PQKlPASAGLTVRELVRLGRfpwrgalgfwRQQDADIIRAAMDKTGVSAFA-------DTFVDE----LSGGERQRAWVA 149
Cdd:TIGR02857 402 PQH-PFLFAGTIAENIRLAR----------PDASDAEIREALERAGLDEFVaalpqglDTPIGEggagLSGGQAQRLALA 470
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 992343279 150 MLLAQESPVLILDEPTSALDVQHQYQLMALLAELnqKQGCGIIVILHDLNLALRyATHIVAL 211
Cdd:TIGR02857 471 RAFLRDAPLLLLDEPTAHLDAETEAEVLEALRAL--AQGRTVLLVTHRLALAAL-ADRIVVL 529
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
22-217 |
6.49e-29 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 114.49 E-value: 6.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 22 LNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLAKAVAFLPQKlpasAGL---TVRELVRL 98
Cdd:COG1132 361 LTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQD----TFLfsgTIRENIRY 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 99 GRfpwRGAlgfwrqQDADIIRAAmDKTGVSAFA-------DTFVDE----LSGGERQRawVA---MLLAQeSPVLILDEP 164
Cdd:COG1132 437 GR---PDA------TDEEVEEAA-KAAQAHEFIealpdgyDTVVGErgvnLSGGQRQR--IAiarALLKD-PPILILDEA 503
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 992343279 165 TSALDVQHQYQLMALLAELnqKQGCGIIVILHDLNlALRYATHIVALKQGRIA 217
Cdd:COG1132 504 TSALDTETEALIQEALERL--MKGRTTIVIAHRLS-TIRNADRILVLDDGRIV 553
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
22-227 |
1.36e-28 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 108.52 E-value: 1.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 22 LNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLS-SKslaKAVAFLPQKLPASAGLTVRELVRLGR 100
Cdd:PRK10771 20 LTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPpSR---RPVSMLFQENNLFSHLTVAQNIGLGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 101 FPWRGALGFWRQQDADIIRaamdKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSALDVQHQYQLMALL 180
Cdd:PRK10771 97 NPGLKLNAAQREKLHAIAR----QMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLV 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 992343279 181 AELNQKQGCGIIVILHDLNLALRYATHIVALKQGRIAFDGPATTLAD 227
Cdd:PRK10771 173 SQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLS 219
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
22-217 |
2.68e-28 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 107.25 E-value: 2.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 22 LNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSlaKAVAFLPQKLPASAGLTVRELVRLGRF 101
Cdd:TIGR01277 19 LNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQ--RPVSMLFQENNLFAHLTVRQNIGLGLH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 102 PWRGALGFWRQQDADIIRaamdKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSALDVQHQYQLMALLA 181
Cdd:TIGR01277 97 PGLKLNAEQQEKVVDAAQ----QVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVK 172
|
170 180 190
....*....|....*....|....*....|....*.
gi 992343279 182 ELNQKQGCGIIVILHDLNLALRYATHIVALKQGRIA 217
Cdd:TIGR01277 173 QLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIK 208
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-220 |
2.95e-28 |
|
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: 106.89 E-value: 2.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 4 LSGVEMVRGGRRILAIEQLNIPTNeLTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKsLAKAVAFLPQK 83
Cdd:cd03264 3 LENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQK-LRRRIGYLPQE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 84 LPASAGLTVRELV----RLGRFPWRgalgfwrQQDADIIRAaMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVL 159
Cdd:cd03264 81 FGVYPNFTVREFLdyiaWLKGIPSK-------EVKARVDEV-LELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSIL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 992343279 160 ILDEPTSALDVQHQYQLMALLAELnqkqGCGIIVIL--HDLNLALRYATHIVALKQGRIAFDG 220
Cdd:cd03264 153 IVDEPTAGLDPEERIRFRNLLSEL----GEDRIVILstHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-241 |
5.96e-28 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 109.42 E-value: 5.96e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 1 MFTLSGVEMVRGGRRILAIEQLNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSskslakA---- 76
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLP------Pekrn 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 77 VAFLPQKLPASAGLTVRELVRLGrfpwrgaLGFWRQQDADI---IRAAMDKTGVSAFADTFVDELSGGERQRawVAM--L 151
Cdd:COG3842 79 VGMVFQDYALFPHLTVAENVAFG-------LRMRGVPKAEIrarVAELLELVGLEGLADRYPHQLSGGQQQR--VALarA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 152 LAQESPVLILDEPTSALDVQHQYQLMALLAELNQKQGCGIIVILHDLNLALRYATHIVALKQGRIAFDGPAttladeqrl 231
Cdd:COG3842 150 LAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTP--------- 220
|
250
....*....|
gi 992343279 232 SDLYQTPITL 241
Cdd:COG3842 221 EEIYERPATR 230
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
22-228 |
3.32e-27 |
|
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: 104.44 E-value: 3.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 22 LNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLAKA-VAFLPQKLPASAGLTVRELVRLGR 100
Cdd:cd03224 21 LTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAgIGYVPEGRRIFPELTVEENLLLGA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 101 FPWRGALGFWRqqdadiiraaMDKtgvsAFA---------DTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSALDVQ 171
Cdd:cd03224 101 YARRRAKRKAR----------LER----VYElfprlkerrKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPK 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 992343279 172 HQYQLMALLAELNqKQGCGIIVILHDLNLALRYATHIVALKQGRIAFDGPATTLADE 228
Cdd:cd03224 167 IVEEIFEAIRELR-DEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
21-223 |
5.38e-27 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 106.77 E-value: 5.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 21 QLNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPL-TSLSSKslAKAVAFLPQklpaSAGL----TVREL 95
Cdd:COG1118 22 SLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLfTNLPPR--ERRVGFVFQ----HYALfphmTVAEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 96 VRLG---RFPWRGALgfwrqqdADIIRAAMDKTGVSAFADTFVDELSGGERQRawVAM--LLAQESPVLILDEPTSALDV 170
Cdd:COG1118 96 IAFGlrvRPPSKAEI-------RARVEELLELVQLEGLADRYPSQLSGGQRQR--VALarALAVEPEVLLLDEPFGALDA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 992343279 171 QHQYQLMALLAELNQKQGCGIIVILHDLNLALRYATHIVALKQGRIA--------FDGPAT 223
Cdd:COG1118 167 KVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEqvgtpdevYDRPAT 227
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
23-234 |
1.18e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 104.45 E-value: 1.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 23 NIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLAKAVAFLPQKlPAS--AGLTVRELVRLG- 99
Cdd:PRK13648 31 NIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGIVFQN-PDNqfVGSIVKYDVAFGl 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 100 ---RFPWrgalgfwrQQDADIIRAAMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSALDVQHQYQL 176
Cdd:PRK13648 110 enhAVPY--------DEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNL 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 992343279 177 MALLAELNQKQGCGIIVILHDLNLALRyATHIVALKQGRIAFDG-PATTLADEQRLSDL 234
Cdd:PRK13648 182 LDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGtPTEIFDHAEELTRI 239
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
32-234 |
2.36e-26 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 107.03 E-value: 2.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 32 VLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSK-SLAKAVAFLPQ--KL-PAsagLTVRELVRLGRFPWRGAL 107
Cdd:COG3845 36 LLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRdAIALGIGMVHQhfMLvPN---LTVAENIVLGLEPTKGGR 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 108 GFWRQQDADiIRAAMDKTGVSAFADTFVDELSGGERQRawVAML--LAQESPVLILDEPTSALDVQHQYQLMALLAELnQ 185
Cdd:COG3845 113 LDRKAARAR-IRELSERYGLDVDPDAKVEDLSVGEQQR--VEILkaLYRGARILILDEPTAVLTPQEADELFEILRRL-A 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 992343279 186 KQGCGIIVILHDLNLALRYATHIVALKQGRIAFDGPATTlADEQRLSDL 234
Cdd:COG3845 189 AEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAE-TSEEELAEL 236
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
28-220 |
3.27e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 103.23 E-value: 3.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 28 ELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLtSLSSKSLAKA---VAFLPQ----KLPASaglTVRELVRLGR 100
Cdd:PRK13639 29 EMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDKKSLLEVrktVGIVFQnpddQLFAP---TVEEDVAFGP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 101 FpwrgALGFWRQQDADIIRAAMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSALDVQHQYQLMALL 180
Cdd:PRK13639 105 L----NLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLL 180
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 992343279 181 AELNqKQGCGIIVILHDLNLALRYATHIVALKQGRIAFDG 220
Cdd:PRK13639 181 YDLN-KEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEG 219
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
22-216 |
3.42e-26 |
|
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: 103.11 E-value: 3.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 22 LNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSL----AKAVAFLPQKLPASAGLTVRELVR 97
Cdd:cd03294 45 LDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSFALLPHRTVLENVA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 98 LGrFPWRGALGFWRQQDAdiiRAAMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSALD----VQHQ 173
Cdd:cd03294 125 FG-LEVQGVPRAEREERA---AEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDplirREMQ 200
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 992343279 174 YQLMALLAELnQKQgcgIIVILHDLNLALRYATHIVALKQGRI 216
Cdd:cd03294 201 DELLRLQAEL-QKT---IVFITHDLDEALRLGDRIAIMKDGRL 239
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
28-220 |
4.66e-26 |
|
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: 101.22 E-value: 4.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 28 ELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSlSSKSL-----AKAVAFLPQKLPASAGLTVRELVRLGrfp 102
Cdd:cd03297 24 EVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFD-SRKKInlppqQRKIGLVFQQYALFPHLNVRENLAFG--- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 103 wrgALGFWRQQDADIIRAAMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSALDVQHQYQLMALLAE 182
Cdd:cd03297 100 ---LKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQ 176
|
170 180 190
....*....|....*....|....*....|....*...
gi 992343279 183 LNQKQGCGIIVILHDLNLALRYATHIVALKQGRIAFDG 220
Cdd:cd03297 177 IKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
3-226 |
5.24e-26 |
|
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: 101.99 E-value: 5.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 3 TLSGVEMVRGGRRIlAIEQLN--IPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLAKAVAFL 80
Cdd:cd03295 2 EFENVTKRYGGGKK-AVNNLNleIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 81 PQklpaSAGL----TVRELVRLgrFPwrgALGFW----RQQDADIIRAAMDkTGVSAFADTFVDELSGGERQRAWVAMLL 152
Cdd:cd03295 81 IQ----QIGLfphmTVEENIAL--VP---KLLKWpkekIRERADELLALVG-LDPAEFADRYPHELSGGQQQRVGVARAL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 992343279 153 AQESPVLILDEPTSALDVQHQYQLMALLAELNQKQGCGIIVILHDLNLALRYATHIVALKQGRIA-FDGPATTLA 226
Cdd:cd03295 151 AADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVqVGTPDEILR 225
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
11-229 |
7.78e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 102.12 E-value: 7.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 11 RGGRRILAIEQLNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLAKAVAFLPQ----KLPA 86
Cdd:PRK13647 15 KDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVFQdpddQVFS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 87 SaglTVRELVRLGRFpwrgALGFWRQQDADIIRAAMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTS 166
Cdd:PRK13647 95 S---TVWDDVAFGPV----NMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 992343279 167 ALDVQHQYQLMALLAELNQkQGCGIIVILHDLNLALRYATHIVALKQGRIAFDGPATTLADEQ 229
Cdd:PRK13647 168 YLDPRGQETLMEILDRLHN-QGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDED 229
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
21-252 |
9.42e-26 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 103.64 E-value: 9.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 21 QLNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSlSSKSLakavaFLP----------QKlpAS--A 88
Cdd:COG4148 19 DFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQD-SARGI-----FLPphrrrigyvfQE--ARlfP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 89 GLTVRELVRLGRfpWRGALGFWRQQDADIIraamDKTGVSAFADTFVDELSGGERQRawVAM---LLAqeSP-VLILDEP 164
Cdd:COG4148 91 HLSVRGNLLYGR--KRAPRAERRISFDEVV----ELLGIGHLLDRRPATLSGGERQR--VAIgraLLS--SPrLLLMDEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 165 TSALDVQHQYQLMALLAELNQKQGCGIIVILHDLNLALRYATHIVALKQGRIAFDGPATTLadeqrLSDLYQTPITLIDH 244
Cdd:COG4148 161 LAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEV-----LSRPDLLPLAGGEE 235
|
....*...
gi 992343279 245 PHAVSEAT 252
Cdd:COG4148 236 AGSVLEAT 243
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
11-220 |
1.49e-25 |
|
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: 99.55 E-value: 1.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 11 RGGRRILAIEQLNIPTNELTVVLGHNGSGKSTLVSLLSGQQAP--DTGSVWLNDAPLtslSSKSLAKAVAFLPQKLPASA 88
Cdd:cd03213 19 KSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRPL---DKRSFRKIIGYVPQDDILHP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 89 GLTVRElvrlgrfpwrgALGFwrqqdADIIRAamdktgvsafadtfvdeLSGGERQRAWVAMLLAQESPVLILDEPTSAL 168
Cdd:cd03213 96 TLTVRE-----------TLMF-----AAKLRG-----------------LSGGERKRVSIALELVSNPSLLFLDEPTSGL 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 992343279 169 DVQHQYQLMALLAELNQkQGCGIIVILHDL-NLALRYATHIVALKQGRIAFDG 220
Cdd:cd03213 143 DSSSALQVMSLLRRLAD-TGRTIICSIHQPsSEIFELFDKLLLLSQGRVIYFG 194
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
22-217 |
1.72e-25 |
|
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: 98.27 E-value: 1.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 22 LNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDapltslsskslaKAVAFLpqklpasaglTVRELVRLGrf 101
Cdd:cd03216 21 LSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG------------KEVSFA----------SPRDARRAG-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 102 pwrgalgfwrqqdadiIRaamdktgvsafadtFVDELSGGERQRAWVAMLLAQESPVLILDEPTSALDVQHQYQLMALLA 181
Cdd:cd03216 77 ----------------IA--------------MVYQLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIR 126
|
170 180 190
....*....|....*....|....*....|....*.
gi 992343279 182 ELnQKQGCGIIVILHDLNLALRYATHIVALKQGRIA 217
Cdd:cd03216 127 RL-RAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
22-225 |
2.29e-25 |
|
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: 101.67 E-value: 2.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 22 LNIPTNELTVVLGHNGSGKSTLVSLLSG---QQAPDTGSVWLNDAPLTSLSSKSL----AKAVAFLPQKlPASA---GLT 91
Cdd:COG0444 26 FDVRRGETLGLVGESGSGKSTLARAILGllpPPGITSGEILFDGEDLLKLSEKELrkirGREIQMIFQD-PMTSlnpVMT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 92 VRELVRLgrfPWRGALGFWRQQDADIIRAAMDKTGVSAfADTFVD----ELSGGERQRAWVAMLLAQESPVLILDEPTSA 167
Cdd:COG0444 105 VGDQIAE---PLRIHGGLSKAEARERAIELLERVGLPD-PERRLDryphELSGGMRQRVMIARALALEPKLLIADEPTTA 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 992343279 168 LDVQHQYQLMALLAELNQKQGCGIIVILHDLNLALRYATHIVALKQGRIAFDGPATTL 225
Cdd:COG0444 181 LDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEEL 238
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
28-244 |
4.02e-25 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 99.62 E-value: 4.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 28 ELTVVLGHNGSGKSTLVSLLSGQqAPDTGSVWLNDAPLTSLSSKSLAKAVAFLPQKLPASAGLTVRELVRLGRfPWRGAL 107
Cdd:PRK03695 23 EILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAAELARHRAYLSQQQTPPFAMPVFQYLTLHQ-PDKTRT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 108 GFWRQQDADIIRAAM--DKTGVSafadtfVDELSGGERQRAWVAMLLAQESP-------VLILDEPTSALDVQHQYQLMA 178
Cdd:PRK03695 101 EAVASALNEVAEALGldDKLGRS------VNQLSGGEWQRVRLAAVVLQVWPdinpagqLLLLDEPMNSLDVAQQAALDR 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 992343279 179 LLAELNQkQGCGIIVILHDLNLALRYATHIVALKQGRIAFDGPATTLADEQRLSDLYQTPITLIDH 244
Cdd:PRK03695 175 LLSELCQ-QGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPENLAQVFGVNFRRLDV 239
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
12-214 |
4.61e-25 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 103.33 E-value: 4.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 12 GGRRILAIEQLNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLAK-AVAFLPQKLPASAGL 90
Cdd:PRK09700 16 GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQlGIGIIYQELSVIDEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 91 TVRELVRLGRFPWRGALGF----WRQQDadiIRAAM--DKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEP 164
Cdd:PRK09700 96 TVLENLYIGRHLTKKVCGVniidWREMR---VRAAMmlLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 992343279 165 TSALDVQHQYQLMALLAELnQKQGCGIIVILHDLNLALRYATHIVALKQG 214
Cdd:PRK09700 173 TSSLTNKEVDYLFLIMNQL-RKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
22-231 |
5.67e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 100.31 E-value: 5.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 22 LNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLtSLSSK---SLAKAVAFL---PQKLPASAglTVREL 95
Cdd:PRK13636 27 INIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSRKglmKLRESVGMVfqdPDNQLFSA--SVYQD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 96 VRLGRFpwrgALGFWRQQDADIIRAAMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSALDVQHQYQ 175
Cdd:PRK13636 104 VSFGAV----NLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 992343279 176 LMALLAELNQKQGCGIIVILHDLNLALRYATHIVALKQGRIAFDG-PATTLADEQRL 231
Cdd:PRK13636 180 IMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGnPKEVFAEKEML 236
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-221 |
6.65e-25 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 100.92 E-value: 6.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 1 MFTLSGVEMV--RGGRRILAIEQ--LNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLAKA 76
Cdd:COG1135 1 MIELENLSKTfpTKGGPVTALDDvsLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 77 -----VAF-----LPQKlpasaglTVRELVRlgrFPWRGAlGFWRQQDADIIRAAMDKTGVSAFADTFVDELSGGERQRA 146
Cdd:COG1135 81 rrkigMIFqhfnlLSSR-------TVAENVA---LPLEIA-GVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 992343279 147 WVAMLLAQESPVLILDEPTSALDVQHQYQLMALLAELNQKQGCGIIVILHDLNLALRYATHIVALKQGRIAFDGP 221
Cdd:COG1135 150 GIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGP 224
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
22-225 |
6.89e-25 |
|
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: 102.84 E-value: 6.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 22 LNIPTNElTVVL-GHNGSGKS----TLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLAK----AVAFLPQKlPASA---- 88
Cdd:COG4172 31 FDIAAGE-TLALvGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRRirgnRIAMIFQE-PMTSlnpl 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 89 ---GLTVRELVRLGRfpwrgalGFWRQQDADIIRAAMDKTGVSAFA---DTFVDELSGGERQRAWVAMLLAQESPVLILD 162
Cdd:COG4172 109 htiGKQIAEVLRLHR-------GLSGAAARARALELLERVGIPDPErrlDAYPHQLSGGQRQRVMIAMALANEPDLLIAD 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 992343279 163 EPTSALDVQHQYQLMALLAELNQKQGCGIIVILHDLNLALRYATHIVALKQGRIAFDGPATTL 225
Cdd:COG4172 182 EPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAEL 244
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
17-220 |
8.26e-25 |
|
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: 98.05 E-value: 8.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 17 LAIEQLNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLAKAVAFLPQKLPASAGlTVRELV 96
Cdd:cd03245 20 LDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGYVPQDVTLFYG-TLRDNI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 97 RLGRFPwrgalgfwrQQDADIIRAAMdKTGVSAFA-------DTFVDE----LSGGERQRAWVAMLLAQESPVLILDEPT 165
Cdd:cd03245 99 TLGAPL---------ADDERILRAAE-LAGVTDFVnkhpnglDLQIGErgrgLSGGQRQAVALARALLNDPPILLLDEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 992343279 166 SALDVQHQYQLMALLAELnqKQGCGIIVILHDLNLaLRYATHIVALKQGRIAFDG 220
Cdd:cd03245 169 SAMDMNSEERLKERLRQL--LGDKTLIIITHRPSL-LDLVDRIIVMDSGRIVADG 220
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-214 |
8.65e-25 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 99.00 E-value: 8.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 1 MFTLSGVEMVRGGRRILAIEQLNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKslaKAVAFL 80
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAE---RGVVFQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 81 PQKLpasagltvrelvrlgrFPWRGAL----------GFWRQQDADIIRAAMDKTGVSAFADTFVDELSGGERQRAWVAM 150
Cdd:PRK11248 78 NEGL----------------LPWRNVQdnvafglqlaGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIAR 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 992343279 151 LLAQESPVLILDEPTSALDVQHQYQLMALLAELNQKQGCGIIVILHDLNLALRYATHIVALKQG 214
Cdd:PRK11248 142 ALAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
16-216 |
8.68e-25 |
|
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: 97.86 E-value: 8.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 16 ILAIEQLN--IPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLAK-----AVAFLPQKLPASa 88
Cdd:cd03292 14 TAALDGINisISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYlrrkiGVVFQDFRLLPD- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 89 gLTVRELVRlgrFPWRgALGFWRQQDADIIRAAMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSAL 168
Cdd:cd03292 93 -RNVYENVA---FALE-VTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 992343279 169 DVQHQYQLMALLAELNqKQGCGIIVILHDLNLALRYATHIVALKQGRI 216
Cdd:cd03292 168 DPDTTWEIMNLLKKIN-KAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
27-221 |
1.42e-24 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 98.93 E-value: 1.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 27 NELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLAKAVAFLPQKlPAS--AGLTVRELVRLGrfpwr 104
Cdd:PRK13635 33 GEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGMVFQN-PDNqfVGATVQDDVAFG----- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 105 gaL---GFWRQQDADIIRAAMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSALDVQHQYQLMALLA 181
Cdd:PRK13635 107 --LeniGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVR 184
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 992343279 182 ELNQKQGCGIIVILHDLNLALRyATHIVALKQGRIAFDGP 221
Cdd:PRK13635 185 QLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGT 223
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
22-217 |
1.82e-24 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 97.42 E-value: 1.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 22 LNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLAK----AVAFLPQKLPASAGLTVRELVR 97
Cdd:TIGR02211 26 LSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAKlrnkKLGFIYQFHHLLPDFTALENVA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 98 LgrfPwrgAL--GFWRQQDADIIRAAMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSALDVQHQYQ 175
Cdd:TIGR02211 106 M---P---LLigKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPSLVLADEPTGNLDNNNAKI 179
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 992343279 176 LMALLAELNQKQGCGIIVILHDLNLALRyATHIVALKQGRIA 217
Cdd:TIGR02211 180 IFDLMLELNRELNTSFLVVTHDLELAKK-LDRVLEMKDGQLF 220
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
22-236 |
1.89e-24 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 97.86 E-value: 1.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 22 LNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGsvwlnDAPLTSLSSKSLAKAVAFLPQKlpasAG-----------L 90
Cdd:PRK09493 22 LNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSG-----DLIVDGLKVNDPKVDERLIRQE----AGmvfqqfylfphL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 91 TVRELVRLGRFPWRGALgfwRQQDADIIRAAMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSALD- 169
Cdd:PRK09493 93 TALENVMFGPLRVRGAS---KEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDp 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 992343279 170 -VQHQ-YQLMALLAElnqkQGCGIIVILHDLNLALRYATHIVALKQGRIAFDGPATTLADE---QRLSDLYQ 236
Cdd:PRK09493 170 eLRHEvLKVMQDLAE----EGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNppsQRLQEFLQ 237
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-241 |
3.18e-24 |
|
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: 96.92 E-value: 3.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 4 LSGVEMVRGGRRILAIEQLNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLAKAVAFlpQK 83
Cdd:cd03300 3 LENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVF--QN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 84 LPASAGLTVRELVRlgrFPWRgalgfWRQQDADIIRA----AMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVL 159
Cdd:cd03300 81 YALFPHLTVFENIA---FGLR-----LKKLPKAEIKErvaeALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 160 ILDEPTSALDVQHQYQLMALLAELNQKQGCGIIVILHDLNLALRYATHIVALKQGRIafdgpattladEQ--RLSDLYQT 237
Cdd:cd03300 153 LLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKI-----------QQigTPEEIYEE 221
|
....
gi 992343279 238 PITL 241
Cdd:cd03300 222 PANR 225
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
22-226 |
3.29e-24 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 99.42 E-value: 3.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 22 LNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSlSSKSL-----AKAVAFLPQKLPASAGLTVRELV 96
Cdd:TIGR02142 18 FTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFD-SRKGIflppeKRRIGYVFQEARLFPHLSVRGNL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 97 RLGRfpWRGALGFWRQQDADIIRAamdkTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSALDVQHQYQL 176
Cdd:TIGR02142 97 RYGM--KRARPSERRISFERVIEL----LGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEI 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 992343279 177 MALLAELNQKQGCGIIVILHDLNLALRYATHIVALKQGRIAFDGPATTLA 226
Cdd:TIGR02142 171 LPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVW 220
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
28-229 |
4.40e-24 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 100.95 E-value: 4.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 28 ELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLAKAVAFLPQKlPASAGLTVRELVrlgrfpwrgAL 107
Cdd:TIGR00958 508 EVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQE-PVLFSGSVRENI---------AY 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 108 GFWRQQDADIIRAAMdktgvSAFADTFVDE---------------LSGGERQRAWVAMLLAQESPVLILDEPTSALDVQH 172
Cdd:TIGR00958 578 GLTDTPDEEIMAAAK-----AANAHDFIMEfpngydtevgekgsqLSGGQKQRIAIARALVRKPRVLILDEATSALDAEC 652
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 992343279 173 QYqlmaLLAELNQKQGCGIIVILHDLNLAlRYATHIVALKQGRIAFDGPATTLADEQ 229
Cdd:TIGR00958 653 EQ----LLQESRSRASRTVLLIAHRLSTV-ERADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
22-216 |
4.51e-24 |
|
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: 96.06 E-value: 4.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 22 LNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSK--SLAKAVAFLPQKLPASAGLTVRELVRLG 99
Cdd:cd03262 21 LTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNinELRQKVGMVFQQFNLFPHLTVLENITLA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 100 rfPwRGALGFWRQQDADIIRAAMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSALD---VQHQYQL 176
Cdd:cd03262 101 --P-IKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDpelVGEVLDV 177
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 992343279 177 MALLAElnqkQGCGIIVILHDLNLALRYATHIVALKQGRI 216
Cdd:cd03262 178 MKDLAE----EGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
10-201 |
7.15e-24 |
|
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: 95.12 E-value: 7.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 10 VRGGRRILAIEQLNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSkSLAKAVAFLPQKLPASAG 89
Cdd:TIGR01189 9 SRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRD-EPHENILYLGHLPGLKPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 90 LTVRElvrlgrfpwrgALGFWRQ--QDADI-IRAAMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTS 166
Cdd:TIGR01189 88 LSALE-----------NLHFWAAihGGAQRtIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTT 156
|
170 180 190
....*....|....*....|....*....|....*
gi 992343279 167 ALDVQHQYQLMALLAELNQKQGCGIIVILHDLNLA 201
Cdd:TIGR01189 157 ALDKAGVALLAGLLRAHLARGGIVLLTTHQDLGLV 191
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
22-223 |
8.43e-24 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 95.96 E-value: 8.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 22 LNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLAKA----VAFLPQKLPASAGLTVRELVR 97
Cdd:COG4181 33 LEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARARLrarhVGFVFQSFQLLPTLTALENVM 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 98 LgrfP--WRGalgfwRQQDADIIRAAMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSALDVQHQYQ 175
Cdd:COG4181 113 L---PleLAG-----RRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQ 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 992343279 176 LMALLAELNQKQGCGIIVILHDLNLALRyATHIVALKQGRIAFDGPAT 223
Cdd:COG4181 185 IIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLVEDTAAT 231
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-216 |
1.20e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 99.37 E-value: 1.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 4 LSGVEMVRGGRRILAIEQLNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLndapltslsSKSLakAVAFLPQK 83
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI---------PKGL--RIGYLPQE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 84 LPASAGLTVRELVRLGRFPWRGALGFWRQ-------QDADIIRAA---------------------MDKTGVS-AFADTF 134
Cdd:COG0488 70 PPLDDDLTVLDTVLDGDAELRALEAELEEleaklaePDEDLERLAelqeefealggweaearaeeiLSGLGFPeEDLDRP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 135 VDELSGGERQRAWVAMLLAQESPVLILDEPTSALDVqhqyQLMALLAE-LNQKQGcGIIVILHDlnlalRY-----ATHI 208
Cdd:COG0488 150 VSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDL----ESIEWLEEfLKNYPG-TVLVVSHD-----RYfldrvATRI 219
|
....*...
gi 992343279 209 VALKQGRI 216
Cdd:COG0488 220 LELDRGKL 227
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
14-234 |
1.65e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 96.24 E-value: 1.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 14 RRILAIEQLNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTS------------------------LS 69
Cdd:PRK13634 20 RRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAgkknkklkplrkkvgivfqfpehqLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 70 SKSLAKAVAFLPQKLPAS---AGLTVRELVRLgrfpwrgaLGFwrqqDADIiraaMDKtgvSAFadtfvdELSGGERQRA 146
Cdd:PRK13634 100 EETVEKDICFGPMNFGVSeedAKQKAREMIEL--------VGL----PEEL----LAR---SPF------ELSGGQMRRV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 147 WVAMLLAQESPVLILDEPTSALDVQHQYQLMALLAELNQKQGCGIIVILHDLNLALRYATHIVALKQGRIAFDG-PATTL 225
Cdd:PRK13634 155 AIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGtPREIF 234
|
....*....
gi 992343279 226 ADEQRLSDL 234
Cdd:PRK13634 235 ADPDELEAI 243
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
22-221 |
1.74e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 96.27 E-value: 1.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 22 LNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSK----------------------SLAKAVAF 79
Cdd:PRK13637 28 IEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKlsdirkkvglvfqypeyqlfeeTIEKDIAF 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 80 LPQKLpasaGLTVRELVRLgrfpwrgalgfwrqqdadiIRAAMDKTGVSAfaDTFVD----ELSGGERQRAWVAMLLAQE 155
Cdd:PRK13637 108 GPINL----GLSEEEIENR-------------------VKRAMNIVGLDY--EDYKDkspfELSGGQKRRVAIAGVVAME 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 992343279 156 SPVLILDEPTSALDVQHQYQLMALLAELNQKQGCGIIVILHDLNLALRYATHIVALKQGRIAFDGP 221
Cdd:PRK13637 163 PKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGT 228
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
5-223 |
1.82e-23 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 95.91 E-value: 1.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 5 SGVEMVRGGRRILAIEQLNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSsKSLAKAV------- 77
Cdd:PRK10419 16 GGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLN-RAQRKAFrrdiqmv 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 78 ------AFLPQKlpasaglTVRELVRLgrfPWRGALGFWRQQDADIIRAAMDKTGVSA-FADTFVDELSGGERQRAWVAM 150
Cdd:PRK10419 95 fqdsisAVNPRK-------TVREIIRE---PLRHLLSLDKAERLARASEMLRAVDLDDsVLDKRPPQLSGGQLQRVCLAR 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 992343279 151 LLAQESPVLILDEPTSALDVQHQYQLMALLAELNQKQGCGIIVILHDLNLALRYATHIVALKQGRIAFDGPAT 223
Cdd:PRK10419 165 ALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVG 237
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
22-216 |
2.25e-23 |
|
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: 94.24 E-value: 2.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 22 LNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLAKAVAFlpQKLPASAGLTVRELVRlgrF 101
Cdd:cd03301 21 LDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIAMVF--QNYALYPHMTVYDNIA---F 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 102 PWRgalgfWRQQDADII----RAAMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSALDVQHQYQLM 177
Cdd:cd03301 96 GLK-----LRKVPKDEIdervREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLRVQMR 170
|
170 180 190
....*....|....*....|....*....|....*....
gi 992343279 178 ALLAELNQKQGCGIIVILHDLNLALRYATHIVALKQGRI 216
Cdd:cd03301 171 AELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-220 |
2.42e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 98.21 E-value: 2.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 1 MFTLSGVEMVRGGRRILAIEQLNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNdaplTSLSskslakaVAFL 80
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLG----ETVK-------IGYF 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 81 PQKLPA-SAGLTVRELVR--------------LGRFpwrgalGFWRQQdadiiraamdktgvsafADTFVDELSGGERQR 145
Cdd:COG0488 384 DQHQEElDPDKTVLDELRdgapggteqevrgyLGRF------LFSGDD-----------------AFKPVGVLSGGEKAR 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 146 AWVAMLLAQESPVLILDEPTSALDVQhqyQLMALLAELNQKQGCgIIVILHDlnlalRY-----ATHIVALKQGRI-AFD 219
Cdd:COG0488 441 LALAKLLLSPPNVLLLDEPTNHLDIE---TLEALEEALDDFPGT-VLLVSHD-----RYfldrvATRILEFEDGGVrEYP 511
|
.
gi 992343279 220 G 220
Cdd:COG0488 512 G 512
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-225 |
3.17e-23 |
|
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: 94.17 E-value: 3.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 2 FTLSGVEMVRGGRRILAIEQLNIPTNELTVVLGHNGSGKSTLVSLLSG-----QQAPDTGSVWLNDAPLTSLSSK--SLA 74
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLDGKDIYDLDVDvlELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 75 KAVAFLPQKlPASAGLTVRELVRLGrfPW-RGALgfWRQQDADIIRAAMDKTGVSAFAD--TFVDELSGGERQRAWVAML 151
Cdd:cd03260 81 RRVGMVFQK-PNPFPGSIYDNVAYG--LRlHGIK--LKEELDERVEEALRKAALWDEVKdrLHALGLSGGQQQRLCLARA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 992343279 152 LAQESPVLILDEPTSALDVQHQYQLMALLAELNQKQgcGIIVILHDLNLALRYATHIVALKQGRIAFDGPATTL 225
Cdd:cd03260 156 LANEPEVLLLDEPTSALDPISTAKIEELIAELKKEY--TIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
22-233 |
4.58e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 94.67 E-value: 4.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 22 LNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLAKAVAFLPQKlPASA--GLTVRELVRLG 99
Cdd:PRK13632 30 FEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGIIFQN-PDNQfiGATVEDDIAFG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 100 ----RFPwrgalgfwRQQDADIIRAAMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSALDVQHQYQ 175
Cdd:PRK13632 109 lenkKVP--------PKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKRE 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 992343279 176 LMALLAELNQKQGCGIIVILHDLNLALRyATHIVALKQGRIAFDG-PATTLADEQRLSD 233
Cdd:PRK13632 181 IKKIMVDLRKTRKKTLISITHDMDEAIL-ADKVIVFSEGKLIAQGkPKEILNNKEILEK 238
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-208 |
6.33e-23 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 93.01 E-value: 6.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 1 MFTLSGVEMVRGGRRILAIEQLNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSsksLAKAVAFL 80
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPD---VAEACHYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 81 PQKLPASAGLTVRELVRLgrfpWRGALGfwrqQDADIIRAAMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLI 160
Cdd:PRK13539 79 GHRNAMKPALTVAENLEF----WAAFLG----GEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWI 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 992343279 161 LDEPTSALDVQHQyqlmALLAELNQ---KQGcGIIVIlhdlnlalryATHI 208
Cdd:PRK13539 151 LDEPTAALDAAAV----ALFAELIRahlAQG-GIVIA----------ATHI 186
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
22-220 |
6.51e-23 |
|
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: 91.99 E-value: 6.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 22 LNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSsKSLAKAVAFLPQKlPASAGLTVRElvRLGRf 101
Cdd:cd03247 23 LELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISVLNQR-PYLFDTTLRN--NLGR- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 102 pwrgalgfwrqqdadiiraamdktgvsafadtfvdELSGGERQRAWVAMLLAQESPVLILDEPTSALDVQHQYQLMALLA 181
Cdd:cd03247 98 -----------------------------------RFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIF 142
|
170 180 190
....*....|....*....|....*....|....*....
gi 992343279 182 ElnQKQGCGIIVILHDLnLALRYATHIVALKQGRIAFDG 220
Cdd:cd03247 143 E--VLKDKTLIWITHHL-TGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
17-216 |
8.12e-23 |
|
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: 93.17 E-value: 8.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 17 LAIEQLNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSlaKAVAFLPQKLPASAGLTVRELV 96
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEK--RDISYVPQNYALFPHMTVYKNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 97 ----RLGRFPwrgalgfwRQQDADIIRAAMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSALDVQH 172
Cdd:cd03299 93 ayglKKRKVD--------KKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRT 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 992343279 173 QYQLMALLAELNQKQGCGIIVILHDLNLALRYATHIVALKQGRI 216
Cdd:cd03299 165 KEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKL 208
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
11-224 |
1.00e-22 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 93.79 E-value: 1.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 11 RGGRRILAIEQLNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLakaVAFLPQ--KLPASA 88
Cdd:PRK15056 17 RNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL---VAYVPQseEVDWSF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 89 GLTVRELVRLGRFPWRGALGFWRQQDADIIRAAMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSAL 168
Cdd:PRK15056 94 PVLVEDVVMMGRYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 992343279 169 DVQHQYQLMALLAELnQKQGCGIIVILHDLNLALRYATHIVALKqGRIAFDGPATT 224
Cdd:PRK15056 174 DVKTEARIISLLREL-RDEGKTMLVSTHNLGSVTEFCDYTVMVK-GTVLASGPTET 227
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
18-231 |
1.11e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 94.10 E-value: 1.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 18 AIEQLN--IPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTgsvwLNDAPLTSLSSKSLAKAVAFLPQKL------PAS-- 87
Cdd:PRK13640 22 ALNDISfsIPRGSWTALIGHNGSGKSTISKLINGLLLPDD----NPNSKITVDGITLTAKTVWDIREKVgivfqnPDNqf 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 88 AGLTVRELVRLGrFPWRGALgfwRQQDADIIRAAMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSA 167
Cdd:PRK13640 98 VGATVGDDVAFG-LENRAVP---RPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSM 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 992343279 168 LDVQHQYQLMALLAELNQKQGCGIIVILHDLNLAlRYATHIVALKQGRI-AFDGPATTLADEQRL 231
Cdd:PRK13640 174 LDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLlAQGSPVEIFSKVEML 237
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
22-216 |
1.82e-22 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 92.29 E-value: 1.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 22 LNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLAKAVAFLPQKLPASAGlTVRELVRLGRF 101
Cdd:cd03254 24 FSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVVLQDTFLFSG-TIMENIRLGRP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 102 pwrgalgfwRQQDADIIRAAmdKTgvsAFADTFVDE---------------LSGGERQRAWVAMLLAQESPVLILDEPTS 166
Cdd:cd03254 103 ---------NATDEEVIEAA--KE---AGAHDFIMKlpngydtvlgenggnLSQGERQLLAIARAMLRDPKILILDEATS 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 992343279 167 ALDVQHQYQLMALLAELNQKQGCgiIVILHDLNlALRYATHIVALKQGRI 216
Cdd:cd03254 169 NIDTETEKLIQEALEKLMKGRTS--IIIAHRLS-TIKNADKILVLDDGKI 215
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
32-222 |
1.97e-22 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 92.45 E-value: 1.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 32 VLGHNGSGKSTLVSLLSGQQAPDTGSVWLND--APLtslssksLAKAVAFLPQklpasagLTVRELVRL-GRFpwrgaLG 108
Cdd:COG1134 57 IIGRNGAGKSTLLKLIAGILEPTSGRVEVNGrvSAL-------LELGAGFHPE-------LTGRENIYLnGRL-----LG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 109 FWRQQdadiIRAAMDKtgVSAFAD--TFVDE----LSGGERQRAWVAMLLAQESPVLILDEPTSALDVQHQYQLMALLAE 182
Cdd:COG1134 118 LSRKE----IDEKFDE--IVEFAElgDFIDQpvktYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRE 191
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 992343279 183 LnQKQGCGIIVILHDLNLALRYATHIVALKQGRIAFDGPA 222
Cdd:COG1134 192 L-RESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDP 230
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
22-225 |
2.52e-22 |
|
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: 91.66 E-value: 2.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 22 LNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSlSSKSLAKAVAFLPQKLPASAGLTVRELV----R 97
Cdd:cd03265 21 FRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQDLSVDDELTGWENLyihaR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 98 LGRFPWRGalgfWRQQdadiIRAAMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSALDVQHQYQLM 177
Cdd:cd03265 100 LYGVPGAE----RRER----IDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVW 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 992343279 178 ALLAELNQKQGCGIIVILHDLNLALRYATHIVALKQGRIAFDGPATTL 225
Cdd:cd03265 172 EYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
32-220 |
2.62e-22 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 91.44 E-value: 2.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 32 VLGHNGSGKSTLVSLLSGQQAPDTGSVWLN--DAPLtslssksLAKAVAFLPQklpasagLTVRELVRL-GRFpwrgaLG 108
Cdd:cd03220 53 LIGRNGAGKSTLLRLLAGIYPPDSGTVTVRgrVSSL-------LGLGGGFNPE-------LTGRENIYLnGRL-----LG 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 109 FWRQQDADIIRAAMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSALDVQHQYQLMALLAELnQKQG 188
Cdd:cd03220 114 LSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLREL-LKQG 192
|
170 180 190
....*....|....*....|....*....|..
gi 992343279 189 CGIIVILHDLNLALRYATHIVALKQGRIAFDG 220
Cdd:cd03220 193 KTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
22-228 |
3.16e-22 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 92.05 E-value: 3.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 22 LNIPTNELTVVLGHNGSGKSTLVSLLSGQQA--PDTGSVWLNDAPLTSLSSKSLAKAVAFL----PQKLPasaGLTVREL 95
Cdd:COG0396 21 LTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSILLDGEDILELSPDERARAGIFLafqyPVEIP---GVSVSNF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 96 VRLgrfpwrgALGFWRQQDADI------IRAAMDKTGVSA-FADTFVDE-LSGGERQRAWVAMLLAQESPVLILDEPTSA 167
Cdd:COG0396 98 LRT-------ALNARRGEELSAreflklLKEKMKELGLDEdFLDRYVNEgFSGGEKKRNEILQMLLLEPKLAILDETDSG 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 992343279 168 LDVQhqyqlmAL--LAE-LNQ--KQGCGIIVILHDLNLaLRY--ATHIVALKQGRIAFDGPAtTLADE 228
Cdd:COG0396 171 LDID------ALriVAEgVNKlrSPDRGILIITHYQRI-LDYikPDFVHVLVDGRIVKSGGK-ELALE 230
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
3-241 |
3.51e-22 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 93.60 E-value: 3.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 3 TLSGVEMVRGGRRILAIEQLNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKslAKAVAFLPQ 82
Cdd:COG3839 5 ELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPK--DRNIAMVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 83 klpaSAGL----TVRE-----LvRLGRFPwrgalgfwRQQDADIIRAAMDKTGVSAFADTFVDELSGGERQRawVAM--L 151
Cdd:COG3839 83 ----SYALyphmTVYEniafpL-KLRKVP--------KAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQR--VALgrA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 152 LAQESPVLILDEPTSALDVQHQYQLMALLAELNQKQGCGIIVILHDLNLALRYATHIVALKQGRIA-FDGPAttladeqr 230
Cdd:COG3839 148 LVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQqVGTPE-------- 219
|
250
....*....|.
gi 992343279 231 lsDLYQTPITL 241
Cdd:COG3839 220 --ELYDRPANL 228
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
22-236 |
5.07e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 91.69 E-value: 5.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 22 LNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLAKAVAFLPQ--KLPASAGLTVRE----- 94
Cdd:COG1101 27 LTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKYIGRVFQdpMMGTAPSMTIEEnlala 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 95 LVRLGRFPWRGALgfwRQQDADIIRAAMDKT--GVSAFADTFVDELSGGERQrAwVAMLLA--QESPVLILDEPTSALDV 170
Cdd:COG1101 107 YRRGKRRGLRRGL---TKKRRELFRELLATLglGLENRLDTKVGLLSGGQRQ-A-LSLLMAtlTKPKLLLLDEHTAALDP 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 171 QHQYQLMALLAELNQKQGCGIIVILHDLNLALRYATHIVALKQGRIAFDgpattLADEQR----LSDLYQ 236
Cdd:COG1101 182 KTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRIILD-----VSGEEKkkltVEDLLE 246
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
13-225 |
5.22e-22 |
|
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: 94.78 E-value: 5.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 13 GRRILAIEQLNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLAKAVAFLPQKLPASAGlTV 92
Cdd:TIGR02203 344 DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFND-TI 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 93 RELVRLGRfpwRGALGfwrqqDADIIRAAMDktgvsAFADTFVDE---------------LSGGERQRAWVAMLLAQESP 157
Cdd:TIGR02203 423 ANNIAYGR---TEQAD-----RAEIERALAA-----AYAQDFVDKlplgldtpigengvlLSGGQRQRLAIARALLKDAP 489
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 992343279 158 VLILDEPTSALDVQHQYQLMALLAELnqKQGCGIIVILHDLNlALRYATHIVALKQGRIAFDGPATTL 225
Cdd:TIGR02203 490 ILILDEATSALDNESERLVQAALERL--MQGRTTLVIAHRLS-TIEKADRIVVMDDGRIVERGTHNEL 554
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
11-201 |
5.40e-22 |
|
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: 90.24 E-value: 5.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 11 RGGRRILAIEQLNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLtSLSSKSLAKAVAFLPQKLPASAGL 90
Cdd:cd03231 10 RDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPL-DFQRDSIARGLLYLGHAPGIKTTL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 91 TVRELVRlgrfpwrgalgFWRQ-QDADIIRAAMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSALD 169
Cdd:cd03231 89 SVLENLR-----------FWHAdHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
170 180 190
....*....|....*....|....*....|..
gi 992343279 170 VQHQYQLMALLAELNQKQGCGIIVILHDLNLA 201
Cdd:cd03231 158 KAGVARFAEAMAGHCARGGMVVLTTHQDLGLS 189
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
22-214 |
5.57e-22 |
|
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: 90.99 E-value: 5.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 22 LNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLakaVAFlpQKLPASAGLTVRELVRLGRF 101
Cdd:TIGR01184 6 LTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM---VVF--QNYSLLPWLTVRENIALAVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 102 PWRGALGfwRQQDADIIRAAMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSALDVQHQYQLMALLA 181
Cdd:TIGR01184 81 RVLPDLS--KSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELM 158
|
170 180 190
....*....|....*....|....*....|...
gi 992343279 182 ELNQKQGCGIIVILHDLNLALRYATHIVALKQG 214
Cdd:TIGR01184 159 QIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
22-220 |
6.60e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 91.73 E-value: 6.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 22 LNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSS----KSLAKAVAFLPQkLPASAGL--TVREL 95
Cdd:PRK13649 28 LTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKnkdiKQIRKKVGLVFQ-FPESQLFeeTVLKD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 96 VRLGrfPWRGALGfwrQQDADiiRAAMDKTGVSAFADTFVD----ELSGGERQRAWVAMLLAQESPVLILDEPTSALDVQ 171
Cdd:PRK13649 107 VAFG--PQNFGVS---QEEAE--ALAREKLALVGISESLFEknpfELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPK 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 992343279 172 HQYQLMALLAELNQKqGCGIIVILHDLNLALRYATHIVALKQGRIAFDG 220
Cdd:PRK13649 180 GRKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSG 227
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
28-229 |
7.37e-22 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 90.30 E-value: 7.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 28 ELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPltslsSKSLAKAVAFLPQK--LPASAGLTVRELVRLGRFPWRG 105
Cdd:TIGR03771 7 ELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGAS-----PGKGWRHIGYVPQRheFAWDFPISVAHTVMSGRTGHIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 106 ALGFWRQQDADIIRAAMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSALDVQHQYQLMALLAELNQ 185
Cdd:TIGR03771 82 WLRRPCVADFAAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLTELFIELAG 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 992343279 186 kQGCGIIVILHDLNLALrYATHIVALKQGRIAFDGPATTLADEQ 229
Cdd:TIGR03771 162 -AGTAILMTTHDLAQAM-ATCDRVVLLNGRVIADGTPQQLQDPA 203
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
28-203 |
8.96e-22 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 90.65 E-value: 8.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 28 ELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKslakavaflpqklpASAGLTVRELVRLGRF----PW 103
Cdd:PRK11629 36 EMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSA--------------AKAELRNQKLGFIYQFhhllPD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 104 RGAL----------GFWRQQDADIIRAAMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSALDVQHQ 173
Cdd:PRK11629 102 FTALenvamplligKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNA 181
|
170 180 190
....*....|....*....|....*....|
gi 992343279 174 YQLMALLAELNQKQGCGIIVILHDLNLALR 203
Cdd:PRK11629 182 DSIFQLLGELNRLQGTAFLVVTHDLQLAKR 211
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
28-216 |
1.58e-21 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 89.84 E-value: 1.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 28 ELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLAKAVAFLPQKlPASAGLTVRELVRLGrfpwrgal 107
Cdd:cd03248 41 EVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVSLVGQE-PVLFARSLQDNIAYG-------- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 108 gfWRQQDADIIRAAMDKTGVSAFA-------DTFVDE----LSGGERQRAWVAMLLAQESPVLILDEPTSALDVQHQYQL 176
Cdd:cd03248 112 --LQSCSFECVKEAAQKAHAHSFIselasgyDTEVGEkgsqLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQV 189
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 992343279 177 MALLAELNQKQgcGIIVILHDLNLALRyATHIVALKQGRI 216
Cdd:cd03248 190 QQALYDWPERR--TVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
22-235 |
1.86e-21 |
|
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: 89.60 E-value: 1.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 22 LNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLAKAVAFLPQKLPASAGlTVRELVRLGRf 101
Cdd:cd03251 23 LDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGLVSQDVFLFND-TVAENIAYGR- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 102 pwRGAlgfwrqQDADIIRAAMdktgvSAFADTFVDE---------------LSGGERQRAWVAMLLAQESPVLILDEPTS 166
Cdd:cd03251 101 --PGA------TREEVEEAAR-----AANAHEFIMElpegydtvigergvkLSGGQRQRIAIARALLKDPPILILDEATS 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 167 ALDVQHQYQLMALLAELnqKQGCGIIVILHDLNlALRYATHIVALKQGRIAFDGP-ATTLADEQRLSDLY 235
Cdd:cd03251 168 ALDTESERLVQAALERL--MKNRTTFVIAHRLS-TIENADRIVVLEDGKIVERGThEELLAQGGVYAKLH 234
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
22-222 |
2.37e-21 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 89.28 E-value: 2.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 22 LNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTsLSSKSLAKA---VAFLPQklpaSAGL----TVRE 94
Cdd:COG1126 22 LDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLT-DSKKDINKLrrkVGMVFQ----QFNLfphlTVLE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 95 LVRLGrfPWRgALGFWRQQDADIIRAAMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSALD---VQ 171
Cdd:COG1126 97 NVTLA--PIK-VKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDpelVG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 992343279 172 HQYQLMALLAelnqKQGCGIIVILHDLNLALRYATHIVALKQGRIAFDGPA 222
Cdd:COG1126 174 EVLDVMRDLA----KEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPP 220
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
22-216 |
2.74e-21 |
|
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: 89.14 E-value: 2.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 22 LNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLAKAVAFLPQKlPASAGLTVRELVRLGRF 101
Cdd:cd03249 24 LTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGLVSQE-PVLFDGTIAENIRYGKP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 102 PwrgalgfwrQQDADIIRAAmdktgVSAFADTFVD---------------ELSGGERQRAWVAMLLAQESPVLILDEPTS 166
Cdd:cd03249 103 D---------ATDEEVEEAA-----KKANIHDFIMslpdgydtlvgergsQLSGGQKQRIAIARALLRNPKILLLDEATS 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 992343279 167 ALDVQHQYQLMALLAELnqKQGCGIIVILHDLNlALRYATHIVALKQGRI 216
Cdd:cd03249 169 ALDAESEKLVQEALDRA--MKGRTTIVIAHRLS-TIRNADLIAVLQNGQV 215
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
14-220 |
3.21e-21 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 88.87 E-value: 3.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 14 RRILAIEQLNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPD---TGSVWLNDAPLtslSSKSLAKAVAFLPQKLPASAGL 90
Cdd:cd03234 20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQPR---KPDQFQKCVAYVRQDDILLPGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 91 TVRELV------RLGR-FPwrgalGFWRQQDADIIRaaMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDE 163
Cdd:cd03234 97 TVRETLtytailRLPRkSS-----DAIRKKRVEDVL--LRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 992343279 164 PTSALDVQHQYQLMALLAELnQKQGCGIIVILH----DLnlaLRYATHIVALKQGRIAFDG 220
Cdd:cd03234 170 PTSGLDSFTALNLVSTLSQL-ARRNRIVILTIHqprsDL---FRLFDRILLLSSGEIVYSG 226
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
22-216 |
3.27e-21 |
|
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: 89.48 E-value: 3.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 22 LNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSL---SSKSLAKAVAFLPQKLPAS--AGLTVRELV 96
Cdd:TIGR02769 32 LSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLdrkQRRAFRRDVQLVFQDSPSAvnPRMTVRQII 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 97 RLgrfPWRGALGFWRQQDADIIRAAMDKTGV-SAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSALDVQHQYQ 175
Cdd:TIGR02769 112 GE---PLRHLTSLDESEQKARIAELLDMVGLrSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAV 188
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 992343279 176 LMALLAELNQKQGCGIIVILHDLNLALRYATHIVALKQGRI 216
Cdd:TIGR02769 189 ILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
13-221 |
3.31e-21 |
|
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: 88.83 E-value: 3.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 13 GRRILAIEQLNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLAKAVAFLPQKLPasagL-- 90
Cdd:cd03253 13 GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVVPQDTV----Lfn 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 91 -TVRELVRLGRfpwrgalgfWRQQDADIIRAAM-----DKTGVSAFA-DTFVDE----LSGGERQRAWVAMLLAQESPVL 159
Cdd:cd03253 89 dTIGYNIRYGR---------PDATDEEVIEAAKaaqihDKIMRFPDGyDTIVGErglkLSGGEKQRVAIARAILKNPPIL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 992343279 160 ILDEPTSALDVQHQYQLMALLAELnqKQGCGIIVILHDLNLALRyATHIVALKQGRIAFDGP 221
Cdd:cd03253 160 LLDEATSALDTHTEREIQAALRDV--SKGRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGT 218
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
17-220 |
3.42e-21 |
|
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: 89.00 E-value: 3.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 17 LAIEQLNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVwlnDAPLTSLSSKslakavaflPQKLPASAGLTVRELV 96
Cdd:cd03237 15 LEVEGGSISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDI---EIELDTVSYK---------PQYIKADYEGTVRDLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 97 RlGRFPWRGALGFWRqqdADIiraaMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSALDVQHqyQL 176
Cdd:cd03237 83 S-SITKDFYTHPYFK---TEI----AKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQ--RL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 992343279 177 MAL-----LAELNQKqgcGIIVILHDLNLALRYATHIvalkqgrIAFDG 220
Cdd:cd03237 153 MASkvirrFAENNEK---TAFVVEHDIIMIDYLADRL-------IVFEG 191
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
21-224 |
3.89e-21 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 88.92 E-value: 3.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 21 QLNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSvwLNDAPLT-SLSSKSLAKAVAFLPQKL----------PAsag 89
Cdd:PRK11124 22 TLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGT--LNIAGNHfDFSKTPSDKAIRELRRNVgmvfqqynlwPH--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 90 LTVRElvRLGRFPWRgALGFWRQQDADIIRAAMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSALD 169
Cdd:PRK11124 97 LTVQQ--NLIEAPCR-VLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALD 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 992343279 170 VQHQYQLMALLAELnqkQGCGI--IVILHDLNLALRYATHIVALKQGRI-------AFDGPATT 224
Cdd:PRK11124 174 PEITAQIVSIIREL---AETGItqVIVTHEVEVARKTASRVVYMENGHIveqgdasCFTQPQTE 234
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
13-228 |
5.95e-21 |
|
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: 91.72 E-value: 5.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 13 GRRILAIEQLNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLAKAVAFLPQKLPASAGlTV 92
Cdd:TIGR01193 486 GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSG-SI 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 93 RELVRLGRFPWRGALGFWRQQDADIIRAAMDK------TGVSAFADTfvdeLSGGERQRAWVAMLLAQESPVLILDEPTS 166
Cdd:TIGR01193 565 LENLLLGAKENVSQDEIWAACEIAEIKDDIENmplgyqTELSEEGSS----ISGGQKQRIALARALLTDSKVLILDESTS 640
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 992343279 167 ALDVQHQYQLMALLAELNQKQgcgIIVILHDLNLALRyATHIVALKQGRIAFDGPATTLADE 228
Cdd:TIGR01193 641 NLDTITEKKIVNNLLNLQDKT---IIFVAHRLSVAKQ-SDKIIVLDHGKIIEQGSHDELLDR 698
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
32-235 |
8.36e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 89.07 E-value: 8.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 32 VLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDA------------------------PLTSLSSKSLAKAVAFLPQKLpas 87
Cdd:PRK13646 38 IVGQTGSGKSTLIQNINALLKPTTGTVTVDDItithktkdkyirpvrkrigmvfqfPESQLFEDTVEREIIFGPKNF--- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 88 aGLTVRElVRLGRFPWRGALGFWRqqdaDIIRAamdktgvSAFadtfvdELSGGERQRAWVAMLLAQESPVLILDEPTSA 167
Cdd:PRK13646 115 -KMNLDE-VKNYAHRLLMDLGFSR----DVMSQ-------SPF------QMSGGQMRKIAIVSILAMNPDIIVLDEPTAG 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 992343279 168 LDVQHQYQLMALLAELNQKQGCGIIVILHDLNLALRYATHIVALKQGRIAFDG-PATTLADEQRLSDLY 235
Cdd:PRK13646 176 LDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTsPKELFKDKKKLADWH 244
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
33-215 |
1.15e-20 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 90.74 E-value: 1.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 33 LGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSK-SLAKAVAFLPQKLPASAGLTVRELVRLGRFPWRGalGFWR 111
Cdd:PRK11288 36 MGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTaALAAGVAIIYQELHLVPEMTVAENLYLGQLPHKG--GIVN 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 112 QQDA-DIIRAAMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSALDVQHQYQLMALLAELnQKQGCG 190
Cdd:PRK11288 114 RRLLnYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIREL-RAEGRV 192
|
170 180
....*....|....*....|....*
gi 992343279 191 IIVILHDLNLALRYATHIVALKQGR 215
Cdd:PRK11288 193 ILYVSHRMEEIFALCDAITVFKDGR 217
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-213 |
1.20e-20 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 87.86 E-value: 1.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 1 MFTLSGVEMVRGGRRILAIEQLNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVwlndapltslsSKSLAKAVAFL 80
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI-----------KRNGKLRIGYV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 81 PQK--LPASAGLTVRELVRLgrfpwRGALgfwrqQDADIIrAAMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPV 158
Cdd:PRK09544 73 PQKlyLDTTLPLTVNRFLRL-----RPGT-----KKEDIL-PALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQL 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 992343279 159 LILDEPTSALDVQHQYQLMALLAELNQKQGCGIIVILHDLNLALRYATHIVALKQ 213
Cdd:PRK09544 142 LVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH 196
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
22-252 |
1.39e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 88.25 E-value: 1.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 22 LNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSS----KSLAKAVAFLPQkLPASAGLTVRELVR 97
Cdd:PRK13643 27 LEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKqkeiKPVRKKVGVVFQ-FPESQLFEETVLKD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 98 LGRFPWRgaLGFWRQQDADIIRAAMDKTGVSA-FADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSALDVQHQYQL 176
Cdd:PRK13643 106 VAFGPQN--FGIPKEKAEKIAAEKLEMVGLADeFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEM 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 992343279 177 MALLAELNQkQGCGIIVILHDLNLALRYATHIVALKQGRIAFDGPAttladeqrlSDLYQTPITLIDHPHAVSEAT 252
Cdd:PRK13643 184 MQLFESIHQ-SGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTP---------SDVFQEVDFLKAHELGVPKAT 249
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
12-228 |
1.41e-20 |
|
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: 87.32 E-value: 1.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 12 GGRRILAIEQLNIPTNELTVVLGHNGSGKSTLVSLLSGQqaPDT----GSVWLNDAPLTSLSSKSLAKAVAFL-PQKLPA 86
Cdd:TIGR01978 11 EDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGH--PSYevtsGTILFKGQDLLELEPDERARAGLFLaFQYPEE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 87 SAGLTVRELVRLGRFPWRGAlgfwRQQDA-------DIIRAAMDKTGVS-AFADTFVDE-LSGGERQRAWVAMLLAQESP 157
Cdd:TIGR01978 89 IPGVSNLEFLRSALNARRSA----RGEEPldlldfeKLLKEKLALLDMDeEFLNRSVNEgFSGGEKKRNEILQMALLEPK 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 992343279 158 VLILDEPTSALDVQhqyQLMALLAELNQ--KQGCGIIVILHDLNLaLRYAT--HIVALKQGRIAFDGPAtTLADE 228
Cdd:TIGR01978 165 LAILDEIDSGLDID---ALKIVAEGINRlrEPDRSFLIITHYQRL-LNYIKpdYVHVLLDGRIVKSGDV-ELAKE 234
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
22-236 |
1.41e-20 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 90.65 E-value: 1.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 22 LNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLAKAVAFLPQKLPASAGlTVRELVRLGRF 101
Cdd:PRK11160 361 LQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSA-TLRDNLLLAAP 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 102 pwrgalgfwrQQDADIIRAAMDKTGVSAFA------DTFVDE----LSGGERQRAWVAMLLAQESPVLILDEPTSALDVQ 171
Cdd:PRK11160 440 ----------NASDEALIEVLQQVGLEKLLeddkglNAWLGEggrqLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAE 509
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 992343279 172 HQYQLMALLAELnqKQGCGIIVILHDLNlALRYATHIVALKQGRIAFDGPATTL-ADEQRLSDLYQ 236
Cdd:PRK11160 510 TERQILELLAEH--AQNKTVLMITHRLT-GLEQFDRICVMDNGQIIEQGTHQELlAQQGRYYQLKQ 572
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
22-216 |
1.58e-20 |
|
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: 86.57 E-value: 1.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 22 LNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLAkavaflpqKLPASAGL----TVRE-LV 96
Cdd:cd03269 21 FSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRIG--------YLPEERGLypkmKVIDqLV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 97 RLGRFPwrgalGFWRQQDADIIRAAMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSALDVQHQYQL 176
Cdd:cd03269 93 YLAQLK-----GLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 992343279 177 MALLAELnQKQGCGIIVILHDLNLALRYATHIVALKQGRI 216
Cdd:cd03269 168 KDVIREL-ARAGKTVILSTHQMELVEELCDRVLLLNKGRA 206
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
22-221 |
1.89e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 88.24 E-value: 1.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 22 LNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTslssKSLAKAVAFLP------QKlpasagLTVRE- 94
Cdd:COG4152 22 FTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD----PEDRRRIGYLPeerglyPK------MKVGEq 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 95 LVRLGRFpwRGalgfwrQQDADIIRAA---MDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSALDVQ 171
Cdd:COG4152 92 LVYLARL--KG------LSKAEAKRRAdewLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPV 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 992343279 172 HQYQLMALLAELNQKqgcGIIVIL--HDLNLALRYATHIVALKQGRIAFDGP 221
Cdd:COG4152 164 NVELLKDVIRELAAK---GTTVIFssHQMELVEELCDRIVIINKGRKVLSGS 212
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-209 |
2.23e-20 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 86.00 E-value: 2.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 1 MFTLSGVEMVRGGRRILAIEQLNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPD---TGSVWLNDAPLTSLssKSLAKAV 77
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTAL--PAEQRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 78 AFLPQKLPASAGLTVRELVRLGRFPwrgalGFWRQQDADIIRAAMDKTGVSAFADTFVDELSGGERQR-AWVAMLLAQes 156
Cdd:COG4136 79 GILFQDDLLFPHLSVGENLAFALPP-----TIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARvALLRALLAE-- 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 992343279 157 P-VLILDEPTSALDVQHQYQLMALLaeLNQKQGCGIIVIL--HDLNLALRYATHIV 209
Cdd:COG4136 152 PrALLLDEPFSKLDAALRAQFREFV--FEQIRQRGIPALLvtHDEEDAPAAGRVLD 205
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
12-198 |
2.24e-20 |
|
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: 89.73 E-value: 2.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 12 GGRRILAIEQLNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLAKAVAFLPQKlPASAGLT 91
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQD-AHLFDTT 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 92 VRELVRLGRFPWRGALGFW---RQQDADIIRAAMDKtgvsafADTFVDE----LSGGERQRAWVAMLLAQESPVLILDEP 164
Cdd:TIGR02868 425 VRENLRLARPDATDEELWAaleRVGLADWLRALPDG------LDTVLGEggarLSGGERQRLALARALLADAPILLLDEP 498
|
170 180 190
....*....|....*....|....*....|....
gi 992343279 165 TSALDVQHQYQLMALLaeLNQKQGCGIIVILHDL 198
Cdd:TIGR02868 499 TEHLDAETADELLEDL--LAALSGRTVVLITHHL 530
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
32-230 |
2.29e-20 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 88.25 E-value: 2.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 32 VLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLAKavafLPQKL------PASA---GLTVRELVRlgrFP 102
Cdd:COG4608 49 LVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRP----LRRRMqmvfqdPYASlnpRMTVGDIIA---EP 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 103 WR--GALGfwRQQDADIIRAAMDKTGVSA-FADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSALDVQHQYQLMAL 179
Cdd:COG4608 122 LRihGLAS--KAERRERVAELLELVGLRPeHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNL 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 992343279 180 LAELNQKQGCGIIVILHDLNLaLRYATHIVA---LkqGRIAFDGPATTLADEQR 230
Cdd:COG4608 200 LEDLQDELGLTYLFISHDLSV-VRHISDRVAvmyL--GKIVEIAPRDELYARPL 250
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
12-220 |
3.78e-20 |
|
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: 85.35 E-value: 3.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 12 GGRRILAIEQLNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSK-----SLAKAVAFLPQklpa 86
Cdd:cd03268 11 GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEAlrrigALIEAPGFYPN---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 87 sagLTVRE-LVRLGRfpwrgALGFWRQqdadIIRAAMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPT 165
Cdd:cd03268 87 ---LTAREnLRLLAR-----LLGIRKK----RIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPT 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 992343279 166 SALDVQHQYQLMALLAELNqKQGCGIIVILHDLNLALRYATHIVALKQGRIAFDG 220
Cdd:cd03268 155 NGLDPDGIKELRELILSLR-DQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
3-219 |
5.43e-20 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 86.27 E-value: 5.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 3 TLSGVEMVRGGRRILAIEQLNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSlsskslakavaflpq 82
Cdd:PRK11247 14 LLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAE--------------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 83 klpasagltVRELVRL----GRF-PWR--------GALGFWRQQdadiIRAAMDKTGVSAFADTFVDELSGGERQRAWVA 149
Cdd:PRK11247 79 ---------AREDTRLmfqdARLlPWKkvidnvglGLKGQWRDA----ALQALAAVGLADRANEWPAALSGGQKQRVALA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 150 MLLAQESPVLILDEPTSALDVQHQYQLMALLAELNQKQGCGIIVILHDLNLALRYATHIVALKQGRIAFD 219
Cdd:PRK11247 146 RALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLD 215
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
14-220 |
6.84e-20 |
|
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: 85.11 E-value: 6.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 14 RRILAIEQL--NIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLndAPLTSLSSKSLAKA-VAFLPQKLPASAGL 90
Cdd:cd03266 16 KTVQAVDGVsfTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATV--DGFDVVKEPAEARRrLGFVSDSTGLYDRL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 91 TVRELVR-LGRFpwrgaLGFWRQQDADIIRAAMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSALD 169
Cdd:cd03266 94 TARENLEyFAGL-----YGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 992343279 170 VQHQYQLMALLAELnQKQGCGIIVILHDLNLALRYATHIVALKQGRIAFDG 220
Cdd:cd03266 169 VMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
17-198 |
7.72e-20 |
|
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: 88.30 E-value: 7.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 17 LAIEQLNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVwlnDAPLTslsskslakaVAFLPQKLPASAGLTVRELV 96
Cdd:COG1245 356 LEVEGGEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV---DEDLK----------ISYKPQYISPDYDGTVEEFL 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 97 RlgrfpwrGALG------FWRqqdADIIRaamdKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSALDV 170
Cdd:COG1245 423 R-------SANTddfgssYYK---TEIIK----PLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDV 488
|
170 180
....*....|....*....|....*...
gi 992343279 171 QHQYQLMALLAELNQKQGCGIIVILHDL 198
Cdd:COG1245 489 EQRLAVAKAIRRFAENRGKTAMVVDHDI 516
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
12-216 |
1.18e-19 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 84.54 E-value: 1.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 12 GGRRILAIEQLNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKS---LAKAVAFLPQKLPASA 88
Cdd:PRK10908 13 GGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQIGMIFQDHHLLM 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 89 GLTVRELVRLGrFPWRGALGfwrqqdADIIR---AAMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPT 165
Cdd:PRK10908 93 DRTVYDNVAIP-LIIAGASG------DDIRRrvsAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPT 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 992343279 166 SALDVQHQYQLMALLAELNqKQGCGIIVILHDLNLALRYATHIVALKQGRI 216
Cdd:PRK10908 166 GNLDDALSEGILRLFEEFN-RVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
28-222 |
1.52e-19 |
|
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: 87.50 E-value: 1.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 28 ELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLAKAVAFLPQklpaSAGL---TVRElvRLGRFPwr 104
Cdd:COG4618 359 EVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQ----DVELfdgTIAE--NIARFG-- 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 105 galgfwrqqDAD---IIRAAMdKTGVSAFA-------DTFVDE----LSGGERQRAWVAMLLAQESPVLILDEPTSALDV 170
Cdd:COG4618 431 ---------DADpekVVAAAK-LAGVHEMIlrlpdgyDTRIGEggarLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDD 500
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 992343279 171 QHQYQLMALLAELnQKQGCGIIVILHDLNLaLRYATHIVALKQGRIAFDGPA 222
Cdd:COG4618 501 EGEAALAAAIRAL-KARGATVVVITHRPSL-LAAVDKLLVLRDGRVQAFGPR 550
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
15-241 |
1.95e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 85.44 E-value: 1.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 15 RILAIEQLNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDA-------------------------PLTSLS 69
Cdd:PRK13645 25 KALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYaipanlkkikevkrlrkeiglvfqfPEYQLF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 70 SKSLAKAVAFLPQKLPASAGLTVRELVRLgrfpwrgalgfwrqqdADIIRAAMDKTGVSAFadtfvdELSGGERQRAWVA 149
Cdd:PRK13645 105 QETIEKDIAFGPVNLGENKQEAYKKVPEL----------------LKLVQLPEDYVKRSPF------ELSGGQKRRVALA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 150 MLLAQESPVLILDEPTSALDVQHQYQLMALLAELNQKQGCGIIVILHDLNLALRYATHIVALKQGRIAFDG-PATTLADE 228
Cdd:PRK13645 163 GIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGsPFEIFSNQ 242
|
250
....*....|...
gi 992343279 229 QRLSDLYQTPITL 241
Cdd:PRK13645 243 ELLTKIEIDPPKL 255
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
4-198 |
2.70e-19 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 86.60 E-value: 2.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 4 LSGVEMVRGGRRILAIEQLNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLAKA-VAFLPQ 82
Cdd:PRK10762 7 LKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAgIGIIHQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 83 KLPASAGLTVRELVRLGRFPwRGALGF--WRQ--QDADIIRAamdKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPV 158
Cdd:PRK10762 87 ELNLIPQLTIAENIFLGREF-VNRFGRidWKKmyAEADKLLA---RLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKV 162
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 992343279 159 LILDEPTSALDVQHQYQLMALLAELnQKQGCGIIVILHDL 198
Cdd:PRK10762 163 IIMDEPTDALTDTETESLFRVIREL-KSQGRGIVYISHRL 201
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
14-217 |
6.22e-19 |
|
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.
Pssm-ID: 274374 [Multi-domain] Cd Length: 220 Bit Score: 82.37 E-value: 6.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 14 RRILAIEQLNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLAKA---VAFLPQKLPASAGL 90
Cdd:TIGR02982 18 KQVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGASKKQLVQLrrrIGYIFQAHNLLGFL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 91 TVRELVRLGrfpWRGALGFWRQQDADIIRAAMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSALDV 170
Cdd:TIGR02982 98 TARQNVQMA---LELQPNLSYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHHPKLVLADEPTAALDS 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 992343279 171 QHQYQLMALLAELNQKQGCGIIVILHDlNLALRYATHIVALKQGRIA 217
Cdd:TIGR02982 175 KSGRDVVELMQKLAKEQGCTILMVTHD-NRILDVADRILQMEDGKLL 220
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
32-225 |
6.89e-19 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 85.51 E-value: 6.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 32 VLGHNGSGKSTL----VSLLsgqqaPDTGSVWLNDAPLTSLSSKSLAKA-----VAFlpQKlPASA---GLTVRELVRLG 99
Cdd:COG4172 317 LVGESGSGKSTLglalLRLI-----PSEGEIRFDGQDLDGLSRRALRPLrrrmqVVF--QD-PFGSlspRMTVGQIIAEG 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 100 RFPWRGALGfwRQQDADIIRAAMDKTGVS-AFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSALDVQHQYQLMA 178
Cdd:COG4172 389 LRVHGPGLS--AAERRARVAEALEEVGLDpAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILD 466
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 992343279 179 LLAELNQKQGCGIIVILHDLNLAlRYATH-IVALKQGRIAFDGPATTL 225
Cdd:COG4172 467 LLRDLQREHGLAYLFISHDLAVV-RALAHrVMVMKDGKVVEQGPTEQV 513
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-221 |
9.15e-19 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 84.08 E-value: 9.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 1 MFTLSGVEMV--RGGRRILAIEQ--LNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLAKA 76
Cdd:PRK11153 1 MIELKNISKVfpQGGRTIHALNNvsLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 77 ---VAFLPQKLPASAGLTVRELVRlgrFPWRgaLGFWRQQDadiIRAA----MDKTGVSAFADTFVDELSGGERQRAWVA 149
Cdd:PRK11153 81 rrqIGMIFQHFNLLSSRTVFDNVA---LPLE--LAGTPKAE---IKARvtelLELVGLSDKADRYPAQLSGGQKQRVAIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 992343279 150 MLLAQESPVLILDEPTSALDVQHQYQLMALLAELNQKQGCGIIVILHDLNLALRYATHIVALKQGRIAFDGP 221
Cdd:PRK11153 153 RALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGT 224
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
22-220 |
9.59e-19 |
|
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: 82.38 E-value: 9.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 22 LNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLAKAVAFLPQK------LPASAGLTV-RE 94
Cdd:cd03267 42 FTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVFGQKtqlwwdLPVIDSFYLlAA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 95 LVRL--GRFpwrgalgfwrQQDADIIRAAMDktgVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSALDVQH 172
Cdd:cd03267 122 IYDLppARF----------KKRLDELSELLD---LEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVA 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 992343279 173 QYQLMALLAELNQKQGCGIIVILHDLNLALRYATHIVALKQGRIAFDG 220
Cdd:cd03267 189 QENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
25-258 |
9.72e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 83.31 E-value: 9.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 25 PTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLAKAVAFLPQKLPASA-GLTVRELVRLGRFpw 103
Cdd:PRK13652 28 PRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPDDQIfSPTVEQDIAFGPI-- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 104 rgALGFWRQQDADIIRAAMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSALDVQHQYQLMALLAEL 183
Cdd:PRK13652 106 --NLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDL 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 992343279 184 NQKQGCGIIVILHDLNLALRYATHIVALKQGRIAFDGPATTLADEQRLsdLYQTPITLIDHPHAVSEATTNKVAI 258
Cdd:PRK13652 184 PETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQPDL--LARVHLDLPSLPKLIRSLQAQGIAI 256
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
6-229 |
1.18e-18 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 82.89 E-value: 1.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 6 GVEMVRGGRRILAIEQLNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSL---AKAVAFLPQ 82
Cdd:PRK11831 12 GVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRKRMSMLFQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 83 KLPASAGLTVRELVrlgRFPWRGAlgfwRQQDADIIRAA----MDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPV 158
Cdd:PRK11831 92 SGALFTDMNVFDNV---AYPLREH----TQLPAPLLHSTvmmkLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 992343279 159 LILDEPTSALDVQHQYQLMALLAELNQKQGCGIIVILHDLNLALRYATHIVALKQGRIAFDGPATTLADEQ 229
Cdd:PRK11831 165 IMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANP 235
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
12-222 |
1.27e-18 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 84.71 E-value: 1.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 12 GGRRILAIEQLNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLAKAVAFLPQKLPASAGLT 91
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTV 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 92 VRELVRLGRFPwrgalgfwrqqDADIIRAAMDKTGVSAFA-------DTFVDE----LSGGERQRAWVAMLLAQESPVLI 160
Cdd:TIGR01842 409 AENIARFGENA-----------DPEKIIEAAKLAGVHELIlrlpdgyDTVIGPggatLSGGQRQRIALARALYGDPKLVV 477
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 992343279 161 LDEPTSALDVQHQYQLMALLAELnQKQGCGIIVILHDLNLaLRYATHIVALKQGRIAFDGPA 222
Cdd:TIGR01842 478 LDEPNSNLDEEGEQALANAIKAL-KARGITVVVITHRPSL-LGCVDKILVLQDGRIARFGER 537
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
28-229 |
1.32e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 84.72 E-value: 1.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 28 ELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLS-SKSLAKAVAFLPQKLPASAGLTVRE--LVRLGRfpwr 104
Cdd:PRK15439 38 EVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTpAKAHQLGIYLVPQEPLLFPNLSVKEniLFGLPK---- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 105 galgfwRQQDADIIRAAMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSALDVQHQYQLMALLAELn 184
Cdd:PRK15439 114 ------RQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPAETERLFSRIREL- 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 992343279 185 QKQGCGIIVILHDLNLALRYATHIVALKQGRIAFDGPATTLADEQ 229
Cdd:PRK15439 187 LAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTDD 231
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
30-216 |
1.47e-18 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 84.63 E-value: 1.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 30 TVVL-GHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLAKAVAFLPQKlpasAGL---TVRELVRLGRfP--- 102
Cdd:PRK13657 363 TVAIvGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQD----AGLfnrSIEDNIRVGR-Pdat 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 103 ---WRGALGfwRQQDADIIRAAMDKTgvsafaDTFVDE----LSGGERQRAWVAMLLAQESPVLILDEPTSALDVQHQYQ 175
Cdd:PRK13657 438 deeMRAAAE--RAQAHDFIERKPDGY------DTVVGErgrqLSGGERQRLAIARALLKDPPILILDEATSALDVETEAK 509
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 992343279 176 LMALLAELnqKQGCGIIVILHDLNlALRYATHIVALKQGRI 216
Cdd:PRK13657 510 VKAALDEL--MKGRTTFIIAHRLS-TVRNADRILVFDNGRV 547
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
13-210 |
1.59e-18 |
|
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: 84.60 E-value: 1.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 13 GRRILaIEQLN--IPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAplTSLS-----------SKSLAKAVaf 79
Cdd:TIGR03719 333 GDKLL-IDDLSfkLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGET--VKLAyvdqsrdaldpNKTVWEEI-- 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 80 lpqklpaSAGLTVREL--------VRLGRFPWRGAlgfwRQQdadiiraamdktgvsafadTFVDELSGGERQRAWVAML 151
Cdd:TIGR03719 408 -------SGGLDIIKLgkreipsrAYVGRFNFKGS----DQQ-------------------KKVGQLSGGERNRVHLAKT 457
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 992343279 152 LAQESPVLILDEPTSALDVQhqyQLMALLAELNQKQGCgIIVILHDLNLALRYATHIVA 210
Cdd:TIGR03719 458 LKSGGNVLLLDEPTNDLDVE---TLRALEEALLNFAGC-AVVISHDRWFLDRIATHILA 512
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
37-224 |
2.26e-18 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 83.91 E-value: 2.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 37 GSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLS-SKSLAKAVAFLPQ--KlpaSAGL----TVRE---LVRLGRFPWRGA 106
Cdd:COG1129 288 GAGRTELARALFGADPADSGEIRLDGKPVRIRSpRDAIRAGIAYVPEdrK---GEGLvldlSIREnitLASLDRLSRGGL 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 107 LGfwRQQDADIIRAAMDKTGVSAF-ADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSALDV---QHQYQLMALLAE 182
Cdd:COG1129 365 LD--RRRERALAEEYIKRLRIKTPsPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVgakAEIYRLIRELAA 442
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 992343279 183 lnqkQGCGIIVILHDLNLALRYATHIVALKQGRIA--FDGPATT 224
Cdd:COG1129 443 ----EGKAVIVISSELPELLGLSDRILVMREGRIVgeLDREEAT 482
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-229 |
2.58e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 82.96 E-value: 2.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 4 LSGVEMVRGGRRILAIEQLNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSlSSKSLAKAVAFLPQK 83
Cdd:PRK13536 44 LAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIGVVPQF 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 84 LPASAGLTVRE-LVRLGRFpwrgaLGFWRQQDADIIRAAMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILD 162
Cdd:PRK13536 123 DNLDLEFTVREnLLVFGRY-----FGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILD 197
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 992343279 163 EPTSALDVQHQY----QLMALLAelnqkQGCGIIVILHDLNLALRYATHIVALKQGRIAFDGPATTLADEQ 229
Cdd:PRK13536 198 EPTTGLDPHARHliweRLRSLLA-----RGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDEH 263
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
4-223 |
2.63e-18 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 81.21 E-value: 2.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 4 LSGVEMVRGGRRILAIEQLNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLtSLSSKSLAKAVAFLPQK 83
Cdd:COG4161 5 LKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQF-DFSQKPSEKAIRLLRQK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 84 L----------PAsagLTVRElvRLGRFPWRgALGFWRQQDadIIRAA--MDKTGVSAFADTFVDELSGGERQRAWVAML 151
Cdd:COG4161 84 VgmvfqqynlwPH---LTVME--NLIEAPCK-VLGLSKEQA--REKAMklLARLRLTDKADRFPLHLSGGQQQRVAIARA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 152 LAQESPVLILDEPTSALDVQHQYQLMALLAELNQKqgcGI--IVILHDLNLALRYATHIVALKQGRI-------AFDGPA 222
Cdd:COG4161 156 LMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQT---GItqVIVTHEVEFARKVASQVVYMEKGRIieqgdasHFTQPQ 232
|
.
gi 992343279 223 T 223
Cdd:COG4161 233 T 233
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
28-245 |
2.64e-18 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 83.79 E-value: 2.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 28 ELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLAKAVAFLPQklpaSAGL---TVRELVRLGRfpwR 104
Cdd:TIGR01192 362 QTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINTVTRESLRKSIATVFQ----DAGLfnrSIRENIRLGR---E 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 105 GAlgfwrqQDADIIRAAmDKTGVSAFA-------DTFVDE----LSGGERQRAWVAMLLAQESPVLILDEPTSALDVQHQ 173
Cdd:TIGR01192 435 GA------TDEEVYEAA-KAAAAHDFIlkrsngyDTLVGErgnrLSGGERQRLAIARAILKNAPILVLDEATSALDVETE 507
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 992343279 174 YQLMALLAELNQKQGCGIIVilHDLNlALRYATHIVALKQGRIAFDGPATTLADEQ-RLSDLYQTPITLIDHP 245
Cdd:TIGR01192 508 ARVKNAIDALRKNRTTFIIA--HRLS-TVRNADLVLFLDQGRLIEKGSFQELIQKDgRFYKLLRRSGLLTNQP 577
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
12-215 |
3.58e-18 |
|
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: 78.64 E-value: 3.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 12 GGRRILAIEQLNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLtslsskslakaVAFLPQklpasaglt 91
Cdd:cd03221 11 GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVK-----------IGYFEQ--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 92 vrelvrlgrfpwrgalgfwrqqdadiiraamdktgvsafadtfvdeLSGGERQRAWVAMLLAQESPVLILDEPTSALDVQ 171
Cdd:cd03221 71 ----------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLE 104
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 992343279 172 HQyqlMALLAELNQKQGCgIIVILHDLNLALRYATHIVALKQGR 215
Cdd:cd03221 105 SI---EALEEALKEYPGT-VILVSHDRYFLDQVATKIIELEDGK 144
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
12-229 |
3.61e-18 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 80.78 E-value: 3.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 12 GGRRILAIEQLNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLAKA-VAFLPQKLPASAGL 90
Cdd:TIGR04406 12 KKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARLgIGYLPQEASIFRKL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 91 TVRELVR--LGRfpwRGALGfwRQQDADIIRAAMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSAL 168
Cdd:TIGR04406 92 TVEENIMavLEI---RKDLD--RAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDEPFAGV 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 992343279 169 D---VQHQYQLMALLAElnqkQGCGIIVILHDLNLALRYATHIVALKQGRIAFDG-PATTLADEQ 229
Cdd:TIGR04406 167 DpiaVGDIKKIIKHLKE----RGIGVLITDHNVRETLDICDRAYIISDGKVLAEGtPAEIVANEK 227
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
13-236 |
4.62e-18 |
|
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: 80.61 E-value: 4.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 13 GRRILAIEQLNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLAKAVAFLPQKLPASAGlTV 92
Cdd:cd03252 14 GPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGVVLQENVLFNR-SI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 93 RELVRLGRfpwrgalgfwRQQDADIIRAAMDKTGVSAFA-------DTFVDE----LSGGERQRAWVAMLLAQESPVLIL 161
Cdd:cd03252 93 RDNIALAD----------PGMSMERVIEAAKLAGAHDFIselpegyDTIVGEqgagLSGGQRQRIAIARALIHNPRILIF 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 992343279 162 DEPTSALDVQHQYQLMAllaelNQKQGCG---IIVILHDLNlALRYATHIVALKQGRIAFDGPATTLADEQ-RLSDLYQ 236
Cdd:cd03252 163 DEATSALDYESEHAIMR-----NMHDICAgrtVIIIAHRLS-TVKNADRIIVMEKGRIVEQGSHDELLAENgLYAYLYQ 235
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
12-228 |
5.74e-18 |
|
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: 79.49 E-value: 5.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 12 GGRRILAIEQLNIPTNELTVVLGHNGSGKSTLVSLLSGQqaPDT----GSVWLNDAPLTSLSSKSLAKAVAFL-PQKLPA 86
Cdd:cd03217 11 GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGH--PKYevteGEILFKGEDITDLPPEERARLGIFLaFQYPPE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 87 SAGLTVRELVRlgrfpwrgalgfwrqqdadiiraamdktgvsafadtFVDE-LSGGERQRAWVAMLLAQESPVLILDEPT 165
Cdd:cd03217 89 IPGVKNADFLR------------------------------------YVNEgFSGGEKKRNEILQLLLLEPDLAILDEPD 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 992343279 166 SALDVQHQYQLMALLAELNqKQGCGIIVILHDLNLaLRY--ATHIVALKQGRIAFDGPAtTLADE 228
Cdd:cd03217 133 SGLDIDALRLVAEVINKLR-EEGKSVLIITHYQRL-LDYikPDRVHVLYDGRIVKSGDK-ELALE 194
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
32-228 |
5.84e-18 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 81.77 E-value: 5.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 32 VLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLAKAVAFlpQKLPASAGLTVRELVRlgrFPWRgALGFWR 111
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHINMVF--QSYALFPHMTVEENVA---FGLK-MRKVPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 112 QQDADIIRAAMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSALDVQHQYQLMALLAELNQKQGCGI 191
Cdd:TIGR01187 75 AEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITF 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 992343279 192 IVILHDLNLALRYATHIVALKQGRIAFDGPATTLADE 228
Cdd:TIGR01187 155 VFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEE 191
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
13-225 |
6.15e-18 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 80.56 E-value: 6.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 13 GRRILAIEQLNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDapLTSLSSKSLAKAVAfLPQKLPASAGLTV 92
Cdd:PRK11264 15 GQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGD--ITIDTARSLSQQKG-LIRQLRQHVGFVF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 93 RELvrlGRFPWRGAL-----------GFWRQQDADIIRAAMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLIL 161
Cdd:PRK11264 92 QNF---NLFPHRTVLeniiegpvivkGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILF 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 992343279 162 DEPTSALDVQHQYQLMALLAELNQKQGCGIIVIlHDLNLALRYATHIVALKQGRIAFDGPATTL 225
Cdd:PRK11264 169 DEPTSALDPELVGEVLNTIRQLAQEKRTMVIVT-HEMSFARDVADRAIFMDQGRIVEQGPAKAL 231
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
12-216 |
6.97e-18 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 81.67 E-value: 6.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 12 GGRRILAIEQLNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSlaKAVAFLPQKLPASAGLT 91
Cdd:PRK10851 13 GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD--RKVGFVFQHYALFRHMT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 92 VRELVRLGR--FPWRgalgfwRQQDADIIRAA----MDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPT 165
Cdd:PRK10851 91 VFDNIAFGLtvLPRR------ERPNAAAIKAKvtqlLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPF 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 992343279 166 SALDVQHQYQLMALLAELNQKQGCGIIVILHDLNLALRYATHIVALKQGRI 216
Cdd:PRK10851 165 GALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNI 215
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
11-236 |
6.99e-18 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 82.84 E-value: 6.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 11 RGGRRILAIEQLNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLAKAVAFLPQKlPASAGL 90
Cdd:PRK10790 351 RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQD-PVVLAD 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 91 TVRELVRLGRFPWRGALgfWRQ----QDADIIRAAMDktGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTS 166
Cdd:PRK10790 430 TFLANVTLGRDISEEQV--WQAletvQLAELARSLPD--GLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATA 505
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 992343279 167 ALDVQHQYQLMALLAELNQKQgcGIIVILHDLNLALRyATHIVALKQGRIAFDGP-ATTLADEQRLSDLYQ 236
Cdd:PRK10790 506 NIDSGTEQAIQQALAAVREHT--TLVVIAHRLSTIVE-ADTILVLHRGQAVEQGThQQLLAAQGRYWQMYQ 573
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
24-257 |
7.92e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 80.64 E-value: 7.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 24 IPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSS----KSLAKAVAFLPQkLPASAGL--TVRELVR 97
Cdd:PRK13641 30 LEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGnknlKKLRKKVSLVFQ-FPEAQLFenTVLKDVE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 98 LGrfPWRgaLGFWRQQDADIIRAAMDKTGVS-AFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSALDVQHQYQL 176
Cdd:PRK13641 109 FG--PKN--FGFSEDEAKEKALKWLKKVGLSeDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEM 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 177 MALLAELnQKQGCGIIVILHDLNLALRYATHIVALKQGR-IAFDGPATTLADEQRLSDlyqtpitlidhpHAVSEATTNK 255
Cdd:PRK13641 185 MQLFKDY-QKAGHTVILVTHNMDDVAEYADDVLVLEHGKlIKHASPKEIFSDKEWLKK------------HYLDEPATSR 251
|
..
gi 992343279 256 VA 257
Cdd:PRK13641 252 FA 253
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
22-225 |
9.85e-18 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 80.13 E-value: 9.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 22 LNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDT----GSVWLNDAPLTSLSSKslAKAVAFLPQKlPASAGLTVRELVR 97
Cdd:PRK10418 24 LTLQRGRVLALVGGSGSGKSLTCAAALGILPAGVrqtaGRVLLDGKPVAPCALR--GRKIATIMQN-PRSAFNPLHTMHT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 98 LGRFPWRgALGfwRQQDADIIRAAMDKTG---VSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSALDVQHQY 174
Cdd:PRK10418 101 HARETCL-ALG--KPADDATLTAALEAVGlenAARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQA 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 992343279 175 QLMALLAELNQKQGCGIIVILHDLNLALRYATHIVALKQGRIAFDGPATTL 225
Cdd:PRK10418 178 RILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETL 228
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
22-231 |
1.14e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 82.20 E-value: 1.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 22 LNIPTNELTVVLGHNGSGKSTLVSLLSGQqAPDTGSVWLNDAPLTSLSSKSLAKAVAFLPQ--KLPASaglTVRELVRLG 99
Cdd:PRK11174 371 FTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIELRELDPESWRKHLSWVGQnpQLPHG---TLRDNVLLG 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 100 RFpwrgalgfwrQQDADIIRAAMDKTGVSAFA-------DTFVDE----LSGGERQRAWVAMLLAQESPVLILDEPTSAL 168
Cdd:PRK11174 447 NP----------DASDEQLQQALENAWVSEFLpllpqglDTPIGDqaagLSVGQAQRLALARALLQPCQLLLLDEPTASL 516
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 992343279 169 DVQHQYQLMALLAELNQKQGCgiIVILHDLNlALRYATHIVALKQGRIAFDGPATTLADEQRL 231
Cdd:PRK11174 517 DAHSEQLVMQALNAASRRQTT--LMVTHQLE-DLAQWDQIWVMQDGQIVQQGDYAELSQAGGL 576
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
22-216 |
1.14e-17 |
|
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: 78.03 E-value: 1.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 22 LNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLAKAVAFLPQKlpasagltvrelvrlgrf 101
Cdd:cd03246 23 FSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLPQD------------------ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 102 pwrgalgfwrqqdadiiraamdktgVSAFADTFVDE-LSGGERQRAWVAMLLAQESPVLILDEPTSALDVQHQYQLMALL 180
Cdd:cd03246 85 -------------------------DELFSGSIAENiLSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAI 139
|
170 180 190
....*....|....*....|....*....|....*.
gi 992343279 181 AELnQKQGCGIIVILHDLNLaLRYATHIVALKQGRI 216
Cdd:cd03246 140 AAL-KAAGATRIVIAHRPET-LASADRILVLEDGRV 173
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1-201 |
1.32e-17 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 78.69 E-value: 1.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 1 MFTLSGVEMVRGGRRILAIEQLNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSkSLAKAVAFL 80
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRD-EYHQDLLYL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 81 PQKLPASAGLTVRELVRlgrfpWRGALGfwRQQDADIIRAAMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLI 160
Cdd:PRK13538 80 GHQPGIKTELTALENLR-----FYQRLH--GPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWI 152
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 992343279 161 LDEPTSALDVQHQYQLMALLAELNQKQGCGIIVILHDLNLA 201
Cdd:PRK13538 153 LDEPFTAIDKQGVARLEALLAQHAEQGGMVILTTHQDLPVA 193
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
118-215 |
1.72e-17 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 81.29 E-value: 1.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 118 IRAAMDKTGVSAFADTFVD---ELSGGERQRAWVAMLLAQESPVLILDEPTSALDVQHQYQLMALLAELNQKQGCGIIVI 194
Cdd:PRK15134 134 ILNCLDRVGIRQAAKRLTDyphQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFI 213
|
90 100
....*....|....*....|.
gi 992343279 195 LHDLNLALRYATHIVALKQGR 215
Cdd:PRK15134 214 THNLSIVRKLADRVAVMQNGR 234
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
132-223 |
1.77e-17 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 80.17 E-value: 1.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 132 DTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSALDVQHQYQLMALLAELNQKQGCGIIVILHDLNLALRYATHIVAL 211
Cdd:PRK11022 148 DVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVM 227
|
90
....*....|..
gi 992343279 212 KQGRIAFDGPAT 223
Cdd:PRK11022 228 YAGQVVETGKAH 239
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
34-225 |
2.13e-17 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 81.29 E-value: 2.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 34 GHNGSGKST----LVSLLSGQqapdtGSVWLNDAPLTSLSSKSLakavafLPQKL--------PASA---GLTVRELVRL 98
Cdd:PRK15134 319 GESGSGKSTtglaLLRLINSQ-----GEIWFDGQPLHNLNRRQL------LPVRHriqvvfqdPNSSlnpRLNVLQIIEE 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 99 G---RFPWRGAlgfwRQQDADIIrAAMDKTGVSAfaDT---FVDELSGGERQRAWVAMLLAQESPVLILDEPTSALDVQH 172
Cdd:PRK15134 388 GlrvHQPTLSA----AQREQQVI-AVMEEVGLDP--ETrhrYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTV 460
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 992343279 173 QYQLMALLAELNQKQGCGIIVILHDLNLALRYATHIVALKQGRIAFDGPATTL 225
Cdd:PRK15134 461 QAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERV 513
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
28-227 |
2.21e-17 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 81.25 E-value: 2.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 28 ELTVVLGHNGSGKSTLVSLLSGQQAPDT---GSVWLNDAPLTSlssKSLAKAVAFLPQK---LPAsagLTVRE------L 95
Cdd:TIGR00955 52 ELLAVMGSSGAGKTTLMNALAFRSPKGVkgsGSVLLNGMPIDA---KEMRAISAYVQQDdlfIPT---LTVREhlmfqaH 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 96 VRLGRfpwrgalGFWRQQDADIIRAAMDKTGVSAFADT------FVDELSGGERQRAWVAMLLAQESPVLILDEPTSALD 169
Cdd:TIGR00955 126 LRMPR-------RVTKKEKRERVDEVLQALGLRKCANTrigvpgRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLD 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 992343279 170 VQHQYQLMALLAELNQKqGCGIIVILHDLNLAL-RYATHIVALKQGRIAFDGPATTLAD 227
Cdd:TIGR00955 199 SFMAYSVVQVLKGLAQK-GKTIICTIHQPSSELfELFDKIILMAEGRVAYLGSPDQAVP 256
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
22-216 |
3.14e-17 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 80.46 E-value: 3.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 22 LNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLA----KAVAFLPQKLPASAGLTVRELVR 97
Cdd:PRK10070 49 LAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELRevrrKKIAMVFQSFALMPHMTVLDNTA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 98 LGrFPWRGALGFWRQQDAdiiRAAMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSALDVQHQYQLM 177
Cdd:PRK10070 129 FG-MELAGINAEERREKA---LDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQ 204
|
170 180 190
....*....|....*....|....*....|....*....
gi 992343279 178 ALLAELNQKQGCGIIVILHDLNLALRYATHIVALKQGRI 216
Cdd:PRK10070 205 DELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEV 243
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
137-243 |
3.40e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 79.36 E-value: 3.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 137 ELSGGERQRAWVAMLLAQESPVLILDEPTSALDVQHQYQLMALLAELNqKQGCGIIVILHDLNLALRYATHIVALKQGRI 216
Cdd:PRK13651 165 ELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLN-KQGKTIILVTHDLDNVLEWTKRTIFFKDGKI 243
|
90 100
....*....|....*....|....*...
gi 992343279 217 AFDG-PATTLADEQRLSDLYQTPITLID 243
Cdd:PRK13651 244 IKDGdTYDILSDNKFLIENNMEPPKLLN 271
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
27-248 |
4.41e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 79.12 E-value: 4.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 27 NELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLND----------APLTSLSS------KSLAKAVAFLPQkLPASAGL 90
Cdd:PRK13631 52 NKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDiyigdkknnhELITNPYSkkiknfKELRRRVSMVFQ-FPEYQLF 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 91 --TVRELVRLGRFpwrgALGFWRQQDADIIRAAMDKTGVSafaDTFVD----ELSGGERQRAWVAMLLAQESPVLILDEP 164
Cdd:PRK13631 131 kdTIEKDIMFGPV----ALGVKKSEAKKLAKFYLNKMGLD---DSYLErspfGLSGGQKRRVAIAGILAIQPEILIFDEP 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 165 TSALDVQHQYQLMALLAElNQKQGCGIIVILHDLNLALRYATHIVALKQGRIAFDG-PATTLADEqrlsDLYQTpiTLID 243
Cdd:PRK13631 204 TAGLDPKGEHEMMQLILD-AKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGtPYEIFTDQ----HIINS--TSIQ 276
|
....*
gi 992343279 244 HPHAV 248
Cdd:PRK13631 277 VPRVI 281
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
17-198 |
6.25e-17 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 79.85 E-value: 6.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 17 LAIEQLNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVwlnDAPLTslsskslakaVAFLPQKLPASAGLTVRELV 96
Cdd:PRK13409 355 LEVEGGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV---DPELK----------ISYKPQYIKPDYDGTVEDLL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 97 R-----LGRFPWRgalgfwrqqdADIIRaamdKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSALDVQ 171
Cdd:PRK13409 422 RsitddLGSSYYK----------SEIIK----PLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVE 487
|
170 180
....*....|....*....|....*..
gi 992343279 172 HQYQLMALLAELNQKQGCGIIVILHDL 198
Cdd:PRK13409 488 QRLAVAKAIRRIAEEREATALVVDHDI 514
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
32-225 |
6.69e-17 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 77.70 E-value: 6.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 32 VLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSK-------------SLAKAVAFLPQKLPASAGLTVRELVRl 98
Cdd:PRK10619 36 IIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKdgqlkvadknqlrLLRTRLTMVFQHFNLWSHMTVLENVM- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 99 gRFPWRgALGFWRQQDADIIRAAMDKTGVSAFA-DTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSALD---VQHQY 174
Cdd:PRK10619 115 -EAPIQ-VLGLSKQEARERAVKYLAKVGIDERAqGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDpelVGEVL 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 992343279 175 QLMALLAElnqkQGCGIIVILHDLNLALRYATHIVALKQGRIAFDGPATTL 225
Cdd:PRK10619 193 RIMQQLAE----EGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQL 239
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
4-199 |
7.82e-17 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 77.06 E-value: 7.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 4 LSGVEMVRGGRRILAIEQLNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLAKAVAFLPQK 83
Cdd:PRK10247 10 LQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 84 lPASAGLTVRE-LVrlgrFPWRgalgfWRQQ--DADIIRAAMDKTGV-SAFADTFVDELSGGERQRawVAMLL-AQESP- 157
Cdd:PRK10247 90 -PTLFGDTVYDnLI----FPWQ-----IRNQqpDPAIFLDDLERFALpDTILTKNIAELSGGEKQR--ISLIRnLQFMPk 157
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 992343279 158 VLILDEPTSALDVQHQYQLMALLAELNQKQGCGIIVILHDLN 199
Cdd:PRK10247 158 VLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKD 199
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-215 |
1.66e-16 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 76.57 E-value: 1.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 1 MFTLSGVEMVRGGrrILAIEQLNIPTNELTVV--LGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLA-KAV 77
Cdd:PRK11300 5 LLSVSGLMMRFGG--LLAVNNVNLEVREQEIVslIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIArMGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 78 AFLPQKLPASAGLTVRE--LVRLGRFPWRGAL-------GFWRQQDADIIRAA--MDKTGVSAFADTFVDELSGGERQRA 146
Cdd:PRK11300 83 VRTFQHVRLFREMTVIEnlLVAQHQQLKTGLFsgllktpAFRRAESEALDRAAtwLERVGLLEHANRQAGNLAYGQQRRL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 992343279 147 WVAMLLAQESPVLILDEPTSALDVQHQYQLMALLAELNQKQGCGIIVILHDLNLALRYATHIVALKQGR 215
Cdd:PRK11300 163 EIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGT 231
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
13-210 |
1.92e-16 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 78.24 E-value: 1.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 13 GRRILaIEQLN--IPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAplTSLSS-----KSLAkavaflPQKlp 85
Cdd:PRK11819 335 GDRLL-IDDLSfsLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGET--VKLAYvdqsrDALD------PNK-- 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 86 asaglTVRELVRLGrfpwrgalgfwrqqdADII---------RAAmdktgVSAF----ADT--FVDELSGGERQRAWVAM 150
Cdd:PRK11819 404 -----TVWEEISGG---------------LDIIkvgnreipsRAY-----VGRFnfkgGDQqkKVGVLSGGERNRLHLAK 458
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 992343279 151 LLAQESPVLILDEPTSALDVQhqyQLMALLAELNQKQGCgIIVILHD---LNlalRYATHIVA 210
Cdd:PRK11819 459 TLKQGGNVLLLDEPTNDLDVE---TLRALEEALLEFPGC-AVVISHDrwfLD---RIATHILA 514
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
32-228 |
2.27e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 77.15 E-value: 2.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 32 VLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLAKaVAFLPQKLPASAGLTVRE-LVRLGRFpwrgaLGFW 110
Cdd:PRK13537 38 LLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQR-VGVVPQFDNLDPDFTVREnLLVFGRY-----FGLS 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 111 RQQDADIIRAAMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSALDVQHQY----QLMALLAelnqk 186
Cdd:PRK13537 112 AAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHlmweRLRSLLA----- 186
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 992343279 187 QGCGIIVILHDLNLALRYATHIVALKQGR-IAFDGPATTLADE 228
Cdd:PRK13537 187 RGKTILLTTHFMEEAERLCDRLCVIEEGRkIAEGAPHALIESE 229
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
37-216 |
2.30e-16 |
|
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: 74.78 E-value: 2.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 37 GSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLS-SKSLAKAVAFLP---QKLPASAGLTVRELVRLGRFpwrgalgfwrq 112
Cdd:cd03215 36 GNGQTELAEALFGLRPPASGEITLDGKPVTRRSpRDAIRAGIAYVPedrKREGLVLDLSVAENIALSSL----------- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 113 qdadiiraamdktgvsafadtfvdeLSGGERQRAWVAMLLAQESPVLILDEPTSALDV---QHQYQLMALLAElnqkQGC 189
Cdd:cd03215 105 -------------------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVgakAEIYRLIRELAD----AGK 155
|
170 180
....*....|....*....|....*..
gi 992343279 190 GIIVILHDLNLALRYATHIVALKQGRI 216
Cdd:cd03215 156 AVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
18-220 |
2.36e-16 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 78.52 E-value: 2.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 18 AIEQLNIP--TNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSlSSKSLAKAVAFLPQKLPASAGLTVREL 95
Cdd:TIGR01257 945 AVDRLNITfyENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNILFHHLTVAEH 1023
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 96 VRlgrfpWRGALGFWRQQDADI-IRAAMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSALDVQHQY 174
Cdd:TIGR01257 1024 IL-----FYAQLKGRSWEEAQLeMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRR 1098
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 992343279 175 QLMALLaeLNQKQGCGIIVILHDLNLALRYATHIVALKQGRIAFDG 220
Cdd:TIGR01257 1099 SIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSG 1142
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
28-220 |
3.09e-16 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 78.00 E-value: 3.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 28 ELTVVLGHNGSGKSTLVSLLSG--QQAPDTGSVWLNDAPLTslssKSLAKAVAFLPQKLPASAGLTVRE---LVRLGRFP 102
Cdd:PLN03211 95 EILAVLGPSGSGKSTLLNALAGriQGNNFTGTILANNRKPT----KQILKRTGFVTQDDILYPHLTVREtlvFCSLLRLP 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 103 wrgaLGFWRQQ-----DADIIRAAMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSALDVQHQYQLM 177
Cdd:PLN03211 171 ----KSLTKQEkilvaESVISELGLTKCENTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLV 246
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 992343279 178 ALLAELNQKqGCGIIVILHDLNLALRYATH-IVALKQGRIAFDG 220
Cdd:PLN03211 247 LTLGSLAQK-GKTIVTSMHQPSSRVYQMFDsVLVLSEGRCLFFG 289
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
12-226 |
3.25e-16 |
|
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: 75.27 E-value: 3.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 12 GGRRILAIEQLNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLAKA-VAFLPQKLPASAGL 90
Cdd:cd03218 11 GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLgIGYLPQEASIFRKL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 91 TVRELVRLgrfpwrgAL---GFWRQQDADIIRAAMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSA 167
Cdd:cd03218 91 TVEENILA-------VLeirGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAG 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 992343279 168 LD---VQhqyQLMALLAELNQKqGCGIIVILHDLNLALRYATHIVALKQGRIAFDGPATTLA 226
Cdd:cd03218 164 VDpiaVQ---DIQKIIKILKDR-GIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIA 221
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-221 |
3.43e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 75.72 E-value: 3.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 3 TLSGVEMVRGGRRILAIEQLNIPTNELTVVLGHNGSGKSTLVSLLSG-----QQAPDTGSVWLNDAPLTSLSSKSLAKAV 77
Cdd:PRK14247 5 EIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRlielyPEARVSGEVYLDGQDIFKMDVIELRRRV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 78 AF---LPQKLPasaGLTVRELVRLGrfPWRGALGFWRQQDADIIRAAMDKTG----VSAFADTFVDELSGGERQRAWVAM 150
Cdd:PRK14247 85 QMvfqIPNPIP---NLSIFENVALG--LKLNRLVKSKKELQERVRWALEKAQlwdeVKDRLDAPAGKLSGGQQQRLCIAR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 992343279 151 LLAQESPVLILDEPTSALDVQHQYQLMALLAELnqKQGCGIIVILHDLNLALRYATHIVALKQGRIAFDGP 221
Cdd:PRK14247 160 ALAFQPEVLLADEPTANLDPENTAKIESLFLEL--KKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGP 228
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
13-229 |
3.43e-16 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 75.70 E-value: 3.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 13 GRRILAIEQLNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLA-KAVAFLPQKLPASAGLT 91
Cdd:PRK10895 15 GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARArRGIGYLPQEASIFRRLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 92 VRELVrLGRFPWRGALGfwRQQDADIIRAAMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSALDVQ 171
Cdd:PRK10895 95 VYDNL-MAVLQIRDDLS--AEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPI 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 992343279 172 HQYQLMALLAELnQKQGCGIIVILHDLNLALRYATHIVALKQGR-IAFDGPATTLADEQ 229
Cdd:PRK10895 172 SVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGHlIAHGTPTEILQDEH 229
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
32-216 |
4.54e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 75.92 E-value: 4.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 32 VLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLAKAVAFLPQKlPAS--AGLTVRELVRLGrfpwrgaL-- 107
Cdd:PRK13650 38 IIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIGMVFQN-PDNqfVGATVEDDVAFG-------Len 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 108 -GFWRQQDADIIRAAMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSALDVQHQYQLMALLAELNQK 186
Cdd:PRK13650 110 kGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDD 189
|
170 180 190
....*....|....*....|....*....|.
gi 992343279 187 QGCGIIVILHDLN-LALryATHIVALKQGRI 216
Cdd:PRK13650 190 YQMTVISITHDLDeVAL--SDRVLVMKNGQV 218
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
28-216 |
4.87e-16 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 75.35 E-value: 4.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 28 ELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVW--LNDAPLTSLsskslakavaflpqklpasAGLTVRELVRLGRFPWrg 105
Cdd:PRK11701 33 EVLGIVGESGSGKTTLLNALSARLAPDAGEVHyrMRDGQLRDL-------------------YALSEAERRRLLRTEW-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 106 alGFWRQQDADIIRAAmdktgVSAFA------------------DTFVDEL-----------------SGGERQRAWVAM 150
Cdd:PRK11701 92 --GFVHQHPRDGLRMQ-----VSAGGnigerlmavgarhygdirATAGDWLerveidaariddlpttfSGGMQQRLQIAR 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 992343279 151 LLAQESPVLILDEPTSALDVQHQYQLMALLAELNQKQGCGIIVILHDLNLALRYATHIVALKQGRI 216
Cdd:PRK11701 165 NLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRV 230
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
37-231 |
7.36e-16 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 76.60 E-value: 7.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 37 GSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLAKA-VAFLP---QKLPASAGLTVRELVRLGRFPWRGALGFWRQ 112
Cdd:COG3845 294 GNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgVAYIPedrLGRGLVPDMSVAENLILGRYRRPPFSRGGFL 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 113 QDADIIRAAMDKtgVSAF------ADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSALDVQ-----HQyQLMALla 181
Cdd:COG3845 374 DRKAIRAFAEEL--IEEFdvrtpgPDTPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGaiefiHQ-RLLEL-- 448
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 992343279 182 elnQKQGCGIIVILHDLNLALRYATHIVALKQGRIAFDGPATTlADEQRL 231
Cdd:COG3845 449 ---RDAGAAVLLISEDLDEILALSDRIAVMYEGRIVGEVPAAE-ATREEI 494
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
4-221 |
1.00e-15 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 75.75 E-value: 1.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 4 LSGVEMVRGGRRILAIEQLNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSK-----SLAKAVA 78
Cdd:PRK09452 17 LRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAEnrhvnTVFQSYA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 79 FLPQklpasagLTVRELVRLGrfpwrgaLGFWRQQDADIIRAAMDK---TGVSAFADTFVDELSGGERQRAWVAMLLAQE 155
Cdd:PRK09452 97 LFPH-------MTVFENVAFG-------LRMQKTPAAEITPRVMEAlrmVQLEEFAQRKPHQLSGGQQQRVAIARAVVNK 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 992343279 156 SPVLILDEPTSALDVQHQYQLMALLAELNQKQGCGIIVILHDLNLALRYATHIVALKQGRIAFDGP 221
Cdd:PRK09452 163 PKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGT 228
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
12-217 |
1.07e-15 |
|
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: 76.40 E-value: 1.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 12 GGRRILAIEQLNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLAKAVAFLPQKlpasaglT 91
Cdd:COG5265 369 PERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQD-------T 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 92 V------RELVRLGRfPwrGAlgfwrqQDADIIRAAmDKTGVSAF-------ADTFVDE----LSGGERQRAWVAMLLAQ 154
Cdd:COG5265 442 VlfndtiAYNIAYGR-P--DA------SEEEVEAAA-RAAQIHDFieslpdgYDTRVGErglkLSGGEKQRVAIARTLLK 511
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 992343279 155 ESPVLILDEPTSALDVQHQyqlMALLAELNQ-KQGCGIIVILHDLNlALRYATHIVALKQGRIA 217
Cdd:COG5265 512 NPPILIFDEATSALDSRTE---RAIQAALREvARGRTTLVIAHRLS-TIVDADEILVLEAGRIV 571
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
13-220 |
1.11e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 74.74 E-value: 1.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 13 GRRILAIEQLNIPTN--ELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDapLTSLSSKSLakavaflpQKLPASAGL 90
Cdd:PRK13633 20 STEKLALDDVNLEVKkgEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDG--LDTSDEENL--------WDIRNKAGM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 91 T------------VRELVRLGrfPWRgaLGFwrqqDADIIRAAMD----KTGVSAFADTFVDELSGGERQRAWVAMLLAQ 154
Cdd:PRK13633 90 VfqnpdnqivatiVEEDVAFG--PEN--LGI----PPEEIRERVDeslkKVGMYEYRRHAPHLLSGGQKQRVAIAGILAM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 992343279 155 ESPVLILDEPTSALDVQHQYQLMALLAELNQKQGCGIIVILHDLNLALRyATHIVALKQGRIAFDG 220
Cdd:PRK13633 162 RPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEG 226
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
32-198 |
1.32e-15 |
|
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: 75.98 E-value: 1.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 32 VLGHNGSGKSTLVSLLSGQQAPDTGSVwlNDAP-----------------LTSLSSKSLAkaVAFLPQ---KLPASAGLT 91
Cdd:COG1245 104 ILGPNGIGKSTALKILSGELKPNLGDY--DEEPswdevlkrfrgtelqdyFKKLANGEIK--VAHKPQyvdLIPKVFKGT 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 92 VRELvrLGRFPWRGALGfwrqqdaDIIraamDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSALDVq 171
Cdd:COG1245 180 VREL--LEKVDERGKLD-------ELA----EKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDI- 245
|
170 180 190
....*....|....*....|....*....|
gi 992343279 172 hqYQLMA---LLAELnQKQGCGIIVILHDL 198
Cdd:COG1245 246 --YQRLNvarLIREL-AEEGKYVLVVEHDL 272
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
137-198 |
1.75e-15 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 74.76 E-value: 1.75e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 992343279 137 ELSGGERQRAWVAMLLAQESPVLILDEPTSALDVQHQYQLMALLAELNQKQGCGIIVILHDL 198
Cdd:PRK09473 161 EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDL 222
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
13-216 |
2.67e-15 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 75.06 E-value: 2.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 13 GRRILAIEQLN--IPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLAKAVAFLPQKLP----- 85
Cdd:PRK11176 353 GKEVPALRNINfkIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHlfndt 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 86 -------ASAGLTVRElvrlgrfpwrgalgfwrqqdaDIIRAA-----MD-----KTGVsafaDTFVDE----LSGGERQ 144
Cdd:PRK11176 433 ianniayARTEQYSRE---------------------QIEEAArmayaMDfinkmDNGL----DTVIGEngvlLSGGQRQ 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 992343279 145 RAWVAMLLAQESPVLILDEPTSALDVQHQYQLMALLAELnQKQGCgIIVILHDLNlALRYATHIVALKQGRI 216
Cdd:PRK11176 488 RIAIARALLRDSPILILDEATSALDTESERAIQAALDEL-QKNRT-SLVIAHRLS-TIEKADEILVVEDGEI 556
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
11-215 |
2.74e-15 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 72.85 E-value: 2.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 11 RGGRRILAIEQ--LNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDApltsLSSKSLAKAvaflpqklpasa 88
Cdd:COG4778 19 QGGKRLPVLDGvsFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHD----GGWVDLAQA------------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 89 glTVRELVRLGR--------F----PWRGAL----------GFWRQQDADIIRAAMDKTGV-----SAFADTFvdelSGG 141
Cdd:COG4778 83 --SPREILALRRrtigyvsqFlrviPRVSALdvvaepllerGVDREEARARARELLARLNLperlwDLPPATF----SGG 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 992343279 142 ERQRAWVAMLLAQESPVLILDEPTSALDVQHQYQLMALLAELnQKQGCGIIVILHDLNLALRYATHIVALKQGR 215
Cdd:COG4778 157 EQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEA-KARGTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
22-214 |
3.51e-15 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 72.36 E-value: 3.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 22 LNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSV-WLNDAPLTSLSSKSLAK---AVAFLPQKlPASAGLTVRELVR 97
Cdd:cd03290 22 IRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhWSNKNESEPSFEATRSRnrySVAYAAQK-PWLLNATVEENIT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 98 LGRfpwrgalGFWRQQDADIIRAAMDKTGVS--AFAD-TFVDE----LSGGERQRAWVAMLLAQESPVLILDEPTSALDV 170
Cdd:cd03290 101 FGS-------PFNKQRYKAVTDACSLQPDIDllPFGDqTEIGErginLSGGQRQRICVARALYQNTNIVFLDDPFSALDI 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 992343279 171 QHQYQLM-ALLAELNQKQGCGIIVILHDLNLaLRYATHIVALKQG 214
Cdd:cd03290 174 HLSDHLMqEGILKFLQDDKRTLVLVTHKLQY-LPHADWIIAMKDG 217
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
21-203 |
9.74e-15 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 71.35 E-value: 9.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 21 QLNIPTN-ELTV-------VLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLS----SKSLAKAVAFLPQKLPASA 88
Cdd:PRK10584 22 ELSILTGvELVVkrgetiaLIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDeearAKLRAKHVGFVFQSFMLIP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 89 GLTVRELVRLGRFpWRGALGFWRQQDAdiiRAAMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSAL 168
Cdd:PRK10584 102 TLNALENVELPAL-LRGESSRQSRNGA---KALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNL 177
|
170 180 190
....*....|....*....|....*....|....*
gi 992343279 169 DVQHQYQLMALLAELNQKQGCGIIVILHDLNLALR 203
Cdd:PRK10584 178 DRQTGDKIADLLFSLNREHGTTLILVTHDLQLAAR 212
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
28-198 |
1.03e-14 |
|
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: 71.63 E-value: 1.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 28 ELTVVLGHNGSGKSTLVSLLSGQQAPDTGSvwLNDAP-----------------LTSLSSKSLAKAVAflPQ---KLPAS 87
Cdd:cd03236 27 QVLGLVGPNGIGKSTALKILAGKLKPNLGK--FDDPPdwdeildefrgselqnyFTKLLEGDVKVIVK--PQyvdLIPKA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 88 AGLTVRELvrLGRFPWRGALgfwrqqdaDIIraaMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSA 167
Cdd:cd03236 103 VKGKVGEL--LKKKDERGKL--------DEL---VDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSY 169
|
170 180 190
....*....|....*....|....*....|.
gi 992343279 168 LDVQHQYQLMALLAELNqKQGCGIIVILHDL 198
Cdd:cd03236 170 LDIKQRLNAARLIRELA-EDDNYVLVVEHDL 199
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
28-220 |
1.32e-14 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 71.40 E-value: 1.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 28 ELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLAKAV---------AFLPQ------KLPASAGLTV 92
Cdd:TIGR02323 30 EVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAELELYQLSEAErrrlmrtewGFVHQnprdglRMRVSAGANI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 93 RE-LVRLGRFPW---RGALGFWRQqdadiiRAAMDKTGVSAFADTFvdelSGGERQRAWVAMLLAQESPVLILDEPTSAL 168
Cdd:TIGR02323 110 GErLMAIGARHYgniRATAQDWLE------EVEIDPTRIDDLPRAF----SGGMQQRLQIARNLVTRPRLVFMDEPTGGL 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 992343279 169 DVQHQYQLMALLAELNQKQGCGIIVILHDLNLALRYATHIVALKQGRIAFDG 220
Cdd:TIGR02323 180 DVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESG 231
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
34-215 |
1.74e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 72.65 E-value: 1.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 34 GHNGSGKSTLVSLLSGQQAPDT--GSVWLNDAPLTSLSSK-SLAKAVAFLPQKLPASAGLTVRELVRLGRFPWRGALGFW 110
Cdd:PRK13549 38 GENGAGKSTLMKVLSGVYPHGTyeGEIIFEGEELQASNIRdTERAGIAIIHQELALVKELSVLENIFLGNEITPGGIMDY 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 111 rqqDADIIRAA--MDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSALDVQHQYQLMALLAELnQKQG 188
Cdd:PRK13549 118 ---DAMYLRAQklLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDL-KAHG 193
|
170 180
....*....|....*....|....*..
gi 992343279 189 CGIIVILHDLNLALRYATHIVALKQGR 215
Cdd:PRK13549 194 IACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
21-215 |
2.36e-14 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 72.07 E-value: 2.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 21 QLNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSK-SLAKAVAFLPQKLPASAGLTVRELVRLG 99
Cdd:PRK10982 18 NLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKeALENGISMVHQELNLVLQRSVMDNMWLG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 100 RFPWRgalGFWRQQDA--DIIRAAMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSAL---DVQHQY 174
Cdd:PRK10982 98 RYPTK---GMFVDQDKmyRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLtekEVNHLF 174
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 992343279 175 QLMALLAElnqkQGCGIIVILHDLNLALRYATHIVALKQGR 215
Cdd:PRK10982 175 TIIRKLKE----RGCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
18-243 |
2.75e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 70.79 E-value: 2.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 18 AIEQLN--IPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSS-KSLAKAVAFLPQKlPAS--AGLTV 92
Cdd:PRK13644 17 ALENINlvIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKlQGIRKLVGIVFQN-PETqfVGRTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 93 RELVRLGrfPWRgaLGFWRQQDADIIRAAMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSALDVQH 172
Cdd:PRK13644 96 EEDLAFG--PEN--LCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDS 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 992343279 173 QYQLMALLAELNQKqGCGIIVILHDLNlALRYATHIVALKQGRIAFDGPATTLADEQRLSDLYQTPITLID 243
Cdd:PRK13644 172 GIAVLERIKKLHEK-GKTIVYITHNLE-ELHDADRIIVMDRGKIVLEGEPENVLSDVSLQTLGLTPPSLIE 240
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
28-232 |
3.13e-14 |
|
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: 71.78 E-value: 3.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 28 ELTVVLGHNGSGKSTLVSLLSGQ-QAPDTGSVWLNDAPLTSLS-SKSLAKAVAFLPQK------LPASAGLTVRELVRLG 99
Cdd:TIGR02633 287 EILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPVDIRNpAQAIRAGIAMVPEDrkrhgiVPILGVGKNITLSVLK 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 100 RFPWRGALGFWRQQDadIIRAAMDKTGVSAFA-DTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSALDVQHQYQLMA 178
Cdd:TIGR02633 367 SFCFKMRIDAAAELQ--IIGSAIQRLKVKTASpFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYK 444
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 992343279 179 LLAELNQkQGCGIIVILHDLNLALRYATHIVALKQGRIAFDGPATTLADEQRLS 232
Cdd:TIGR02633 445 LINQLAQ-EGVAIIVVSSELAEVLGLSDRVLVIGEGKLKGDFVNHALTQEQVLA 497
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
22-240 |
3.51e-14 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 71.68 E-value: 3.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 22 LNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLAKA----VAFLPQKLPASAGLTVRELVR 97
Cdd:PRK10535 29 LDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQLrrehFGFIFQRYHLLSHLTAAQNVE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 98 LGRFpWRGALGFWRQQDAdiiRAAMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSALDVQHQYQLM 177
Cdd:PRK10535 109 VPAV-YAGLERKQRLLRA---QELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVM 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 992343279 178 ALLAELNQkQGCGIIVILHDLNLALRyATHIVALKQGRIAFDGPATTLADEQRLSDLYQTPIT 240
Cdd:PRK10535 185 AILHQLRD-RGHTVIIVTHDPQVAAQ-AERVIEIRDGEIVRNPPAQEKVNVAGGTEPVVNTAS 245
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
33-221 |
6.23e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 70.12 E-value: 6.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 33 LGHNGSGKSTLVSLLSGQQAPDTGSV-------WLNdapltslsSKSLAK--AVAFlPQK------LPASAGLTV-RELV 96
Cdd:COG4586 54 IGPNGAGKSTTIKMLTGILVPTSGEVrvlgyvpFKR--------RKEFARriGVVF-GQRsqlwwdLPAIDSFRLlKAIY 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 97 RLgrfpwrgalgfwrqqDADIIRAAMDKT----GVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSALDVQH 172
Cdd:COG4586 125 RI---------------PDAEYKKRLDELvellDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVS 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 992343279 173 QYQLMALLAELNQKQGCGIIVILHDLN----LALRyathIVALKQGRIAFDGP 221
Cdd:COG4586 190 KEAIREFLKEYNRERGTTILLTSHDMDdieaLCDR----VIVIDHGRIIYDGS 238
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
19-241 |
1.42e-13 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 69.36 E-value: 1.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 19 IEQLN--IPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKS-----LAKAVAFLPQklpASAGLT 91
Cdd:PRK11432 22 IDNLNltIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQrdicmVFQSYALFPH---MSLGEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 92 VRELVRLgrfpwrgaLGFWRQQDADIIRAAMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSALDVQ 171
Cdd:PRK11432 99 VGYGLKM--------LGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDAN 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 172 HQYQLMALLAELNQKQGCGIIVILHDLNLALRYATHIVALKQGRIAFDGPAttladeqrlSDLYQTPITL 241
Cdd:PRK11432 171 LRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSP---------QELYRQPASR 231
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
21-219 |
1.43e-13 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 69.52 E-value: 1.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 21 QLNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKslakavAFLPQklpasagltvrELVRLG- 99
Cdd:PRK11144 18 NLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKG------ICLPP-----------EKRRIGy 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 100 -----R-FPW---RGAL-----GFWRQQDADIIRAamdkTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPT 165
Cdd:PRK11144 81 vfqdaRlFPHykvRGNLrygmaKSMVAQFDKIVAL----LGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 992343279 166 SALDVQHQYQLMALLAELNQKQGCGIIVILHDLNLALRYATHIVALKQGRI-AFD 219
Cdd:PRK11144 157 ASLDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVkAFG 211
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
16-215 |
1.98e-13 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 67.11 E-value: 1.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 16 ILAIEQLNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNdapltslsskslaKAVAFLPQK---LPAsaglTV 92
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVP-------------GSIAYVSQEpwiQNG----TI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 93 RELVRLGRfPWrgalgfwrqqDAD----IIRAAMDKTGVSAFAD---TFVDE----LSGGERQRAWVAMLLAQESPVLIL 161
Cdd:cd03250 83 RENILFGK-PF----------DEEryekVIKACALEPDLEILPDgdlTEIGEkginLSGGQKQRISLARAVYSDADIYLL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 992343279 162 DEPTSALDV---QHQYQ--LMALLaeLNQKQgcgIIVILHDLNLaLRYATHIVALKQGR 215
Cdd:cd03250 152 DDPLSAVDAhvgRHIFEncILGLL--LNNKT---RILVTHQLQL-LPHADQIVVLDNGR 204
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
22-220 |
2.93e-13 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 69.42 E-value: 2.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 22 LNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWlndapltslssksLAKAVAFLPQKlpasagltvrelvrlgrf 101
Cdd:PTZ00243 681 VSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW-------------AERSIAYVPQQ------------------ 729
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 102 PW------RGALGFWRQQDA----DIIRAAM---DKTGVSAFADTFVDE----LSGGERQRAWVAMLLAQESPVLILDEP 164
Cdd:PTZ00243 730 AWimnatvRGNILFFDEEDAarlaDAVRVSQleaDLAQLGGGLETEIGEkgvnLSGGQKARVSLARAVYANRDVYLLDDP 809
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 992343279 165 TSALDVqHQYQLMALLAELNQKQGCGIIVILHDLNLALRyATHIVALKQGRIAFDG 220
Cdd:PTZ00243 810 LSALDA-HVGERVVEECFLGALAGKTRVLATHQVHVVPR-ADYVVALGDGRVEFSG 863
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
137-215 |
3.07e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 69.11 E-value: 3.07e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 992343279 137 ELSGGERQRAWVAMLLAQESPVLILDEPTSALDVQHQYQLMALLAELNQKQGCGIIVILHDLNLALRYATHIVALKQGR 215
Cdd:PRK10261 168 QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGE 246
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
32-225 |
4.37e-13 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 67.68 E-value: 4.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 32 VLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSS---KSLAKAVAFLPQKLPASagLTVRELVR--LGRfPWRGA 106
Cdd:PRK11308 46 VVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPeaqKLLRQKIQIVFQNPYGS--LNPRKKVGqiLEE-PLLIN 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 107 LGFWRQQDADIIRAAMDKTGVSA-FADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSALDVQHQYQLMALLAELNQ 185
Cdd:PRK11308 123 TSLSAAERREKALAMMAKVGLRPeHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQ 202
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 992343279 186 KQGCGIIVILHDLNLALRYATHIVALKQGRIAFDGPATTL 225
Cdd:PRK11308 203 ELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQI 242
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
19-225 |
4.48e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 67.43 E-value: 4.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 19 IEQLN-----IPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLAKAVAFLPQKlPAS--AGLT 91
Cdd:PRK13642 20 VNQLNgvsfsITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQN-PDNqfVGAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 92 VRELVRLGRfpwrGALGFWRQQDADIIRAAMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSALDVQ 171
Cdd:PRK13642 99 VEDDVAFGM----ENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPT 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 992343279 172 HQYQLMALLAELNQKQGCGIIVILHDLNLALRyATHIVALKQGRIAFDGPATTL 225
Cdd:PRK13642 175 GRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSEL 227
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
13-214 |
6.10e-13 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 67.91 E-value: 6.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 13 GRRILAIEQLNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDApltslsskslaKAVAFLPQK--LPASagl 90
Cdd:COG4178 375 GRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAG-----------ARVLFLPQRpyLPLG--- 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 91 TVRELVRLGRFPwrgalgfwRQQDADIIRAAMDKTGVSAFA---DTFVD---ELSGGERQRAWVAMLLAQESPVLILDEP 164
Cdd:COG4178 441 TLREALLYPATA--------EAFSDAELREALEAVGLGHLAerlDEEADwdqVLSLGEQQRLAFARLLLHKPDWLFLDEA 512
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 992343279 165 TSALDVQHQYQLMALLAElnQKQGCGIIVILHDLNLAlRYATHIVALKQG 214
Cdd:COG4178 513 TSALDEENEAALYQLLRE--ELPGTTVISVGHRSTLA-AFHDRVLELTGD 559
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
32-198 |
6.65e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 67.91 E-value: 6.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 32 VLGHNGSGKSTLVSLLSGQQAPDTGSVwlNDAP-----------------LTSLSSKSLAkaVAFLPQ---KLPASAGLT 91
Cdd:PRK13409 104 ILGPNGIGKTTAVKILSGELIPNLGDY--EEEPswdevlkrfrgtelqnyFKKLYNGEIK--VVHKPQyvdLIPKVFKGK 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 92 VRELVRlgRFPWRGALGfwrqqdaDIIraamDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSALDVq 171
Cdd:PRK13409 180 VRELLK--KVDERGKLD-------EVV----ERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDI- 245
|
170 180 190
....*....|....*....|....*....|
gi 992343279 172 hqYQLMA---LLAELNQKQgcGIIVILHDL 198
Cdd:PRK13409 246 --RQRLNvarLIRELAEGK--YVLVVEHDL 271
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
8-206 |
7.74e-13 |
|
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: 64.69 E-value: 7.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 8 EMVRGGRRILAIEQ-LNIPTNELTVVLGHNGSGKSTLVsllsgqqapdtgsvwlndapltslsskslaKAVAFLpqKLPA 86
Cdd:cd03227 1 KIVLGRFPSYFVPNdVTFGEGSLTIITGPNGSGKSTIL------------------------------DAIGLA--LGGA 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 87 SAGLTVRELVRLGrfpwrgalgfwrqqdadIIRAAmdktgVSAFADTFVDELSGGERQRAWVAMLLA----QESPVLILD 162
Cdd:cd03227 49 QSATRRRSGVKAG-----------------CIVAA-----VSAELIFTRLQLSGGEKELSALALILAlaslKPRPLYILD 106
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 992343279 163 EPTSALDVQHQYQLMALLAELNQKqGCGIIVILHDLNLALRYAT 206
Cdd:cd03227 107 EIDRGLDPRDGQALAEAILEHLVK-GAQVIVITHLPELAELADK 149
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
37-231 |
1.01e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 67.24 E-value: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 37 GSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLAKA-VAFLPQKLPAS---AGLTVRELVRLGRFPWRGALGF--- 109
Cdd:PRK11288 289 GAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRAgIMLCPEDRKAEgiiPVHSVADNINISARRHHLRAGClin 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 110 --WRQQDADIIRAAMD-KTgvsAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSALDV--QHQ-YQLMALLAEl 183
Cdd:PRK11288 369 nrWEAENADRFIRSLNiKT---PSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVgaKHEiYNVIYELAA- 444
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 992343279 184 nqkQGCGIIVILHDLNLALRYATHIVALKQGRIAFDGPATTlADEQRL 231
Cdd:PRK11288 445 ---QGVAVLFVSSDLPEVLGVADRIVVMREGRIAGELAREQ-ATERQA 488
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
37-229 |
1.08e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 67.26 E-value: 1.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 37 GSGKSTLVSLLSGQ-QAPDTGSVWLNDAPLT-SLSSKSLAKAVAFLPQK---------LPASAGLTvreLVRLGRFPWRG 105
Cdd:PRK13549 298 GAGRTELVQCLFGAyPGRWEGEIFIDGKPVKiRNPQQAIAQGIAMVPEDrkrdgivpvMGVGKNIT---LAALDRFTGGS 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 106 ALGFWRQQDadIIRAAMDKTGV-SAFADTFVDELSGGERQRAWVA-MLLAQESpVLILDEPTSALDVQHQYQLMALLAEL 183
Cdd:PRK13549 375 RIDDAAELK--TILESIQRLKVkTASPELAIARLSGGNQQKAVLAkCLLLNPK-ILILDEPTRGIDVGAKYEIYKLINQL 451
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 992343279 184 NQkQGCGIIVILHDLNLALRYATHIVALKQGRIAFDGPATTLADEQ 229
Cdd:PRK13549 452 VQ-QGVAIIVISSELPEVLGLSDRVLVMHEGKLKGDLINHNLTQEQ 496
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
15-211 |
1.60e-12 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 66.08 E-value: 1.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 15 RILAIEQLNIPTNELTV--VLGHNGSGKSTLVSLLSGQQaPDTGSV-----WLNDAPLTSLSSKS----LAKAVAF---- 79
Cdd:COG4170 19 RVKAVDRVSLTLNEGEIrgLVGESGSGKSLIAKAICGIT-KDNWHVtadrfRWNGIDLLKLSPRErrkiIGREIAMifqe 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 80 --------------LPQKLPASaglTVRelvrlGRFpWRGAlgFWRQQDAdiiRAAMDKTGV---SAFADTFVDELSGGE 142
Cdd:COG4170 98 psscldpsakigdqLIEAIPSW---TFK-----GKW-WQRF--KWRKKRA---IELLHRVGIkdhKDIMNSYPHELTEGE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 992343279 143 RQRAWVAMLLAQESPVLILDEPTSALDVQHQYQLMALLAELNQKQGCGIIVILHDLNLALRYATHIVAL 211
Cdd:COG4170 164 CQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVL 232
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
32-216 |
1.94e-12 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 65.20 E-value: 1.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 32 VLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLAKAVAFLPQKlpASAGLTVRElvRLGR---FPWRGALG 108
Cdd:PRK15112 44 IIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQD--PSTSLNPRQ--RISQildFPLRLNTD 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 109 FWRQQDADIIRAAMDKTGVSA-FADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSALDVQHQYQLMALLAELNQKQ 187
Cdd:PRK15112 120 LEPEQREKQIIETLRQVGLLPdHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQ 199
|
170 180
....*....|....*....|....*....
gi 992343279 188 GCGIIVILHDLNLALRYATHIVALKQGRI 216
Cdd:PRK15112 200 GISYIYVTQHLGMMKHISDQVLVMHQGEV 228
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
32-220 |
2.65e-12 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 66.11 E-value: 2.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 32 VLGHNGSGKSTLVSLLSGQQAPDTGSVWLndapltslsskSLAKAVAFLPQKLPASAGLTVRELVRLGRFPWRGALGFWR 111
Cdd:TIGR03719 36 VLGLNGAGKSTLLRIMAGVDKDFNGEARP-----------QPGIKVGYLPQEPQLDPTKTVRENVEEGVAEIKDALDRFN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 112 Q-------QDAD-------------IIRAA----MD-KTGVSAFA------DTFVDELSGGERQRAWVAMLLAQESPVLI 160
Cdd:TIGR03719 105 EisakyaePDADfdklaaeqaelqeIIDAAdawdLDsQLEIAMDAlrcppwDADVTKLSGGERRRVALCRLLLSKPDMLL 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 992343279 161 LDEPTSALDVQHQYQLMALLAELnqkQGCgIIVILHDlnlalRY-----ATHIVALKQGR-IAFDG 220
Cdd:TIGR03719 185 LDEPTNHLDAESVAWLERHLQEY---PGT-VVAVTHD-----RYfldnvAGWILELDRGRgIPWEG 241
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-250 |
2.89e-12 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 66.00 E-value: 2.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 1 MFTLSGVEMVRGGRRILAIEQLNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDT--GSVWLNDAPLTSLS-SKSLAKAV 77
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKASNiRDTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 78 AFLPQKLPASAGLTVRELVRLGRfpwRGALGFWRQQDADIIRAA---MDKTGVSAFADT-FVDELSGGERQRAWVAMLLA 153
Cdd:TIGR02633 81 VIIHQELTLVPELSVAENIFLGN---EITLPGGRMAYNAMYLRAknlLRELQLDADNVTrPVGDYGGGQQQLVEIAKALN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 154 QESPVLILDEPTSALDVQHQYQLMALLAELNQKqGCGIIVILHDLNLALRYATHIVALKQGRIAFDGPATTLADEQRLSD 233
Cdd:TIGR02633 158 KQARLLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSEDDIITM 236
|
250
....*....|....*....
gi 992343279 234 LYQTPITLI--DHPHAVSE 250
Cdd:TIGR02633 237 MVGREITSLypHEPHEIGD 255
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
32-198 |
3.92e-12 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 65.11 E-value: 3.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 32 VLGHNGSGKSTLVSLLSGQ-QAPDTGSVWLNDApLTSLSSKSLA---KAVAFLPQKLPASAG--LTVRELVRLGRFPWRG 105
Cdd:PRK15079 52 VVGESGCGKSTFARAIIGLvKATDGEVAWLGKD-LLGMKDDEWRavrSDIQMIFQDPLASLNprMTIGEIIAEPLRTYHP 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 106 ALGfwRQQDADIIRAAMDKTGV-SAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSALDVQHQYQLMALLAELN 184
Cdd:PRK15079 131 KLS--RQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQ 208
|
170
....*....|....
gi 992343279 185 QKQGCGIIVILHDL 198
Cdd:PRK15079 209 REMGLSLIFIAHDL 222
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
37-217 |
3.97e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 65.46 E-value: 3.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 37 GSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKS-LAKAVAFLPQK-------LPASAGLTVRELVRlgrfpwrGALG 108
Cdd:PRK15439 299 GAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQrLARGLVYLPEDrqssglyLDAPLAWNVCALTH-------NRRG 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 109 FW--RQQDADII---RAAMdktGVS-AFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSALDVQHQ---YQLMAL 179
Cdd:PRK15439 372 FWikPARENAVLeryRRAL---NIKfNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARndiYQLIRS 448
|
170 180 190
....*....|....*....|....*....|....*...
gi 992343279 180 LAelnqKQGCGIIVILHDLNLALRYATHIVALKQGRIA 217
Cdd:PRK15439 449 IA----AQNVAVLFISSDLEEIEQMADRVLVMHQGEIS 482
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
6-196 |
6.25e-12 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 63.44 E-value: 6.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 6 GVEMVRGGRRILAIEQLNIPTNELTVVLGHNGSGKSTLVSLLSGQQ--APDTGSVWLNDAPLTS--------LSSKSLAK 75
Cdd:COG2401 35 GVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQFGReaslidaiGRKGDFKD 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 76 AVAFLpqklpASAGLTvrelvrlgrfpwrgalgfwrqqDADIIRAAmdktgvsafadtfVDELSGGERQRAWVAMLLAQE 155
Cdd:COG2401 115 AVELL-----NAVGLS----------------------DAVLWLRR-------------FKELSTGQKFRFRLALLLAER 154
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 992343279 156 SPVLILDEPTSALDVQHQYQLMALLAELNQKQGCGIIVILH 196
Cdd:COG2401 155 PKLLVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATH 195
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-216 |
6.76e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 63.91 E-value: 6.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 1 MFTLSGVEMVRGGRRILAIEQLNIPTNELTVVLGHNGSGKSTLVSLLS------GQQAPDTGSVWLNDAPLTSLSSKSLA 74
Cdd:PRK14246 10 VFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNrlieiyDSKIKVDGKVLYFGKDIFQIDAIKLR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 75 KAVAFLPQKLPASAGLTVRELVRlgrFPWRGALGFWRQQDADIIRAAMDKTG----VSAFADTFVDELSGGERQRAWVAM 150
Cdd:PRK14246 90 KEVGMVFQQPNPFPHLSIYDNIA---YPLKSHGIKEKREIKKIVEECLRKVGlwkeVYDRLNSPASQLSGGQQQRLTIAR 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 992343279 151 LLAQESPVLILDEPTSALDVQHQYQLMALLAELnqKQGCGIIVILHDLNLALRYATHIVALKQGRI 216
Cdd:PRK14246 167 ALALKPKVLLMDEPTSMIDIVNSQAIEKLITEL--KNEIAIVIVSHNPQQVARVADYVAFLYNGEL 230
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
15-195 |
8.15e-12 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 64.65 E-value: 8.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 15 RILAIEQLNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLAKAVAFLPQKL--------PA 86
Cdd:PRK10938 17 KTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKLVSDEWQRNntdmlspgED 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 87 SAGLTVRELVRLGrfpwrgalgfwrQQDADIIRAAMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTS 166
Cdd:PRK10938 97 DTGRTTAEIIQDE------------VKDPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFD 164
|
170 180
....*....|....*....|....*....
gi 992343279 167 ALDVQHQYQLMALLAELNQkQGCGIIVIL 195
Cdd:PRK10938 165 GLDVASRQQLAELLASLHQ-SGITLVLVL 192
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
37-217 |
2.09e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 63.26 E-value: 2.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 37 GSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSS-KSLAKAVAFLPQKLPASA---GLTVRELVRLGRF----PWRGALG 108
Cdd:PRK09700 299 GSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPlDAVKKGMAYITESRRDNGffpNFSIAQNMAISRSlkdgGYKGAMG 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 109 FW----RQQDADIIRAAMDKTGVSAfaDTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSALDVQHQ---YQLMALLA 181
Cdd:PRK09700 379 LFhevdEQRTAENQRELLALKCHSV--NQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKaeiYKVMRQLA 456
|
170 180 190
....*....|....*....|....*....|....*.
gi 992343279 182 ElnqkQGCGIIVILHDLNLALRYATHIVALKQGRIA 217
Cdd:PRK09700 457 D----DGKVILMVSSELPEIITVCDRIAVFCEGRLT 488
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
22-215 |
2.21e-11 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 62.93 E-value: 2.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 22 LNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSS-----KSLAKAVAFLPQklpasagLTVRELV 96
Cdd:PRK11607 40 LTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPyqrpiNMMFQSYALFPH-------MTVEQNI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 97 RLG----RFPwrgalgfwRQQDADIIRAAMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSALDVQH 172
Cdd:PRK11607 113 AFGlkqdKLP--------KAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKL 184
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 992343279 173 QYQLMALLAELNQKQGCGIIVILHDLNLALRYATHIVALKQGR 215
Cdd:PRK11607 185 RDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGK 227
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
2-196 |
2.31e-11 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 60.63 E-value: 2.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 2 FTLSGVEMVRGGRRILAIE-QLNIPTNELTVVLGHNGSGKSTLVSLLSGqqapdtgsVWlndaPLTSLSSKSLAKA-VAF 79
Cdd:cd03223 1 IELENLSLATPDGRVLLKDlSFEIKPGDRLLITGPSGTGKSSLFRALAG--------LW----PWGSGRIGMPEGEdLLF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 80 LPQK--LPASaglTVRELVRlgrFPWRgalgfwrqqdadiiraamdktgvsafadtfvDELSGGERQRAWVAMLLAQESP 157
Cdd:cd03223 69 LPQRpyLPLG---TLREQLI---YPWD-------------------------------DVLSGGEQQRLAFARLLLHKPK 111
|
170 180 190
....*....|....*....|....*....|....*....
gi 992343279 158 VLILDEPTSALDVQHQYQLMALLaelnQKQGCGIIVILH 196
Cdd:cd03223 112 FVFLDEATSALDEESEDRLYQLL----KELGITVISVGH 146
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
22-226 |
2.52e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 62.33 E-value: 2.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 22 LNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLA--KAVAFLPQKLPASAGLTvrELVRLG 99
Cdd:PRK13638 22 LDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLLAlrQQVATVFQDPEQQIFYT--DIDSDI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 100 RFPWRGaLGFWRQQDADIIRAAMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSALDVQHQYQLMAL 179
Cdd:PRK13638 100 AFSLRN-LGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAI 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 992343279 180 LAELNQkQGCGIIVILHDLNLALRYATHIVALKQGRI-AFDGPATTLA 226
Cdd:PRK13638 179 IRRIVA-QGNHVIISSHDIDLIYEISDAVYVLRQGQIlTHGAPGEVFA 225
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
22-217 |
2.86e-11 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 62.74 E-value: 2.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 22 LNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVW-----LNDAPLTSLSSKSLAKAVAFLPQklpasagLTVRELV 96
Cdd:PRK11000 24 LDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFigekrMNDVPPAERGVGMVFQSYALYPH-------LSVAENM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 97 RLGrfpwrgaLGFWRQQDADI---IRAAMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSALDVQHQ 173
Cdd:PRK11000 97 SFG-------LKLAGAKKEEInqrVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALR 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 992343279 174 YQLMALLAELNQKQGCGIIVILHDLNLALRYATHIVALKQGRIA 217
Cdd:PRK11000 170 VQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVA 213
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
22-221 |
3.06e-11 |
|
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: 61.36 E-value: 3.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 22 LNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLAKAVAFLPQKLPASAGlTVRE-LVRLGR 100
Cdd:cd03244 25 FSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISIIPQDPVLFSG-TIRSnLDPFGE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 101 FPwrgalgfwrqqDADIIRAaMDKTGVSAFA-------DTFVDE----LSGGERQ-----RAwvamlLAQESPVLILDEP 164
Cdd:cd03244 104 YS-----------DEELWQA-LERVGLKEFVeslpgglDTVVEEggenLSVGQRQllclaRA-----LLRKSKILVLDEA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 992343279 165 TSALDVQHQYQLMALLAElnQKQGCGIIVILHDLNLALRYAtHIVALKQGRIA-FDGP 221
Cdd:cd03244 167 TASVDPETDALIQKTIRE--AFKDCTVLTIAHRLDTIIDSD-RILVLDKGRVVeFDSP 221
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-228 |
4.51e-11 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 61.05 E-value: 4.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 1 MFTLSGVEMVRGGRRILAIEQLNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSL-SSKSLAKAVAF 79
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWqTAKIMREAVAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 80 LPQKLPASAGLTVRELVRLGrfpwrgalGFW--RQQDADIIRAAMDktgvsAFADTF------VDELSGGERQRAWVAML 151
Cdd:PRK11614 85 VPEGRRVFSRMTVEENLAMG--------GFFaeRDQFQERIKWVYE-----LFPRLHerriqrAGTMSGGEQQMLAIGRA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 992343279 152 LAQESPVLILDEPTSALDVQHQYQLMALLAELNQkQGCGIIVILHDLNLALRYATHIVALKQGRIAF-DGPATTLADE 228
Cdd:PRK11614 152 LMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLRE-QGMTIFLVEQNANQALKLADRGYVLENGHVVLeDTGDALLANE 228
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
12-225 |
4.59e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 61.65 E-value: 4.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 12 GGRRILAIEQLNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLAKAVAFL---------PQ 82
Cdd:PRK14271 32 AGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSIFNYRDVLEFRrrvgmlfqrPN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 83 KLPAS------AGLTVRELVRLGRFpwRGaLGFWRQQDADIIRAAMDKTGVSAFadtfvdELSGGERQRAWVAMLLAQES 156
Cdd:PRK14271 112 PFPMSimdnvlAGVRAHKLVPRKEF--RG-VAQARLTEVGLWDAVKDRLSDSPF------RLSGGQQQLLCLARTLAVNP 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 992343279 157 PVLILDEPTSALDVQHQYQLMALLAELNQKqgCGIIVILHDLNLALRYATHIVALKQGRIAFDGPATTL 225
Cdd:PRK14271 183 EVLLLDEPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQL 249
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
34-254 |
4.72e-11 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 62.42 E-value: 4.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 34 GHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLAKAVAFLPQKlPASAGLTVRELVRLGRfPwrgalGFWRQQ 113
Cdd:PRK10789 348 GPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQT-PFLFSDTVANNIALGR-P-----DATQQE 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 114 DADIIRAAM---DKTGVSAFADTFVDE----LSGGERQRAWVAMLLAQESPVLILDEPTSALDVQHQYQLMALLAELNQK 186
Cdd:PRK10789 421 IEHVARLASvhdDILRLPQGYDTEVGErgvmLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEG 500
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 992343279 187 QgcGIIVILHDLNlALRYATHIVALKQGRIAFDGPATTLADEQR-LSDLY---QTPITLIDHPHAVSEATTN 254
Cdd:PRK10789 501 R--TVIISAHRLS-ALTEASEILVMQHGHIAQRGNHDQLAQQSGwYRDMYryqQLEAALDDAPEIREEAVDA 569
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
137-215 |
5.44e-11 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 61.74 E-value: 5.44e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 992343279 137 ELSGGERQRAWVAMLLAQESPVLILDEPTSALDVQHQYQLMALLAELNQKQGCGIIVILHDLNLALRYATHIVALKQGR 215
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQ 236
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
22-219 |
6.21e-11 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 62.12 E-value: 6.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 22 LNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSS---KSLAKAV---AFLPQKLPASAGLTVREL 95
Cdd:COG4615 353 LTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNReayRQLFSAVfsdFHLFDRLLGLDGEADPAR 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 96 VRlgrfPWrgalgfwrqqdadIIRAAMD-KTGVS--AFADTfvdELSGGERQRawVAMLLA--QESPVLILDEPTSaldv 170
Cdd:COG4615 433 AR----EL-------------LERLELDhKVSVEdgRFSTT---DLSQGQRKR--LALLVAllEDRPILVFDEWAA---- 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 171 qHQ--------YQlmALLAELnQKQGCGIIVILHDlnlaLRY---ATHIVALKQGRIAFD 219
Cdd:COG4615 487 -DQdpefrrvfYT--ELLPEL-KARGKTVIAISHD----DRYfdlADRVLKMDYGKLVEL 538
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
34-215 |
7.84e-11 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 61.73 E-value: 7.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 34 GHNGSGKSTLVSLLSGQQAPDT--GSVWLNDAPLT--SLSSkSLAKAVAFLPQKLPASAGLTVRELVRLGRFPWRGALGF 109
Cdd:NF040905 34 GENGAGKSTLMKVLSGVYPHGSyeGEILFDGEVCRfkDIRD-SEALGIVIIHQELALIPYLSIAENIFLGNERAKRGVID 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 110 WRQQdadIIRAA--MDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSAL---DVQHqyqLMALLAELn 184
Cdd:NF040905 113 WNET---NRRARelLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTAALneeDSAA---LLDLLLEL- 185
|
170 180 190
....*....|....*....|....*....|.
gi 992343279 185 QKQGCGIIVILHDLNLALRYATHIVALKQGR 215
Cdd:NF040905 186 KAQGITSIIISHKLNEIRRVADSITVLRDGR 216
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
32-204 |
7.87e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 61.67 E-value: 7.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 32 VLGHNGSGKSTLVSLLSGQQAPDTGSVWLndAPLTSlsskslakaVAFLPQKLPASAGLTVRELVRLG---------RFP 102
Cdd:PRK11819 38 VLGLNGAGKSTLLRIMAGVDKEFEGEARP--APGIK---------VGYLPQEPQLDPEKTVRENVEEGvaevkaaldRFN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 103 WRGALgfWRQQDAD-------------IIRA------------AMDKTGVSAfADTFVDELSGGERQRawVAM--LLAQE 155
Cdd:PRK11819 107 EIYAA--YAEPDADfdalaaeqgelqeIIDAadawdldsqleiAMDALRCPP-WDAKVTKLSGGERRR--VALcrLLLEK 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 992343279 156 SPVLILDEPTSALDvqhqyqlmallAE--------LNQKQGCgIIVILHDlnlalRY 204
Cdd:PRK11819 182 PDMLLLDEPTNHLD-----------AEsvawleqfLHDYPGT-VVAVTHD-----RY 221
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
29-209 |
1.03e-10 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 59.54 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 29 LTVVLGHNGSGKSTLVSLLS----GQQAPDTGSVwlndAPLTSLSSKSLAKAVAFLPQKLPASAGLTV-RELVRLgrfpw 103
Cdd:cd03240 24 LTLIVGQNGAGKTTIIEALKyaltGELPPNSKGG----AHDPKLIREGEVRAQVKLAFENANGKKYTItRSLAIL----- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 104 RGALgFWRQQDADIIRAAMdktgvsafadtfVDELSGGERQ------RAWVAMLLAQESPVLILDEPTSALDVQHQY-QL 176
Cdd:cd03240 95 ENVI-FCHQGESNWPLLDM------------RGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEeSL 161
|
170 180 190
....*....|....*....|....*....|...
gi 992343279 177 MALLAELNQKQGCGIIVILHDLNLaLRYATHIV 209
Cdd:cd03240 162 AEIIEERKSQKNFQLIVITHDEEL-VDAADHIY 193
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
33-203 |
1.28e-10 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 61.29 E-value: 1.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 33 LGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSlssKSLA--KAVAFLPQKLPASAGLTVRE-LV---RLGRFPwrga 106
Cdd:NF033858 298 LGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDA---GDIAtrRRVGYMSQAFSLYGELTVRQnLElhaRLFHLP---- 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 107 lgfwrqqDADI---IRAAMDKTGVSAFADTFVDELSGGERQR---AwVAMLLAQEspVLILDEPTSALDVQHQYQLMALL 180
Cdd:NF033858 371 -------AAEIaarVAEMLERFDLADVADALPDSLPLGIRQRlslA-VAVIHKPE--LLILDEPTSGVDPVARDMFWRLL 440
|
170 180
....*....|....*....|...
gi 992343279 181 AELNQKQGCGIIVILHDLNLALR 203
Cdd:NF033858 441 IELSREDGVTIFISTHFMNEAER 463
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
2-221 |
2.21e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 60.64 E-value: 2.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 2 FTLSGVEMVRGGRRILAIEQLNI---PTNELTVVlGHNGSGKST----LVSLLSGQQapdtGSVWLNDAPLTSLSS---K 71
Cdd:PRK10261 323 FPLRSGLLNRVTREVHAVEKVSFdlwPGETLSLV-GESGSGKSTtgraLLRLVESQG----GEIIFNGQRIDTLSPgklQ 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 72 SLAKAVAFLPQKLPAS------AGLTVRELVRLgrfpwRGALgfwrQQDADIIRAA--MDKTGVSA-FADTFVDELSGGE 142
Cdd:PRK10261 398 ALRRDIQFIFQDPYASldprqtVGDSIMEPLRV-----HGLL----PGKAAAARVAwlLERVGLLPeHAWRYPHEFSGGQ 468
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 992343279 143 RQRAWVAMLLAQESPVLILDEPTSALDVQHQYQLMALLAELNQKQGCGIIVILHDLNLALRYATHIVALKQGRIAFDGP 221
Cdd:PRK10261 469 RQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGP 547
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
21-221 |
3.20e-10 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 59.82 E-value: 3.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 21 QLNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSV-------WLNDAPLTSLSSKSLAKAVAFLPQK---------- 83
Cdd:TIGR03269 304 SLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdeWVDMTKPGPDGRGRAKRYIGILHQEydlyphrtvl 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 84 --LPASAGLTV-RELVRLGRFPWRGALGFwrqqDADIIRAAMDKtgvsafadtFVDELSGGERQRAWVAMLLAQESPVLI 160
Cdd:TIGR03269 384 dnLTEAIGLELpDELARMKAVITLKMVGF----DEEKAEEILDK---------YPDELSEGERHRVALAQVLIKEPRIVI 450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 992343279 161 LDEPTSALD----VQHQYQLMALLAELNQKqgcgIIVILHDLNLALRYATHIVALKQGRIAFDGP 221
Cdd:TIGR03269 451 LDEPTGTMDpitkVDVTHSILKAREEMEQT----FIIVSHDMDFVLDVCDRAALMRDGKIVKIGD 511
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
31-169 |
3.74e-10 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 58.50 E-value: 3.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 31 VV--LGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLAKA-VAFLPQKlpASA--GLTVR-------ELVRL 98
Cdd:COG1137 31 IVglLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARLgIGYLPQE--ASIfrKLTVEdnilavlELRKL 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 992343279 99 GRfpwrgalgfwrQQDADIIRAAMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSALD 169
Cdd:COG1137 109 SK-----------KEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVD 168
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
21-236 |
3.89e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 59.99 E-value: 3.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 21 QLNIPTNELTVVLGHNGSGKSTLVSLLSGQQAP-DTGSVwlndapltslsskSLAKAVAFLPQkLPASAGLTVRELVRLG 99
Cdd:PLN03232 637 NLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHaETSSV-------------VIRGSVAYVPQ-VSWIFNATVRENILFG 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 100 ------RFpWRGALGFWRQQDADII----RAAMDKTGVSafadtfvdeLSGGERQRAWVAMLLAQESPVLILDEPTSALD 169
Cdd:PLN03232 703 sdfeseRY-WRAIDVTALQHDLDLLpgrdLTEIGERGVN---------ISGGQKQRVSMARAVYSNSDIYIFDDPLSALD 772
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 992343279 170 --VQHQYQLMALLAELNQKQGCGIIVILHDLNLALRyathIVALKQGRIAFDGpatTLADEQRLSDLYQ 236
Cdd:PLN03232 773 ahVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDR----IILVSEGMIKEEG---TFAELSKSGSLFK 834
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
22-203 |
5.16e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 58.25 E-value: 5.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 22 LNIPTNELTVVLGHNGSGKSTLVSLLS--GQQAPD---TGSVWLNDAPLTSLSSKS--LAKAVAFLPQKlPASAGLTVRE 94
Cdd:PRK14239 26 LDFYPNEITALIGPSGSGKSTLLRSINrmNDLNPEvtiTGSIVYNGHNIYSPRTDTvdLRKEIGMVFQQ-PNPFPMSIYE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 95 LVRLGrfpwrgaLGFWRQQDADIIRAAMDKTGVSA-----FADTFVDE---LSGGERQRAWVAMLLAQESPVLILDEPTS 166
Cdd:PRK14239 105 NVVYG-------LRLKGIKDKQVLDEAVEKSLKGAsiwdeVKDRLHDSalgLSGGQQQRVCIARVLATSPKIILLDEPTS 177
|
170 180 190
....*....|....*....|....*....|....*..
gi 992343279 167 ALDVQHQYQLMALLAELNQKQgcGIIVILHDLNLALR 203
Cdd:PRK14239 178 ALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASR 212
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
25-228 |
6.16e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 59.22 E-value: 6.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 25 PTNELTVVlGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLAKAVAFLPQKlPASAGLTVRelVRLGRFPWR 104
Cdd:PLN03232 1261 PSEKVGVV-GRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQS-PVLFSGTVR--FNIDPFSEH 1336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 105 GALGFWRQQDADIIRAAMDKTGVSAFADTFV--DELSGGERQRAWVAMLLAQESPVLILDEPTSALDVQHQYQLMALLAE 182
Cdd:PLN03232 1337 NDADLWEALERAHIKDVIDRNPFGLDAEVSEggENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIRE 1416
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 992343279 183 lnQKQGCGIIVILHDLNLALRyATHIVALKQGRI-AFDGPATTLADE 228
Cdd:PLN03232 1417 --EFKSCTMLVIAHRLNTIID-CDKILVLSSGQVlEYDSPQELLSRD 1460
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
32-231 |
6.27e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 58.86 E-value: 6.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 32 VLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSK-SLAKAVAFLPQKLPASA---GLTVRE---LVRLGRFpwr 104
Cdd:PRK10762 283 VSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQdGLANGIVYISEDRKRDGlvlGMSVKEnmsLTALRYF--- 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 105 galgfwrQQDADIIRAAMDKTGVSAFADTF----------VDELSGGERQRAWVAMLLAQESPVLILDEPTSALDV---Q 171
Cdd:PRK10762 360 -------SRAGGSLKHADEQQAVSDFIRLFniktpsmeqaIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVgakK 432
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 992343279 172 HQYQLmallaeLNQ--KQGCGIIVILHDLNLALRYATHIVALKQGRIAFDGPATTlADEQRL 231
Cdd:PRK10762 433 EIYQL------INQfkAEGLSIILVSSEMPEVLGMSDRILVMHEGRISGEFTREQ-ATQEKL 487
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
12-228 |
8.54e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 57.73 E-value: 8.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 12 GGRRILAIEQLNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPD--TGSVWLNDAPLTSLSSKSLAKAVAFLPQKLPAS-A 88
Cdd:CHL00131 18 NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKilEGDILFKGESILDLEPEERAHLGIFLAFQYPIEiP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 89 GLTVRELVRLGRFPWRGALGfwrQQDAD------IIRAAMDKTGVSA-FADTFVDE-LSGGERQRAWVAMLLAQESPVLI 160
Cdd:CHL00131 98 GVSNADFLRLAYNSKRKFQG---LPELDplefleIINEKLKLVGMDPsFLSRNVNEgFSGGEKKRNEILQMALLDSELAI 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 992343279 161 LDEPTSALDVQhqyQLMALLAELNQ--KQGCGIIVILHDLNLaLRYA----THIvaLKQGRIAFDGPAtTLADE 228
Cdd:CHL00131 175 LDETDSGLDID---ALKIIAEGINKlmTSENSIILITHYQRL-LDYIkpdyVHV--MQNGKIIKTGDA-ELAKE 241
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
17-209 |
1.94e-09 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 55.41 E-value: 1.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 17 LAIEQLNIPTNELTVVLGHNGSGKSTLVSllsgqqapdTGSVWLNDAPLTSLSSKSLAKAVAFLPQklpasagltVRELV 96
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVN---------EGLYASGKARLISFLPKFSRNKLIFIDQ---------LQFLI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 97 RLGrfpwrgaLGFWRqqdadIIRAAmdktgvsafadtfvDELSGGERQRAWVAMLLAQESP--VLILDEPTSALDVQHQY 174
Cdd:cd03238 73 DVG-------LGYLT-----LGQKL--------------STLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDIN 126
|
170 180 190
....*....|....*....|....*....|....*
gi 992343279 175 QLMALLAELNQkQGCGIIVILHDLNLaLRYATHIV 209
Cdd:cd03238 127 QLLEVIKGLID-LGNTVILIEHNLDV-LSSADWII 159
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
21-216 |
2.62e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 57.27 E-value: 2.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 21 QLNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNdapltslssKSLAkaVAFLPQKLPASAGLTV-------- 92
Cdd:PRK11147 23 ELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYE---------QDLI--VARLQQDPPRNVEGTVydfvaegi 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 93 -----------------------RELVRLGRFPWR-GALGFWRQQDAdiIRAAMDKTGVSAfaDTFVDELSGGERQRAWV 148
Cdd:PRK11147 92 eeqaeylkryhdishlvetdpseKNLNELAKLQEQlDHHNLWQLENR--INEVLAQLGLDP--DAALSSLSGGWLRKAAL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 992343279 149 AMLLAQESPVLILDEPTSALDVQHQYQLMALLAELnqkQGCgIIVILHDLNLALRYATHIVALKQGRI 216
Cdd:PRK11147 168 GRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTF---QGS-IIFISHDRSFIRNMATRIVDLDRGKL 231
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
7-183 |
4.98e-09 |
|
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: 54.56 E-value: 4.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 7 VEMVRGGRRILAIEQLNIPTNELTVVLGHNGSGKSTLVSLLSGQ--QAPDTGSVWLNDAPLTslssKSLAKAVAFLPQKL 84
Cdd:cd03232 13 VPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRktAGVITGEILINGRPLD----KNFQRSTGYVEQQD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 85 PASAGLTVRElvrlgrfpwrgALGFwrqqdadiiraamdktgvSAfadtFVDELSGGERQRAWVAMLLAQESPVLILDEP 164
Cdd:cd03232 89 VHSPNLTVRE-----------ALRF------------------SA----LLRGLSVEQRKRLTIGVELAAKPSILFLDEP 135
|
170
....*....|....*....
gi 992343279 165 TSALDVQHQYQLMALLAEL 183
Cdd:cd03232 136 TSGLDSQAAYNIVRFLKKL 154
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
32-220 |
5.62e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 56.05 E-value: 5.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 32 VLGHNGSGKSTLVSLLSGQQAPDTGSV-WLNDApltslsskslakAVAFLPQKLPA--SAGLTVrelvrlgrFPWrgaLG 108
Cdd:PRK15064 350 IIGENGVGKTTLLRTLVGELEPDSGTVkWSENA------------NIGYYAQDHAYdfENDLTL--------FDW---MS 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 109 FWRQQDAD--IIRAAMDKTGVSAfaDTF---VDELSGGERQRAWVAMLLAQESPVLILDEPTSALDVQhqyQLMALLAEL 183
Cdd:PRK15064 407 QWRQEGDDeqAVRGTLGRLLFSQ--DDIkksVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDME---SIESLNMAL 481
|
170 180 190
....*....|....*....|....*....|....*...
gi 992343279 184 NQKQGCGIIVIlHDLNLALRYATHIVALK-QGRIAFDG 220
Cdd:PRK15064 482 EKYEGTLIFVS-HDREFVSSLATRIIEITpDGVVDFSG 518
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
12-234 |
1.64e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 54.79 E-value: 1.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 12 GGRRILAIEQLNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVwlndapltslsskSLAKAVA---FLPQKLpasa 88
Cdd:PRK10636 323 GDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI-------------GLAKGIKlgyFAQHQL---- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 89 gltvrELVRLGRFPWRGALGFWRQQDADIIRaamDKTGVSAFADTFVDE----LSGGERQRAWVAMLLAQESPVLILDEP 164
Cdd:PRK10636 386 -----EFLRADESPLQHLARLAPQELEQKLR---DYLGGFGFQGDKVTEetrrFSGGEKARLVLALIVWQRPNLLLLDEP 457
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 992343279 165 TSALDVQHQYQLMALLAELNQkqgcGIIVILHDLNLaLRYATHIVAL-KQGRIA-FDGpatTLADEQR-LSDL 234
Cdd:PRK10636 458 TNHLDLDMRQALTEALIDFEG----ALVVVSHDRHL-LRSTTDDLYLvHDGKVEpFDG---DLEDYQQwLSDV 522
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
34-197 |
2.82e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 54.19 E-value: 2.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 34 GHNGSGKSTLVSLLSGQQAPDTGSVWLNdaplTSLSskslakaVAFL--------PQKlpasaglTV--------RELVR 97
Cdd:PRK11147 352 GPNGCGKTTLLKLMLGQLQADSGRIHCG----TKLE-------VAYFdqhraeldPEK-------TVmdnlaegkQEVMV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 98 LGRFpwRGALGFWrqQDadiiraamdktgvsaF------ADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSALDVQ 171
Cdd:PRK11147 414 NGRP--RHVLGYL--QD---------------FlfhpkrAMTPVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVE 474
|
170 180
....*....|....*....|....*.
gi 992343279 172 HQYQLMALLAELnqkQGCGIIVIlHD 197
Cdd:PRK11147 475 TLELLEELLDSY---QGTVLLVS-HD 496
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
22-237 |
2.84e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 53.31 E-value: 2.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 22 LNIPTNELTVVLGHNGSGKSTLVSLLS-----GQQAPDTGSVWLNDAPLTS--LSSKSLAKAVAFLPQKLPASAGLTVRE 94
Cdd:PRK14267 25 LKIPQNGVFALMGPSGCGKSTLLRTFNrllelNEEARVEGEVRLFGRNIYSpdVDPIEVRREVGMVFQYPNPFPHLTIYD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 95 LVRLGrFPWRGALGFWRQQDaDIIRAAMDKTG----VSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSALDV 170
Cdd:PRK14267 105 NVAIG-VKLNGLVKSKKELD-ERVEWALKKAAlwdeVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDP 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 992343279 171 QHQYQLMALLAELnqKQGCGIIVILHDLNLALRYATHIVALKQGRIAFDGPATTLAD--EQRLSDLYQT 237
Cdd:PRK14267 183 VGTAKIEELLFEL--KKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFEnpEHELTEKYVT 249
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
32-214 |
3.35e-08 |
|
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: 54.25 E-value: 3.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 32 VLGHNGSGKSTLVSLLSGQQAPDTGSVWL-NDAPLTSLSSksLAKAVAFLPQKLPASAGLTVRELVRLgrfpWRGALGFW 110
Cdd:TIGR01257 1970 LLGVNGAGKTTTFKMLTGDTTVTSGDATVaGKSILTNISD--VHQNMGYCPQFDAIDDLLTGREHLYL----YARLRGVP 2043
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 111 RQQDADIIRAAMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSALDVQHQYQLMALLAELnQKQGCG 190
Cdd:TIGR01257 2044 AEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSI-IREGRA 2122
|
170 180
....*....|....*....|....
gi 992343279 191 IIVILHDLNLALRYATHIVALKQG 214
Cdd:TIGR01257 2123 VVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
22-169 |
3.43e-08 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 52.73 E-value: 3.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 22 LNIPTNELTVVLGHNGSGKSTLVS-------LLSGQQApdTGSVWLNDAPLtsLSSK----SLAKAVAFLPQK---LPAS 87
Cdd:COG1117 32 LDIPENKVTALIGPSGCGKSTLLRclnrmndLIPGARV--EGEILLDGEDI--YDPDvdvvELRRRVGMVFQKpnpFPKS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 88 ------AGLtvrelvRLGRFPWRGALgfwrqqdADII-----RAAM-----DKTGVSAFAdtfvdeLSGGERQRAWVAML 151
Cdd:COG1117 108 iydnvaYGL------RLHGIKSKSEL-------DEIVeeslrKAALwdevkDRLKKSALG------LSGGQQQRLCIARA 168
|
170
....*....|....*...
gi 992343279 152 LAQESPVLILDEPTSALD 169
Cdd:COG1117 169 LAVEPEVLLMDEPTSALD 186
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
17-205 |
5.97e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 52.48 E-value: 5.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 17 LAIEQ--LNIPTNELTVVLGHNGSGKSTLV-------SLLSGQQApdTGSVWLNDAPLTSLS------------------ 69
Cdd:PRK14243 24 LAVKNvwLDIPKNQITAFIGPSGCGKSTILrcfnrlnDLIPGFRV--EGKVTFHGKNLYAPDvdpvevrrrigmvfqkpn 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 70 --SKSLAKAVAFLPQKLPASAGLTvrELVRlgRFPWRGALgfWrqqdaDIIRAAMDKTGVSafadtfvdeLSGGERQRAW 147
Cdd:PRK14243 102 pfPKSIYDNIAYGARINGYKGDMD--ELVE--RSLRQAAL--W-----DEVKDKLKQSGLS---------LSGGQQQRLC 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 992343279 148 VAMLLAQESPVLILDEPTSALDVQHQYQLMALLAELnqKQGCGIIVILHDLNLALRYA 205
Cdd:PRK14243 162 IARAIAVQPEVILMDEPCSALDPISTLRIEELMHEL--KEQYTIIIVTHNMQQAARVS 217
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
5-171 |
6.23e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 51.77 E-value: 6.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 5 SGVEMVRGGRRILAIEQLNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSkslAKAVAFLPQkL 84
Cdd:PRK13543 15 HALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDR---SRFMAYLGH-L 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 85 PASAgltvRELVRLGRFPWRGALGFWRQQDADiiRAAMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEP 164
Cdd:PRK13543 91 PGLK----ADLSTLENLHFLCGLHGRRAKQMP--GSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEP 164
|
....*..
gi 992343279 165 TSALDVQ 171
Cdd:PRK13543 165 YANLDLE 171
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
32-231 |
1.18e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 52.17 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 32 VLGHNGSGKSTLVSLLSGQQAPDTGSVWlndapltslssKSLAKAVAFLPQKLPASAGLTVRELVRLGR-FPwrgalGFW 110
Cdd:PLN03073 540 MVGPNGIGKSTILKLISGELQPSSGTVF-----------RSAKVRMAVFSQHHVDGLDLSSNPLLYMMRcFP-----GVP 603
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 111 RQQdadiIRAAMDKTGVSA-FADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSALDVQhqyQLMALLAELNQKQGc 189
Cdd:PLN03073 604 EQK----LRAHLGSFGVTGnLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLD---AVEALIQGLVLFQG- 675
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 992343279 190 GIIVILHDLNLALRYATHIVALKQGRIA-FDGpatTLADEQRL 231
Cdd:PLN03073 676 GVLMVSHDEHLISGSVDELWVVSEGKVTpFHG---TFHDYKKT 715
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
17-226 |
1.59e-07 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 52.26 E-value: 1.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 17 LAIEQLNIPTN--ELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLAKAVAFLPQKLPASAGLtvre 94
Cdd:TIGR00957 1300 LVLRHINVTIHggEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGS---- 1375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 95 lVRLGRFPwrgalgFWRQQDADI---IRAAMDKTGVSAFADTFVDE-------LSGGERQRAWVAMLLAQESPVLILDEP 164
Cdd:TIGR00957 1376 -LRMNLDP------FSQYSDEEVwwaLELAHLKTFVSALPDKLDHEcaeggenLSVGQRQLVCLARALLRKTKILVLDEA 1448
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 992343279 165 TSALDVQHQYQLMALLAelNQKQGCGIIVILHDLNLALRYaTHIVALKQGRIA-FDGPATTLA 226
Cdd:TIGR00957 1449 TAAVDLETDNLIQSTIR--TQFEDCTVLTIAHRLNTIMDY-TRVIVLDKGEVAeFGAPSNLLQ 1508
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
25-228 |
2.84e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 51.28 E-value: 2.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 25 PTNELTVVlGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLAKAVAFLPQKlPASAGLTVRelVRLGRFPWR 104
Cdd:PLN03130 1264 PSEKVGIV-GRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQA-PVLFSGTVR--FNLDPFNEH 1339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 105 GALGFW----RQQDADIIRAamDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSALDVQHQyqlmALL 180
Cdd:PLN03130 1340 NDADLWesleRAHLKDVIRR--NSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTD----ALI 1413
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 992343279 181 aelnQK------QGCGIIVILHDLNLALRyATHIVALKQGRIA-FDGPATTLADE 228
Cdd:PLN03130 1414 ----QKtireefKSCTMLIIAHRLNTIID-CDRILVLDAGRVVeFDTPENLLSNE 1463
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
32-221 |
2.92e-07 |
|
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: 49.72 E-value: 2.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 32 VLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLAKAVAFLPQKLPASAGlTVRElvRLGRFPwrgalgfwR 111
Cdd:cd03369 39 IVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTIIPQDPTLFSG-TIRS--NLDPFD--------E 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 112 QQDADIIRAAMDKTGVSafadtfvdELSGGERQRAWVAMLLAQESPVLILDEPTSALDvqhqYQLMALLAELNQK--QGC 189
Cdd:cd03369 108 YSDEEIYGALRVSEGGL--------NLSQGQRQLLCLARALLKRPRVLVLDEATASID----YATDALIQKTIREefTNS 175
|
170 180 190
....*....|....*....|....*....|...
gi 992343279 190 GIIVILHDLNLALRYAtHIVALKQGRIA-FDGP 221
Cdd:cd03369 176 TILTIAHRLRTIIDYD-KILVMDAGEVKeYDHP 207
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
127-211 |
3.12e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 51.18 E-value: 3.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 127 VSAFADTF-------VDELSGGERQRAWVAMLLAQESPVLILDEPTSALDVQHQYQLMALLAELNQKQGCGIIVILHDLN 199
Cdd:PTZ00265 562 VSALPDKYetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLS 641
|
90
....*....|..
gi 992343279 200 lALRYATHIVAL 211
Cdd:PTZ00265 642 -TIRYANTIFVL 652
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
22-220 |
4.85e-07 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 49.18 E-value: 4.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 22 LNIPTNELTVVLGHNGSGKSTLV--------------SL-------LSGQQAPDTGSVwLNDAPLTSLSSKSLAKAvafl 80
Cdd:cd03270 16 VDIPRNKLVVITGVSGSGKSSLAfdtiyaegqrryveSLsayarqfLGQMDKPDVDSI-EGLSPAIAIDQKTTSRN---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 81 pqklPASAGLTVREL---VRL--GRFPWRGALGFwrqqdadIIRAAMDKTGVSAFADTfvdeLSGGERQRAWVAMLL-AQ 154
Cdd:cd03270 91 ----PRSTVGTVTEIydyLRLlfARVGIRERLGF-------LVDVGLGYLTLSRSAPT----LSGGEAQRIRLATQIgSG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 992343279 155 ESPVL-ILDEPTSALDVQHQYQLMALLAELnQKQGCGIIVILHDLNLaLRYATHIVAL------KQGRIAFDG 220
Cdd:cd03270 156 LTGVLyVLDEPSIGLHPRDNDRLIETLKRL-RDLGNTVLVVEHDEDT-IRAADHVIDIgpgagvHGGEIVAQG 226
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
14-203 |
4.85e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 49.65 E-value: 4.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 14 RRILAIEQLNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDT-----GSVWLNDAPLTS--LSSKSLAKAVAFL---PQK 83
Cdd:PRK14258 20 QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIYErrVNLNRLRRQVSMVhpkPNL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 84 LPASAGLTVRELVRLgrFPWRGALGF-----WRQQDADIIRAAMDKTGVSAFadtfvdELSGGERQRAWVAMLLAQESPV 158
Cdd:PRK14258 100 FPMSVYDNVAYGVKI--VGWRPKLEIddiveSALKDADLWDEIKHKIHKSAL------DLSGGQQQRLCIARALAVKPKV 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 992343279 159 LILDEPTSALDVQHQYQLMALLAELNQKQGCGIIVILHDLNLALR 203
Cdd:PRK14258 172 LLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSR 216
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
133-235 |
5.24e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 50.11 E-value: 5.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 133 TFVDELSGGERQRAWVAMLLAQESPVLILDEPTSALDVQHQYQLMALLAELNQKqGCGIIVILHDLNLALRYATHIVALK 212
Cdd:PRK10982 387 TQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMS 465
|
90 100
....*....|....*....|....*
gi 992343279 213 QGRIA--FDGPATTLADEQRLSDLY 235
Cdd:PRK10982 466 NGLVAgiVDTKTTTQNEILRLASLH 490
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
4-169 |
6.09e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 50.12 E-value: 6.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 4 LSGVEMVRGGRRILAIEQLNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSS-KSLAKAVAFLPQ 82
Cdd:NF033858 4 LEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHrRAVCPRIAYMPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 83 KLpasaG------LTVRELV----RLgrFpwrgalGFWRQQDADIIRAAMDKTGVSAFADTFVDELSGGERQRAWVAMLL 152
Cdd:NF033858 84 GL----GknlyptLSVFENLdffgRL--F------GQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCAL 151
|
170
....*....|....*..
gi 992343279 153 AQESPVLILDEPTSALD 169
Cdd:NF033858 152 IHDPDLLILDEPTTGVD 168
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
28-220 |
7.90e-07 |
|
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: 48.41 E-value: 7.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 28 ELTVVLGHNGSGKSTLVSLLSGQQAPD---TGSVWLNDapLTSLSSKSLAKA-VAFLPQKLPASAGLTVRELVrlgrfpw 103
Cdd:cd03233 34 EMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNG--IPYKEFAEKYPGeIIYVSEEDVHFPTLTVRETL------- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 104 rgalgfwrqqdadiiraamdKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSALDVQHQYQLMALLAEL 183
Cdd:cd03233 105 --------------------DFALRCKGNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIRTM 164
|
170 180 190
....*....|....*....|....*....|....*....
gi 992343279 184 NQKQGCGIIVILHDLNLALrYAT--HIVALKQGRIAFDG 220
Cdd:cd03233 165 ADVLKTTTFVSLYQASDEI-YDLfdKVLVLYEGRQIYYG 202
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
17-214 |
8.76e-07 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 47.95 E-value: 8.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 17 LAIEQLNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLndaPLTSLSSKslakavaflPQKLpasagltvrelv 96
Cdd:cd03222 15 LLVELGVVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEW---DGITPVYK---------PQYI------------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 97 rlgrfpwrgalgfwrqqdadiiraamdktgvsafadtfvdELSGGERQRAWVAMLLAQESPVLILDEPTSALDVQHQYQL 176
Cdd:cd03222 71 ----------------------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNA 110
|
170 180 190
....*....|....*....|....*....|....*...
gi 992343279 177 MALLAELNQKQGCGIIVILHDLnLALRYATHIVALKQG 214
Cdd:cd03222 111 ARAIRRLSEEGKKTALVVEHDL-AVLDYLSDRIHVFEG 147
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-170 |
1.10e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 49.40 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 1 MFTLSGVEMVRGGRRILAIEQLNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSV---------WLN---------- 61
Cdd:PRK10636 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYtfpgnwqlaWVNqetpalpqpa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 62 --------------DAPLTSLSSKSLAKAVAFLPQKLPASAGLTVRElvrlgrfpwRGA-----LGFWRQQdadiiraam 122
Cdd:PRK10636 81 leyvidgdreyrqlEAQLHDANERNDGHAIATIHGKLDAIDAWTIRS---------RAAsllhgLGFSNEQ--------- 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 992343279 123 DKTGVSAFadtfvdelSGGERQRAWVAMLLAQESPVLILDEPTSALDV 170
Cdd:PRK10636 143 LERPVSDF--------SGGWRMRLNLAQALICRSDLLLLDEPTNHLDL 182
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-220 |
1.19e-06 |
|
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: 49.03 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 3 TLSGVEMVRGGRRILAIEQLNIPTNELTVVLGHNGSGKSTLVSLLSG--QQAPDTGSVWLNdaplTSLSSKSLAKAV-AF 79
Cdd:TIGR03269 2 EVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIIYH----VALCEKCGYVERpSK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 80 LPQKLPASAGLTVRELVRL--------GRFPWRGALGFWR-------QQDADIIRAAMDKTGVSAFA--DTFVD------ 136
Cdd:TIGR03269 78 VGEPCPVCGGTLEPEEVDFwnlsdklrRRIRKRIAIMLQRtfalygdDTVLDNVLEALEEIGYEGKEavGRAVDliemvq 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 137 ----------ELSGGERQRAWVAMLLAQESPVLILDEPTSALDVQHQYQLMALLAELNQKQGCGIIVILHDLNLALRYAT 206
Cdd:TIGR03269 158 lshrithiarDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSD 237
|
250
....*....|....
gi 992343279 207 HIVALKQGRIAFDG 220
Cdd:TIGR03269 238 KAIWLENGEIKEEG 251
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
7-169 |
1.85e-06 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 48.75 E-value: 1.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 7 VEMVRGGRRILAIEQLNIPTNELTVVLGHNGSGKSTLVSLLSgQQAPDTGSVWLNDAPLTSLSSKSLAKAVAFLPQKLPA 86
Cdd:TIGR01271 1225 AKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALL-RLLSTEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFI 1303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 87 SAGltvreLVRLGRFPWRgalgfwRQQDADIIRAAmDKTGVSAFADTFVDE-----------LSGGERQRAWVAMLLAQE 155
Cdd:TIGR01271 1304 FSG-----TFRKNLDPYE------QWSDEEIWKVA-EEVGLKSVIEQFPDKldfvlvdggyvLSNGHKQLMCLARSILSK 1371
|
170
....*....|....
gi 992343279 156 SPVLILDEPTSALD 169
Cdd:TIGR01271 1372 AKILLLDEPSAHLD 1385
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
22-197 |
2.12e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 48.43 E-value: 2.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 22 LNIPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSS---KSLAKAVaFL----------PQKLPASA 88
Cdd:PRK10522 344 LTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPedyRKLFSAV-FTdfhlfdqllgPEGKPANP 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 89 GLTVRELVRLGrfpwrgalgfwrqqdadiiraaM-DKTGVS--AFADTfvdELSGGERQRawVAMLLA--QESPVLILDE 163
Cdd:PRK10522 423 ALVEKWLERLK----------------------MaHKLELEdgRISNL---KLSKGQKKR--LALLLAlaEERDILLLDE 475
|
170 180 190
....*....|....*....|....*....|....*..
gi 992343279 164 PTSALDVQHQ---YQLmaLLAELnQKQGCGIIVILHD 197
Cdd:PRK10522 476 WAADQDPHFRrefYQV--LLPLL-QEMGKTIFAISHD 509
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
24-216 |
2.65e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 47.96 E-value: 2.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 24 IPTNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNdapltslSSKSLAKAVAFLPQKLpasAGLTVRELVRLgrfpw 103
Cdd:PRK13545 47 VPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIK-------GSAALIAISSGLNGQL---TGIENIELKGL----- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 104 rgALGFWRQQDADIIRAAMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEptsALDVQHQYQLMALLAEL 183
Cdd:PRK13545 112 --MMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDE---ALSVGDQTFTKKCLDKM 186
|
170 180 190
....*....|....*....|....*....|....*
gi 992343279 184 NQ--KQGCGIIVILHDLNLALRYATHIVALKQGRI 216
Cdd:PRK13545 187 NEfkEQGKTIFFISHSLSQVKSFCTKALWLHYGQV 221
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
28-196 |
3.46e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 47.80 E-value: 3.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 28 ELTVVLGHNGSGKSTLVSLLSGQQapDTGSV-----WLNDAPLTSlsskSLAKAVAFLPQKLPASAGLTVRELVRLGRFp 102
Cdd:TIGR00956 790 TLTALMGASGAGKTTLLNVLAERV--TTGVItggdrLVNGRPLDS----SFQRSIGYVQQQDLHLPTSTVRESLRFSAY- 862
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 103 WRGALGFWRQQDADIIRAAMDKTGVSAFADTFVDE----LSGGERQRAWVAM-LLAQESPVLILDEPTSALDVQHQYQLM 177
Cdd:TIGR00956 863 LRQPKSVSKSEKMEYVEEVIKLLEMESYADAVVGVpgegLNVEQRKRLTIGVeLVAKPKLLLFLDEPTSGLDSQTAWSIC 942
|
170
....*....|....*....
gi 992343279 178 ALLAELnQKQGCGIIVILH 196
Cdd:TIGR00956 943 KLMRKL-ADHGQAILCTIH 960
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
19-170 |
3.55e-06 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 47.82 E-value: 3.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 19 IEQLN--IPTNELTVVLGHNGSGKSTLVSLLsgqqapdtGSVWLNDAPLTSLSSKSlakAVAFLPQKLPASAGlTVRELV 96
Cdd:TIGR00954 468 IESLSfeVPSGNNLLICGPNGCGKSSLFRIL--------GELWPVYGGRLTKPAKG---KLFYVPQRPYMTLG-TLRDQI 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 97 ----RLGRFPWRGalgfWRQQDADIIRAAMDKT-------GVSAFADtFVDELSGGERQRAWVAMLLAQESPVLILDEPT 165
Cdd:TIGR00954 536 iypdSSEDMKRRG----LSDKDLEQILDNVQLThileregGWSAVQD-WMDVLSGGEKQRIAMARLFYHKPQFAILDECT 610
|
....*
gi 992343279 166 SALDV 170
Cdd:TIGR00954 611 SAVSV 615
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
26-212 |
6.80e-06 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 45.06 E-value: 6.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 26 TNELTVVLGHNGSGKSTLVSLLSGQQAPDTGSVwlndapltslsskslakavaflpqklpasagltvrelVRLgrfpwrg 105
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV-------------------------------------IYI------- 36
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 106 algfwrqqDADIIRAAMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPVLILDEPTSALDVQHQYQLMAL-----L 180
Cdd:smart00382 37 --------DGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrlL 108
|
170 180 190
....*....|....*....|....*....|....*...
gi 992343279 181 AELNQKQGCGIIVI------LHDLNLALRYATHIVALK 212
Cdd:smart00382 109 LLLKSEKNLTVILTtndekdLGPALLRRRFDRRIVLLL 146
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1-195 |
1.56e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 44.48 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 1 MFTLSGVEMVRGGRRILAIEQLNIPTNeLTVVLGHNGSGKSTLVSLLSGQQAPDTGSVWLNDAPLTSLSSKSLakavAFL 80
Cdd:PRK13541 1 MLSLHQLQFNIEQKNLFDLSITFLPSA-ITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYC----TYI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 81 PQKLPASAGLTVRElvrlgrfpwrgALGFWRQ--QDADIIRAAMDKTGVSAFADTFVDELSGGERQRAWVAMLLAQESPV 158
Cdd:PRK13541 76 GHNLGLKLEMTVFE-----------NLKFWSEiyNSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDL 144
|
170 180 190
....*....|....*....|....*....|....*..
gi 992343279 159 LILDEPTSALDVQHQYQLMALLAelnQKQGCGIIVIL 195
Cdd:PRK13541 145 WLLDEVETNLSKENRDLLNNLIV---MKANSGGIVLL 178
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
136-197 |
2.29e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.42 E-value: 2.29e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 992343279 136 DELSGGERQ------RAWVAMLLAQ------ESPVLILDEPTSALDVQHQYQLMALLaELNQKQGCG-IIVILHD 197
Cdd:PRK02224 780 EQLSGGERAlfnlslRCAIYRLLAEgiegdaPLPPLILDEPTVFLDSGHVSQLVDLV-ESMRRLGVEqIVVVSHD 853
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
137-211 |
2.68e-05 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 44.53 E-value: 2.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 137 ELSGGERQRAWVAMLLAQESP---VLILDEPTSAL---DVQHqyqLMALLAELnQKQGCGIIVILHDLNLaLRYATHIVA 210
Cdd:cd03271 169 TLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLhfhDVKK---LLEVLQRL-VDKGNTVVVIEHNLDV-IKCADWIID 243
|
.
gi 992343279 211 L 211
Cdd:cd03271 244 L 244
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
138-196 |
2.82e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 45.02 E-value: 2.82e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 992343279 138 LSGGERQRAWVAMLLAQESPVLILDEPTSALDVQHQYQLMALLAELNQKQGCGIIVILH 196
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH 1417
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
138-211 |
8.22e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 43.66 E-value: 8.22e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 992343279 138 LSGGERQRAWVA--MLLAQESPVL-ILDEPTSALDVQHQYQLMALLAELNQkQGCGIIVILHDLNLaLRYATHIVAL 211
Cdd:PRK00635 810 LSGGEIQRLKLAyeLLAPSKKPTLyVLDEPTTGLHTHDIKALIYVLQSLTH-QGHTVVIIEHNMHV-VKVADYVLEL 884
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
138-211 |
1.02e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 43.46 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 138 LSGGERQRAWVAMLLAQES---PVLILDEPTSAL---DVQhqyQLMALLAELnQKQGCGIIVILHDLNLaLRYATHIVAL 211
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKRStgrTLYILDEPTTGLhfdDIK---KLLEVLQRL-VDKGNTVVVIEHNLDV-IKTADYIIDL 904
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
135-194 |
1.72e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 42.47 E-value: 1.72e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 135 VDELSGGERQRAWVAMLLAQESPVLILDEPTSALDVQHQYQLMALLAELnQKQGCGIIVI 194
Cdd:NF040905 402 VGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINEL-AAEGKGVIVI 460
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
135-254 |
1.97e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.51 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 135 VDELSGGERQRAWVAMLLAQE--SPVLILDEPTSALDVQHQYQLMALLAELnQKQGCGIIVILHDLNLaLRYATHIVALK 212
Cdd:PRK00635 474 LATLSGGEQERTALAKHLGAEliGITYILDEPSIGLHPQDTHKLINVIKKL-RDQGNTVLLVEHDEQM-ISLADRIIDIG 551
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 992343279 213 Q------GRIAFDG-PATTLADEQRLSDLYQTPITLIDHPH---------AVSEATTN 254
Cdd:PRK00635 552 PgagifgGEVLFNGsPREFLAKSDSLTAKYLRQELTIPIPEkrtnslgtlTLSKATKH 609
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
138-205 |
1.98e-04 |
|
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.
Pssm-ID: 213206 [Multi-domain] Cd Length: 178 Bit Score: 41.14 E-value: 1.98e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 992343279 138 LSGGERQRAWVAMLLA----QESPVLILDEPTSALDVQHQYQLMALLAElNQKQGCGIIVILHDLNLALRYA 205
Cdd:cd03239 95 LSGGEKSLSALALIFAlqeiKPSPFYVLDEIDAALDPTNRRRVSDMIKE-MAKHTSQFIVITLKKEMFENAD 165
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
53-235 |
2.49e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 42.31 E-value: 2.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 53 PDTGSVWLNDAPLTSLSSKSLAKAVAFLPQ-KLPASAGLTVRELVRlgrfPWRGALGFwrqqdadIIRAAMDKTGVSAFA 131
Cdd:TIGR00630 418 PEALAVTVGGKSIADVSELSIREAHEFFNQlTLTPEEKKIAEEVLK----EIRERLGF-------LIDVGLDYLSLSRAA 486
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 132 DTfvdeLSGGERQRAWVAMLL-AQESPVL-ILDEPTSALDVQHQYQLMALLAELnQKQGCGIIVILHDLNlALRYATHIV 209
Cdd:TIGR00630 487 GT----LSGGEAQRIRLATQIgSGLTGVLyVLDEPSIGLHQRDNRRLINTLKRL-RDLGNTLIVVEHDED-TIRAADYVI 560
|
170 180 190
....*....|....*....|....*....|...
gi 992343279 210 AL------KQGRIAFDG-PATTLADEQRLSDLY 235
Cdd:TIGR00630 561 DIgpgageHGGEVVASGtPEEILANPDSLTGQY 593
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
150-231 |
3.89e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.74 E-value: 3.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 150 MLLAQESPVL-ILDEPTSALDVQHQYQLMALLAELnQKQGCGIIVILHDLNLaLRYATHIVAL-----KQ-GRIAFDGPA 222
Cdd:PRK00635 1714 LYLPPKHPTLfLLDEIATSLDNQQKSALLVQLRTL-VSLGHSVIYIDHDPAL-LKQADYLIEMgpgsgKTgGKILFSGPP 1791
|
....*....
gi 992343279 223 TTLADEQRL 231
Cdd:PRK00635 1792 KDISASKDS 1800
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
34-233 |
4.30e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 41.42 E-value: 4.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 34 GHNGSGKSTLVSLLSGQQAPDTGSVwlndapltslsSKSLAKAVAFLPQKLPASAGLTVRELVRLGRfpwrgaLGFWR-Q 112
Cdd:PRK15064 34 GANGCGKSTFMKILGGDLEPSAGNV-----------SLDPNERLGKLRQDQFAFEEFTVLDTVIMGH------TELWEvK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 113 QDADIIRA---AMDKTGV------SAFA--DTFVDELSGGE----------------RQRA--W-VAMLLAQ----ESPV 158
Cdd:PRK15064 97 QERDRIYAlpeMSEEDGMkvadleVKFAemDGYTAEARAGElllgvgipeeqhyglmSEVApgWkLRVLLAQalfsNPDI 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 159 LILDEPTSALDVqhqYQLMALLAELNQKQgCGIIVILHD---LNlalRYATHIVALKQGRIA-FDG------PATTLADE 228
Cdd:PRK15064 177 LLLDEPTNNLDI---NTIRWLEDVLNERN-STMIIISHDrhfLN---SVCTHMADLDYGELRvYPGnydeymTAATQARE 249
|
....*
gi 992343279 229 QRLSD 233
Cdd:PRK15064 250 RLLAD 254
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
137-172 |
4.84e-04 |
|
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213240 [Multi-domain] Cd Length: 251 Bit Score: 40.36 E-value: 4.84e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 992343279 137 ELSGGerQRAWVA------MLLAQESPVLILDEPTSALDVQH 172
Cdd:cd03273 166 ELSGG--QRSLVAlslilaLLLFKPAPMYILDEVDAALDLSH 205
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
137-224 |
5.40e-04 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 40.60 E-value: 5.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 137 ELSGGERQRawVAMLLA--QESPVLILDEPTSALD----VQHQYQLMALLAELNQKQgcgiIVILHDLNLALRYATHIVA 210
Cdd:PRK11650 134 ELSGGQRQR--VAMGRAivREPAVFLFDEPLSNLDaklrVQMRLEIQRLHRRLKTTS----LYVTHDQVEAMTLADRVVV 207
|
90 100
....*....|....*....|..
gi 992343279 211 LKQGRI--------AFDGPATT 224
Cdd:PRK11650 208 MNGGVAeqigtpveVYEKPAST 229
|
|
| COG3910 |
COG3910 |
Predicted ATPase [General function prediction only]; |
16-207 |
5.78e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443116 [Multi-domain] Cd Length: 239 Bit Score: 40.13 E-value: 5.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 16 ILAIEQLNIPTNeLTVVLGHNGSGKSTLVsllsgqQA--------PDTGSVWLNDAPLTSLSSksLAKAVaflpqklpas 87
Cdd:COG3910 27 VRNLEGLEFHPP-VTFFVGENGSGKSTLL------EAiavaagfnPEGGSKNFRFSTRESESA--LGEYL---------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 88 agltvrELVRLGRFPWRG-------ALGFWRQQDAdiiRAAMDKTGVSAFADTFVDELSGGErqrAWVAMLLAQESP--V 158
Cdd:COG3910 88 ------RLSRGLPKPRDGfflraesFFNVATYLDE---LAAEGPGILDSYGGRSLHEQSHGE---SFLALFENRFRGngL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 992343279 159 LILDEPTSALDVQHQYQLMALLAELnQKQGCGIIVilhdlnlalryATH 207
Cdd:COG3910 156 YLLDEPEAALSPSRQLALLALIHDL-VREGSQFII-----------ATH 192
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
7-169 |
1.58e-03 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 39.07 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 7 VEMVRGGRRILAIEQLNIPTNELTVVLGHNGSGKSTLVS----LLSGQqapdtGSVWLNDAPLTSLSSKSLAKAVAFLPQ 82
Cdd:cd03289 10 AKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSaflrLLNTE-----GDIQIDGVSWNSVPLQKWRKAFGVIPQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 83 KLPASAGLtvrelVRLGRFPWrgalGFWrqQDADIIRAAmDKTGVSAFADTFVDEL-----------SGGERQRAWVAML 151
Cdd:cd03289 85 KVFIFSGT-----FRKNLDPY----GKW--SDEEIWKVA-EEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLARS 152
|
170
....*....|....*...
gi 992343279 152 LAQESPVLILDEPTSALD 169
Cdd:cd03289 153 VLSKAKILLLDEPSAHLD 170
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
18-47 |
1.63e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 39.14 E-value: 1.63e-03
10 20 30
....*....|....*....|....*....|
gi 992343279 18 AIEQLNIPTNELTVVLGHNGSGKSTLVSLL 47
Cdd:COG4637 12 SLRDLELPLGPLTVLIGANGSGKSNLLDAL 41
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
138-198 |
1.81e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 39.62 E-value: 1.81e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 992343279 138 LSGGERQRAWVAMLLAQESP---VLILDEPTSAL---DVQHqyqlmaLLAELNQ--KQGCGIIVILHDL 198
Cdd:COG0178 827 LSGGEAQRVKLASELSKRSTgktLYILDEPTTGLhfhDIRK------LLEVLHRlvDKGNTVVVIEHNL 889
|
|
| COG4938 |
COG4938 |
Predicted ATPase [General function prediction only]; |
18-49 |
2.67e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443965 [Multi-domain] Cd Length: 277 Bit Score: 38.41 E-value: 2.67e-03
10 20 30
....*....|....*....|....*....|..
gi 992343279 18 AIEQLNIPTNELTVVLGHNGSGKSTLVSLLSG 49
Cdd:COG4938 11 PFKEAELELKPLTLLIGPNGSGKSTLIQALLL 42
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
138-198 |
2.69e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 38.90 E-value: 2.69e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 992343279 138 LSGGERQRawvaMLLAQEspvL----------ILDEPTSAL---DVQhqyQLMALLAELnQKQGCGIIVILHDL 198
Cdd:PRK00349 831 LSGGEAQR----VKLAKE---LskrstgktlyILDEPTTGLhfeDIR---KLLEVLHRL-VDKGNTVVVIEHNL 893
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
136-196 |
3.12e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 38.80 E-value: 3.12e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 992343279 136 DELSGGERQRAWVAMLLA----QESPVLILDEPTSALDVQHqyqlMALLAEL--NQKQGCGIIVILH 196
Cdd:pfam02463 1076 DLLSGGEKTLVALALIFAiqkyKPAPFYLLDEIDAALDDQN----VSRVANLlkELSKNAQFIVISL 1138
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
135-196 |
3.37e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 38.73 E-value: 3.37e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 992343279 135 VDELSGGERQ------RAWVAMLLAQESPVLILDEPTSALDVQHQYQLMALLaELNQKQGCGI---IVILH 196
Cdd:PRK01156 799 IDSLSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTNLKDII-EYSLKDSSDIpqvIMISH 868
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
128-215 |
4.08e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 38.07 E-value: 4.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992343279 128 SAFADTF-VDELSGGERQRAWVAMLLA------QESPV----LILDEP-TSALDVQHQYQLMALLAELNqkqGCGIIVIL 195
Cdd:PHA02562 458 SRGREDFsYASFSQGEKARIDLALLFTwrdvasKVSGVdtnlLILDEVfDGALDAEGTKALLSILDSLK---DTNVFVIS 534
|
90 100
....*....|....*....|
gi 992343279 196 HDLNLALRYATHIVALKQGR 215
Cdd:PHA02562 535 HKDHDPQKFDRHLKMEKVGR 554
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
138-169 |
4.48e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 38.12 E-value: 4.48e-03
10 20 30
....*....|....*....|....*....|....*...
gi 992343279 138 LSGGERQ------RAWVAMLLAQESPVLILDEPTSALD 169
Cdd:PRK03918 789 LSGGERIalglafRLALSLYLAGNIPLLILDEPTPFLD 826
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
116-169 |
4.66e-03 |
|
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213242 [Multi-domain] Cd Length: 247 Bit Score: 37.55 E-value: 4.66e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 992343279 116 DIIRAAMDKTGVSAFADtfVDELSGGERQRAWVAMLLA----QESPVLILDEPTSALD 169
Cdd:cd03275 136 DVESIASKNPPGKRFRD--MDNLSGGEKTMAALALLFAihsyQPAPFFVLDEVDAALD 191
|
|
| RecF |
COG1195 |
Recombinational DNA repair ATPase RecF [Replication, recombination and repair]; |
138-184 |
5.98e-03 |
|
Recombinational DNA repair ATPase RecF [Replication, recombination and repair];
Pssm-ID: 440808 [Multi-domain] Cd Length: 352 Bit Score: 37.44 E-value: 5.98e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 992343279 138 LSGGErQRAWV-AMLLAQ---------ESPVLILDEPTSALDVQHQYQLMALLAELN 184
Cdd:COG1195 276 ASQGQ-QKSLVlALKLAQaellkeetgEAPILLLDDVFAELDEERREALLELLADLG 331
|
|
| RloC |
COG4694 |
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis]; |
29-57 |
6.26e-03 |
|
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 443729 [Multi-domain] Cd Length: 692 Bit Score: 37.79 E-value: 6.26e-03
10 20
....*....|....*....|....*....
gi 992343279 29 LTVVLGHNGSGKSTLVSLLSGQQAPDTGS 57
Cdd:COG4694 26 LNLIYGENGSGKSTLSRILRSLELGDTSS 54
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
22-44 |
9.53e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 37.31 E-value: 9.53e-03
|
| |
