|
Name |
Accession |
Description |
Interval |
E-value |
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
8-1313 |
0e+00 |
|
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: 716.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 8 ARLAASAGNLLFFASFFPYNFISEYYGMLNLTTKITACLSANVALALGINILIKLEIQEIGVKWHNLWTPANLEDNLNFG 87
Cdd:TIGR01257 758 ASLAAACSGVIYFTLYLPHILCFAWQDRMTADLKTAVSLLSPVAFGFGTEYLVRFEEQGLGLQWSNIGNSPLEGDEFSFL 837
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 88 YMLGMLLFDAFLYSLVTWYVEAVFPGQCGVPQPWYFFLMRSYWFGKPKIRKTTEEA--KCTPI------------VHNCY 153
Cdd:TIGR01257 838 LSMKMMLLDAALYGLLAWYLDQVFPGDYGTPLPWYFLLQESYWLGGEGCSTREERAleKTEPLteemedpehpegINDSF 917
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 154 -EAEPPNLEAGIHIMHLHKEFK--NKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISDN 230
Cdd:TIGR01257 918 fERELPGLVPGVCVKNLVKIFEpsGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETN 997
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 231 MIEVRKDLGFCPQHDLLFDDLTLSEHLFFYCMVKGIPQNINCEEIDRMLSAFNLQENYHTLSGSASGGVRRKLSIVLALM 310
Cdd:TIGR01257 998 LDAVRQSLGMCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFV 1077
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 311 AGSKVVILDEPSSGMDPVSRRATWDILQHYKHNRTILLTTHYMDEADVLGDRVAIMVRGTLHCCGSSVFLKQIYGAGYHI 390
Cdd:TIGR01257 1078 GDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFLKNCFGTGFYL 1157
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 391 VMEKQQ------------YC--------------------------DVDNIIAMIQQHVPGAVLENNIENELSFILPKKY 432
Cdd:TIGR01257 1158 TLVRKMkniqsqrggcegTCsctskgfstrcparvdeitpeqvldgDVNELMDLVYHHVPEAKLVECIGQELIFLLPNKN 1237
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 433 VSR--FETLFTELEMRQKALGIASFGASITTMEEVFVKVNKLA---------TPQK--SIQTIQPYYLAYRKMRQDEQQN 499
Cdd:TIGR01257 1238 FKQraYASLFRELEETLADLGLSSFGISDTPLEEIFLKVTEDAdsgslfaggAQQKreNANLRHPCSGPTEKAGQTPQAS 1317
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 500 VN----MPINYSKPNFPYLSEIATVKFNTGVPLYRQQFYSLFIKRALFISRNWK-----------FMLLQIIVVMVVTTY 564
Cdd:TIGR01257 1318 HTcspgQPAAHPEGQPPPEPEDPGVPLNTGARLILQHVQALLVKRFQHTIRSHKdflaqivlpatFVFLALMLSIIIPPF 1397
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 565 ------------LLLALHLNNNDIPERE---------LNLSHYGRTIV-----PYSTSGNS------DLALNLTknlNIF 612
Cdd:TIGR01257 1398 geypaltlhpwmYGQQYTFFSMDEPNSEhlevladvlLNKPGFGNRCLkeewlPEYPCGNStpwktpSVSPNIT---HLF 1474
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 613 LKSK------------------------------------NQNLRKIRGDMNDYILKNKDCHTF-CLVALSIKV------ 649
Cdd:TIGR01257 1475 QKQKwtaahpspscrcstrekltmlpecpegagglpppqrTQRSTEILQDLTDRNISDFLVKTYpALIRSSLKSkfwvne 1554
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 650 ------------------------------------------ERNKTV------------LTIFFNNEAYHSPAISLSIL 675
Cdd:TIGR01257 1555 qryggisiggklpaipitgealvgflsdlgqmmnvsggpvtrEASKEMpdflkhletednIKVWFNNKGWHALVSFLNVA 1634
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 676 DN-ILFMTL----SGPDASITVFNKPQPLPHYGSNIVPVNGLQI----VQCLAFGISVVVGSFSIQTVTERTSQAKHIQF 746
Cdd:TIGR01257 1635 HNaILRASLpkdrDPEEYGITVISQPLNLTKEQLSEITVLTTSVdavvAICVIFAMSFVPASFVLYLIQERVNKAKHLQF 1714
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 747 LTGVCVHTYWLSALLCDLIFFFFACCVLLAIFKFCQLEAFVVHYNFLDTILIFMLYGWCVVPLTYIASFLFNSSTAAYIK 826
Cdd:TIGR01257 1715 ISGVSPTTYWLTNFLWDIMNYAVSAGLVVGIFIGFQKKAYTSPENLPALVALLMLYGWAVIPMMYPASFLFDVPSTAYVA 1794
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 827 ITLFNYFSTMFSIIIYTIIQFYGNDFPNF-VHILIRAILMALPSYNLAMSIskyfddyeVKRLCAREFKSIYLDCSDPYT 905
Cdd:TIGR01257 1795 LSCANLFIGINSSAITFVLELFENNRTLLrFNAMLRKLLIVFPHFCLGRGL--------IDLALSQAVTDVYAQFGEEHS 1866
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 906 QNNvygFGEHGIGKFLITLATIGlvflllllslesvscslksfvfrniIFYFYNKLRKGRNAIPSN---QRTKE---DED 979
Cdd:TIGR01257 1867 ANP---FQWDLIGKNLVAMAVEG-------------------------VVYFLLTLLIQHHFFLSRwiaEPAKEpifDED 1918
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 980 EDIKKEKGKVFTlllRLQNTPLL-LNEVTKIYfKCPVVKAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSG 1058
Cdd:TIGR01257 1919 DDVAEERQRIIS---GGNKTDILrLNELTKVY-SGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSG 1994
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1059 IAFIDGNSVTRTPRKIRSRIGYCPQTESVLNHMTGRESLVMYARLWGVLEQDINEYVEAFLHSVHLEPIADQFIHTYSAG 1138
Cdd:TIGR01257 1995 DATVAGKSILTNISDVHQNMGYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGG 2074
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1139 SKRRLSTAIALMGKSSVVFLDEPSIGMDPVAQHLLWETITWICKTGKAIIITSHRMEECEALCTRLAIMVKGRFTCLGTP 1218
Cdd:TIGR01257 2075 NKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTI 2154
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1219 QHVRKRFGHVYTLTVRINIAKDE--DKVEEFKNFIKVTFPGNIKFQEFHGTIGYYIPSKEIywGKVFAILEEAKVLFKLE 1296
Cdd:TIGR01257 2155 QHLKSKFGDGYIVTMKIKSPKDDllPDLNPVEQFFQGNFPGSVQRERHYNMLQFQVSSSSL--ARIFQLLISHKDSLLIE 2232
|
1530
....*....|....*..
gi 525313703 1297 DYSVKRVTLEQIFLTFA 1313
Cdd:TIGR01257 2233 EYSVTQTTLDQVFVNFA 2249
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
164-381 |
7.67e-98 |
|
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: 311.75 E-value: 7.67e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 164 IHIMHLHKEFKN--KPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISDNMIEVRKDLGFC 241
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 242 PQHDLLFDDLTLSEHLFFYCMVKGIPQNINCEEIDRMLSAFNLQENYHTLSGSASGGVRRKLSIVLALMAGSKVVILDEP 321
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 322 SSGMDPVSRRATWDILQHYKHNRTILLTTHYMDEADVLGDRVAIMVRGTLHCCGSSVFLK 381
Cdd:cd03263 161 TSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1001-1222 |
1.23e-88 |
|
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: 286.32 E-value: 1.23e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1001 LLLNEVTKIYfKCPVVKAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTRTPRKIRSRIGY 1080
Cdd:cd03263 1 LQIRNLTKTY-KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1081 CPQTESVLNHMTGRESLVMYARLWGVLEQDINEYVEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIALMGKSSVVFLDE 1160
Cdd:cd03263 80 CPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 525313703 1161 PSIGMDPVAQHLLWETITWIcKTGKAIIITSHRMEECEALCTRLAIMVKGRFTCLGTPQHVR 1222
Cdd:cd03263 160 PTSGLDPASRRAIWDLILEV-RKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
1003-1225 |
1.18e-73 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 244.97 E-value: 1.18e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1003 LNEVTKIYFKcpvVKAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTRTPRKIRSRIGYCP 1082
Cdd:COG1131 3 VRGLTKRYGD---KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1083 QTESVLNHMTGRESLVMYARLWGVLEQDINEYVEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIALMGKSSVVFLDEPS 1162
Cdd:COG1131 80 QEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 525313703 1163 IGMDPVAQHLLWETITWICKTGKAIIITSHRMEECEALCTRLAIMVKGRFTCLGTPQHVRKRF 1225
Cdd:COG1131 160 SGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARL 222
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
164-376 |
1.23e-73 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 244.97 E-value: 1.23e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 164 IHIMHLHKEFKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISDNMIEVRKDLGFCPQ 243
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 244 HDLLFDDLTLSEHLFFYCMVKGIPQNINCEEIDRMLSAFNLQENYHTLSGSASGGVRRKLSIVLALMAGSKVVILDEPSS 323
Cdd:COG1131 81 EPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 525313703 324 GMDPVSRRATWDILQHYK-HNRTILLTTHYMDEADVLGDRVAIMVRGTLHCCGS 376
Cdd:COG1131 161 GLDPEARRELWELLRELAaEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGT 214
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
164-371 |
4.70e-60 |
|
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: 203.40 E-value: 4.70e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 164 IHIMHLHKEFKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISDNMIEVRKDLGFCPQ 243
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 244 HDLLFDDLTLSEHLFFycmvkgipqninceeidrmlsafnlqenyhtlsgsaSGGVRRKLSIVLALMAGSKVVILDEPSS 323
Cdd:cd03230 81 EPSLYENLTVRENLKL------------------------------------SGGMKQRLALAQALLHDPELLILDEPTS 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 525313703 324 GMDPVSRRATWDILQHY-KHNRTILLTTHYMDEADVLGDRVAIMVRGTL 371
Cdd:cd03230 125 GLDPESRREFWELLRELkKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1018-1218 |
9.61e-59 |
|
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: 201.83 E-value: 9.61e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1018 AVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTRTPRKIRSRIGYCPQTESVLNHMTGRESL 1097
Cdd:cd03265 15 AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIVFQDLSVDDELTGWENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1098 VMYARLWGVLEQDINEYVEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIALMGKSSVVFLDEPSIGMDPVAQHLLWETI 1177
Cdd:cd03265 95 YIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYI 174
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 525313703 1178 TWICKT-GKAIIITSHRMEECEALCTRLAIMVKGRFTCLGTP 1218
Cdd:cd03265 175 EKLKEEfGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTP 216
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1005-1227 |
1.05e-56 |
|
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: 196.62 E-value: 1.05e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1005 EVTKIYFKCPVVKAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTRTPRKIRSRIGYCPQT 1084
Cdd:COG4555 3 EVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGVLPDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1085 ESVLNHMTGRESLVMYARLWGVLEQDINEYVEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIALMGKSSVVFLDEPSIG 1164
Cdd:COG4555 83 RGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNG 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 525313703 1165 MDPVAQHLLWETITWICKTGKAIIITSHRMEECEALCTRLAIMVKGRFTCLGTPQHVRKRFGH 1227
Cdd:COG4555 163 LDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGE 225
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
164-371 |
4.14e-55 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 191.99 E-value: 4.14e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 164 IHIMHLHKEFKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISDNMIEVRKDLGFCPQ 243
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGVLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 244 HDLLFDDLTLSEHLFFYCMVKGIPQNINCEEIDRMLSAFNLQENYHTLSGSASGGVRRKLSIVLALMAGSKVVILDEPSS 323
Cdd:COG4555 82 ERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTN 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 525313703 324 GMDPVSRRATWDILQHYK-HNRTILLTTHYMDEADVLGDRVAIMVRGTL 371
Cdd:COG4555 162 GLDVMARRLLREILRALKkEGKTVLFSSHIMQEVEALCDRVVILHKGKV 210
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
164-381 |
8.22e-55 |
|
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: 190.27 E-value: 8.22e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 164 IHIMHLHKEFKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISDNMIEVRKDLGFCPQ 243
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 244 HDLLFDDLTLSEHLFFYCMVKGIPQNINCEEIDRMLSAFNLQENYHTLSGSASGGVRRKLSIVLALMAGSKVVILDEPSS 323
Cdd:cd03265 81 DLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 324 GMDPVSRRATWDILQHYK--HNRTILLTTHYMDEADVLGDRVAIMVRGTLHCCGSSVFLK 381
Cdd:cd03265 161 GLDPQTRAHVWEYIEKLKeeFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1003-1212 |
5.08e-54 |
|
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: 186.06 E-value: 5.08e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1003 LNEVTKIYfkcPVVKAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTRTPRKIRSRIGYCP 1082
Cdd:cd03230 3 VRNLSKRY---GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1083 QTESVLNHMTGRESLvmyarlwgvleqdineyveaflhsvhlepiadqfihTYSAGSKRRLSTAIALMGKSSVVFLDEPS 1162
Cdd:cd03230 80 EEPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPT 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 525313703 1163 IGMDPVAQHLLWETITWICKTGKAIIITSHRMEECEALCTRLAIMVKGRF 1212
Cdd:cd03230 124 SGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
171-469 |
3.85e-52 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 185.67 E-value: 3.85e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 171 KEFKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISDNMIEVRKDLGFCPQHDLLFDD 250
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVRRSIGIVPQYASVDED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 251 LTLSEHLFFYCMVKGIPQNINCEEIDRMLSAFNLQENYHTLSGSASGGVRRKLSIVLALMAGSKVVILDEPSSGMDPVSR 330
Cdd:TIGR01188 81 LTGRENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 331 RATWDILQHYKH-NRTILLTTHYMDEADVLGDRVAIMVRGTLHCCGSSVFLKQIYGaGYHIVMEKQQYCDVDNIIAMIQQ 409
Cdd:TIGR01188 161 RAIWDYIRALKEeGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKRRLG-KDTLESRPRDIQSLKVEVSMLIA 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 525313703 410 HVPGAVLE-NNIENELSFIlpKKYVSRFETLFTEL--EMRQKALGIASFGASITTMEEVFVKV 469
Cdd:TIGR01188 240 ELGETGLGlLAVTVDSDRI--KILVPDGDETVPEIveAAIRNGIRIRSISTERPSLDDVFLKL 300
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
166-474 |
3.11e-51 |
|
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: 199.47 E-value: 3.11e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 166 IMHLHKEFK-----NKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISDNMIEVRKDLGF 240
Cdd:TIGR01257 1937 ILRLNELTKvysgtSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNMGY 2016
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 241 CPQHDLLFDDLTLSEHLFFYCMVKGIPqninCEEIDRM----LSAFNLQENYHTLSGSASGGVRRKLSIVLALMAGSKVV 316
Cdd:TIGR01257 2017 CPQFDAIDDLLTGREHLYLYARLRGVP----AEEIEKVanwsIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLV 2092
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 317 ILDEPSSGMDPVSRRATWD-ILQHYKHNRTILLTTHYMDEADVLGDRVAIMVRGTLHCCGSSVFLKQIYGAGYHIVMEKQ 395
Cdd:TIGR01257 2093 LLDEPTTGMDPQARRMLWNtIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSKFGDGYIVTMKIK 2172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 396 Q-----YCDVDNIIAMIQQHVPGAVLENNIENELSFILPKKYVSRfetLFTELEMRQKALGIASFGASITTMEEVFVKVN 470
Cdd:TIGR01257 2173 SpkddlLPDLNPVEQFFQGNFPGSVQRERHYNMLQFQVSSSSLAR---IFQLLISHKDSLLIEEYSVTQTTLDQVFVNFA 2249
|
....
gi 525313703 471 KLAT 474
Cdd:TIGR01257 2250 KQQT 2253
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
164-375 |
2.45e-48 |
|
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: 171.61 E-value: 2.45e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 164 IHIMHLHKEFKNKPAVNNLSLNIYEGqVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISDNMIEVRKDLGFCPQ 243
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 244 HDLLFDDLTLSEHLFFYCMVKGIPQNINCEEIDRMLSAFNLQENYHTLSGSASGGVRRKLSIVLALMAGSKVVILDEPSS 323
Cdd:cd03264 80 EFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 525313703 324 GMDPVSRRATWDILQHYKHNRTILLTTHYMDEADVLGDRVAIMVRGTLHCCG 375
Cdd:cd03264 160 GLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
1003-1211 |
1.93e-45 |
|
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: 163.16 E-value: 1.93e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1003 LNEVTKIYFKcpvVKAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTRtPRKIRSRIGYCP 1082
Cdd:cd03268 3 TNDLTKTYGK---KRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQK-NIEALRRIGALI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1083 QTESVLNHMTGRESLVMYARLWGVLEQDINEyveaFLHSVHLEPIADQFIHTYSAGSKRRLSTAIALMGKSSVVFLDEPS 1162
Cdd:cd03268 79 EAPGFYPNLTARENLRLLARLLGIRKKRIDE----VLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPT 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 525313703 1163 IGMDPVAQHLLWETITWICKTGKAIIITSHRMEECEALCTRLAIMVKGR 1211
Cdd:cd03268 155 NGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGK 203
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1000-1219 |
2.90e-45 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 166.13 E-value: 2.90e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1000 PLLLNEVTKIYFKCPVVKavkNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTRTPRKIRSRIG 1079
Cdd:PRK13537 7 PIDFRNVEKRYGDKLVVD---GLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1080 YCPQTESVLNHMTGRESLVMYARLWGVLEQDINEYVEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIALMGKSSVVFLD 1159
Cdd:PRK13537 84 VVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1160 EPSIGMDPVAQHLLWETITWICKTGKAIIITSHRMEECEALCTRLAIMVKGRFTCLGTPQ 1219
Cdd:PRK13537 164 EPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPH 223
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1001-1213 |
6.57e-44 |
|
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: 158.90 E-value: 6.57e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1001 LLLNEVTKIYFKCpvvKAVKNISLVVKKSeCFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTRTPRKIRSRIGY 1080
Cdd:cd03264 1 LQLENLTKRYGKK---RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1081 CPQTESVLNHMTGRESLVMYARLWGVLEQDINEYVEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIALMGKSSVVFLDE 1160
Cdd:cd03264 77 LPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 525313703 1161 PSIGMDPVAQHLLWETITWICKTgKAIIITSHRMEECEALCTRLAIMVKGRFT 1213
Cdd:cd03264 157 PTAGLDPEERIRFRNLLSELGED-RIVILSTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1003-1219 |
2.76e-43 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 161.54 E-value: 2.76e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1003 LNEVTKIYFKCPVVKAVkniSLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTRTPRKIRSRIGYCP 1082
Cdd:PRK13536 44 LAGVSKSYGDKAVVNGL---SFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARARIGVVP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1083 QTESVLNHMTGRESLVMYARLWGVLEQDINEYVEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIALMGKSSVVFLDEPS 1162
Cdd:PRK13536 121 QFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPT 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 525313703 1163 IGMDPVAQHLLWETITWICKTGKAIIITSHRMEECEALCTRLAIMVKGRFTCLGTPQ 1219
Cdd:PRK13536 201 TGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPH 257
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1001-1211 |
4.54e-43 |
|
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: 156.76 E-value: 4.54e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1001 LLLNEVTKIY-FKCPVVKAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTRTPRKIRSRIG 1079
Cdd:cd03266 2 ITADALTKRFrDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1080 YCPQTESVLNHMTGRESLVMYARLWGVLEQDINEYVEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIALMGKSSVVFLD 1159
Cdd:cd03266 82 FVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 525313703 1160 EPSIGMDPVAQHLLWETITWICKTGKAIIITSHRMEECEALCTRLAIMVKGR 1211
Cdd:cd03266 162 EPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGR 213
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1001-1211 |
1.15e-42 |
|
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: 155.13 E-value: 1.15e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1001 LLLNEVTKIYFKcpvVKAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTRTPRkirSRIGY 1080
Cdd:cd03269 1 LEVENVTKRFGR---VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAAR---NRIGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1081 CPQTESVLNHMTGRESLVMYARLWGVLEQDINEYVEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIALMGKSSVVFLDE 1160
Cdd:cd03269 75 LPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 525313703 1161 PSIGMDPVAQHLLWETITWICKTGKAIIITSHRMEECEALCTRLAIMVKGR 1211
Cdd:cd03269 155 PFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGR 205
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1001-1309 |
1.77e-42 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 157.58 E-value: 1.77e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1001 LLLNEVTKIYFKcpvVKAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTRtprKIRSRIGY 1080
Cdd:COG4152 2 LELKGLTKRFGD---KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDP---EDRRRIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1081 CPQTESVLNHMTGRESLVMYARLWGVLEQDINEYVEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIALMGKSSVVFLDE 1160
Cdd:COG4152 76 LPEERGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1161 PSIGMDPVAQHLLWETITWICKTGKAIIITSHRMEECEALCTRLAIMVKGRFTCLGTPQHVRKRFG-HVYTLTVRINIAK 1239
Cdd:COG4152 156 PFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQFGrNTLRLEADGDAGW 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 525313703 1240 DED-----KVEEFKNFIKVTFPGNIKFQEfhgtigyyipskeiywgkvfaILEEAKVLFKLEDYSVKRVTLEQIF 1309
Cdd:COG4152 236 LRAlpgvtVVEEDGDGAELKLEDGADAQE---------------------LLRALLARGPVREFEEVRPSLNEIF 289
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
164-372 |
6.08e-42 |
|
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: 153.29 E-value: 6.08e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 164 IHIMHLHKEFKNKP----AVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISDNMIEVRKDLG 239
Cdd:cd03266 2 ITADALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 240 FCPQHDLLFDDLTLSEHLFFYCMVKGI-PQNINcEEIDRMLSAFNLQENYHTLSGSASGGVRRKLSIVLALMAGSKVVIL 318
Cdd:cd03266 82 FVSDSTGLYDRLTARENLEYFAGLYGLkGDELT-ARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 525313703 319 DEPSSGMDPVSRRATWDILQHYKH-NRTILLTTHYMDEADVLGDRVAIMVRGTLH 372
Cdd:cd03266 161 DEPTTGLDVMATRALREFIRQLRAlGKCILFSTHIMQEVERLCDRVVVLHRGRVV 215
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
164-363 |
3.61e-39 |
|
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: 144.93 E-value: 3.61e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 164 IHIMHLHKEFKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISDNMIEVRKDLGFCPQ 243
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYLGH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 244 HDLLFDDLTLSEHLFFYCMVKGIPQNIncEEIDRMLSAFNLQENYHTLSGSASGGVRRKLSIVLALMAGSKVVILDEPSS 323
Cdd:COG4133 83 ADGLKPELTVRENLRFWAALYGLRADR--EAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFT 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 525313703 324 GMDPVSRRATWDIL-QHYKHNRTILLTTHymDEADVLGDRV 363
Cdd:COG4133 161 ALDAAGVALLAELIaAHLARGGAVLLTTH--QPLELAAARV 199
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1001-1218 |
4.99e-38 |
|
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: 142.68 E-value: 4.99e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1001 LLLNEVTKIYFKCPVVKavkNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTRTPRKIRSR--I 1078
Cdd:cd03218 1 LRAENLSKRYGKRKVVN---GVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARlgI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1079 GYCPQTESVLNHMTGRESLVMYARLWGVLEQDINEYVEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIALMGKSSVVFL 1158
Cdd:cd03218 78 GYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1159 DEPSIGMDPVAQHLLWETITWICKTGKAIIITSHRMEECEALCTRLAIMVKGRFTCLGTP 1218
Cdd:cd03218 158 DEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTP 217
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
174-370 |
5.92e-38 |
|
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: 141.45 E-value: 5.92e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 174 KNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISDNMI-EVRKDLGFCPQH-DLLFDDL 251
Cdd:cd03225 12 GARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLkELRRKVGLVFQNpDDQFFGP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 252 TLSEHLFFYCMVKGIPQNINCEEIDRMLSAFNLQE----NYHTLsgsaSGGVRRKLSIVLALMAGSKVVILDEPSSGMDP 327
Cdd:cd03225 92 TVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGlrdrSPFTL----SGGQKQRVAIAGVLAMDPDILLLDEPTAGLDP 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 525313703 328 VSRRATWDILQHYKH-NRTILLTTHYMDEADVLGDRVAIMVRGT 370
Cdd:cd03225 168 AGRRELLELLKKLKAeGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1017-1211 |
8.14e-38 |
|
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: 141.07 E-value: 8.14e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1017 KAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVT-RTPRKIRSRIGYCPQ-TES-VLNHMTG 1093
Cdd:cd03225 15 PALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTkLSLKELRRKVGLVFQnPDDqFFGPTVE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1094 REslVMYA-RLWGVLEQDINEYVEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIALMGKSSVVFLDEPSIGMDPVAQHL 1172
Cdd:cd03225 95 EE--VAFGlENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRE 172
|
170 180 190
....*....|....*....|....*....|....*....
gi 525313703 1173 LWETITWICKTGKAIIITSHRMEECEALCTRLAIMVKGR 1211
Cdd:cd03225 173 LLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1016-1221 |
1.35e-37 |
|
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: 141.32 E-value: 1.35e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1016 VKAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTR-TPRKIRSRIGYCPQ-------TESV 1087
Cdd:COG1122 14 TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKkNLRELRRKVGLVFQnpddqlfAPTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1088 LnhmtgREslVMYA-RLWGVLEQDINEYVEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIALMGKSSVVFLDEPSIGMD 1166
Cdd:COG1122 94 E-----ED--VAFGpENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 525313703 1167 PVAQHLLWETITWICKTGKAIIITSHRMEECEALCTRLAIMVKGRFTCLGTPQHV 1221
Cdd:COG1122 167 PRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREV 221
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
172-376 |
2.88e-37 |
|
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: 140.16 E-value: 2.88e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 172 EFKN--------KPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISD-NMIEVRKDLGFCP 242
Cdd:COG1122 2 ELENlsfsypggTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKkNLRELRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 243 QH--DLLFDDlTLSEHLFFYCMVKGIPQnincEEIDR----MLSAFNLQE----NYHTLsgsaSGGVRRKLSI--VLALm 310
Cdd:COG1122 82 QNpdDQLFAP-TVEEDVAFGPENLGLPR----EEIRErveeALELVGLEHladrPPHEL----SGGQKQRVAIagVLAM- 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 525313703 311 aGSKVVILDEPSSGMDPVSRRATWDILQHYKH-NRTILLTTHYMDEADVLGDRVAIMVRGTLHCCGS 376
Cdd:COG1122 152 -EPEVLVLDEPTAGLDPRGRRELLELLKRLNKeGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGT 217
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1005-1211 |
2.99e-37 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 137.76 E-value: 2.99e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1005 EVTKIYFKCPVVKAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTR-TPRKIRSRIGYCPQ 1083
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKlPLEELRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1084 tesvlnhmtgreslvmyarlwgvleqdineyveaflhsvhlepiadqfihtYSAGSKRRLSTAIALMGKSSVVFLDEPSI 1163
Cdd:cd00267 81 ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTS 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 525313703 1164 GMDPVAQHLLWETITWICKTGKAIIITSHRMEECEALCTRLAIMVKGR 1211
Cdd:cd00267 110 GLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
164-469 |
3.48e-37 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 142.17 E-value: 3.48e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 164 IHIMHLHKEFKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISDnmiEVRKDLGFCPQ 243
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDP---EDRRRIGYLPE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 244 HDLLFDDLTLSEHLFFYCMVKGIPQNINCEEIDRMLSAFNLQENYHTLSGSASGGVRRKLSIVLALMAGSKVVILDEPSS 323
Cdd:COG4152 79 ERGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 324 GMDPVSRRATWDILQHYKHN-RTILLTTHYMDEADVLGDRVAIMVRGTLHCCGSSVFLKQIYGAGYHIVmekqqycDVDN 402
Cdd:COG4152 159 GLDPVNVELLKDVIRELAAKgTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQFGRNTLRL-------EADG 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 525313703 403 IIAMIQQhVPGAVLENNIENELSFILPKKYVSrfETLFTELemrQKALGIASFGASITTMEEVFVKV 469
Cdd:COG4152 232 DAGWLRA-LPGVTVVEEDGDGAELKLEDGADA--QELLRAL---LARGPVREFEEVRPSLNEIFIEV 292
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
168-370 |
1.64e-36 |
|
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: 135.45 E-value: 1.64e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 168 HLHKEFKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISDNMI-EVRKDLGFCPQhdl 246
Cdd:cd00267 4 NLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLeELRRRIGYVPQ--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 247 lfddltlsehlffycmvkgipqninceeidrmlsafnlqenyhtlsgsASGGVRRKLSIVLALMAGSKVVILDEPSSGMD 326
Cdd:cd00267 81 ------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLD 112
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 525313703 327 PVSRRATWDIL-QHYKHNRTILLTTHYMDEADVLGDRVAIMVRGT 370
Cdd:cd00267 113 PASRERLLELLrELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
164-369 |
1.99e-36 |
|
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: 137.03 E-value: 1.99e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 164 IHIMHLHKEFKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISdnmIEVRKDLGFCPQ 243
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD---IAARNRIGYLPE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 244 HDLLFDDLTLSEHLFFYCMVKGIPQNINCEEIDRMLSAFNLQENYHTLSGSASGGVRRKLSIVLALMAGSKVVILDEPSS 323
Cdd:cd03269 78 ERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFS 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 525313703 324 GMDPVSRRATWDILQHYKHN-RTILLTTHYMDEADVLGDRVAIMVRG 369
Cdd:cd03269 158 GLDPVNVELLKDVIRELARAgKTVILSTHQMELVEELCDRVLLLNKG 204
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
164-371 |
2.76e-36 |
|
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: 136.58 E-value: 2.76e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 164 IHIMHLHKEFKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISDNmIEVRKDLGFCPQ 243
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKN-IEALRRIGALIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 244 HDLLFDDLTLSEHLFFYCMVKGIPQnincEEIDRMLSAFNLQENYHTLSGSASGGVRRKLSIVLALMAGSKVVILDEPSS 323
Cdd:cd03268 80 APGFYPNLTARENLRLLARLLGIRK----KRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTN 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 525313703 324 GMDPVSRRATWDILQHY-KHNRTILLTTHYMDEADVLGDRVAIMVRGTL 371
Cdd:cd03268 156 GLDPDGIKELRELILSLrDQGITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1006-1221 |
8.33e-36 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 136.31 E-value: 8.33e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1006 VTKIYFKCPVVKavkNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTRTPRKIRSR--IGYCPQ 1083
Cdd:COG1137 9 LVKSYGKRTVVK---DVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARlgIGYLPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1084 TESVLNHMTGRESLVMYARLWGVLEQDINEYVEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIALMGKSSVVFLDEPSI 1163
Cdd:COG1137 86 EASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEPFA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 525313703 1164 GMDPVA----QHLlwetITWICKTGKAIIITSHRMEECEALCTRLAIMVKGRFTCLGTPQHV 1221
Cdd:COG1137 166 GVDPIAvadiQKI----IRHLKERGIGVLITDHNVRETLGICDRAYIISEGKVLAEGTPEEI 223
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1016-1223 |
2.08e-35 |
|
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: 135.26 E-value: 2.08e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1016 VKAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTRTPRKIRSR--IGYCPQTESVLNHMTG 1093
Cdd:cd03219 13 LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARlgIGRTFQIPRLFPELTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1094 RESLVM--------YARLWGVL--EQDINEYVEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIALMGKSSVVFLDEPSI 1163
Cdd:cd03219 93 LENVMVaaqartgsGLLLARARreEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAA 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1164 GMDPVAQHLLWETITWICKTGKAIIITSHRMEECEALCTRLAIMVKGRFTCLGTPQHVRK 1223
Cdd:cd03219 173 GLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1020-1192 |
3.38e-34 |
|
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: 130.68 E-value: 3.38e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1020 KNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTRTPRKIRSRIGYCPQTESVLNHMTGRESLVM 1099
Cdd:COG4133 19 SGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYLGHADGLKPELTVRENLRF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1100 YARLWGVLEQDinEYVEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIALMGKSSVVFLDEPSIGMDPVAQHLLWETITW 1179
Cdd:COG4133 99 WAALYGLRADR--EAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAA 176
|
170
....*....|...
gi 525313703 1180 ICKTGKAIIITSH 1192
Cdd:COG4133 177 HLARGGAVLLTTH 189
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1019-1161 |
6.18e-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: 127.76 E-value: 6.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1019 VKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTRTPRKI-RSRIGYCPQTESVLNHMTGRESL 1097
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSlRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 525313703 1098 VMYARLWGVLEQDINEYVEAFLHSVHLEPIADQFI----HTYSAGSKRRLSTAIALMGKSSVVFLDEP 1161
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVgerpGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
168-371 |
9.02e-34 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 129.55 E-value: 9.02e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 168 HLHKEFKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISD-NMIEVRKDLGFCPQHDL 246
Cdd:COG4619 5 GLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAmPPPEWRRQVAYVPQEPA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 247 LFDDlTLSEHLFFYCMVKGipQNINCEEIDRMLSAFNLQENY-----HTLSGsasgGVRRKLSIVLALMAGSKVVILDEP 321
Cdd:COG4619 85 LWGG-TVRDNLPFPFQLRE--RKFDRERALELLERLGLPPDIldkpvERLSG----GERQRLALIRALLLQPDVLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 525313703 322 SSGMDPVSRRATWDILQHY--KHNRTILLTTHYMDEADVLGDRVAIMVRGTL 371
Cdd:COG4619 158 TSALDPENTRRVEELLREYlaEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1018-1221 |
2.18e-33 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 129.44 E-value: 2.18e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1018 AVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGnsvtRTPRKIRSRIGYCPQTESVLNH--MTGRE 1095
Cdd:COG1121 21 VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFG----KPPRRARRRIGYVPQRAEVDWDfpITVRD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1096 sLVMYAR-----LWGVLEQDINEYVEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIALMGKSSVVFLDEPSIGMDPVAQ 1170
Cdd:COG1121 97 -VVLMGRygrrgLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 525313703 1171 HLLWETITWICKTGKAIIITSHRMEECEALCTRLAIMVKGRFtCLGTPQHV 1221
Cdd:COG1121 176 EALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLV-AHGPPEEV 225
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1015-1253 |
3.88e-33 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 131.36 E-value: 3.88e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1015 VVKAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGnsvtRTP----RKIRSRIGycpqteSVLN- 1089
Cdd:COG4586 34 EVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLG----YVPfkrrKEFARRIG------VVFGq 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1090 ------HMTGRESLVMYARLWGVLEQD----INEYVEAFlhsvHLEPIADQFIHTYSAGSKRRLSTAIALMGKSSVVFLD 1159
Cdd:COG4586 104 rsqlwwDLPAIDSFRLLKAIYRIPDAEykkrLDELVELL----DLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLD 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1160 EPSIGMDPVAQHLLWETITWICKTGKA-IIITSHRMEECEALCTRLAIMVKGRFTCLGTPQHVRKRFGHVYTLTVRInia 1238
Cdd:COG4586 180 EPTIGLDVVSKEAIREFLKEYNRERGTtILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEELKERFGPYKTIVLEL--- 256
|
250
....*....|....*
gi 525313703 1239 KDEDKVEEFKNFIKV 1253
Cdd:COG4586 257 AEPVPPLELPRGGEV 271
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1016-1223 |
7.70e-33 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 128.23 E-value: 7.70e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1016 VKAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTR-TPRKI-RSRIGYCPQTESVLNHMTG 1093
Cdd:COG0411 17 LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGlPPHRIaRLGIARTFQNPRLFPELTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1094 RESLVMYA-------------RLWGVL--EQDINEYVEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIALMGKSSVVFL 1158
Cdd:COG0411 97 LENVLVAAharlgrgllaallRLPRARreEREARERAEELLERVGLADRADEPAGNLSYGQQRRLEIARALATEPKLLLL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 525313703 1159 DEPSIGMDPVAQHLLWETITWICK-TGKAIIITSHRMEECEALCTRLAIMVKGRFTCLGTPQHVRK 1223
Cdd:COG0411 177 DEPAAGLNPEETEELAELIRRLRDeRGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAEVRA 242
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
1017-1221 |
9.89e-33 |
|
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: 127.39 E-value: 9.89e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1017 KAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTRTPRKIRSR--IGYCPQTESVLNHMTGR 1094
Cdd:TIGR04406 15 KVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARlgIGYLPQEASIFRKLTVE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1095 ESLVmyarlwGVLE-------QDINEYVEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIALMGKSSVVFLDEPSIGMDP 1167
Cdd:TIGR04406 95 ENIM------AVLEirkdldrAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDEPFAGVDP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 525313703 1168 VAQHLLWETITWICKTGKAIIITSHRMEECEALCTRLAIMVKGRFTCLGTPQHV 1221
Cdd:TIGR04406 169 IAVGDIKKIIKHLKERGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEI 222
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
179-323 |
1.12e-32 |
|
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: 124.30 E-value: 1.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 179 VNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISDNMIE-VRKDLGFCPQHDLLFDDLTLSEHL 257
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKsLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 258 FFYCMVKGIPQNINCEEIDRMLSAFNLQENYHTLSGSA----SGGVRRKLSIVLALMAGSKVVILDEPSS 323
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVGERpgtlSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
164-375 |
1.19e-32 |
|
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: 126.48 E-value: 1.19e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 164 IHIMHLHKEFKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISDNMIEvRKDLGFCPQ 243
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE-RRNIGMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 244 HDLLFDDLTLSEHLFFYCMVKGIP---QNINCEEIDRMLSAFNLQENY-HTLsgsaSGGVRRKLSIVLALMAGSKVVILD 319
Cdd:cd03259 80 DYALFPHLTVAENIAFGLKLRGVPkaeIRARVRELLELVGLEGLLNRYpHEL----SGGQQQRVALARALAREPSLLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 525313703 320 EPSSGMDPVSRRATWDILQHYKHNR--TILLTTHYMDEADVLGDRVAIMVRGTLHCCG 375
Cdd:cd03259 156 EPLSALDAKLREELREELKELQRELgiTTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
164-366 |
2.31e-32 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 125.66 E-value: 2.31e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 164 IHIMHLHKEFKNK----PAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISdnmiEVRKDLG 239
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVT----GPGPDRG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 240 FCPQHDLLFDDLTLSEHLFFYCMVKGIPQNINCEEIDRMLSAFNLQ--ENY--HTLSGsasgGVRRKLSIVLALMAGSKV 315
Cdd:cd03293 77 YVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSgfENAypHQLSG----GMRQRVALARALAVDPDV 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 525313703 316 VILDEPSSGMDPVSRRATWD-ILQHY-KHNRTILLTTHYMDEADVLGDRVAIM 366
Cdd:cd03293 153 LLLDEPFSALDALTREQLQEeLLDIWrETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
158-400 |
3.12e-32 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 128.38 E-value: 3.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 158 PNLEAGIHIMHLHKEFKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISDNMIEVRKD 237
Cdd:PRK13537 2 PMSVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 238 LGFCPQHDLLFDDLTLSEHLFFYCMVKGIPQNINCEEIDRMLSAFNLQENYHTLSGSASGGVRRKLSIVLALMAGSKVVI 317
Cdd:PRK13537 82 VGVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 318 LDEPSSGMDPVSRRATWDILQH-YKHNRTILLTTHYMDEADVLGDRVAIMVRGtlhccgssvflKQIYGAGYHIVMEKQQ 396
Cdd:PRK13537 162 LDEPTTGLDPQARHLMWERLRSlLARGKTILLTTHFMEEAERLCDRLCVIEEG-----------RKIAEGAPHALIESEI 230
|
....
gi 525313703 397 YCDV 400
Cdd:PRK13537 231 GCDV 234
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
168-376 |
5.20e-32 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 125.24 E-value: 5.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 168 HLHKEFKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISDNMIEVRKDLG----FcpQ 243
Cdd:cd03219 5 GLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGigrtF--Q 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 244 HDLLFDDLT------------LSEHLFFYCMVKGIPQNIncEEIDRMLSAFNLQENYHTLSGSASGGVRRKLSIVLALMA 311
Cdd:cd03219 83 IPRLFPELTvlenvmvaaqarTGSGLLLARARREEREAR--ERAEELLERVGLADLADRPAGELSYGQQRRLEIARALAT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 525313703 312 GSKVVILDEPSSGMDPVSRRATWDILQHYK-HNRTILLTTHYMDEADVLGDRVAIMVRGTLHCCGS 376
Cdd:cd03219 161 DPKLLLLDEPAAGLNPEETEELAELIRELReRGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGT 226
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
164-370 |
7.64e-32 |
|
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: 122.68 E-value: 7.64e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 164 IHIMHLHKEFKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISDNMIEV---RKDLGF 240
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELpplRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 241 CPQHDLLFDDLTlsehlffycmvkgIPQNInceeidrmlsAFNLqenyhtlsgsaSGGVRRKLSIVLALMAGSKVVILDE 320
Cdd:cd03229 81 VFQDFALFPHLT-------------VLENI----------ALGL-----------SGGQQQRVALARALAMDPDVLLLDE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 525313703 321 PSSGMDPVSRRATWDILQ--HYKHNRTILLTTHYMDEADVLGDRVAIMVRGT 370
Cdd:cd03229 127 PTSALDPITRREVRALLKslQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1003-1221 |
8.77e-32 |
|
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: 125.11 E-value: 8.77e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1003 LNEVTKIYFKCPvvKAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTRT-PRKIRSRIGYC 1081
Cdd:cd03295 3 FENVTKRYGGGK--KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQdPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1082 PQTESVLNHMTGRESLVMYARLWGVLEQDINEYVEAFLHSVHLEP--IADQFIHTYSAGSKRRLSTAIALMGKSSVVFLD 1159
Cdd:cd03295 81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPaeFADRYPHELSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 525313703 1160 EPSIGMDPVAQHLLWETITWICKT-GKAIIITSHRMEECEALCTRLAIMVKGRFTCLGTPQHV 1221
Cdd:cd03295 161 EPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEI 223
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
168-371 |
9.91e-32 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 124.58 E-value: 9.91e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 168 HLHKEFKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISD-NMIE-VRKDLGFCPQHD 245
Cdd:cd03218 5 NLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKlPMHKrARLGIGYLPQEA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 246 LLFDDLTLSEHLFFYCMVKGIPQNINCEEIDRMLSAFNLQENYHTLSGSASGGVRRKLSIVLALMAGSKVVILDEPSSGM 325
Cdd:cd03218 85 SIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGV 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 525313703 326 DPVSRRATWDILQHYKhNRTI--LLTTHYMDEADVLGDRVAIMVRGTL 371
Cdd:cd03218 165 DPIAVQDIQKIIKILK-DRGIgvLITDHNVRETLSITDRAYIIYEGKV 211
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1018-1219 |
1.05e-31 |
|
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: 124.08 E-value: 1.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1018 AVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSG-IAFiDGNSVTRTP--RKIRSRIGYCPQTESVLNHMTGR 1094
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGsIRF-DGRDITGLPphERARAGIGYVPEGRRIFPELTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1095 ESLVM--YARLWGVLEQDINEYVEAFlhsvhlePIADQFIH----TYSAGSKRRLSTAIALMGKSSVVFLDEPSIGMDPV 1168
Cdd:cd03224 94 ENLLLgaYARRRAKRKARLERVYELF-------PRLKERRKqlagTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPK 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 525313703 1169 AQHLLWETITWICKTGKAIIITSHRMEECEALCTRLAIMVKGRFTCLGTPQ 1219
Cdd:cd03224 167 IVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAA 217
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
164-371 |
1.05e-31 |
|
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: 124.72 E-value: 1.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 164 IHIMHLHKEFKN-KPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISD-NMIEVRKDLGFC 241
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREqDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 242 PQHDLLFDDLTLSEHLFFYCMVKGIPQNINCEEIDRMLSAFNL--QENYHTLSGSASGGVRRKLSIVLALMAGSKVVILD 319
Cdd:cd03295 81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 525313703 320 EPSSGMDPVSRRATWDILQHYKH--NRTILLTTHYMDEADVLGDRVAIMVRGTL 371
Cdd:cd03295 161 EPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIDEAFRLADRIAIMKNGEI 214
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1015-1211 |
1.33e-31 |
|
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: 124.37 E-value: 1.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1015 VVKAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTRTPRKIRSRIGYC-PQTESVLNHMTG 1093
Cdd:cd03267 33 EVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVfGQKTQLWWDLPV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1094 RESLVMYARLWGVLEQDINEYVEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIALMGKSSVVFLDEPSIGMDPVAQHLL 1173
Cdd:cd03267 113 IDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENI 192
|
170 180 190
....*....|....*....|....*....|....*....
gi 525313703 1174 WETITWICK-TGKAIIITSHRMEECEALCTRLAIMVKGR 1211
Cdd:cd03267 193 RNFLKEYNReRGTTVLLTSHYMKDIEALARRVLVIDKGR 231
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
177-369 |
1.48e-31 |
|
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: 123.70 E-value: 1.48e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 177 PAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISD---NMIeVRKDLGFCPQHDLLFDDLTL 253
Cdd:cd03224 14 QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGlppHER-ARAGIGYVPEGRRIFPELTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 254 SEHLFFYCMVKGIPQNIncEEIDRMLSAF-NLQENYHTLSGSASGGVRRKLSIVLALMAGSKVVILDEPSSGMDPVSRRA 332
Cdd:cd03224 93 EENLLLGAYARRRAKRK--ARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEE 170
|
170 180 190
....*....|....*....|....*....|....*...
gi 525313703 333 TWDILQHYK-HNRTILLTTHYMDEADVLGDRVAIMVRG 369
Cdd:cd03224 171 IFEAIRELRdEGVTILLVEQNARFALEIADRAYVLERG 208
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
153-371 |
4.81e-31 |
|
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: 122.44 E-value: 4.81e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 153 YEAEPPNLEAGIHImhLHKEFKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISDNMI 232
Cdd:cd03267 13 YSKEPGLIGSLKSL--FKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 233 EVRKDLGFC-PQHDLLFDDLTLSEHLFFYCMVKGIPQNINCEEIDRMLSAFNLQENYHTLSGSASGGVRRKLSIVLALMA 311
Cdd:cd03267 91 KFLRRIGVVfGQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLH 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 525313703 312 GSKVVILDEPSSGMDPVSRRATWDILQHY--KHNRTILLTTHYMDEADVLGDRVAIMVRGTL 371
Cdd:cd03267 171 EPEILFLDEPTIGLDVVAQENIRNFLKEYnrERGTTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1018-1226 |
8.33e-31 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 131.79 E-value: 8.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1018 AVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTRTPRKIRSRIGYCPQTESVLNHMTGRESL 1097
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIATRRRVGYMSQAFSLYGELTVRQNL 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1098 VMYARLWGVLEQDINEYVEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIALMGKSSVVFLDEPSIGMDPVAQHLLWET- 1176
Cdd:NF033858 361 ELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLl 440
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 525313703 1177 ITWICKTGKAIIITSHRMEECEaLCTRLAIMVKGRFTCLGTPQHVRKRFG 1226
Cdd:NF033858 441 IELSREDGVTIFISTHFMNEAE-RCDRISLMHAGRVLASDTPAALVAARG 489
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1019-1235 |
1.22e-30 |
|
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: 122.07 E-value: 1.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1019 VKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTRTPRKIRSR-IGYCPQTESVLNHMTGREsL 1097
Cdd:COG1120 17 LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARrIAYVPQEPPAPFGLTVRE-L 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1098 VMYAR-----LWGVL-EQDInEYVEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIALMGKSSVVFLDEPSIGMDPVAQH 1171
Cdd:COG1120 96 VALGRyphlgLFGRPsAEDR-EAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQL 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 525313703 1172 LLWETITWICKT-GKAIIITSHRMEECEALCTRLAIMVKGRFTCLGTPQHV--RKRFGHVYTLTVRI 1235
Cdd:COG1120 175 EVLELLRRLARErGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVltPELLEEVYGVEARV 241
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1001-1211 |
3.52e-30 |
|
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: 119.16 E-value: 3.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1001 LLLNEVTKIYFKcpvVKAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTRTPrKIRSRIGY 1080
Cdd:cd03259 1 LELKGLSKTYGS---VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVP-PERRNIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1081 CPQTESVLNHMTGRESLVMYARLWGVLEQDINEYVEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIALMGKSSVVFLDE 1160
Cdd:cd03259 77 VFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 525313703 1161 PSIGMDP-VAQHLLWETITWICKTGKAIIITSHRMEECEALCTRLAIMVKGR 1211
Cdd:cd03259 157 PLSALDAkLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGR 208
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
164-371 |
8.55e-30 |
|
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: 118.36 E-value: 8.55e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 164 IHIMHLHKEFKN----KPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISdNMIEVRKD-- 237
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDIS-KLSEKELAaf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 238 ----LGFCPQHDLLFDDLTLSEHLFFYCMVKGIPQNINCEEIDRMLSAFNLQENYHTLSGSASGGVRRKLSIVLALMAGS 313
Cdd:cd03255 80 rrrhIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 314 KVVILDEPSSGMDPVSRRATWDILQ--HYKHNRTILLTTHYMDEADvLGDRVAIMVRGTL 371
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVMELLRelNKEAGTTIVVVTHDPELAE-YADRIIELRDGKI 218
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
999-1221 |
9.43e-30 |
|
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: 125.40 E-value: 9.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 999 TPLLLNEVTKIYFKCPVVKAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTG---EETITSGIAFIDGNSVTRTPRKIR 1075
Cdd:COG1123 2 TPLLEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGllpHGGRISGEVLLDGRDLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1076 SR-IGYCPQ-TESVLNHMTGRESLVMYARLWGVLEQDINEYVEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIALMGKS 1153
Cdd:COG1123 82 GRrIGMVFQdPMTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 525313703 1154 SVVFLDEPSIGMDPVAQHLLWETITWICK-TGKAIIITSHRMEECEALCTRLAIMVKGRFTCLGTPQHV 1221
Cdd:COG1123 162 DLLIADEPTTALDVTTQAEILDLLRELQReRGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
999-1230 |
9.43e-30 |
|
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: 125.40 E-value: 9.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 999 TPLL-LNEVTKIY--FKCPVVKAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVT----RTP 1071
Cdd:COG1123 258 EPLLeVRNLSKRYpvRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTklsrRSL 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1072 RKIRSRIGYCPQ-TESVLN-HMTGRESLVMYARLWGVL-EQDINEYVEAFLHSVHLEP-IADQFIHTYSAGSKRRLSTAI 1147
Cdd:COG1123 338 RELRRRVQMVFQdPYSSLNpRMTVGDIIAEPLRLHGLLsRAERRERVAELLERVGLPPdLADRYPHELSGGQRQRVAIAR 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1148 ALMGKSSVVFLDEPSIGMDPVAQH----LLWEtitwICK-TGKAIIITSHRMEECEALCTRLAIMVKGRFTCLGTPQHVR 1222
Cdd:COG1123 418 ALALEPKLLILDEPTSALDVSVQAqilnLLRD----LQReLGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVF 493
|
....*...
gi 525313703 1223 KRFGHVYT 1230
Cdd:COG1123 494 ANPQHPYT 501
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
171-375 |
2.15e-29 |
|
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: 117.37 E-value: 2.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 171 KEFKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRF---AATRGEAYINGYNISDNmiEVRKDLGFCPQHDLL 247
Cdd:cd03234 15 NWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVeggGTTSGQILFNGQPRKPD--QFQKCVAYVRQDDIL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 248 FDDLTLSEHLFFYCMVKGipQNINCEEIDRM------LSAFNLQENYHTLSGSASGGVRRKLSIVLALMAGSKVVILDEP 321
Cdd:cd03234 93 LPGLTVRETLTYTAILRL--PRKSSDAIRKKrvedvlLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 525313703 322 SSGMDPVSRRATWDILQHY-KHNRTILLTTHyMDEADV--LGDRVAIMVRGTLHCCG 375
Cdd:cd03234 171 TSGLDSFTALNLVSTLSQLaRRNRIVILTIH-QPRSDLfrLFDRILLLSSGEIVYSG 226
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
164-376 |
2.38e-29 |
|
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: 117.77 E-value: 2.38e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 164 IHIMHLHKEFKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNIS----DNMIEVRKDLG 239
Cdd:COG1127 6 IEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITglseKELYELRRRIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 240 FCPQHDLLFDDLT--------LSEHlffycmvKGIPQnincEEIDRM----LSAFNLQENYHTLSGSASGGVRRKLSIVL 307
Cdd:COG1127 86 MLFQGGALFDSLTvfenvafpLREH-------TDLSE----AEIRELvlekLELVGLPGAADKMPSELSGGMRKRVALAR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 525313703 308 ALMAGSKVVILDEPSSGMDPVSRRATWD-ILQ-HYKHNRTILLTTHYMDEADVLGDRVAIMVRGTLHCCGS 376
Cdd:COG1127 155 ALALDPEILLYDEPTAGLDPITSAVIDElIRElRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGT 225
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
168-371 |
2.49e-29 |
|
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: 117.76 E-value: 2.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 168 HLHKEFKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISD-NMIE-VRKDLGFCPQHD 245
Cdd:TIGR04406 6 NLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHlPMHErARLGIGYLPQEA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 246 LLFDDLTLSEHLffycMV-----KGIPQNINCEEIDRMLSAFNLQENYHTLSGSASGGVRRKLSIVLALMAGSKVVILDE 320
Cdd:TIGR04406 86 SIFRKLTVEENI----MAvleirKDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 525313703 321 PSSGMDPVsrrATWDILQHYKHNRT----ILLTTHYMDEADVLGDRVAIMVRGTL 371
Cdd:TIGR04406 162 PFAGVDPI---AVGDIKKIIKHLKErgigVLITDHNVRETLDICDRAYIISDGKV 213
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
164-376 |
2.92e-29 |
|
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: 117.22 E-value: 2.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 164 IHIMHLHKEFKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISDN----MIEVRKDLG 239
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLseaeLYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 240 FCPQHDLLFDDLTLSEHLFFYcmvkgIPQNINC--EEIDRM----LSAFNLQENYHTLSGSASGGVRRKLSIVLALMAGS 313
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFP-----LREHTRLseEEIREIvlekLEAVGLRGAEDLYPAELSGGMKKRVALARALALDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 525313703 314 KVVILDEPSSGMDPVSRRATWDILQHYK--HNRTILLTTHYMDEADVLGDRVAIMVRGTLHCCGS 376
Cdd:cd03261 156 ELLLYDEPTAGLDPIASGVIDDLIRSLKkeLGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGT 220
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
168-376 |
5.19e-29 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 117.45 E-value: 5.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 168 HLHKEFKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISDNMIEVRKDLG----FcpQ 243
Cdd:COG0411 9 GLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLGiartF--Q 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 244 HDLLFDDLTLSEHL----------FFYCMVKGIPQNI-----NCEEIDRMLSAFNLQENYHTLSGSASGGVRRKLSIVLA 308
Cdd:COG0411 87 NPRLFPELTVLENVlvaaharlgrGLLAALLRLPRARreereARERAEELLERVGLADRADEPAGNLSYGQQRRLEIARA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 525313703 309 LMAGSKVVILDEPSSGMDPVSRRATWDILQHYK--HNRTILLTTHYMDEadVLG--DRVAIMVRGTLHCCGS 376
Cdd:COG0411 167 LATEPKLLLLDEPAAGLNPEETEELAELIRRLRdeRGITILLIEHDMDL--VMGlaDRIVVLDFGRVIAEGT 236
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1003-1221 |
5.67e-29 |
|
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: 116.57 E-value: 5.67e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1003 LNEVTKIYFKCPvvkAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTRTPRKIRsRIGYCP 1082
Cdd:cd03300 3 LENVSKFYGGFV---ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKR-PVNTVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1083 QTESVLNHMTGRESLVMYARLWGVLEQDINEYVEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIALMGKSSVVFLDEPS 1162
Cdd:cd03300 79 QNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1163 IGMD-PVAQHLLWETITWICKTGKAIIITSHRMEECEALCTRLAIMVKGRFTCLGTPQHV 1221
Cdd:cd03300 159 GALDlKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
174-366 |
6.28e-29 |
|
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: 114.40 E-value: 6.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 174 KNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISD-NMIEVRKDLGFCPQHDLLFDDlT 252
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDlDLESLRKNIAYVPQDPFLFSG-T 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 253 LSEhlffycmvkgipqNInceeidrmLsafnlqenyhtlsgsaSGGVRRKLSIVLALMAGSKVVILDEPSSGMDPVSRRA 332
Cdd:cd03228 92 IRE-------------NI--------L----------------SGGQRQRIAIARALLRDPPILILDEATSALDPETEAL 134
|
170 180 190
....*....|....*....|....*....|....
gi 525313703 333 TWDILQHYKHNRTILLTTHYMDEADvLGDRVAIM 366
Cdd:cd03228 135 ILEALRALAKGKTVIVIAHRLSTIR-DADRIIVL 167
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1017-1221 |
6.47e-29 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 116.53 E-value: 6.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1017 KAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTRTPRKIRSR--IGYCPQTESVLNHMTgr 1094
Cdd:PRK10895 17 RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARrgIGYLPQEASIFRRLS-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1095 eslvMYARLWGVLE--QDIN-----EYVEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIALMGKSSVVFLDEPSIGMDP 1167
Cdd:PRK10895 95 ----VYDNLMAVLQirDDLSaeqreDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 525313703 1168 VAQHLLWETITWICKTGKAIIITSHRMEECEALCTRLAIMVKGRFTCLGTPQHV 1221
Cdd:PRK10895 171 ISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEI 224
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
161-366 |
7.98e-29 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 116.73 E-value: 7.98e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 161 EAGIHIMHLHKEFKNK----PAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISdnmiEVRK 236
Cdd:COG1116 5 APALELRGVSKRFPTGgggvTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVT----GPGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 237 DLGFCPQHDLLFDDLTLSEHLFFYCMVKGIPQNINCEEIDRMLSAFNLQ--ENY--HTLSGsasgGVRRKLSIVLALMAG 312
Cdd:COG1116 81 DRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAgfEDAypHQLSG----GMRQRVAIARALAND 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 525313703 313 SKVVILDEPSSGMDPVSRRATWDILQ--HYKHNRTILLTTHYMDEADVLGDRVAIM 366
Cdd:COG1116 157 PEVLLMDEPFGALDALTRERLQDELLrlWQETGKTVLFVTHDVDEAVFLADRVVVL 212
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
160-375 |
8.76e-29 |
|
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: 116.97 E-value: 8.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 160 LEAGIHIMHLHKEFKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNIS----DNMIEVR 235
Cdd:cd03294 21 LAKGKSKEEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAamsrKELRELR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 236 -KDLGFCPQHDLLFDDLTLSEHLFFYCMVKGIPQNINCEEIDRMLSAFNLQENYHTLSGSASGGVRRKLSIVLALMAGSK 314
Cdd:cd03294 101 rKKISMVFQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPD 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 525313703 315 VVILDEPSSGMDPVSRRATWDILQ--HYKHNRTILLTTHYMDEADVLGDRVAIMVRGTLHCCG 375
Cdd:cd03294 181 ILLMDEAFSALDPLIRREMQDELLrlQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVG 243
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1003-1227 |
9.48e-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: 115.76 E-value: 9.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1003 LNEVTKIYF-KCPVVKAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTRTP----RKIRSR 1077
Cdd:cd03258 4 LKNVSKVFGdTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSgkelRKARRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1078 IGYCPQTESVLNHMTGRESlVMYA-RLWGVLEQDINEYVEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIALMGKSSVV 1156
Cdd:cd03258 84 IGMIFQHFNLLSSRTVFEN-VALPlEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 525313703 1157 FLDEPSIGMDPVAQHLLWETITWI-CKTGKAIIITSHRMEECEALCTRLAIMVKGRFTCLGTpqhVRKRFGH 1227
Cdd:cd03258 163 LCDEATSALDPETTQSILALLRDInRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGT---VEEVFAN 231
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
164-403 |
4.17e-28 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 117.24 E-value: 4.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 164 IHIMHLHKEFKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISDNMIEVRKDLGFCPQ 243
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARARIGVVPQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 244 HDLLFDDLTLSEHLFFYCMVKGIPQNINCEEIDRMLSAFNLQENYHTLSGSASGGVRRKLSIVLALMAGSKVVILDEPSS 323
Cdd:PRK13536 122 FDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTT 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 324 GMDPVSRRATWDILQH-YKHNRTILLTTHYMDEADVLGDRVAIMVRGtlhccgssvflKQIYGAGYHIVMEKQQYCDVDN 402
Cdd:PRK13536 202 GLDPHARHLIWERLRSlLARGKTILLTTHFMEEAERLCDRLCVLEAG-----------RKIAEGRPHALIDEHIGCQVIE 270
|
.
gi 525313703 403 I 403
Cdd:PRK13536 271 I 271
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1018-1216 |
1.49e-27 |
|
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: 111.86 E-value: 1.49e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1018 AVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSvtrtPRKIRSRIGYCPQTESVLNHM--TGRE 1095
Cdd:cd03235 14 VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKP----LEKERKRIGYVPQRRSIDRDFpiSVRD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1096 SLVM----YARLWGVLEQDINEYVEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIALMGKSSVVFLDEPSIGMDPVAQH 1171
Cdd:cd03235 90 VVLMglygHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQE 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 525313703 1172 LLWETITWICKTGKAIIITSHRMEECEALCTRlAIMVKGRFTCLG 1216
Cdd:cd03235 170 DIYELLRELRREGMTILVVTHDLGLVLEYFDR-VLLLNRTVVASG 213
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
168-385 |
2.47e-27 |
|
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: 112.44 E-value: 2.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 168 HLHKEFKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISD-NMIEVRKDLGFCPQHDL 246
Cdd:COG1120 6 NLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASlSRRELARRIAYVPQEPP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 247 LFDDLTLSE--------HLFFYcmvkGIPQNINCEEIDRMLSAFNLQE----NYHTLsgsaSGGVRRKLSIVLALMAGSK 314
Cdd:COG1120 86 APFGLTVRElvalgrypHLGLF----GRPSAEDREAVEEALERTGLEHladrPVDEL----SGGERQRVLIARALAQEPP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 525313703 315 VVILDEPSSGMDPVSRRATWDILQHY--KHNRTILLTTHYMDEADVLGDRVAIMVRGTLHCCGS--SVF----LKQIYG 385
Cdd:COG1120 158 LLLLDEPTSHLDLAHQLEVLELLRRLarERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPpeEVLtpelLEEVYG 236
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
174-371 |
2.76e-27 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 110.33 E-value: 2.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 174 KNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGR--FAATRGEAYINGYNISDNmiEVRKDLGFCPQHDLLFDDL 251
Cdd:cd03213 20 SGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLINGRPLDKR--SFRKIIGYVPQDDILHPTL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 252 TLSEHLFFYCMVKGIpqninceeidrmlsafnlqenyhtlsgsaSGGVRRKLSIVLALMAGSKVVILDEPSSGMDPVSRR 331
Cdd:cd03213 98 TVRETLMFAAKLRGL-----------------------------SGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSAL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 525313703 332 ATWDILQHY-KHNRTILLTTHYM-DEADVLGDRVAIMVRGTL 371
Cdd:cd03213 149 QVMSLLRRLaDTGRTIICSIHQPsSEIFELFDKLLLLSQGRV 190
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
177-369 |
4.03e-27 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 111.23 E-value: 4.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 177 PAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISDNMIE--VRKDLGFCPQHDLLFDDLTLS 254
Cdd:COG0410 17 HVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHriARLGIGYVPEGRRIFPSLTVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 255 EHLFFYCMVKGIPQNINcEEIDRMLSAF-NLQENYHTLSGSASGGVRRKLSIVLALMAGSKVVILDEPSSGMDPVSRRAT 333
Cdd:COG0410 97 ENLLLGAYARRDRAEVR-ADLERVYELFpRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEI 175
|
170 180 190
....*....|....*....|....*....|....*..
gi 525313703 334 WDILQHYK-HNRTILLTTHYMDEADVLGDRVAIMVRG 369
Cdd:COG0410 176 FEIIRRLNrEGVTILLVEQNARFALEIADRAYVLERG 212
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1015-1211 |
4.15e-27 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 111.06 E-value: 4.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1015 VVKAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTRTPRKI----RSRIGYCPQTE-SVLN 1089
Cdd:cd03257 17 SVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLrkirRKEIQMVFQDPmSSLN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1090 -HMTGRESLVMYARLWGVL--EQDINEYVEAFLHSVHLEP-IADQFIHTYSAGSKRRLSTAIALMGKSSVVFLDEPSIGM 1165
Cdd:cd03257 97 pRMTIGEQIAEPLRIHGKLskKEARKEAVLLLLVGVGLPEeVLNRYPHELSGGQRQRVAIARALALNPKLLIADEPTSAL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 525313703 1166 DPVAQHLLWETITWICK-TGKAIIITSHRMEECEALCTRLAIMVKGR 1211
Cdd:cd03257 177 DVSVQAQILDLLKKLQEeLGLTLLFITHDLGVVAKIADRVAVMYAGK 223
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1019-1211 |
4.21e-27 |
|
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: 111.71 E-value: 4.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1019 VKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGiafidgNSVTR--------TPRKIRSRIGY--------CP 1082
Cdd:COG1119 19 LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYG------NDVRLfgerrggeDVWELRKRIGLvspalqlrFP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1083 QTESVLNH-MTGRESLVMyarLWGVLEQDINEYVEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIALMGKSSVVFLDEP 1161
Cdd:COG1119 93 RDETVLDVvLSGFFDSIG---LYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 525313703 1162 SIGMDPVAQHLLWETITWICKTG-KAIIITSHRMEECEALCTRLAIMVKGR 1211
Cdd:COG1119 170 TAGLDLGARELLLALLDKLAAEGaPTLVLVTHHVEEIPPGITHVLLLKDGR 220
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
175-391 |
9.57e-27 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 110.56 E-value: 9.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 175 NKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISdnmiEVRKDLGFCPQH---DLLF--- 248
Cdd:COG1121 18 GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPR----RARRRIGYVPQRaevDWDFpit 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 249 -DDLTLS----EHLFFycmvkGIPQNINCEEIDRMLSAFNLQENYHTLSGSASGGVRRKLSIVLALMAGSKVVILDEPSS 323
Cdd:COG1121 94 vRDVVLMgrygRRGLF-----RRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 525313703 324 GMDPVSRRATWDILQHY-KHNRTILLTTHYMDEADVLGDRVaIMVRGTLHCCGS--SVF----LKQIYGAGYHIV 391
Cdd:COG1121 169 GVDAATEEALYELLRELrREGKTILVVTHDLGAVREYFDRV-LLLNRGLVAHGPpeEVLtpenLSRAYGGPVALL 242
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
169-371 |
1.07e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 112.49 E-value: 1.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 169 LHKEFKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISDNMIEVRKDLGFC-PQHDLL 247
Cdd:COG4586 28 FRREYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFARRIGVVfGQRSQL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 248 FDDLTLSEHLFFYCMVKGIPQNINCEEIDRMLSAFNLQENYHTlsgsasgGVrRKLS--------IVLALMAGSKVVILD 319
Cdd:COG4586 108 WWDLPAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGELLDT-------PV-RQLSlgqrmrceLAAALLHRPKILFLD 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 525313703 320 EPSSGMDPVSRRATWDILQHY--KHNRTILLTTHYMDEADVLGDRVAIMVRGTL 371
Cdd:COG4586 180 EPTIGLDVVSKEAIREFLKEYnrERGTTILLTSHDMDDIEALCDRVIVIDHGRI 233
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
154-369 |
5.67e-26 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 115.99 E-value: 5.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 154 EAEPPNLEAgihiMHLHKEFKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISDNMIE 233
Cdd:NF033858 261 DDDEPAIEA----RGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 234 VRKDLGFCPQHDLLFDDLT------LSEHLFfycmvkGIPQNINCEEIDRMLSAFNLQENYHTLSGSASGGVRRKLSIVL 307
Cdd:NF033858 337 TRRRVGYMSQAFSLYGELTvrqnleLHARLF------HLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAV 410
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 525313703 308 ALMAGSKVVILDEPSSGMDPVSRRATWDILQHYKHNR--TILLTTHYMDEADvLGDRVAIMVRG 369
Cdd:NF033858 411 AVIHKPELLILDEPTSGVDPVARDMFWRLLIELSREDgvTIFISTHFMNEAE-RCDRISLMHAG 473
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1001-1207 |
5.71e-26 |
|
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: 107.56 E-value: 5.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1001 LLLNEVTKIYF-KCPVVKAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTRTPRkirsRIG 1079
Cdd:cd03293 1 LEVRNVSKTYGgGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGP----DRG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1080 YCPQTESVLNHMTGRESLVMYARLWGVLEQDINEYVEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIALMGKSSVVFLD 1159
Cdd:cd03293 77 YVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLD 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 525313703 1160 EPSIGMDPVAQHLLWETITWIC-KTGKAIIITSHRMEECEALCTRLAIM 1207
Cdd:cd03293 157 EPFSALDALTREQLQEELLDIWrETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
176-389 |
9.10e-26 |
|
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: 113.71 E-value: 9.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 176 KPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISD-NMIEVRKDLGFCPQHDLLFDDlTLS 254
Cdd:COG4987 348 RPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDlDEDDLRRRIAVVPQRPHLFDT-TLR 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 255 EHLffyCMVKGipqNINCEEIDRMLSA-------FNLQENYHTLSGSA----SGGVRRKLSIVLALMAGSKVVILDEPSS 323
Cdd:COG4987 427 ENL---RLARP---DATDEELWAALERvglgdwlAALPDGLDTWLGEGgrrlSGGERRRLALARALLRDAPILLLDEPTE 500
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 525313703 324 GMDPVSRRATWDILQHYKHNRTILLTTHYMDEADvLGDRVAIMVRGTLHCCGSSVFLKQIYGAGYH 389
Cdd:COG4987 501 GLDAATEQALLADLLEALAGRTVLLITHRLAGLE-RMDRILVLEDGRIVEQGTHEELLAQNGRYRQ 565
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
168-375 |
1.03e-25 |
|
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: 105.21 E-value: 1.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 168 HLHKEFKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISD-NMIEVRKDLGFCPQhdl 246
Cdd:cd03214 4 NLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASlSPKELARKIAYVPQ--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 247 lfddltlsehlffycmvkgipqninceeidrMLSAFNLQE----NYHTLsgsaSGGVRRKLSIVLALMAGSKVVILDEPS 322
Cdd:cd03214 81 -------------------------------ALELLGLAHladrPFNEL----SGGERQRVLLARALAQEPPILLLDEPT 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 525313703 323 SGMDPVSRRATWDILQHYK--HNRTILLTTHYMDEADVLGDRVAIMVRGTLHCCG 375
Cdd:cd03214 126 SHLDIAHQIELLELLRRLAreRGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
161-369 |
1.31e-25 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 107.04 E-value: 1.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 161 EAGIHIMHLHKEFKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISDNMIEVR--KDL 238
Cdd:COG1137 1 MMTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRarLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 239 GFCPQHDLLFDDLTLSEHLffycM----VKGIPQNINCEEIDRMLSAFNLQENYHTLSGSASGGVRRKLSIVLALMAGSK 314
Cdd:COG1137 81 GYLPQEASIFRKLTVEDNI----LavleLRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPK 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 525313703 315 VVILDEPSSGMDPVSRRATWDILQHYKH-NRTILLTTHYMDEAdvLG--DRVAIMVRG 369
Cdd:COG1137 157 FILLDEPFAGVDPIAVADIQKIIRHLKErGIGVLITDHNVRET--LGicDRAYIISEG 212
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1020-1223 |
1.39e-25 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 106.82 E-value: 1.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1020 KNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTRTPRK----IRSRIGYCPQTESVLNHMTGRE 1095
Cdd:cd03261 17 KGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAelyrLRRRMGMLFQSGALFDSLTVFE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1096 SLVMYARLWGVL-EQDINEYVEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIALMGKSSVVFLDEPSIGMDPVAQHLLW 1174
Cdd:cd03261 97 NVAFPLREHTRLsEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEPTAGLDPIASGVID 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 525313703 1175 ETITWICKT-GKAIIITSHRMEECEALCTRLAIMVKGRFTCLGTPQHVRK 1223
Cdd:cd03261 177 DLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
176-379 |
2.67e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 107.44 E-value: 2.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 176 KPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISD---NMIEVRKDLGFCPQHdllfddlt 252
Cdd:PRK13637 20 KKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDkkvKLSDIRKKVGLVFQY-------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 253 lSEH-LFFYCMVKGI---PQNINC--EEI-DRMLSAFNL----QENYHTLSG-SASGGVRRKLSI--VLALMagSKVVIL 318
Cdd:PRK13637 92 -PEYqLFEETIEKDIafgPINLGLseEEIeNRVKRAMNIvgldYEDYKDKSPfELSGGQKRRVAIagVVAME--PKILIL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 525313703 319 DEPSSGMDPVSRRatwDILQ-----HYKHNRTILLTTHYMDEADVLGDRVAIMVRGTLHCCG--SSVF 379
Cdd:PRK13637 169 DEPTAGLDPKGRD---EILNkikelHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGtpREVF 233
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1001-1211 |
2.71e-25 |
|
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: 105.26 E-value: 2.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1001 LLLNEVTKIYFKCPV-VKAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTRTPRKIRSR-- 1077
Cdd:cd03255 1 IELKNLSKTYGGGGEkVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAfr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1078 ---IGYCPQTESVLNHMTGRESLVMYARLWGVLEQDINEYVEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIALMGKSS 1154
Cdd:cd03255 81 rrhIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 525313703 1155 VVFLDEPSIGMDPVAQHLLWETITWICK-TGKAIIITSHRMEEcEALCTRLAIMVKGR 1211
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKeAGTTIVVVTHDPEL-AEYADRIIELRDGK 217
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
163-376 |
2.99e-25 |
|
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: 105.88 E-value: 2.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 163 GIHIMHLHKEFKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISDNMIEVRkDLGFCP 242
Cdd:cd03296 2 SIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQER-NVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 243 QHDLLFDDLTLSEHLFFYCMVKGIPQNINCEEIDRMLSAF-------NLQENY-HTLsgsaSGGVRRKLSIVLALMAGSK 314
Cdd:cd03296 81 QHYALFRHMTVFDNVAFGLRVKPRSERPPEAEIRAKVHELlklvqldWLADRYpAQL----SGGQRQRVALARALAVEPK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 525313703 315 VVILDEPSSGMDPVSRRA--TWDILQHYKHNRTILLTTHYMDEADVLGDRVAIMVRGTLHCCGS 376
Cdd:cd03296 157 VLLLDEPFGALDAKVRKElrRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGT 220
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
175-375 |
6.11e-25 |
|
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: 104.15 E-value: 6.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 175 NKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISDnmieVRKDLGFCPQHdLLFD----- 249
Cdd:cd03235 11 GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEK----ERKRIGYVPQR-RSIDrdfpi 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 250 ---DLTLSEhLFFYCMVKGIPQNINCEEIDRMLSAFNLQENYHTLSGSASGGVRRKLSIVLALMAGSKVVILDEPSSGMD 326
Cdd:cd03235 86 svrDVVLMG-LYGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 525313703 327 PVSRRATWDILQHYK-HNRTILLTTHYMDEADVLGDRVaIMVRGTLHCCG 375
Cdd:cd03235 165 PKTQEDIYELLRELRrEGMTILVVTHDLGLVLEYFDRV-LLLNRTVVASG 213
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1016-1225 |
6.68e-25 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 104.68 E-value: 6.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1016 VKAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSG-IAFiDGNSVTRTP--RKIRSRIGYCPQTESVLNHMT 1092
Cdd:COG0410 16 IHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGsIRF-DGEDITGLPphRIARLGIGYVPEGRRIFPSLT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1093 GRESLVM--YARLWGVLEQDINEYV-EAFlhsvhlePIADQFIH----TYSAGSKRRLSTAIALMGKSSVVFLDEPSIGM 1165
Cdd:COG0410 95 VEENLLLgaYARRDRAEVRADLERVyELF-------PRLKERRRqragTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 525313703 1166 DPVAQHLLWETITWICKTGKAIIITSHRMEECEALCTRLAIMVKGRFTCLGTPQ------HVRKRF 1225
Cdd:COG0410 168 APLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAelladpEVREAY 233
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
153-351 |
7.33e-25 |
|
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: 111.85 E-value: 7.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 153 YEAEPPNLEAGIHIMHLHK--EFKN---------KPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAY 221
Cdd:COG2274 454 LPPEREEGRSKLSLPRLKGdiELENvsfrypgdsPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRIL 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 222 INGYNISD-NMIEVRKDLGFCPQHDLLFDDlTLSEhlffycmvkgipqNINC-------EEIDRMLSAFNLQE------- 286
Cdd:COG2274 534 IDGIDLRQiDPASLRRQIGVVLQDVFLFSG-TIRE-------------NITLgdpdatdEEIIEAARLAGLHDfiealpm 599
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 525313703 287 NYHTL---SGSA-SGGVRRKLSIVLALMAGSKVVILDEPSSGMDPVSRRATWDILQHYKHNRTILLTTH 351
Cdd:COG2274 600 GYDTVvgeGGSNlSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAH 668
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1001-1211 |
7.62e-25 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 102.65 E-value: 7.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1001 LLLNEVTKIYFKcpvVKAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTRT---PRKIRSR 1077
Cdd:cd03229 1 LELKNVSKRYGQ---KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLedeLPPLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1078 IGYCPQTESVLNHMTGRESLVMyaRLwgvleqdineyveaflhsvhlepiadqfihtySAGSKRRLSTAIALMGKSSVVF 1157
Cdd:cd03229 78 IGMVFQDFALFPHLTVLENIAL--GL--------------------------------SGGQQQRVALARALAMDPDVLL 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 525313703 1158 LDEPSIGMDPVAQHLLWETITWICKT-GKAIIITSHRMEECEALCTRLAIMVKGR 1211
Cdd:cd03229 124 LDEPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1007-1211 |
1.35e-24 |
|
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: 103.38 E-value: 1.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1007 TKIYFKCPVVKAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGiafidgnSVTRTpRKIRSRIGYcpqTES 1086
Cdd:cd03220 26 LGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSG-------TVTVR-GRVSSLLGL---GGG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1087 VLNHMTGRESLVMYARLWGVLEQDINEYVEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIALMGKSSVVFLDEP-SIGm 1165
Cdd:cd03220 95 FNPELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVlAVG- 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 525313703 1166 DPVAQHLLWETITWICKTGKAIIITSHRMEECEALCTRLAIMVKGR 1211
Cdd:cd03220 174 DAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGK 219
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
164-371 |
1.69e-24 |
|
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: 103.41 E-value: 1.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 164 IHIMHLHKEFKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTG-----RFAATRGEAYING---YNISDNMIEVR 235
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLDGkdiYDLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 236 KDLGFCPQHDLLFDdLTLSEHLFFYCMVKGIPQNINCEEIDR-MLSAFNLQENYH--TLSGSASGGVRRKLSIVLALMAG 312
Cdd:cd03260 81 RRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIKLKEELDERVEeALRKAALWDEVKdrLHALGLSGGQQQRLCLARALANE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 525313703 313 SKVVILDEPSSGMDPVSRRATWDILQHYKHNRTILLTTHYMDEADVLGDRVAIMVRGTL 371
Cdd:cd03260 160 PEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVADRTAFLLNGRL 218
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
176-376 |
1.88e-24 |
|
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: 109.85 E-value: 1.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 176 KPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISD-NMIEVRKDLGFCPQHDLLFDDlTLS 254
Cdd:COG4988 350 RPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDlDPASWRRQIAWVPQNPYLFAG-TIR 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 255 EHLFFYCmvkgipQNINCEEIDR-----MLSAF--NLQENYHTLSGSA----SGGVRRKLSIVLALMAGSKVVILDEPSS 323
Cdd:COG4988 429 ENLRLGR------PDASDEELEAaleaaGLDEFvaALPDGLDTPLGEGgrglSGGQAQRLALARALLRDAPLLLLDEPTA 502
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 525313703 324 GMDPVSRRATWDILQHYKHNRTILLTTHymDEADV-LGDRVAIMVRGTLHCCGS 376
Cdd:COG4988 503 HLDAETEAEILQALRRLAKGRTVILITH--RLALLaQADRILVLDDGRIVEQGT 554
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
164-371 |
1.91e-24 |
|
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: 103.35 E-value: 1.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 164 IHIMHLHKEFKNK----PAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISDNMIEVRKDLG 239
Cdd:cd03257 2 LEVKNLSVSFPTGggsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 240 FCPQhdLLFDD--------LTLSEHLF--FYCMVKGIPQNINCEEIDRMLSAFNLQENY-----HTLSGsasgGVRRKLS 304
Cdd:cd03257 82 KEIQ--MVFQDpmsslnprMTIGEQIAepLRIHGKLSKKEARKEAVLLLLVGVGLPEEVlnrypHELSG----GQRQRVA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 525313703 305 IVLALMAGSKVVILDEPSSGMDPVSRRATWDILQ--HYKHNRTILLTTHYMDEADVLGDRVAIMVRGTL 371
Cdd:cd03257 156 IARALALNPKLLIADEPTSALDVSVQAQILDLLKklQEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
164-371 |
2.75e-24 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 108.84 E-value: 2.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 164 IHIMHLHKEFKN--KPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTG---RFAATRGEAYINGYNISDNMIEVR-KD 237
Cdd:COG1123 5 LEVRDLSVRYPGgdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGllpHGGRISGEVLLDGRDLLELSEALRgRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 238 LGFCPQH-DLLFDDLTLSEHLFFYCMVKGIPQNINCEEIDRMLSAFNLQENYHTLSGSASGGVRRKLSIVLALMAGSKVV 316
Cdd:COG1123 85 IGMVFQDpMTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 525313703 317 ILDEPSSGMDPVSRRATWDILQ--HYKHNRTILLTTHYMDEADVLGDRVAIMVRGTL 371
Cdd:COG1123 165 IADEPTTALDVTTQAEILDLLRelQRERGTTVLLITHDLGVVAEIADRVVVMDDGRI 221
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
994-1211 |
4.74e-24 |
|
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: 99.81 E-value: 4.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 994 LRLQNtplllneVTKIYfkcPVVKAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVT-RTPR 1072
Cdd:cd03216 1 LELRG-------ITKRF---GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSfASPR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1073 K-IRSRIGycpqtesvlnhmtgreslvmyarlwgvleqdineyveaflhsvhlepiadqFIHTYSAGSKRRLSTAIALMG 1151
Cdd:cd03216 71 DaRRAGIA---------------------------------------------------MVYQLSVGERQMVEIARALAR 99
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 525313703 1152 KSSVVFLDEPSIGMDPV-AQHLLwETITWICKTGKAIIITSHRMEECEALCTRLAIMVKGR 1211
Cdd:cd03216 100 NARLLILDEPTAALTPAeVERLF-KVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGR 159
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1019-1211 |
4.94e-24 |
|
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: 101.09 E-value: 4.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1019 VKNISLVVKKSECFGLLGLNGAGKTTTFKMLTG--EETITSGIAFIDGnsVTRTPRKIRSRIGYCPQTESVLNHMTGRES 1096
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLING--RPLDKRSFRKIIGYVPQDDILHPTLTVRET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1097 LVMYARLWGVleqdineyveaflhsvhlepiadqfihtySAGSKRRLSTAIALMGKSSVVFLDEPSIGMDPVAQHLLWET 1176
Cdd:cd03213 103 LMFAAKLRGL-----------------------------SGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSL 153
|
170 180 190
....*....|....*....|....*....|....*.
gi 525313703 1177 ITWICKTGKAIIITSHRM-EECEALCTRLAIMVKGR 1211
Cdd:cd03213 154 LRRLADTGRTIICSIHQPsSEIFELFDKLLLLSQGR 189
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
168-371 |
6.92e-24 |
|
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: 107.30 E-value: 6.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 168 HLHKEFKNK-----PAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISD----NMIEVRKDL 238
Cdd:COG1123 265 NLSKRYPVRgkggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKlsrrSLRELRRRV 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 239 GFCPQH--DLLFDDLTLSEHLFFYCMVKGI--PQNINcEEIDRMLSAFNLQENY-----HTLsgsaSGGVRRKLSIVLAL 309
Cdd:COG1123 345 QMVFQDpySSLNPRMTVGDIIAEPLRLHGLlsRAERR-ERVAELLERVGLPPDLadrypHEL----SGGQRQRVAIARAL 419
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 525313703 310 MAGSKVVILDEPSSGMDPVSRRATWDILQHYK--HNRTILLTTHYMDEADVLGDRVAIMVRGTL 371
Cdd:COG1123 420 ALEPKLLILDEPTSALDVSVQAQILNLLRDLQreLGLTYLFISHDLAVVRYIADRVAVMYDGRI 483
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1001-1216 |
8.18e-24 |
|
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: 100.79 E-value: 8.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1001 LLLNEVTKIYFKcpvVKAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTRTPRKIRSrIGY 1080
Cdd:cd03301 1 VELENVTKRFGN---VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRD-IAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1081 CPQTESVLNHMTGRESLVMYARLWGVLEQDINEYVEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIALMGKSSVVFLDE 1160
Cdd:cd03301 77 VFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1161 PSIGMDpvaQHLLWETITWICK----TGKAIIITSHRMEECEALCTRLAIMVKGRFTCLG 1216
Cdd:cd03301 157 PLSNLD---AKLRVQMRAELKRlqqrLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
168-376 |
1.05e-23 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 101.51 E-value: 1.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 168 HLHKEFKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISDNMI--EVRKDLGFCPQHD 245
Cdd:PRK10895 8 NLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLhaRARRGIGYLPQEA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 246 LLFDDLTLSEHLFfycMVKGIPQNINCEE----IDRMLSAFNLQENYHTLSGSASGGVRRKLSIVLALMAGSKVVILDEP 321
Cdd:PRK10895 88 SIFRRLSVYDNLM---AVLQIRDDLSAEQredrANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 525313703 322 SSGMDPVSRRATWDILQHYK-HNRTILLTTHYMDEADVLGDRVAIMVRGTLHCCGS 376
Cdd:PRK10895 165 FAGVDPISVIDIKRIIEHLRdSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGT 220
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
987-1221 |
1.39e-23 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 104.53 E-value: 1.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 987 GKVFTLLLRLQNtplllneVTKIYFKCPvvkAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNS 1066
Cdd:PRK11607 13 RKALTPLLEIRN-------LTKSFDGQH---AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1067 VTRTPRKIRSrIGYCPQTESVLNHMTGRESLVMYARLWGVLEQDINEYVEAFLHSVHLEPIADQFIHTYSAGSKRRLSTA 1146
Cdd:PRK11607 83 LSHVPPYQRP-INMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 525313703 1147 IALMGKSSVVFLDEPSIGMD-PVAQHLLWETITWICKTGKAIIITSHRMEECEALCTRLAIMVKGRFTCLGTPQHV 1221
Cdd:PRK11607 162 RSLAKRPKLLLLDEPMGALDkKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
164-369 |
1.71e-23 |
|
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: 100.73 E-value: 1.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 164 IHIMHLHKEFKNK----PAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISD----NMIEVR 235
Cdd:cd03258 2 IELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLlsgkELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 236 KDLGFCPQHDLLFDDLTLSEHLFFYCMVKGIPQNINCEEIDRMLSAFNLQENYHTLSGSASGGVRRKLSIVLALMAGSKV 315
Cdd:cd03258 82 RRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 525313703 316 VILDEPSSGMDPVSRRATWDILQ--HYKHNRTILLTTHYMDEADVLGDRVAIMVRG 369
Cdd:cd03258 162 LLCDEATSALDPETTQSILALLRdiNRELGLTIVLITHEMEVVKRICDRVAVMEKG 217
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
164-371 |
2.66e-23 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 99.53 E-value: 2.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 164 IHIMHLHKEFKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISD---NMIEVRKDLGF 240
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDdkkNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 241 CPQHDLLFDDLTLSEHLFFYCM-VKGIPQNINCEEIDRMLSAFNLQENYHTLSGSASGGVRRKLSIVLALMAGSKVVILD 319
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPIkVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 525313703 320 EPSSGMDPVSRRATWDILQHYKH-NRTILLTTHYMDEADVLGDRVAIMVRGTL 371
Cdd:cd03262 161 EPTSALDPELVGEVLDVMKDLAEeGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
164-369 |
3.01e-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: 99.25 E-value: 3.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 164 IHIMHLHKEFKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISDNMIEVRkDLGFCPQ 243
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDR-DIAMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 244 HDLLFDDLTLSEHLFFYCMVKGIPQnincEEIDR-------MLSAFNLQENY-HTLsgsaSGGVRRKLSIVLALMAGSKV 315
Cdd:cd03301 80 NYALYPHMTVYDNIAFGLKLRKVPK----DEIDErvrevaeLLQIEHLLDRKpKQL----SGGQRQRVALGRAIVREPKV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 525313703 316 VILDEPSSGMDPVSRRATWDILQ--HYKHNRTILLTTHYMDEADVLGDRVAIMVRG 369
Cdd:cd03301 152 FLMDEPLSNLDAKLRVQMRAELKrlQQRLGTTTIYVTHDQVEAMTMADRIAVMNDG 207
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
162-371 |
3.02e-23 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 102.87 E-value: 3.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 162 AGIHIMHLHKEFKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISDnmIEVRK-DLGF 240
Cdd:COG3842 4 PALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTG--LPPEKrNVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 241 CPQHDLLFDDLTLSEHLFFYCMVKGIPQnincEEIDR----MLSAFNLqENY-----HTLsgsaSGGVRRKLSIVLALMA 311
Cdd:COG3842 82 VFQDYALFPHLTVAENVAFGLRMRGVPK----AEIRArvaeLLELVGL-EGLadrypHQL----SGGQQQRVALARALAP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 525313703 312 GSKVVILDEPSSGMDPVSRRATW----DILQhyKHNRTILLTTHYMDEADVLGDRVAIMVRGTL 371
Cdd:COG3842 153 EPRVLLLDEPLSALDAKLREEMReelrRLQR--ELGITFIYVTHDQEEALALADRIAVMNDGRI 214
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
164-384 |
3.03e-23 |
|
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: 100.00 E-value: 3.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 164 IHIMHLHKEFKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISDNMIEVRKdLGFCPQ 243
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRP-VNTVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 244 HDLLFDDLTLSEHLFFYCMVKGIPQNINCEEIDRMLSAFNLQENYHTLSGSASGGVRRKLSIVLALMAGSKVVILDEPSS 323
Cdd:cd03300 80 NYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLG 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 525313703 324 GMDPVSRRatwDILQHYK--HNR---TILLTTHYMDEADVLGDRVAIMVRGTLHCCGSSvflKQIY 384
Cdd:cd03300 160 ALDLKLRK---DMQLELKrlQKElgiTFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTP---EEIY 219
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
172-369 |
3.54e-23 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 99.20 E-value: 3.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 172 EFKN---------KPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISD-NMIEVRKDLGFC 241
Cdd:cd03245 4 EFRNvsfsypnqeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQlDPADLRRNIGYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 242 PQHDLLF-----DDLTLS------EHLFFYCMVKGIPQ--NINCEEIDRMLS--AFNLqenyhtlsgsaSGGVRRKLSIV 306
Cdd:cd03245 84 PQDVTLFygtlrDNITLGapladdERILRAAELAGVTDfvNKHPNGLDLQIGerGRGL-----------SGGQRQAVALA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 525313703 307 LALMAGSKVVILDEPSSGMDPVSRRATWDILQHYKHNRTILLTTHYMdEADVLGDRVAIMVRG 369
Cdd:cd03245 153 RALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRP-SLLDLVDRIIVMDSG 214
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1016-1211 |
3.87e-23 |
|
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: 99.27 E-value: 3.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1016 VKAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTG---EETITSGIAFIDGnsVTRTPRKIRSRIGYCPQTESVLNHMT 1092
Cdd:cd03234 20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGrveGGGTTSGQILFNG--QPRKPDQFQKCVAYVRQDDILLPGLT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1093 GRESLVMYARLWGVLEQD--INEYVEAF--LHSVHLEPIADQFIHTYSAGSKRRLSTAIALMGKSSVVFLDEPSIGMDPV 1168
Cdd:cd03234 98 VRETLTYTAILRLPRKSSdaIRKKRVEDvlLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSF 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 525313703 1169 AQHLLWETITWICKTGKAIIITSH--RMEECEaLCTRLAIMVKGR 1211
Cdd:cd03234 178 TALNLVSTLSQLARRNRIVILTIHqpRSDLFR-LFDRILLLSSGE 221
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1020-1223 |
4.29e-23 |
|
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: 99.67 E-value: 4.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1020 KNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTRTPRK----IRSRIGYCPQTESVLNHMTGRE 1095
Cdd:COG1127 22 DGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKelyeLRRRIGMLFQGGALFDSLTVFE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1096 ----SLVMYARLwgvLEQDINEYVEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIALMGKSSVVFLDEPSIGMDPVAQH 1171
Cdd:COG1127 102 nvafPLREHTDL---SEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILLYDEPTAGLDPITSA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 525313703 1172 LLWETITWICKT-GKAIIITSHRMEECEALCTRLAIMVKGRFTCLGTPQHVRK 1223
Cdd:COG1127 179 VIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLA 231
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1001-1221 |
1.29e-22 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 100.94 E-value: 1.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1001 LLLNEVTKIYfkcPVVKAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTRTP---RkirsR 1077
Cdd:COG3842 6 LELENVSKRY---GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPpekR----N 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1078 IGYCPQTESVLNHMTGRESlVMYA-RLWGVLEQDINEYVEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIALMGKSSVV 1156
Cdd:COG3842 79 VGMVFQDYALFPHLTVAEN-VAFGlRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 525313703 1157 FLDEPSIGMDP-VAQHLLWETITWICKTGKAIIITSHRMEECEALCTRLAIMVKGRFTCLGTPQHV 1221
Cdd:COG3842 158 LLDEPLSALDAkLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEI 223
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
168-371 |
2.05e-22 |
|
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: 95.19 E-value: 2.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 168 HLHKEFKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISdnmievrkdlgfcpqhdll 247
Cdd:cd03216 5 GITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVS------------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 248 FDDLTLSEHLffycmvkGIpqninceeidRMLsafnlqenyHTLsgsaSGGVRRKLSIVLALMAGSKVVILDEPSSGMDP 327
Cdd:cd03216 66 FASPRDARRA-------GI----------AMV---------YQL----SVGERQMVEIARALARNARLLILDEPTAALTP 115
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 525313703 328 VSRRATWDIL-QHYKHNRTILLTTHYMDEADVLGDRVAIMVRGTL 371
Cdd:cd03216 116 AEVERLFKVIrRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
164-366 |
2.31e-22 |
|
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: 97.64 E-value: 2.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 164 IHIMHLHKEFKN-KPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISD----NMIEVRKDL 238
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKlkgkALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 239 GFCPQHDLLFDDLT---------LSEHLFFycmvKGIPQNINCEEIDRMLSA---FNLQENYHTLSGSASGGVRRKLSIV 306
Cdd:cd03256 81 GMIFQQFNLIERLSvlenvlsgrLGRRSTW----RSLFGLFPKEEKQRALAAlerVGLLDKAYQRADQLSGGQQQRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 525313703 307 LALMAGSKVVILDEPSSGMDPVSRRATWDILQ--HYKHNRTILLTTHYMDEADVLGDRVAIM 366
Cdd:cd03256 157 RALMQQPKLILADEPVASLDPASSRQVMDLLKriNREEGITVIVSLHQVDLAREYADRIVGL 218
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1005-1216 |
2.42e-22 |
|
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: 95.58 E-value: 2.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1005 EVTKIYFKCPVVKAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTRTPRKIRSR-IGYCPQ 1083
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARkIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1084 tesvlnhmtgreslvmyarlwgVLEQdineyveaflhsVHLEPIADQFIHTYSAGSKRRLSTAIALMGKSSVVFLDEPSI 1163
Cdd:cd03214 81 ----------------------ALEL------------LGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTS 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 525313703 1164 GMDPVAQHLLWETITWICK-TGKAIIITSHRMEECEALCTRLAIMVKGRFTCLG 1216
Cdd:cd03214 127 HLDIAHQIELLELLRRLAReRGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1003-1192 |
3.70e-22 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 96.27 E-value: 3.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1003 LNEVTKIYFKcpVVKAVKNISLVVKKSE-CFgLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTRTPRK----IRSR 1077
Cdd:COG2884 4 FENVSKRYPG--GREALSDVSLEIEKGEfVF-LTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRReipyLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1078 IGYCPQTESVLNHMTGRE--SLVMYARlwGVLEQDINEYVEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIALMGKSSV 1155
Cdd:COG2884 81 IGVVFQDFRLLPDRTVYEnvALPLRVT--GKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPEL 158
|
170 180 190
....*....|....*....|....*....|....*..
gi 525313703 1156 VFLDEPSIGMDPVAQHLLWETITWICKTGKAIIITSH 1192
Cdd:COG2884 159 LLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATH 195
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
172-375 |
4.05e-22 |
|
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: 97.08 E-value: 4.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 172 EFKN-------KPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGR-FAATRGEAYI-----NGYNISdnmiEVRKDL 238
Cdd:COG1119 5 ELRNvtvrrggKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDlPPTYGNDVRLfgerrGGEDVW----ELRKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 239 GFC-PQhdlLFDDLTLSEHLF------FYCMVkGIPQNINCEEIDR---MLSAFNLQE----NYHTLsgsaSGGVRRKLS 304
Cdd:COG1119 81 GLVsPA---LQLRFPRDETVLdvvlsgFFDSI-GLYREPTDEQRERareLLELLGLAHladrPFGTL----SQGEQRRVL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 525313703 305 IVLALMAGSKVVILDEPSSGMDPVSRRATWDILQHY--KHNRTILLTTHYMDEADVLGDRVAIMVRGTLHCCG 375
Cdd:COG1119 153 IARALVKDPELLILDEPTAGLDLGARELLLALLDKLaaEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAG 225
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
176-371 |
4.71e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 97.37 E-value: 4.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 176 KPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNIS-DNMIEVRKDLGFCPQH-DLLFDDLTL 253
Cdd:PRK13632 22 NNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISkENLKEIRKKIGIIFQNpDNQFIGATV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 254 SEHLFFycmvkGIP-QNINCEEIDRMLSAFNLQ---ENY-----HTLsgsaSGGVRRKLSI--VLALmaGSKVVILDEPS 322
Cdd:PRK13632 102 EDDIAF-----GLEnKKVPPKKMKDIIDDLAKKvgmEDYldkepQNL----SGGQKQRVAIasVLAL--NPEIIIFDEST 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 525313703 323 SGMDPVSRRATWDILQ--HYKHNRTILLTTHYMDEAdVLGDRVAIMVRGTL 371
Cdd:PRK13632 171 SMLDPKGKREIKKIMVdlRKTRKKTLISITHDMDEA-ILADKVIVFSEGKL 220
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
164-371 |
6.44e-22 |
|
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: 96.41 E-value: 6.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 164 IHIMHLHKEF----KNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISDnmievRKDLG 239
Cdd:COG1124 2 LEVRNLSVSYgqggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTR-----RRRKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 240 FCPQHDLLFDD--------LTLSEHLF--FYCMvkGIPQNinCEEIDRMLSAFNLQENY-----HTLSGsasgGVRRKLS 304
Cdd:COG1124 77 FRRRVQMVFQDpyaslhprHTVDRILAepLRIH--GLPDR--EERIAELLEQVGLPPSFldrypHQLSG----GQRQRVA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 525313703 305 IVLALMAGSKVVILDEPSSGMDPVSRRATWDILQHYK--HNRTILLTTHYMDEADVLGDRVAIMVRGTL 371
Cdd:COG1124 149 IARALILEPELLLLDEPTSALDVSVQAEILNLLKDLReeRGLTYLFVSHDLAVVAHLCDRVAVMQNGRI 217
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
1005-1213 |
7.23e-22 |
|
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: 95.02 E-value: 7.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1005 EVTKIYFKCP-VVKAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTRTPRkiRSRIGYCPQ 1083
Cdd:cd03226 1 RIENISFSYKkGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKER--RKSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1084 -------TESVlnhmtgRESLVMYARLWGvleqDINEYVEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIALMGKSSVV 1156
Cdd:cd03226 79 dvdyqlfTDSV------REELLLGLKELD----AGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 525313703 1157 FLDEPSIGMDPVAQHLLWETITWICKTGKAIIITSHRMEECEALCTRLAIMVKGRFT 1213
Cdd:cd03226 149 IFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
171-369 |
9.14e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 97.08 E-value: 9.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 171 KEFKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISD--NMIEVRKDLGFCPQH---- 244
Cdd:PRK13633 18 EESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDeeNLWDIRNKAGMVFQNpdnq 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 245 --------DLLFDdltlSEHLffycmvkGIPQNINCEEIDRMLSAFNLQEnY-----HTLsgsaSGGVRRKLSI--VLAL 309
Cdd:PRK13633 98 ivativeeDVAFG----PENL-------GIPPEEIRERVDESLKKVGMYE-YrrhapHLL----SGGQKQRVAIagILAM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 525313703 310 MagSKVVILDEPSSGMDPVSRRATWDILQ--HYKHNRTILLTTHYMDEAdVLGDRVAIMVRG 369
Cdd:PRK13633 162 R--PECIIFDEPTAMLDPSGRREVVNTIKelNKKYGITIILITHYMEEA-VEADRIIVMDSG 220
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1015-1221 |
1.26e-21 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 95.53 E-value: 1.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1015 VVKAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGiafidgnSVtrtprKIRSRIGycpqteSVL------ 1088
Cdd:COG1134 38 EFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSG-------RV-----EVNGRVS------ALLelgagf 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1089 -NHMTGRESLVMYARLWGVLEQDINE---YVEAFlhsvhlepiAD--QFIH----TYSAGSKRRLSTAIALMGKSSVVFL 1158
Cdd:COG1134 100 hPELTGRENIYLNGRLLGLSRKEIDEkfdEIVEF---------AElgDFIDqpvkTYSSGMRARLAFAVATAVDPDILLV 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 525313703 1159 DEP-SIGmDPVAQHLLWETITWICKTGKAIIITSHRMEECEALCTRLAIMVKGRFTCLGTPQHV 1221
Cdd:COG1134 171 DEVlAVG-DAAFQKKCLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEV 233
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1016-1211 |
1.47e-21 |
|
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: 95.33 E-value: 1.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1016 VKAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTRTP----RKIRSRIGYCPQT------- 1084
Cdd:cd03256 14 KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKgkalRQLRRQIGMIFQQfnlierl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1085 ---ESVLNHMTGRESLV-MYARLWGvlEQDINEYVEAfLHSVHLEPIADQFIHTYSAGSKRRLSTAIALMGKSSVVFLDE 1160
Cdd:cd03256 94 svlENVLSGRLGRRSTWrSLFGLFP--KEEKQRALAA-LERVGLLDKAYQRADQLSGGQQQRVAIARALMQQPKLILADE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 525313703 1161 PSIGMDPVAQHLLWETITWICKT-GKAIIITSHRMEECEALCTRLAIMVKGR 1211
Cdd:cd03256 171 PVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDLAREYADRIVGLKDGR 222
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1016-1211 |
1.58e-21 |
|
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: 92.83 E-value: 1.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1016 VKAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTR-TPRKIRSRIGYCPQtESVLNHMTGR 1094
Cdd:cd03228 15 KPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDlDLESLRKNIAYVPQ-DPFLFSGTIR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1095 ESLVmyarlwgvleqdineyveaflhsvhlepiadqfihtySAGSKRRLSTAIALMGKSSVVFLDEPSIGMDPVAQHLLW 1174
Cdd:cd03228 94 ENIL-------------------------------------SGGQRQRIAIARALLRDPPILILDEATSALDPETEALIL 136
|
170 180 190
....*....|....*....|....*....|....*..
gi 525313703 1175 ETITWICKtGKAIIITSHRMEECEaLCTRLAIMVKGR 1211
Cdd:cd03228 137 EALRALAK-GKTVIVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
1018-1231 |
2.08e-21 |
|
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: 100.23 E-value: 2.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1018 AVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTRTPRK-IRSRIGYCPQtESVLNHMTGRES 1096
Cdd:COG4987 350 VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDdLRRRIAVVPQ-RPHLFDTTLREN 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1097 LVMyAR-------LWGVLEQdineyveaflhsVHLEPIADQFIHTY-----------SAGSKRRLSTAIALMGKSSVVFL 1158
Cdd:COG4987 429 LRL-ARpdatdeeLWAALER------------VGLGDWLAALPDGLdtwlgeggrrlSGGERRRLALARALLRDAPILLL 495
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 525313703 1159 DEPSIGMDPVAQHLLWETITWICKtGKAIIITSHRMEECEAlCTRLAIMVKGRFTCLGTPQHVRKRFGHVYTL 1231
Cdd:COG4987 496 DEPTEGLDAATEQALLADLLEALA-GRTVLLITHRLAGLER-MDRILVLEDGRIVEQGTHEELLAQNGRYRQL 566
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
173-376 |
2.30e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 94.80 E-value: 2.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 173 FKnkpAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISdNMIEV--------RKdlgFcpQH 244
Cdd:COG4674 23 FK---ALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLT-GLDEHeiarlgigRK---F--QK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 245 DLLFDDLTLSEHL---------FFYCMVKGIPQNINcEEIDRMLSAFNLQENYHTLSGSASGGVRRKLSIVLALMAGSKV 315
Cdd:COG4674 94 PTVFEELTVFENLelalkgdrgVFASLFARLTAEER-DRIEEVLETIGLTDKADRLAGLLSHGQKQWLEIGMLLAQDPKL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 525313703 316 VILDEPSSGMDPVSRRATWDILQHYKHNRTILLTTHYMDEADVLGDRVAIMVRGTLHCCGS 376
Cdd:COG4674 173 LLLDEPVAGMTDAETERTAELLKSLAGKHSVVVVEHDMEFVRQIARKVTVLHQGSVLAEGS 233
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1009-1219 |
2.89e-21 |
|
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: 95.02 E-value: 2.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1009 IYFKCPVVKAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTRTPRK----IRS-RIGYCPQ 1083
Cdd:cd03294 30 ILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKelreLRRkKISMVFQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1084 TESVLNHMTGRESLVMYARLWGVLEQDINEYVEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIALMGKSSVVFLDEPSI 1163
Cdd:cd03294 110 SFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFS 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1164 GMDPV----AQHLLWETITwicKTGKAIIITSHRMEECEALCTRLAIMVKGRFTCLGTPQ 1219
Cdd:cd03294 190 ALDPLirreMQDELLRLQA---ELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPE 246
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1006-1221 |
2.97e-21 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 94.33 E-value: 2.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1006 VTKIYfkcPVVKAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTRTPrkIRSR-IGYCPQT 1084
Cdd:cd03296 8 VSKRF---GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVP--VQERnVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1085 ESVLNHMTGRES----LVMYARLWGVLEQDINEYVEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIALMGKSSVVFLDE 1160
Cdd:cd03296 83 YALFRHMTVFDNvafgLRVKPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 525313703 1161 PSIGMDPVAQHllwETITWICKTGKAIIITS----HRMEECEALCTRLAIMVKGRFTCLGTPQHV 1221
Cdd:cd03296 163 PFGALDAKVRK---ELRRWLRRLHDELHVTTvfvtHDQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
178-369 |
4.20e-21 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 93.79 E-value: 4.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 178 AVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISDNMIE--VRKDLGFCPQHDLLFDDLTLSE 255
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAkiMREAVAIVPEGRRVFSRMTVEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 256 HL----FFycmvkgIPQNINCEEIDRMLSAF-NLQENYHTLSGSASGGVRRKLSIVLALMAGSKVVILDEPSSGMDPVSR 330
Cdd:PRK11614 100 NLamggFF------AERDQFQERIKWVYELFpRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIII 173
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 525313703 331 RATWDILQHYKHN-RTILLTTHYMDEADVLGDRVAIMVRG 369
Cdd:PRK11614 174 QQIFDTIEQLREQgMTIFLVEQNANQALKLADRGYVLENG 213
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
174-369 |
5.74e-21 |
|
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: 91.61 E-value: 5.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 174 KNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISDNMIEVRKDLGFCPQHDLLFDDlTL 253
Cdd:cd03247 13 QEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVLNQRPYLFDT-TL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 254 SEHLffycmvkGIPqninceeidrmlsafnlqenyhtlsgsASGGVRRKLSIVLALMAGSKVVILDEPSSGMDPVSRRAT 333
Cdd:cd03247 92 RNNL-------GRR---------------------------FSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQL 137
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 525313703 334 WDILQHYKHNRTILLTTH------YMDEADVLgDRVAIMVRG 369
Cdd:cd03247 138 LSLIFEVLKDKTLIWITHhltgieHMDKILFL-ENGKIIMQG 178
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
171-371 |
5.89e-21 |
|
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: 5.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 171 KEFKnkpaVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISdNMIEVRKDLGFCPQHDLLFDD 250
Cdd:cd03299 11 KEFK----LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDIT-NLPPEKRDISYVPQNYALFPH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 251 LTLSEHLFFYCMVKGIPQNINCEEIDRMLSAFNLQENYHTLSGSASGGVRRKLSIVLALMAGSKVVILDEPSSGMDPVSR 330
Cdd:cd03299 86 MTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTK 165
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 525313703 331 RATWDILQ--HYKHNRTILLTTHYMDEADVLGDRVAIMVRGTL 371
Cdd:cd03299 166 EKLREELKkiRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKL 208
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
998-1211 |
6.12e-21 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 98.18 E-value: 6.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 998 NTPLL-LNEVTKIYfkcPVVKAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVT-RTPRK-I 1074
Cdd:COG3845 2 MPPALeLRGITKRF---GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRiRSPRDaI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1075 RSRIGYCPQ------TESVL-NHMTGRESLVMYARLWGVLEQDINEYVEAFlhSVHLEPiaDQFIHTYSAGSKRRLSTAI 1147
Cdd:COG3845 79 ALGIGMVHQhfmlvpNLTVAeNIVLGLEPTKGGRLDRKAARARIRELSERY--GLDVDP--DAKVEDLSVGEQQRVEILK 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 525313703 1148 ALMGKSSVVFLDEPSIGMDPV-AQHLLwETITWICKTGKAIIITSHRMEECEALCTRLAIMVKGR 1211
Cdd:COG3845 155 ALYRGARILILDEPTAVLTPQeADELF-EILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGK 218
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
166-388 |
7.84e-21 |
|
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: 91.82 E-value: 7.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 166 IMHLHKEFKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTG--RFAATRGEAYINGYNISDNMIE--VRKDLGFC 241
Cdd:cd03217 3 IKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpKYEVTEGEILFKGEDITDLPPEerARLGIFLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 242 PQHDLLFDDLTLSEHLffycmvkgipqninceeidRmlsafNLQENYhtlsgsaSGGVRRKLSIVLALMAGSKVVILDEP 321
Cdd:cd03217 83 FQYPPEIPGVKNADFL-------------------R-----YVNEGF-------SGGEKKRNEILQLLLLEPDLAILDEP 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 525313703 322 SSGMDPVSRRATWDILQHYKH-NRTILLTTHYMDEAD-VLGDRVAIMVRGTLHCCGSSVFLKQIYGAGY 388
Cdd:cd03217 132 DSGLDIDALRLVAEVINKLREeGKSVLIITHYQRLLDyIKPDRVHVLYDGRIVKSGDKELALEIEKKGY 200
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
164-372 |
1.15e-20 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 92.41 E-value: 1.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 164 IHIMHLHKEFKNK----PAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNIS----DNMIEVR 235
Cdd:COG1136 5 LELRNLTKSYGTGegevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISslseRELARLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 236 -KDLGFCPQHDLLFDDLTLSEHLFFYCMVKGIPQNINCEEIDRMLSAFNLQENYHTLSGSASGGVRRKLSIVLALMAGSK 314
Cdd:COG1136 85 rRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRPK 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 315 VVILDEPSSGMDPVSRRATWDILQHY--KHNRTILLTTHYMDEADvLGDRVAIMVRGTLH 372
Cdd:COG1136 165 LILADEPTGNLDSKTGEEVLELLRELnrELGTTIVMVTHDPELAA-RADRVIRLRDGRIV 223
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
178-369 |
1.58e-20 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 95.87 E-value: 1.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 178 AVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISD----NMIEV-RKDLGFCPQHDLLFDDLT 252
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKisdaELREVrRKKIAMVFQSFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 253 LSEHLFFYCMVKGIPQNINCEEIDRMLSAFNLQENYHTLSGSASGGVRRKLSIVLALMAGSKVVILDEPSSGMDPVSRRA 332
Cdd:PRK10070 123 VLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
|
170 180 190
....*....|....*....|....*....|....*....
gi 525313703 333 TWDIL--QHYKHNRTILLTTHYMDEADVLGDRVAIMVRG 369
Cdd:PRK10070 203 MQDELvkLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNG 241
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
164-387 |
2.23e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 92.77 E-value: 2.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 164 IHIMHLHKEFKN--KPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISDNMI-EVRKDLGF 240
Cdd:PRK13635 6 IRVEHISFRYPDaaTYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVwDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 241 CPQH-DLLFDDLTLSEHLFFYCMVKGIPQNINCEEIDRMLSAFNLQENYHTLSGSASGGVRRKLSIVLALMAGSKVVILD 319
Cdd:PRK13635 86 VFQNpDNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILD 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 320 EPSSGMDPVSRRATWDILQHYKHNR--TILLTTHYMDEAdVLGDRVAIMVRGTLHCCGSSvflKQIYGAG 387
Cdd:PRK13635 166 EATSMLDPRGRREVLETVRQLKEQKgiTVLSITHDLDEA-AQADRVIVMNKGEILEEGTP---EEIFKSG 231
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
161-384 |
2.75e-20 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 91.76 E-value: 2.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 161 EAGIHIMHLHKEFKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTgRF------AATRGEAYINGYNI---SDNM 231
Cdd:PRK14239 3 EPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSIN-RMndlnpeVTITGSIVYNGHNIyspRTDT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 232 IEVRKDLGFCPQHDLLFDdLTLSEHLFFYCMVKGIP-QNINCEEIDRMLSAFNL----QENYHTLSGSASGGVRRKLSIV 306
Cdd:PRK14239 82 VDLRKEIGMVFQQPNPFP-MSIYENVVYGLRLKGIKdKQVLDEAVEKSLKGASIwdevKDRLHDSALGLSGGQQQRVCIA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 525313703 307 LALMAGSKVVILDEPSSGMDPVSRRATWDILQHYKHNRTILLTTHYMDEADVLGDRVAIMVRGTLHCCGSSvflKQIY 384
Cdd:PRK14239 161 RVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDT---KQMF 235
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
998-1212 |
2.99e-20 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 95.86 E-value: 2.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 998 NTPLL-LNEVTKIYfkcPVVKAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVT-RTPRK-I 1074
Cdd:COG1129 1 AEPLLeMRGISKSF---GGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRfRSPRDaQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1075 RSRIGYCPQTESVLNHMTGRESLVM--YARLWGVL-EQDINEYVEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIALMG 1151
Cdd:COG1129 78 AAGIAIIHQELNLVPNLSVAENIFLgrEPRRGGLIdWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 525313703 1152 KSSVVFLDEPSIGMDPV-AQHLLwETITWICKTGKAIIITSHRMEECEALCTRLAIMVKGRF 1212
Cdd:COG1129 158 DARVLILDEPTASLTEReVERLF-RIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRL 218
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1021-1211 |
4.07e-20 |
|
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: 90.43 E-value: 4.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1021 NISLVVKkSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTRTPRKI-----RSRIGYCPQTESVLNHMTGRE 1095
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKInlppqQRKIGLVFQQYALFPHLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1096 SLVMYARLWGVLEQDINeyVEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIALMGKSSVVFLDEPSIGMD-PVAQHLLW 1174
Cdd:cd03297 95 NLAFGLKRKRNREDRIS--VDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDrALRLQLLP 172
|
170 180 190
....*....|....*....|....*....|....*..
gi 525313703 1175 ETITWICKTGKAIIITSHRMEECEALCTRLAIMVKGR 1211
Cdd:cd03297 173 ELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGR 209
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1001-1224 |
5.21e-20 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 93.21 E-value: 5.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1001 LLLNEVTKIYFKcpvVKAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTRTPRKIRsRIGY 1080
Cdd:COG3839 4 LELENVSKSYGG---VEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDR-NIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1081 CPQTESVLNHMTGRESLVMYARLWGVLEQDINEYVEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIALMGKSSVVFLDE 1160
Cdd:COG3839 80 VFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 525313703 1161 PSIGMDPvaqHLLWETITWICK----TGKAIIITSHRMEECEALCTRLAIMVKGRFTCLGTPQHVRKR 1224
Cdd:COG3839 160 PLSNLDA---KLRVEMRAEIKRlhrrLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDR 224
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
1016-1244 |
5.26e-20 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 93.26 E-value: 5.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1016 VKAVKNISLVVKKSECFGLLGLNGAGKTTTfkmltgeetitSGIAFIDGNSVTRTP----------RKIRSRIG-YCPQT 1084
Cdd:NF000106 26 VKAVDGVDLDVREGTVLGVLGP*GAA**RG-----------ALPAHV*GPDAGRRPwrf*twcanrRALRRTIG*HRPVR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1085 ESVLNHMTGRESLVMYARLWGVLEQDINEYVEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIALMGKSSVVFLDEPSIG 1164
Cdd:NF000106 95 *GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1165 MDPVAQHLLWETITWICKTGKAIIITSHRMEECEALCTRLAIMVKGRFTCLGTPQHVRKRFGHvYTLTVRINIAKDEDKV 1244
Cdd:NF000106 175 LDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVGG-RTLQIRPAHAAELDRM 253
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1017-1223 |
8.51e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 91.26 E-value: 8.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1017 KAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTRTPRK---IRSRIGYCPQ-TESVLNHMT 1092
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKlsdIRKKVGLVFQyPEYQLFEET 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1093 GRESLVMYARLWGVLEQDINEYVEAFLHSVHL--EPIADQFIHTYSAGSKRRLSTAIALMGKSSVVFLDEPSIGMDPVAQ 1170
Cdd:PRK13637 101 IEKDIAFGPINLGLSEEEIENRVKRAMNIVGLdyEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGR 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 525313703 1171 HLLWETITWICKTGK-AIIITSHRMEECEALCTRLAIMVKGRFTCLGTPQHVRK 1223
Cdd:PRK13637 181 DEILNKIKELHKEYNmTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFK 234
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
999-1221 |
9.85e-20 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 94.47 E-value: 9.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 999 TPLLlnEVTKIYFKCPVVKAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTRTPRKIRSR- 1077
Cdd:PRK09700 3 TPYI--SMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1078 -IGYCPQTESVLNHMTGRESLVM----YARLWGVLEQDINEY---VEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIAL 1149
Cdd:PRK09700 81 gIGIIYQELSVIDELTVLENLYIgrhlTKKVCGVNIIDWREMrvrAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 525313703 1150 MGKSSVVFLDEPSIGMDPVAQHLLWETITWICKTGKAIIITSHRMEECEALCTRLAIMVKGRFTCLGTPQHV 1221
Cdd:PRK09700 161 MLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDV 232
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
996-1221 |
1.26e-19 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 92.70 E-value: 1.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 996 LQNTPLL-LNEVTKIY-FKCpvvkAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTRTPRK 1073
Cdd:PRK09452 9 SSLSPLVeLRGISKSFdGKE----VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1074 IRSrIGYCPQTESVLNHMTGRESLVMYARLWGVLEQDINEYVEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIALMGKS 1153
Cdd:PRK09452 85 NRH-VNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 525313703 1154 SVVFLDEPSIGMD-PVAQHLLWETITWICKTGKAIIITSHRMEECEALCTRLAIMVKGRFTCLGTPQHV 1221
Cdd:PRK09452 164 KVLLLDESLSALDyKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREI 232
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
1018-1231 |
1.33e-19 |
|
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: 94.90 E-value: 1.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1018 AVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTR-TPRKIRSRIGYCPQtESVLNHMTGRES 1096
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQiDPASLRRQIGVVLQ-DVFLFSGTIREN 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1097 LVM------YARLWGVLEQ-DINEYVEAF---LHSVhLEPIADQFihtySAGSKRRLSTAIALMGKSSVVFLDEPSIGMD 1166
Cdd:COG2274 569 ITLgdpdatDEEIIEAARLaGLHDFIEALpmgYDTV-VGEGGSNL----SGGQRQRLAIARALLRNPRILILDEATSALD 643
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 525313703 1167 PVAQHLLWETITWICKtGKAIIITSHRMeECEALCTRLAIMVKGRFTCLGTPQHVRKRFGHVYTL 1231
Cdd:COG2274 644 AETEAIILENLRRLLK-GRTVIIIAHRL-STIRLADRIIVLDKGRIVEDGTHEELLARKGLYAEL 706
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
164-372 |
1.40e-19 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 88.96 E-value: 1.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 164 IHIMHLHKEFKN-KPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNIS----DNMIEVRKDL 238
Cdd:COG2884 2 IRFENVSKRYPGgREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSrlkrREIPYLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 239 GFCPQ-HDLLfDDLTLSEHLFFYCMVKGIPQnincEEIDR----MLSAFNLQENYHTLSGSASGGVRRKLSIVLALMAGS 313
Cdd:COG2884 82 GVVFQdFRLL-PDRTVYENVALPLRVTGKSR----KEIRRrvreVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 525313703 314 KVVILDEPSSGMDPvsrRATWDILQHYKH-NR---TILLTTHYMDEADVLGDRVAIMVRGTLH 372
Cdd:COG2884 157 ELLLADEPTGNLDP---ETSWEIMELLEEiNRrgtTVLIATHDLELVDRMPKRVLELEDGRLV 216
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
164-369 |
1.68e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 89.76 E-value: 1.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 164 IHIMHLHKEFKN-----KPAVNNLSLNIYEGQ-VTVLlGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISdNMIE---- 233
Cdd:COG1101 2 LELKNLSKTFNPgtvneKRALDGLNLTIEEGDfVTVI-GSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVT-KLPEykra 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 234 -----VRKD--LGFCPqhdllfdDLTLSEHLffyCM------VKGIPQNINCEEIDR---MLSAFNLQ-ENY-HTLSGSA 295
Cdd:COG1101 80 kyigrVFQDpmMGTAP-------SMTIEENL---ALayrrgkRRGLRRGLTKKRRELfreLLATLGLGlENRlDTKVGLL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 296 SGGVRRKLSIVLALMAGSKVVILDEPSSGMDPvsRRA------TWDILQhyKHNRTILLTTHYMDEADVLGDRVAIMVRG 369
Cdd:COG1101 150 SGGQRQALSLLMATLTKPKLLLLDEHTAALDP--KTAalvlelTEKIVE--ENNLTTLMVTHNMEQALDYGNRLIMMHEG 225
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
175-371 |
1.99e-19 |
|
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: 88.23 E-value: 1.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 175 NKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISD----NMIEVRKDLGFCPQHDLLFDD 250
Cdd:cd03292 13 GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDlrgrAIPYLRRKIGVVFQDFRLLPD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 251 LTLSEHLFFYCMVKGIPQNINCEEIDRMLSAFNLQENYHTLSGSASGGVRRKLSIVLALMAGSKVVILDEPSSGMDPVSR 330
Cdd:cd03292 93 RNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTT 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 525313703 331 RATWDILQHY-KHNRTILLTTHYMDEADVLGDRVAIMVRGTL 371
Cdd:cd03292 173 WEIMNLLKKInKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
165-372 |
2.01e-19 |
|
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: 88.08 E-value: 2.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 165 HIMHLHKEFKNKP-AVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISDNmiEVRKDLGFCPQ 243
Cdd:cd03226 1 RIENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAK--ERRKSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 244 H--DLLFDDlTLSEHLFFYCMVKGIPQNInCEEIDRMLSAFNLQENY-HTLsgsaSGGVRRKLSIVLALMAGSKVVILDE 320
Cdd:cd03226 79 DvdYQLFTD-SVREELLLGLKELDAGNEQ-AETVLKDLDLYALKERHpLSL----SGGQKQRLAIAAALLSGKDLLIFDE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 525313703 321 PSSGMDPVSRRATWDILQH-YKHNRTILLTTHYMDEADVLGDRVAIMVRGTLH 372
Cdd:cd03226 153 PTSGLDYKNMERVGELIRElAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1005-1211 |
2.03e-19 |
|
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: 88.23 E-value: 2.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1005 EVTKIYfkCPVVKAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTRTPRK----IRSRIGY 1080
Cdd:cd03292 5 NVTKTY--PNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRaipyLRRKIGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1081 CPQTESVLNHMTGRESLVMYARLWGVLEQDINEYVEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIALMGKSSVVFLDE 1160
Cdd:cd03292 83 VFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 525313703 1161 PSIGMDPVAQHLLWETITWICKTGKAIIITSHRMEECEALCTRLAIMVKGR 1211
Cdd:cd03292 163 PTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGK 213
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
177-370 |
2.06e-19 |
|
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: 94.01 E-value: 2.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 177 PAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISD-NMIEVRKDLGFCPQHDLLFDDlTLSE 255
Cdd:TIGR02203 346 PALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADyTLASLRRQVALVSQDVVLFND-TIAN 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 256 HLFFycmvkGIPQNINCEEIDRMLSAFNLQE-------NYHTLSGSA----SGGVRRKLSIVLALMAGSKVVILDEPSSG 324
Cdd:TIGR02203 425 NIAY-----GRTEQADRAEIERALAAAYAQDfvdklplGLDTPIGENgvllSGGQRQRLAIARALLKDAPILILDEATSA 499
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 525313703 325 MDPVSRRATWDILQHYKHNRTILLTTHYM---DEAD--VLGDRVAIMVRGT 370
Cdd:TIGR02203 500 LDNESERLVQAALERLMQGRTTLVIAHRLstiEKADriVVMDDGRIVERGT 550
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
177-351 |
2.10e-19 |
|
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: 93.51 E-value: 2.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 177 PAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISD-NMIEVRKDLGFCPQHDLLFDDlTLSE 255
Cdd:TIGR02857 336 PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADaDADSWRDQIAWVPQHPFLFAG-TIAE 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 256 HLFFYC------MVKGIPQNInceEIDRMLSAfnLQENYHTLSGSA----SGGVRRKLSIVLALMAGSKVVILDEPSSGM 325
Cdd:TIGR02857 415 NIRLARpdasdaEIREALERA---GLDEFVAA--LPQGLDTPIGEGgaglSGGQAQRLALARAFLRDAPLLLLDEPTAHL 489
|
170 180
....*....|....*....|....*.
gi 525313703 326 DPVSRRATWDILQHYKHNRTILLTTH 351
Cdd:TIGR02857 490 DAETEAEVLEALRALAQGRTVLLVTH 515
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
996-1211 |
2.14e-19 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 88.78 E-value: 2.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 996 LQNTPLLLNEVTKIYFKcpvVKAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVT--RTPRK 1073
Cdd:PRK11614 1 MEKVMLSFDKVSAHYGK---IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITdwQTAKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1074 IRSRIGYCPQTESVLNHMTGRESLVMyarlwGVLEQDINEYVEAFLHSVHLEP-IADQFIH---TYSAGSKRRLSTAIAL 1149
Cdd:PRK11614 78 MREAVAIVPEGRRVFSRMTVEENLAM-----GGFFAERDQFQERIKWVYELFPrLHERRIQragTMSGGEQQMLAIGRAL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 525313703 1150 MGKSSVVFLDEPSIGMDPVAQHLLWETITWICKTGKAIIITSHRMEECEALCTRLAIMVKGR 1211
Cdd:PRK11614 153 MSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGH 214
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
178-372 |
3.18e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 89.04 E-value: 3.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 178 AVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNIS-DNMIEVRKDLGFCPQ------------H 244
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITdDNFEKLRKHIGIVFQnpdnqfvgsivkY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 245 DLLFDdltLSEHLFFY-CMVKGIPQNIncEEIDrMLSAFNLQENyhtlsgSASGGVRRKLSI--VLALmaGSKVVILDEP 321
Cdd:PRK13648 104 DVAFG---LENHAVPYdEMHRRVSEAL--KQVD-MLERADYEPN------ALSGGQKQRVAIagVLAL--NPSVIILDEA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 525313703 322 SSGMDPVSRRATWDILQHYK--HNRTILLTTHYMDEAdVLGDRVAIMVRGTLH 372
Cdd:PRK13648 170 TSMLDPDARQNLLDLVRKVKseHNITIISITHDLSEA-MEADHVIVMNKGTVY 221
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
178-390 |
4.10e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 89.45 E-value: 4.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 178 AVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNIS----DNMIE-VRKDLGFCPQ--HDLLFDD 250
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIThktkDKYIRpVRKRIGMVFQfpESQLFED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 251 LTLSEHLFFycmvkgiPQN--INCEEID----RMLSAFNLQENYHTLSG-SASGGVRRKLSIVLALMAGSKVVILDEPSS 323
Cdd:PRK13646 102 TVEREIIFG-------PKNfkMNLDEVKnyahRLLMDLGFSRDVMSQSPfQMSGGQMRKIAIVSILAMNPDIIVLDEPTA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 525313703 324 GMDPVSRRATWDILQHY--KHNRTILLTTHYMDEADVLGDRVAIMVRGTL--HCCGSSVFLKQIYGAGYHI 390
Cdd:PRK13646 175 GLDPQSKRQVMRLLKSLqtDENKTIILVSHDMNEVARYADEVIVMKEGSIvsQTSPKELFKDKKKLADWHI 245
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
175-351 |
4.68e-19 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 92.42 E-value: 4.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 175 NKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISD-NMIEVRKDLGFCPQHDLLFDDlTL 253
Cdd:TIGR02868 347 APPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSlDQDEVRRRVSVCAQDAHLFDT-TV 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 254 SEHLFFYCmvkgipQNINCEEIDRMLSAFNL-------QENYHTLSG----SASGGVRRKLSIVLALMAGSKVVILDEPS 322
Cdd:TIGR02868 426 RENLRLAR------PDATDEELWAALERVGLadwlralPDGLDTVLGeggaRLSGGERQRLALARALLADAPILLLDEPT 499
|
170 180
....*....|....*....|....*....
gi 525313703 323 SGMDPVSRRATWDILQHYKHNRTILLTTH 351
Cdd:TIGR02868 500 EHLDAETADELLEDLLAALSGRTVVLITH 528
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
158-369 |
4.92e-19 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 90.66 E-value: 4.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 158 PNLEagihIMHLHKEFKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISDnMIEVRKD 237
Cdd:PRK11607 18 PLLE----IRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSH-VPPYQRP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 238 LGFCPQHDLLFDDLTLSEHLFFYCMVKGIPQNINCEEIDRMLSAFNLQENYHTLSGSASGGVRRKLSIVLALMAGSKVVI 317
Cdd:PRK11607 93 INMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 525313703 318 LDEPSSGMDPVSRR----ATWDILQhyKHNRTILLTTHYMDEADVLGDRVAIMVRG 369
Cdd:PRK11607 173 LDEPMGALDKKLRDrmqlEVVDILE--RVGVTCVMVTHDQEEAMTMAGRIAIMNRG 226
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
181-371 |
5.09e-19 |
|
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: 86.97 E-value: 5.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 181 NLSLNI---YEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGY-----NISDNMIEVRKDLGFCPQHDLLFDDLT 252
Cdd:cd03297 12 DFTLKIdfdLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfdsRKKINLPPQQRKIGLVFQQYALFPHLN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 253 LSEHLFFycMVKGIPQNINCEEIDRMLSAFNLQENYHTLSGSASGGVRRKLSIVLALMAGSKVVILDEPSSGMDPVSRra 332
Cdd:cd03297 92 VRENLAF--GLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALR-- 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 525313703 333 twDILQHY-----KH-NRTILLTTHYMDEADVLGDRVAIMVRGTL 371
Cdd:cd03297 168 --LQLLPElkqikKNlNIPVIFVTHDLSEAEYLADRIVVMEDGRL 210
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1017-1211 |
6.49e-19 |
|
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: 86.81 E-value: 6.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1017 KAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTRTPR---KIRSRIGYCPQTESVLNHMTG 1093
Cdd:cd03262 14 HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKninELRQKVGMVFQQFNLFPHLTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1094 RESlVMYA--RLWGVLEQDINEYVEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIALMGKSSVVFLDEPSIGMDP--VA 1169
Cdd:cd03262 94 LEN-ITLApiKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPelVG 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 525313703 1170 QHLlwETITWICKTGKAIIITSHRMEECEALCTRLAIMVKGR 1211
Cdd:cd03262 173 EVL--DVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGR 212
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1019-1221 |
6.52e-19 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 87.76 E-value: 6.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1019 VKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTR-TPRKIRSRIGYCPQTESVLNHMTGREsL 1097
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMlSSRQLARRLALLPQHHLTPEGITVRE-L 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1098 VMYAR-----LWGVLEQDINEYVEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIALMGKSSVVFLDEPSIGMDPVAQHL 1172
Cdd:PRK11231 97 VAYGRspwlsLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVE 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 525313703 1173 LWETITWICKTGKAIIITSHRMEECEALCTRLAIMVKGRFTCLGTPQHV 1221
Cdd:PRK11231 177 LMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEV 225
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
172-351 |
8.85e-19 |
|
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: 86.90 E-value: 8.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 172 EFKN--------KPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISD-NMIEVRKDLGFCP 242
Cdd:cd03254 4 EFENvnfsydekKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDiSRKSLRSMIGVVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 243 QHDLLFDDlTLSEHLFFycmvkGIPqNINCEEIDRMLSAFN-------LQENYHTLSGSA----SGGVRRKLSIVLALMA 311
Cdd:cd03254 84 QDTFLFSG-TIMENIRL-----GRP-NATDEEVIEAAKEAGahdfimkLPNGYDTVLGENggnlSQGERQLLAIARAMLR 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 525313703 312 GSKVVILDEPSSGMDPVSRRATWDILQHYKHNRTILLTTH 351
Cdd:cd03254 157 DPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAH 196
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1016-1211 |
1.06e-18 |
|
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: 86.49 E-value: 1.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1016 VKAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTR-TPRKIRSRIGYCPQtESVLNHMTGR 1094
Cdd:cd03245 17 IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQlDPADLRRNIGYVPQ-DVTLFYGTLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1095 ESLVMyarlwGVLEQDINEYVEAFLHSVhlepiADQFIHTY---------------SAGSKRRLSTAIALMGKSSVVFLD 1159
Cdd:cd03245 96 DNITL-----GAPLADDERILRAAELAG-----VTDFVNKHpngldlqigergrglSGGQRQAVALARALLNDPPILLLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 525313703 1160 EPSIGMDPVAQHLLWETI-TWICktGKAIIITSHRMEECEaLCTRLAIMVKGR 1211
Cdd:cd03245 166 EPTSAMDMNSEERLKERLrQLLG--DKTLIIITHRPSLLD-LVDRIIVMDSGR 215
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1017-1235 |
1.55e-18 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 86.99 E-value: 1.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1017 KAVKNISLVVKKSECFGLLGLNGAGKTTTFK----MLTGEETITSGIAFIdGNSVTRTP------RKIRSRIGYCPQTES 1086
Cdd:PRK09984 18 QALHAVDLNIHHGEMVALLGPSGSGKSTLLRhlsgLITGDKSAGSHIELL-GRTVQREGrlardiRKSRANTGYIFQQFN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1087 VLNHMTGRESLVMYA----RLWGV----LEQDINEYVEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIALMGKSSVVFL 1158
Cdd:PRK09984 97 LVNRLSVLENVLIGAlgstPFWRTcfswFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILA 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 525313703 1159 DEPSIGMDPVAQHLLWETITWICKT-GKAIIITSHRMEECEALCTRLAIMVKGRFTCLGTPQHV-RKRFGHVYTLTVRI 1235
Cdd:PRK09984 177 DEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQFdNERFDHLYRSINRV 255
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1003-1258 |
1.74e-18 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 88.60 E-value: 1.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1003 LNEVTKIY-FKCPVVKAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTRTP----RKIRSR 1077
Cdd:COG1135 4 LENLSKTFpTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSerelRAARRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1078 IGYCPQTESVLNHMTGRESlVMYA-RLWGVLEQDINEYVEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIALMGKSSVV 1156
Cdd:COG1135 84 IGMIFQHFNLLSSRTVAEN-VALPlEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKVL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1157 FLDEPSIGMDPvaqhllwETITWIC--------KTGKAIIITSHRMEECEALCTRLAIMVKGR-------FTCLGTPQH- 1220
Cdd:COG1135 163 LCDEATSALDP-------ETTRSILdllkdinrELGLTIVLITHEMDVVRRICDRVAVLENGRiveqgpvLDVFANPQSe 235
|
250 260 270
....*....|....*....|....*....|....*....
gi 525313703 1221 VRKRF-GHVYTLTVRINIAKDEDKVEEFKNFIKVTFPGN 1258
Cdd:COG1135 236 LTRRFlPTVLNDELPEELLARLREAAGGGRLVRLTFVGE 274
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1006-1219 |
2.51e-18 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 85.91 E-value: 2.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1006 VTKIYFKCPVVKavkNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVT---RTPRKIRSRIGYCP 1082
Cdd:PRK09493 7 VSKHFGPTQVLH---NIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpkVDERLIRQEAGMVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1083 QTESVLNHMTGRESlVMYA--RLWGVLEQDINEYVEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIALMGKSSVVFLDE 1160
Cdd:PRK09493 84 QQFYLFPHLTALEN-VMFGplRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 525313703 1161 PSIGMDPVAQHLLWETITWICKTGKAIIITSHRMEECEALCTRLAIMVKGRFTCLGTPQ 1219
Cdd:PRK09493 163 PTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQ 221
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
174-351 |
2.99e-18 |
|
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: 85.36 E-value: 2.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 174 KNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISD-NMIEVRKDLGFCPQHDLLFDDlT 252
Cdd:cd03251 13 DGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDyTLASLRRQIGLVSQDVFLFND-T 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 253 LSEHLFFycmvkGIPqNINCEEIDRMLSAFNLQE-------NYHTLSGSA----SGGVRRKLSIVLALMAGSKVVILDEP 321
Cdd:cd03251 92 VAENIAY-----GRP-GATREEVEEAARAANAHEfimelpeGYDTVIGERgvklSGGQRQRIAIARALLKDPPILILDEA 165
|
170 180 190
....*....|....*....|....*....|
gi 525313703 322 SSGMDPVSRRATWDILQHYKHNRTILLTTH 351
Cdd:cd03251 166 TSALDTESERLVQAALERLMKNRTTFVIAH 195
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1016-1221 |
3.04e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 86.40 E-value: 3.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1016 VKAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTRTP-RKIRSRIGYCPQTESVLNHMTGR 1094
Cdd:PRK13652 17 KEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENiREVRKFVGLVFQNPDDQIFSPTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1095 ESLVMYARL-WGVLEQDINEYVEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIALMGKSSVVFLDEPSIGMDPVAQHLL 1173
Cdd:PRK13652 97 EQDIAFGPInLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKEL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 525313703 1174 WETITWICKT-GKAIIITSHRMEECEALCTRLAIMVKGRFTCLGTPQHV 1221
Cdd:PRK13652 177 IDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1017-1213 |
4.35e-18 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 89.31 E-value: 4.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1017 KAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVT-RTPRK-IRSRIGYCP---QTESVLNHM 1091
Cdd:COG1129 266 GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRiRSPRDaIRAGIAYVPedrKGEGLVLDL 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1092 TGRE--SLVMYARL--WGVL-EQDINEYVEAFLHSVHLE-PIADQFIHTYSAGSKRRLSTAIALMGKSSVVFLDEPSIGM 1165
Cdd:COG1129 346 SIREniTLASLDRLsrGGLLdRRRERALAEEYIKRLRIKtPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGI 425
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 525313703 1166 DPVA----QHLLWEtitwICKTGKAIIITSHRMEECEALCTRLAIMVKGRFT 1213
Cdd:COG1129 426 DVGAkaeiYRLIRE----LAAEGKAVIVISSELPELLGLSDRILVMREGRIV 473
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
164-369 |
6.29e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 85.56 E-value: 6.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 164 IHIMHLHKEFKN-KPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNIS-DNMIEVRKDLGFC 241
Cdd:PRK13647 5 IEVEDLHFRYKDgTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNaENEKWVRSKVGLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 242 PQ--HDLLF-----DDLTLSehlffycmvkgiPQN--INCEEIDR----MLSAFNLQENYHTLSGSASGGVRRKLSIVLA 308
Cdd:PRK13647 85 FQdpDDQVFsstvwDDVAFG------------PVNmgLDKDEVERrveeALKAVRMWDFRDKPPYHLSYGQKKRVAIAGV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 525313703 309 LMAGSKVVILDEPSSGMDPVSRRATWDILQHYkHNR--TILLTTHYMDEADVLGDRVAIMVRG 369
Cdd:PRK13647 153 LAMDPDVIVLDEPMAYLDPRGQETLMEILDRL-HNQgkTVIVATHDVDLAAEWADQVIVLKEG 214
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1003-1221 |
6.36e-18 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 88.71 E-value: 6.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1003 LNEVTKIYFKCP--VVKAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSG-IAFIDGNS-VTRTPRKIRSR- 1077
Cdd:TIGR03269 282 VRNVSKRYISVDrgVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGeVNVRVGDEwVDMTKPGPDGRg 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1078 -----IGYCPQTESVLNHMTGRESLV---------MYARLWGVLEQDINEYVEAflhsvHLEPIADQFIHTYSAGSKRRL 1143
Cdd:TIGR03269 362 rakryIGILHQEYDLYPHRTVLDNLTeaiglelpdELARMKAVITLKMVGFDEE-----KAEEILDKYPDELSEGERHRV 436
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 525313703 1144 STAIALMGKSSVVFLDEPSIGMDPVAQHLLWETITWICKT-GKAIIITSHRMEECEALCTRLAIMVKGRFTCLGTPQHV 1221
Cdd:TIGR03269 437 ALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEmEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEI 515
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
177-371 |
6.56e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 85.57 E-value: 6.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 177 PAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNI---SDN--MIEVRKDLGFCPQ--HDLLFD 249
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItstSKNkdIKQIRKKVGLVFQfpESQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 250 DLTLSEHLFFycmvkgiPQN--INCEEIDRM----LSAFNLQENYHTLSG-SASGGVRRKLSIVLALMAGSKVVILDEPS 322
Cdd:PRK13649 101 ETVLKDVAFG-------PQNfgVSQEEAEALarekLALVGISESLFEKNPfELSGGQMRRVAIAGILAMEPKILVLDEPT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 525313703 323 SGMDPVSRRATWDILQHYKHN-RTILLTTHYMDEADVLGDRVAIMVRGTL 371
Cdd:PRK13649 174 AGLDPKGRKELMTLFKKLHQSgMTIVLVTHLMDDVANYADFVYVLEKGKL 223
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
162-376 |
6.58e-18 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 87.05 E-value: 6.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 162 AGIHIMHLHKEFKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISDnmIEVRK-DLGF 240
Cdd:COG3839 2 ASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTD--LPPKDrNIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 241 CPQHDLLFDDLTLSEHLFFYCMVKGIPQnincEEIDR----MLSAFNLQENYHTLSGSASGGVRRKLSIVLALMAGSKVV 316
Cdd:COG3839 80 VFQSYALYPHMTVYENIAFPLKLRKVPK----AEIDRrvreAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVF 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 525313703 317 ILDEPSSGMDPVSR---RAtwDILQ-HYKHNRTILLTTHYMDEADVLGDRVAIMVRGTLHCCGS 376
Cdd:COG3839 156 LLDEPLSNLDAKLRvemRA--EIKRlHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGT 217
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
997-1224 |
7.42e-18 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 86.70 E-value: 7.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 997 QNTPLLLNEVTKIYFKCPVVKavkNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTRtpRKIRS 1076
Cdd:PRK11432 3 QKNFVVLKNITKRFGSNTVID---NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTH--RSIQQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1077 R-IGYCPQTESVLNHMTGRESLVMYARLWGVLEQDINEYVEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIALMGKSSV 1155
Cdd:PRK11432 78 RdICMVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 525313703 1156 VFLDEPSIGMDPVAQHLLWETITwicKTGKAIIITS----HRMEECEALCTRLAIMVKGRFTCLGTPQHVRKR 1224
Cdd:PRK11432 158 LLFDEPLSNLDANLRRSMREKIR---ELQQQFNITSlyvtHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQ 227
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
170-369 |
8.08e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 85.17 E-value: 8.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 170 HKEFKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNIS-DNMIEVRKDLGFCPQH-DLL 247
Cdd:PRK13650 14 YKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTeENVWDIRHKIGMVFQNpDNQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 248 FDDLTLSEHLFFYCMVKGIPQNINCEEIDRMLSAFNLQENYHTLSGSASGGVRRKLSIVLALMAGSKVVILDEPSSGMDP 327
Cdd:PRK13650 94 FVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDP 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 525313703 328 VSRRATWDILQHYK--HNRTILLTTHYMDEAdVLGDRVAIMVRG 369
Cdd:PRK13650 174 EGRLELIKTIKGIRddYQMTVISITHDLDEV-ALSDRVLVMKNG 216
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
178-371 |
1.05e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 84.74 E-value: 1.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 178 AVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNIS-DN--MIEVRKDLGFCPQH--DLLFDDlT 252
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKyDKksLLEVRKTVGIVFQNpdDQLFAP-T 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 253 LSEHLFFYCMVKGIPQnincEEIDRM---------LSAFNLQENYHTlsgsaSGGVRRKLSIVLALMAGSKVVILDEPSS 323
Cdd:PRK13639 96 VEEDVAFGPLNLGLSK----EEVEKRvkealkavgMEGFENKPPHHL-----SGGQKKRVAIAGILAMKPEIIVLDEPTS 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 525313703 324 GMDPVSRRATWDILqhYKHNR---TILLTTHYMDEADVLGDRVAIMVRGTL 371
Cdd:PRK13639 167 GLDPMGASQIMKLL--YDLNKegiTIIISTHDVDLVPVYADKVYVMSDGKI 215
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
176-378 |
1.44e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 84.47 E-value: 1.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 176 KPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRF---AATRGEAYINGYNI-SDNMIEVRKDLGFCPQH-DLLFDD 250
Cdd:PRK13640 20 KPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGITLtAKTVWDIREKVGIVFQNpDNQFVG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 251 LTLSEHLFFYCMVKGIPQNINCEEIDRMLSAFNLQENYHTLSGSASGGVRRKLSIVLALMAGSKVVILDEPSSGMDPVSR 330
Cdd:PRK13640 100 ATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGK 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 525313703 331 RATWDILQHY--KHNRTILLTTHYMDEAdVLGDRVAIMVRGTLHCCGSSV 378
Cdd:PRK13640 180 EQILKLIRKLkkKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPV 228
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1018-1221 |
1.51e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 84.51 E-value: 1.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1018 AVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTRTPR---KIRSRIGYCPQT-ESVLNHMTG 1093
Cdd:PRK13636 21 ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKglmKLRESVGMVFQDpDNQLFSASV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1094 RESLVMYARLWGVLEQDINEYVEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIALMGKSSVVFLDEPSIGMDPVAQHLL 1173
Cdd:PRK13636 101 YQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEI 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 525313703 1174 WETITWICK-TGKAIIITSHRMEECEALCTRLAIMVKGRFTCLGTPQHV 1221
Cdd:PRK13636 181 MKLLVEMQKeLGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEV 229
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
179-369 |
1.65e-17 |
|
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: 83.28 E-value: 1.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 179 VNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNIS----DNMIEVrkdlgfcpQHDLLFDDLTLS 254
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITepgpDRMVVF--------QNYSLLPWLTVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 255 EHLffYCMVKGIPQNINCEE----IDRMLSAFNLQENYHTLSGSASGGVRRKLSIVLALMAGSKVVILDEPSSGMDPVSR 330
Cdd:TIGR01184 73 ENI--ALAVDRVLPDLSKSErraiVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTR 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 525313703 331 RATWD-ILQHYKHNR-TILLTTHYMDEADVLGDRVAIMVRG 369
Cdd:TIGR01184 151 GNLQEeLMQIWEEHRvTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
174-351 |
1.71e-17 |
|
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: 81.91 E-value: 1.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 174 KNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAA--TRGEAYINGYNISDNMievRKDLGFCPQHDLLFDDL 251
Cdd:cd03232 18 GKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAgvITGEILINGRPLDKNF---QRSTGYVEQQDVHSPNL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 252 TLSEHLFFYCMVKGIpqninceeidrmlsafNLQEnyhtlsgsasggvRRKLSIVLALMAGSKVVILDEPSSGMDPvsrR 331
Cdd:cd03232 95 TVREALRFSALLRGL----------------SVEQ-------------RKRLTIGVELAAKPSILFLDEPTSGLDS---Q 142
|
170 180
....*....|....*....|....
gi 525313703 332 ATWDILQHYK----HNRTILLTTH 351
Cdd:cd03232 143 AAYNIVRFLKkladSGQAILCTIH 166
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
168-366 |
1.82e-17 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 87.38 E-value: 1.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 168 HLHKEFKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISDNMIEVRKDLG--FCPQHD 245
Cdd:COG1129 9 GISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAGiaIIHQEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 246 LLFDDLTLSEHLFF--YCMVKGIpqnIN----CEEIDRMLSAFNLQENYHTLSGSASGGVRRKLSIVLALMAGSKVVILD 319
Cdd:COG1129 89 NLVPNLSVAENIFLgrEPRRGGL---IDwramRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 525313703 320 EPSSGMDPVSRRATWDILQHYK-HNRTILLTTHYMDEADVLGDRVAIM 366
Cdd:COG1129 166 EPTASLTEREVERLFRIIRRLKaQGVAIIYISHRLDEVFEIADRVTVL 213
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1017-1211 |
1.87e-17 |
|
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: 83.00 E-value: 1.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1017 KAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTG-----EETITSGIAFIDG---NSVTRTPRKIRSRIGYCPQTESVL 1088
Cdd:cd03260 14 HALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLDGkdiYDLDVDVLELRRRVGMVFQKPNPF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1089 nHMTGRESLVMYARLWGVLEQDINEY-VEAFLHSVHLEPIADQFIHTY--SAGSKRRLSTAIALMGKSSVVFLDEPSIGM 1165
Cdd:cd03260 94 -PGSIYDNVAYGLRLHGIKLKEELDErVEEALRKAALWDEVKDRLHALglSGGQQQRLCLARALANEPEVLLLDEPTSAL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 525313703 1166 DPVAQHLLWETITWICKTgKAIIITSHRMEECEALCTRLAIMVKGR 1211
Cdd:cd03260 173 DPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGR 217
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
175-359 |
1.90e-17 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 82.53 E-value: 1.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 175 NKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAA---TRGEAYINGYNISDNMIEVRKdLGFCPQHDLLFDDL 251
Cdd:COG4136 13 GRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAEQRR-IGILFQDDLLFPHL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 252 TLSEHLFFycmvkGIPQNINCEE----IDRMLSAFNLQENYHTLSGSASGGVRRKLSIVLALMAGSKVVILDEPSSGMDP 327
Cdd:COG4136 92 SVGENLAF-----ALPPTIGRAQrrarVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDA 166
|
170 180 190
....*....|....*....|....*....|....*...
gi 525313703 328 VSR---RA-TWDILQHykhnRTI--LLTTHymDEADVL 359
Cdd:COG4136 167 ALRaqfREfVFEQIRQ----RGIpaLLVTH--DEEDAP 198
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
164-369 |
2.36e-17 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 87.00 E-value: 2.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 164 IHIMHLHKEFKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYING--YNISDNMIEVRKDLGFC 241
Cdd:COG3845 6 LELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGkpVRIRSPRDAIALGIGMV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 242 PQHDLLFDDLTLSEHLfFYCMVKGIPQNIN----CEEIDRMLSAFNLQENYHTLSGSASGGVRRKLSIVLALMAGSKVVI 317
Cdd:COG3845 86 HQHFMLVPNLTVAENI-VLGLEPTKGGRLDrkaaRARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARILI 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 525313703 318 LDEPSSGMDPVSRRATWDILQHYKHN-RTILLTTHYMDEADVLGDRVAIMVRG 369
Cdd:COG3845 165 LDEPTAVLTPQEADELFEILRRLAAEgKSIIFITHKLREVMAIADRVTVLRRG 217
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
179-371 |
2.55e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 83.99 E-value: 2.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 179 VNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNIS-DNMIEVRKDLGFCPQH-DLLFDDLTLSEH 256
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTaENVWNLRRKIGMVFQNpDNQFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 257 LFFYCMVKGIPQNINCEEIDRMLSAFNLQENYHTLSGSASGGVRRKLSIVLALMAGSKVVILDEPSSGMDPVSRRATWDI 336
Cdd:PRK13642 103 VAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRV 182
|
170 180 190
....*....|....*....|....*....|....*..
gi 525313703 337 LQHY--KHNRTILLTTHYMDEAdVLGDRVAIMVRGTL 371
Cdd:PRK13642 183 IHEIkeKYQLTVLSITHDLDEA-ASSDRILVMKAGEI 218
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
172-351 |
3.05e-17 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 87.14 E-value: 3.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 172 EFKN--------KPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISD-NMIEVRKDLGFCP 242
Cdd:COG1132 341 EFENvsfsypgdRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDlTLESLRRQIGVVP 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 243 QHDLLFDDlTLSEHLFFycmvkGIPqNINCEEIDRMLSA-----F--NLQENYHTLSGSA----SGGVRRKLSIVLALMA 311
Cdd:COG1132 421 QDTFLFSG-TIRENIRY-----GRP-DATDEEVEEAAKAaqaheFieALPDGYDTVVGERgvnlSGGQRQRIAIARALLK 493
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 525313703 312 GSKVVILDEPSSGMDPVSRRATWDILQHYKHNRTILLTTH 351
Cdd:COG1132 494 DPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAH 533
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
180-351 |
3.21e-17 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 87.02 E-value: 3.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 180 NNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAA---TRGEAYINGYNISDNMIEVRKdlGFCPQHDLLFDDLTLSEH 256
Cdd:TIGR00955 42 KNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPIDAKEMRAIS--AYVQQDDLFIPTLTVREH 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 257 LFFYCMVK---GIPQNINCEEIDRMLSAFNLQENYHTLSGSA------SGGVRRKLSIVLALMAGSKVVILDEPSSGMDP 327
Cdd:TIGR00955 120 LMFQAHLRmprRVTKKEKRERVDEVLQALGLRKCANTRIGVPgrvkglSGGERKRLAFASELLTDPPLLFCDEPTSGLDS 199
|
170 180
....*....|....*....|....*
gi 525313703 328 VSRRATWDILQHYKHN-RTILLTTH 351
Cdd:TIGR00955 200 FMAYSVVQVLKGLAQKgKTIICTIH 224
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
164-370 |
3.22e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 83.74 E-value: 3.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 164 IHIMHLHKEFKN-KPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNI---SDNMIEVRKDLG 239
Cdd:PRK13636 6 LKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdysRKGLMKLRESVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 240 FC---PQHDLLfdDLTLSEHLFFYCMVKGIPQNINCEEIDRMLSAFNLQENYHTLSGSASGGVRRKLSIVLALMAGSKVV 316
Cdd:PRK13636 86 MVfqdPDNQLF--SASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 525313703 317 ILDEPSSGMDPVSRRATWDILQHYKH--NRTILLTTHYMDEADVLGDRVAIMVRGT 370
Cdd:PRK13636 164 VLDEPTAGLDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIVPLYCDNVFVMKEGR 219
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
159-375 |
3.26e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 86.38 E-value: 3.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 159 NLEAGIHIMHLHKEFKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYING--YNISDNMIEVRK 236
Cdd:PRK09700 1 MATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNinYNKLDHKLAAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 237 DLGFCPQHDLLFDDLTLSEHLFF-------YCMVKGIPQNINCEEIDRMLSAFNLQENYHTLSGSASGGVRRKLSIVLAL 309
Cdd:PRK09700 81 GIGIIYQELSVIDELTVLENLYIgrhltkkVCGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 525313703 310 MAGSKVVILDEPSSGMDPVSRRATWDIL-QHYKHNRTILLTTHYMDEADVLGDRVAIMVRGTLHCCG 375
Cdd:PRK09700 161 MLDAKVIIMDEPTSSLTNKEVDYLFLIMnQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
164-351 |
3.33e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 81.53 E-value: 3.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 164 IHIMHLHKEFKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISDNMIEVRKDLGFCPQ 243
Cdd:PRK13540 2 LDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 244 HDLLFDDLTLSEHLFFycmvkGIPQNINCEEIDRMLSAFNLQENYHTLSGSASGGVRRKLSIVLALMAGSKVVILDEPSS 323
Cdd:PRK13540 82 RSGINPYLTLRENCLY-----DIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLV 156
|
170 180
....*....|....*....|....*....
gi 525313703 324 GMDPVSRRATWDILQ-HYKHNRTILLTTH 351
Cdd:PRK13540 157 ALDELSLLTIITKIQeHRAKGGAVLLTSH 185
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
178-381 |
3.51e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 83.53 E-value: 3.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 178 AVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNIS-----DNMIEVRKDLGFC---PQHDLlFD 249
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITagkknKKLKPLRKKVGIVfqfPEHQL-FE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 250 DlTLSEHLFFYCMVKGIPQNINCEEIDRMLSAFNLQENYHTLSG-SASGGVRRKLSI--VLALMagSKVVILDEPSSGMD 326
Cdd:PRK13634 101 E-TVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEELLARSPfELSGGQMRRVAIagVLAME--PEVLVLDEPTAGLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 525313703 327 PVSRRATWDILQ--HYKHNRTILLTTHYMDEADVLGDRVAIMVRGTLHCCGS--SVFLK 381
Cdd:PRK13634 178 PKGRKEMMEMFYklHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTprEIFAD 236
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1005-1221 |
3.71e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 83.20 E-value: 3.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1005 EVTKIYFKCPV-VKAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTRTPR---KIRSRIGY 1080
Cdd:PRK13639 3 ETRDLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKsllEVRKTVGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1081 CPQT-ESVLNHMTGRESLVMYARLWGVLEQDINEYVEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIALMGKSSVVFLD 1159
Cdd:PRK13639 83 VFQNpDDQLFAPTVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 525313703 1160 EPSIGMDPVAQHLLWETITWICKTGKAIIITSHRMEECEALCTRLAIMVKGRFTCLGTPQHV 1221
Cdd:PRK13639 163 EPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEV 224
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1003-1192 |
9.31e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 85.12 E-value: 9.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1003 LNEVTKIYfkcPVVKAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGiafidgnSVTRTPRKirsRIGYCP 1082
Cdd:COG0488 1 LENLSKSF---GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSG-------EVSIPKGL---RIGYLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1083 Q------TESVLNHM----------------------TGRESLVMYARLWGVLEqDINEY-----VEAFLHSVHLEPI-A 1128
Cdd:COG0488 68 QepplddDLTVLDTVldgdaelraleaeleeleaklaEPDEDLERLAELQEEFE-ALGGWeaearAEEILSGLGFPEEdL 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 525313703 1129 DQFIHTYSAGSKRRLSTAIALMGKSSVVFLDEPSigmdpvaQHLLWETITW----ICKTGKAIIITSH 1192
Cdd:COG0488 147 DRPVSELSGGWRRRVALARALLSEPDLLLLDEPT-------NHLDLESIEWleefLKNYPGTVLVVSH 207
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
178-379 |
1.97e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 81.32 E-value: 1.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 178 AVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISDNMIE-----VRKDLGFCPQ--HDLLFDD 250
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQkeikpVRKKVGVVFQfpESQLFEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 251 LTLSEHLFFycmvkgiPQN--INCEEIDRM----LSAFNLQENYHTLSG-SASGGVRRKLSIVLALMAGSKVVILDEPSS 323
Cdd:PRK13643 101 TVLKDVAFG-------PQNfgIPKEKAEKIaaekLEMVGLADEFWEKSPfELSGGQMRRVAIAGILAMEPEVLVLDEPTA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 525313703 324 GMDPVSRRATWDILQH-YKHNRTILLTTHYMDEADVLGDRVAIMVRGTLHCCG--SSVF 379
Cdd:PRK13643 174 GLDPKARIEMMQLFESiHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGtpSDVF 232
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1017-1219 |
2.26e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 80.94 E-value: 2.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1017 KAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVT-RTPRKIRSRIGYCPQT-ESVLNHMTGR 1094
Cdd:PRK13647 19 KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNaENEKWVRSKVGLVFQDpDDQVFSSTVW 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1095 ESLVMYARLWGVLEQDINEYVEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIALMGKSSVVFLDEPSIGMDPVAQHLLW 1174
Cdd:PRK13647 99 DDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLM 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 525313703 1175 ETITWICKTGKAIIITSHRMEECEALCTRLAIMVKGRFTCLGTPQ 1219
Cdd:PRK13647 179 EILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKS 223
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1019-1211 |
5.00e-16 |
|
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: 77.26 E-value: 5.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1019 VKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTRT-PRKIRSRIGYCPQTesvlnhmtgresl 1097
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWdPNELGDHVGYLPQD------------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1098 vmyarlwgvleqdineyVEAFLHSvhlepIADQFIhtySAGSKRRLSTAIALMGKSSVVFLDEPSIGMDPVAQHLLWETI 1177
Cdd:cd03246 85 -----------------DELFSGS-----IAENIL---SGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAI 139
|
170 180 190
....*....|....*....|....*....|....
gi 525313703 1178 TWICKTGKAIIITSHRMEECEAlCTRLAIMVKGR 1211
Cdd:cd03246 140 AALKAAGATRIVIAHRPETLAS-ADRILVLEDGR 172
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1016-1221 |
5.56e-16 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 81.81 E-value: 5.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1016 VKAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSV-TRTPRKIRSRIGYCPQTESVLNHMTGR 1094
Cdd:PRK09536 16 TTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVeALSARAASRRVASVPQDTSLSFEFDVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1095 ESLVM-----YARLWGVLEQDiNEYVEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIALMGKSSVVFLDEPSIGMDPVA 1169
Cdd:PRK09536 96 QVVEMgrtphRSRFDTWTETD-RAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDINH 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 525313703 1170 QHLLWETITWICKTGKAIIITSHRMEECEALCTRLAIMVKGRFTCLGTPQHV 1221
Cdd:PRK09536 175 QVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADV 226
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
172-376 |
5.69e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 80.05 E-value: 5.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 172 EFKnkpAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISDNMIEV------RKDLGFC---P 242
Cdd:PRK13645 23 EFK---ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKIkevkrlRKEIGLVfqfP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 243 QHDLLFDdlTLSEHLFFYCMVKGIPQNINCEEIDRMLSAFNLQENYHTLSG-SASGGVRRKLSIVLALMAGSKVVILDEP 321
Cdd:PRK13645 100 EYQLFQE--TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDYVKRSPfELSGGQKRRVALAGIIAMDGNTLVLDEP 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 525313703 322 SSGMDPVSRRATWDILQHYKHN--RTILLTTHYMDEADVLGDRVAIMVRGTLHCCGS 376
Cdd:PRK13645 178 TGGLDPKGEEDFINLFERLNKEykKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGS 234
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
652-885 |
5.88e-16 |
|
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter family pfam01061.
Pssm-ID: 463674 [Multi-domain] Cd Length: 345 Bit Score: 80.90 E-value: 5.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 652 NKTVLTIFFNNEAYHSPAISLSILDNILFMTL---SGPDASITVFNKPQPL-PHYGSNIVPVNGLQIVQCLAFGISVVVG 727
Cdd:pfam12698 97 ESATVTVYINSSNLLVSKLILNALQSLLQQLNasaLVLLLEALSTSAPIPVeSTPLFNPQSGYAYYLVGLILMIIILIGA 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 728 SFSIQ-TVTERTSQAKHIQFLTGVCVHTYWLSALLCDLIFFFFACCVLLAIFkfcqLEAFVVHYNFLDTILIFMLYGWCV 806
Cdd:pfam12698 177 AIIAVsIVEEKESRIKERLLVSGVSPLQYWLGKILGDFLVGLLQLLIILLLL----FGIGIPFGNLGLLLLLFLLYGLAY 252
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 525313703 807 VPLTYIASFLFNSSTAAYIKITLFNYFSTMFSIIIYTIiqfygNDFPNFVhILIRAILMALPSYNLAMSISKYFDDYEV 885
Cdd:pfam12698 253 IALGYLLGSLFKNSEDAQSIIGIVILLLSGFFGGLFPL-----EDPPSFL-QWIFSIIPFFSPIDGLLRLIYGDSLWEI 325
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
164-384 |
5.90e-16 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 81.53 E-value: 5.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 164 IHIMHLHKEFKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISDNMIEVRkDLGFCPQ 243
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENR-HVNTVFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 244 HDLLFDDLTLSEHLFFYCMVKGIPQnincEEID-RMLSAFNL-------QENYHTLsgsaSGGVRRKLSIVLALMAGSKV 315
Cdd:PRK09452 94 SYALFPHMTVFENVAFGLRMQKTPA----AEITpRVMEALRMvqleefaQRKPHQL----SGGQQQRVAIARAVVNKPKV 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 525313703 316 VILDEPSSGMDPVSRRATWDILQHY--KHNRTILLTTHYMDEADVLGDRVAIMVRGTLHCCGSSvflKQIY 384
Cdd:PRK09452 166 LLLDESLSALDYKLRKQMQNELKALqrKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTP---REIY 233
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
168-351 |
6.00e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 82.42 E-value: 6.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 168 HLHKEFKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYInGYNISdnmievrkdLGFCPQH-DL 246
Cdd:COG0488 320 GLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK---------IGYFDQHqEE 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 247 LFDDLTLSEHlffycMVKGIPQNINcEEIDRMLSAFNLQENY-HTLSGSASGGVRRKLSIVLALMAGSKVVILDEPSSGM 325
Cdd:COG0488 390 LDPDKTVLDE-----LRDGAPGGTE-QEVRGYLGRFLFSGDDaFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHL 463
|
170 180
....*....|....*....|....*.
gi 525313703 326 DPVSRRATWDILQHYKHnrTILLTTH 351
Cdd:COG0488 464 DIETLEALEEALDDFPG--TVLLVSH 487
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1017-1222 |
6.79e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 79.01 E-value: 6.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1017 KAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTRTPRKIRSRIGYCP--QTESVLNHMTGR 1094
Cdd:COG4674 24 KALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGLDEHEIARLGIGRkfQKPTVFEELTVF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1095 ESLVMYA----RLWGVL----EQDINEYVEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIALMGKSSVVFLDEPSIGMD 1166
Cdd:COG4674 104 ENLELALkgdrGVFASLfarlTAEERDRIEEVLETIGLTDKADRLAGLLSHGQKQWLEIGMLLAQDPKLLLLDEPVAGMT 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 525313703 1167 PVAQHLLWETITWICKTgKAIIITSHRMEECEALCTRLAIMVKGRFTCLGTPQHVR 1222
Cdd:COG4674 184 DAETERTAELLKSLAGK-HSVVVVEHDMEFVRQIARKVTVLHQGSVLAEGSLDEVQ 238
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1018-1221 |
8.59e-16 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 81.23 E-value: 8.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1018 AVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTRTP----RKI-RSRIGYCPQTESVLNHMT 1092
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISdaelREVrRKKIAMVFQSFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1093 GRESLVMYARLWGVLEQDINEYVEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIALMGKSSVVFLDEPSIGMDP-VAQH 1171
Cdd:PRK10070 123 VLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPlIRTE 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 525313703 1172 LLWETITWICKTGKAIIITSHRMEECEALCTRLAIMVKGRFTCLGTPQHV 1221
Cdd:PRK10070 203 MQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEI 252
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
176-371 |
9.31e-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: 76.70 E-value: 9.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 176 KPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYING--YNISDNMIEVRKDLGFCP---QHDLLFDD 250
Cdd:cd03215 13 KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGkpVTRRSPRDAIRAGIAYVPedrKREGLVLD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 251 LTLSEhlffycmvkgipqNINceeIDRMLSAFNLQenyhtlsgsasggvrrKLSIVLALMAGSKVVILDEPSSGMDPVSR 330
Cdd:cd03215 93 LSVAE-------------NIA---LSSLLSGGNQQ----------------KVVLARWLARDPRVLILDEPTRGVDVGAK 140
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 525313703 331 RATWD-ILQHYKHNRTILLTTHYMDEADVLGDRVAIMVRGTL 371
Cdd:cd03215 141 AEIYRlIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
1018-1220 |
1.07e-15 |
|
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: 82.11 E-value: 1.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1018 AVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTR-TPRKIRSRIGYCPQTeSVLNHMTGRES 1096
Cdd:COG4988 352 ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDlDPASWRRQIAWVPQN-PYLFAGTIREN 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1097 LVMY------ARLWGVLEQ-DINEYVEAF---LHSvhlePIADQFiHTYSAGSKRRLSTAIALMGKSSVVFLDEPSIGMD 1166
Cdd:COG4988 431 LRLGrpdasdEELEAALEAaGLDEFVAALpdgLDT----PLGEGG-RGLSGGQAQRLALARALLRDAPLLLLDEPTAHLD 505
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 525313703 1167 PVAQHLLWETITWICKtGKAIIITSHRMEECeALCTRLAIMVKGRFTCLGTPQH 1220
Cdd:COG4988 506 AETEAEILQALRRLAK-GRTVILITHRLALL-AQADRILVLDDGRIVEQGTHEE 557
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
164-369 |
1.30e-15 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 80.13 E-value: 1.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 164 IHIMHLHKEFKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISDNMIEVRKdLGFCPQ 243
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRK-VGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 244 HDLLFDDLTLSEHLFFYCMVKGIPQNINCEEIDR-------MLSAFNLQENYHTlsgSASGGVRRKLSIVLALMAGSKVV 316
Cdd:PRK10851 82 HYALFRHMTVFDNIAFGLTVLPRRERPNAAAIKAkvtqlleMVQLAHLADRYPA---QLSGGQKQRVALARALAVEPQIL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 525313703 317 ILDEPSSGMDPVSRRA--TWDILQHYKHNRTILLTTHYMDEADVLGDRVAIMVRG 369
Cdd:PRK10851 159 LLDEPFGALDAQVRKElrRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQG 213
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
170-376 |
1.44e-15 |
|
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: 77.53 E-value: 1.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 170 HKEFKNKP----AVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISDNMIE-VRKDLGFCPQH 244
Cdd:cd03252 5 HVRFRYKPdgpvILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAwLRRQVGVVLQE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 245 DLLF-----DDLTLSEhlffycmvKGIPQNiNCEEIDRMLSAFN----LQENYHTLSG----SASGGVRRKLSIVLALMA 311
Cdd:cd03252 85 NVLFnrsirDNIALAD--------PGMSME-RVIEAAKLAGAHDfiseLPEGYDTIVGeqgaGLSGGQRQRIAIARALIH 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 525313703 312 GSKVVILDEPSSGMDPVSRRATWDILQHYKHNRTILLTTHYMdEADVLGDRVAIMVRGTLHCCGS 376
Cdd:cd03252 156 NPRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRL-STVKNADRIIVMEKGRIVEQGS 219
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
182-371 |
1.48e-15 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 77.15 E-value: 1.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 182 LSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGynisdnmievrKDLGFCPQHD----LLFDDLTLSEHL 257
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLING-----------VDVTAAPPADrpvsMLFQENNLFAHL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 258 ffycmvkGIPQNINC-------------EEIDRMLSAFNLQENYHTLSGSASGGVRRKLSIVLALMAGSKVVILDEPSSG 324
Cdd:cd03298 86 -------TVEQNVGLglspglkltaedrQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 525313703 325 MDPVSRRATWDILQ--HYKHNRTILLTTHYMDEADVLGDRVAIMVRGTL 371
Cdd:cd03298 159 LDPALRAEMLDLVLdlHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1019-1236 |
1.81e-15 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 77.89 E-value: 1.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1019 VKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTR-TPRKIRSRIGYCPQTESVLNHMTGRESL 1097
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADwSPAELARRRAVLPQHSSLSFPFTVEEVV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1098 VMYARLWGVLEQDINEYVEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIALM------GKSSVVFLDEPSIGMDPVAQH 1171
Cdd:PRK13548 98 AMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSALDLAHQH 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 525313703 1172 LLWETITWICKT-GKAIIITSHRMEECEALCTRLAIMVKGRFTCLGTPQHV--RKRFGHVYTLTVRIN 1236
Cdd:PRK13548 178 HVLRLARQLAHErGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVltPETLRRVYGADVLVQ 245
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1018-1222 |
1.83e-15 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 77.72 E-value: 1.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1018 AVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTRTPRKIRSRIGYCPQTESV--LNHMTGRE 1095
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGVVRTFQHVrlFREMTVIE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1096 SLvMYAR--------LWGVL--------EQDINEYVEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIALMGKSSVVFLD 1159
Cdd:PRK11300 100 NL-LVAQhqqlktglFSGLLktpafrraESEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLD 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 525313703 1160 EPSIGMDPVAQHLLWETITWICKT-GKAIIITSHRMEECEALCTRLAIMVKGRFTCLGTPQHVR 1222
Cdd:PRK11300 179 EPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIR 242
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
168-371 |
1.99e-15 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 79.38 E-value: 1.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 168 HLHKEFKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISDNMIEVRkDLGFCPQHDLL 247
Cdd:PRK11432 11 NITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQR-DICMVFQSYAL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 248 FDDLTLSEHLFFYCMVKGIPQnincEEI-DRMLSAFNLQEnyhtLSGSA-------SGGVRRKLSIVLALMAGSKVVILD 319
Cdd:PRK11432 90 FPHMSLGENVGYGLKMLGVPK----EERkQRVKEALELVD----LAGFEdryvdqiSGGQQQRVALARALILKPKVLLFD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 525313703 320 EPSSGMDPVSRRATWDI---LQHyKHNRTILLTTHYMDEADVLGDRVAIMVRGTL 371
Cdd:PRK11432 162 EPLSNLDANLRRSMREKireLQQ-QFNITSLYVTHDQSEAFAVSDTVIVMNKGKI 215
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
948-1210 |
2.43e-15 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 81.69 E-value: 2.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 948 FVFRNIIFYFYNKLRKGRNAIPSNQRT------KEDEDEDIKK---EKGKVFTLLLRLQNTPLLLNEVTKIYFKCPVVKA 1018
Cdd:TIGR00956 682 FFFVYILLTEFNKGAKQKGEILVFRRGslkrakKAGETSASNKndiEAGEVLGSTDLTDESDDVNDEKDMEKESGEDIFH 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1019 -----------------VKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEET---ITSGIAFIDGNSVTRT-PRkirsR 1077
Cdd:TIGR00956 762 wrnltyevkikkekrviLNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTtgvITGGDRLVNGRPLDSSfQR----S 837
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1078 IGYCPQTESVLNHMTGRESLVMYARLW---GVLEQDINEYVEAFLHSVHLEPIADQFIHTYSAG----SKRRLSTAIALM 1150
Cdd:TIGR00956 838 IGYVQQQDLHLPTSTVRESLRFSAYLRqpkSVSKSEKMEYVEEVIKLLEMESYADAVVGVPGEGlnveQRKRLTIGVELV 917
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 525313703 1151 GK-SSVVFLDEPSIGMDPVAQHLLWETITWICKTGKAIIITSHR-----MEECEalctRLAIMVKG 1210
Cdd:TIGR00956 918 AKpKLLLFLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQpsailFEEFD----RLLLLQKG 979
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1018-1221 |
2.64e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 77.82 E-value: 2.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1018 AVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDG--NSVTRTPRKIRSRIGYCPQT----------- 1084
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldTSDEENLWDIRNKAGMVFQNpdnqivative 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1085 ESVlnhMTGRESLvmyarlwGVLEQDINEYVEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIALMGKSSVVFLDEPSIG 1164
Cdd:PRK13633 105 EDV---AFGPENL-------GIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAM 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 525313703 1165 MDPVAQHLLWETITWICKT-GKAIIITSHRMEECeALCTRLAIMVKGRFTCLGTPQHV 1221
Cdd:PRK13633 175 LDPSGRREVVNTIKELNKKyGITIILITHYMEEA-VEADRIIVMDSGKVVMEGTPKEI 231
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
174-370 |
3.25e-15 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 80.45 E-value: 3.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 174 KNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISD-NMIEVRKDLGFCPQHDLLFDDlT 252
Cdd:PRK11176 354 KEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDyTLASLRNQVALVSQNVHLFND-T 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 253 LSEHLFFYCMVKGIPQNIncEEIDRMLSAF----NLQENYHTLSG----SASGGVRRKLSIVLALMAGSKVVILDEPSSG 324
Cdd:PRK11176 433 IANNIAYARTEQYSREQI--EEAARMAYAMdfinKMDNGLDTVIGengvLLSGGQRQRIAIARALLRDSPILILDEATSA 510
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 525313703 325 MDPVSRRATWDILQHYKHNRTILLTTHYM---DEAD--VLGDRVAIMVRGT 370
Cdd:PRK11176 511 LDTESERAIQAALDELQKNRTSLVIAHRLstiEKADeiLVVEDGEIVERGT 561
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
175-369 |
3.57e-15 |
|
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: 80.55 E-value: 3.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 175 NKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISD-NMIEVRKDLGFCPQHDLLFDDlTL 253
Cdd:TIGR01193 486 GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDiDRHTLRQFINYLPQEPYIFSG-SI 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 254 SEHLFFycmvkGIPQNINCEEIDRMLSAF-------NLQENYHT-LS---GSASGGVRRKLSIVLALMAGSKVVILDEPS 322
Cdd:TIGR01193 565 LENLLL-----GAKENVSQDEIWAACEIAeikddieNMPLGYQTeLSeegSSISGGQKQRIALARALLTDSKVLILDEST 639
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 525313703 323 SGMDPVSRRATWDILQHYKHnRTILLTTHYMDEADvLGDRVAIMVRG 369
Cdd:TIGR01193 640 SNLDTITEKKIVNNLLNLQD-KTIIFVAHRLSVAK-QSDKIIVLDHG 684
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
978-1161 |
3.72e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 80.11 E-value: 3.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 978 EDEDIKKEKGKV---FTLLLRLQNTPLLLNEVTKIYfkcPVVKAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEET 1054
Cdd:COG0488 290 EREEPPRRDKTVeirFPPPERLGKKVLELEGLSKSY---GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELE 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1055 ITSGIAFIdGNSVtrtprkirsRIGYCPQTESVLN-HMTGRESLVMYARlwGVLEQDINEYVEAFLHSvhlEPIADQFIH 1133
Cdd:COG0488 367 PDSGTVKL-GETV---------KIGYFDQHQEELDpDKTVLDELRDGAP--GGTEQEVRGYLGRFLFS---GDDAFKPVG 431
|
170 180
....*....|....*....|....*...
gi 525313703 1134 TYSAGSKRRLSTAIALMGKSSVVFLDEP 1161
Cdd:COG0488 432 VLSGGEKARLALAKLLLSPPNVLLLDEP 459
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
164-386 |
5.34e-15 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 76.35 E-value: 5.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 164 IHIMHLHKEFKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISD-NMIEVRKDLGFCP 242
Cdd:PRK13548 3 LEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADwSPAELARRRAVLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 243 QHDLLFDDLTLSEhlffycMVK--GIPQNINCEE----IDRMLSAFNLQE----NYHTLsgsaSGG--VRRKLSIVLALM 310
Cdd:PRK13548 83 QHSSLSFPFTVEE------VVAmgRAPHGLSRAEddalVAAALAQVDLAHlagrDYPQL----SGGeqQRVQLARVLAQL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 311 A----GSKVVILDEPSSGMDPVSRRATWDILQHYKHNR-----TIL----LTTHYmdeadvlGDRVAIMVRGTLHCCGS- 376
Cdd:PRK13548 153 WepdgPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERglaviVVLhdlnLAARY-------ADRIVLLHQGRLVADGTp 225
|
250
....*....|....*
gi 525313703 377 -SVF----LKQIYGA 386
Cdd:PRK13548 226 aEVLtpetLRRVYGA 240
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
175-351 |
5.38e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 75.30 E-value: 5.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 175 NKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISD-NMIEVRKDLGfcpQHDLLFDDLTL 253
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDpDVAEACHYLG---HRNAMKPALTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 254 SEHLFFYCMVKGIPQnincEEIDRMLSAFNLQENYHTLSGSASGGVRRKLSIVLALMAGSKVVILDEPSSGMDPVSRRAT 333
Cdd:PRK13539 91 AENLEFWAAFLGGEE----LDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALF 166
|
170
....*....|....*....
gi 525313703 334 WDILQ-HYKHNRTILLTTH 351
Cdd:PRK13539 167 AELIRaHLAQGGIVIAATH 185
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
163-409 |
6.02e-15 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 77.85 E-value: 6.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 163 GIHIMHLHKEFKNKPAVNNLSLNIYEGQVTVLLGHNGAG--KTTTLSVLTGRFAATRGEAYINGyniSDNMIEVRKDLGF 240
Cdd:NF000106 13 AVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPDAGRRPWRF*TW---CANRRALRRTIG* 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 241 C-PQHDLLFDDLTLSEHLFFYCMVKGIPQNINCEEIDRMLSAFNLQENYHTLSGSASGGVRRKLSIVLALMAGSKVVILD 319
Cdd:NF000106 90 HrPVR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 320 EPSSGMDPVSRRATWD-ILQHYKHNRTILLTTHYMDEADVLGDRVAIMVRGTLHCCGSSVFLKQIYGaGYHIVMEKQQYC 398
Cdd:NF000106 170 EPTTGLDPRTRNEVWDeVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVG-GRTLQIRPAHAA 248
|
250
....*....|.
gi 525313703 399 DVDNIIAMIQQ 409
Cdd:NF000106 249 ELDRMVGAIAQ 259
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
176-371 |
8.61e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 76.41 E-value: 8.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 176 KPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNI-----SDNMIEVRKDLGFCPQ--HDLLF 248
Cdd:PRK13641 20 KKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItpetgNKNLKKLRKKVSLVFQfpEAQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 249 DDLTLSEHLFFycmvkgiPQNINCEEID------RMLSAFNLQENYHTLSG-SASGGVRRKLSIVLALMAGSKVVILDEP 321
Cdd:PRK13641 100 ENTVLKDVEFG-------PKNFGFSEDEakekalKWLKKVGLSEDLISKSPfELSGGQMRRVAIAGVMAYEPEILCLDEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 525313703 322 SSGMDPVSRRATWDILQHY-KHNRTILLTTHYMDEADVLGDRVAIMVRGTL 371
Cdd:PRK13641 173 AAGLDPEGRKEMMQLFKDYqKAGHTVILVTHNMDDVAEYADDVLVLEHGKL 223
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
169-366 |
1.01e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 78.51 E-value: 1.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 169 LHKEFKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISDNMIEVRKDLGFCPQH-DL- 246
Cdd:PRK10762 10 IDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAGIGIIHqELn 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 247 LFDDLTLSEHLF----FYCMVKGIPQNINCEEIDRMLSAFNLQENYHTLSGSASGGVRRKLSIVLALMAGSKVVILDEPS 322
Cdd:PRK10762 90 LIPQLTIAENIFlgreFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPT 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 525313703 323 SGMDPVSRRATWDILQHYK-HNRTILLTTHYMDEADVLGDRVAIM 366
Cdd:PRK10762 170 DALTDTETESLFRVIRELKsQGRGIVYISHRLKEIFEICDDVTVF 214
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1003-1227 |
1.58e-14 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 74.66 E-value: 1.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1003 LNEVTKIYfkcPVVKAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSV-------TRTPRKIR 1075
Cdd:COG4161 5 LKNINCFY---GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsqkpsEKAIRLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1076 SRIGYCPQTESVLNHMTGRESLVMY-ARLWGVLEQDINEYVEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIALMGKSS 1154
Cdd:COG4161 82 QKVGMVFQQYNLWPHLTVMENLIEApCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 525313703 1155 VVFLDEPSIGMDPVAQHLLWETITWICKTGKAIIITSHRMEECEALCTRLAIMVKGRF------TCLGTPQhvRKRFGH 1227
Cdd:COG4161 162 VLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIieqgdaSHFTQPQ--TEAFAH 238
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
178-370 |
1.67e-14 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 75.03 E-value: 1.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 178 AVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNI---SDNMIeVRKDLGFCPQHDLLFDDLTLS 254
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIeglPGHQI-ARMGVVRTFQHVRLFREMTVI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 255 EHL-----------FFYCMVKgIP--QNINCEEIDRM---LSAFNLQENYHTLSGSASGGVRRKLSIVLALMAGSKVVIL 318
Cdd:PRK11300 99 ENLlvaqhqqlktgLFSGLLK-TPafRRAESEALDRAatwLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILML 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 525313703 319 DEPSSGMDPvsrRATWDiLQHY------KHNRTILLTTHYMDEADVLGDRVAIMVRGT 370
Cdd:PRK11300 178 DEPAAGLNP---KETKE-LDELiaelrnEHNVTVLLIEHDMKLVMGISDRIYVVNQGT 231
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1017-1220 |
1.89e-14 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 74.67 E-value: 1.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1017 KAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNS--VTRTP-----RKIRSRIGYCPQTESVLN 1089
Cdd:PRK11124 16 QALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHfdFSKTPsdkaiRELRRNVGMVFQQYNLWP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1090 HMTGRESLVMY-ARLWGVLEQDINEYVEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIALMGKSSVVFLDEPSIGMDP- 1167
Cdd:PRK11124 96 HLTVQQNLIEApCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPe 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 525313703 1168 -VAQhlLWETITWICKTGKAIIITSHRMEECEALCTRLAIMVKGRFTCLGTPQH 1220
Cdd:PRK11124 176 iTAQ--IVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASC 227
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
178-371 |
1.91e-14 |
|
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: 77.92 E-value: 1.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 178 AVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINgynISDNMIEVRKdLGFC------PQHDLLFDDL 251
Cdd:TIGR03269 299 AVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVR---VGDEWVDMTK-PGPDgrgrakRYIGILHQEY 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 252 TLSEHlffYCMVKGIPQNINCE---EIDRM-----LSAFNLQENY-----HTLSGSASGGVRRKLSIVLALMAGSKVVIL 318
Cdd:TIGR03269 375 DLYPH---RTVLDNLTEAIGLElpdELARMkavitLKMVGFDEEKaeeilDKYPDELSEGERHRVALAQVLIKEPRIVIL 451
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 525313703 319 DEPSSGMDPVSRRATWDILQHYKH--NRTILLTTHYMDEADVLGDRVAIMVRGTL 371
Cdd:TIGR03269 452 DEPTGTMDPITKVDVTHSILKAREemEQTFIIVSHDMDFVLDVCDRAALMRDGKI 506
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
177-351 |
2.15e-14 |
|
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: 73.16 E-value: 2.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 177 PAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISDNMIEVRKDLGFCPQHDLLFDDLTLSEH 256
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPELSALEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 257 LFFYCMVKGIPQNinceEIDRMLSAFNLQENYHTLSGSASGGVRRKLSIVLALMAGSKVVILDEPSSGMDPVS-RRATWD 335
Cdd:TIGR01189 94 LHFWAAIHGGAQR----TIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGvALLAGL 169
|
170
....*....|....*.
gi 525313703 336 ILQHYKHNRTILLTTH 351
Cdd:TIGR01189 170 LRAHLARGGIVLLTTH 185
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1003-1225 |
2.39e-14 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 75.99 E-value: 2.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1003 LNEVTKIY-FKCPVVKAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTRTP----RKIRSR 1077
Cdd:PRK11153 4 LKNISKVFpQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSekelRKARRQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1078 IGYCPQTESVLNHMTGRESLVMYARLWGVLEQDINEYVEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIALMGKSSVVF 1157
Cdd:PRK11153 84 IGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1158 LDEPSIGMDPvaqhllwETITWICKTGKAI---------IITsHRMEECEALCTRLAIMVKGRFTCLGT-------PQH- 1220
Cdd:PRK11153 164 CDEATSALDP-------ATTRSILELLKDInrelgltivLIT-HEMDVVKRICDRVAVIDAGRLVEQGTvsevfshPKHp 235
|
....*
gi 525313703 1221 VRKRF 1225
Cdd:PRK11153 236 LTREF 240
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
175-371 |
2.50e-14 |
|
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: 72.25 E-value: 2.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 175 NKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISD-NMIEVRKDLGFCPQHDLLFDDlTL 253
Cdd:cd03246 14 EPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQwDPNELGDHVGYLPQDDELFSG-SI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 254 SEHLFfycmvkgipqninceeidrmlsafnlqenyhtlsgsaSGGVRRKLSIVLALMAGSKVVILDEPSSGMDPVSRRAT 333
Cdd:cd03246 93 AENIL-------------------------------------SGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERAL 135
|
170 180 190
....*....|....*....|....*....|....*....
gi 525313703 334 WDILQHYK-HNRTILLTTHYMdEADVLGDRVAIMVRGTL 371
Cdd:cd03246 136 NQAIAALKaAGATRIVIAHRP-ETLASADRILVLEDGRV 173
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1007-1221 |
3.41e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 74.27 E-value: 3.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1007 TKIYFKCPVVKAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTRTPR---KIRSRIGYCPQ 1083
Cdd:PRK13638 5 SDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRgllALRQQVATVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1084 TESVLNHMTGRESLVMYA-RLWGVLEQDINEYVEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIALMGKSSVVFLDEPS 1162
Cdd:PRK13638 85 DPEQQIFYTDIDSDIAFSlRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 525313703 1163 IGMDPVAQHLLWETITWICKTGKAIIITSHRMEECEALCTRLAIMVKGRFTCLGTPQHV 1221
Cdd:PRK13638 165 AGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEV 223
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
177-371 |
3.94e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 74.25 E-value: 3.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 177 PAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISD--NMIEVRKDLGFCPQH-DLLFDDLTL 253
Cdd:PRK13644 16 PALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDfsKLQGIRKLVGIVFQNpETQFVGRTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 254 SEHLFFYcmvkgiPQNInC-------EEIDRMLSAFNLQENYHTLSGSASGGVRRKLSIVLALMAGSKVVILDEPSSGMD 326
Cdd:PRK13644 96 EEDLAFG------PENL-ClppieirKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLD 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 525313703 327 PVSRRATWD-ILQHYKHNRTILLTTHYMDEADVlGDRVAIMVRGTL 371
Cdd:PRK13644 169 PDSGIAVLErIKKLHEKGKTIVYITHNLEELHD-ADRIIVMDRGKI 213
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
1020-1192 |
5.21e-14 |
|
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: 71.89 E-value: 5.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1020 KNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEET--ITSGIAFIDGNSVTRTprkIRSRIGYCPQTESVLNHMTGRESL 1097
Cdd:cd03232 24 NNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTagVITGEILINGRPLDKN---FQRSTGYVEQQDVHSPNLTVREAL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1098 VMYARLWGVleqdineyveaflhsvhlepiadqfihtySAGSKRRLSTAIALMGKSSVVFLDEPSIGMDPVAQHLLWETI 1177
Cdd:cd03232 101 RFSALLRGL-----------------------------SVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFL 151
|
170
....*....|....*
gi 525313703 1178 TWICKTGKAIIITSH 1192
Cdd:cd03232 152 KKLADSGQAILCTIH 166
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1001-1212 |
6.49e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 76.10 E-value: 6.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1001 LLLNEVTKIYfkcPVVKAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSV--TRTPRKIRSRI 1078
Cdd:PRK11288 5 LSFDGIGKTF---PGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfASTTAALAAGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1079 GYCPQTESVLNHMTGRESLvMYARL---WGVL-EQDINEYVEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIALMGKSS 1154
Cdd:PRK11288 82 AIIYQELHLVPEMTVAENL-YLGQLphkGGIVnRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNAR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 525313703 1155 VVFLDEPSIGMDPVAQHLLWETITWICKTGKAIIITSHRMEECEALCTRLAIMVKGRF 1212
Cdd:PRK11288 161 VIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRY 218
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1005-1221 |
7.05e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 73.51 E-value: 7.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1005 EVTKIYFKCPVVK--AVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVT-RTPRKIRSRIGYC 1081
Cdd:PRK13635 7 RVEHISFRYPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSeETVWDVRRQVGMV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1082 PQTESvlNHMTG---RESLVMYARLWGVLEQDINEYVEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIALMGKSSVVFL 1158
Cdd:PRK13635 87 FQNPD--NQFVGatvQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIIL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 525313703 1159 DEPSIGMDPVAQHLLWETITWICKTGKAIIIT-SHRMEECeALCTRLAIMVKGRFTCLGTPQHV 1221
Cdd:PRK13635 165 DEATSMLDPRGRREVLETVRQLKEQKGITVLSiTHDLDEA-AQADRVIVMNKGEILEEGTPEEI 227
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
191-376 |
7.52e-14 |
|
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: 74.76 E-value: 7.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 191 VTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISDNMIEV-----RKDLGFCPQHDLLFDDLTLSEHLFF-YCMVK 264
Cdd:TIGR02142 25 VTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIflppeKRRIGYVFQEARLFPHLSVRGNLRYgMKRAR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 265 GIPQNINCEEIDRMLSAFNLQENYhtlSGSASGGVRRKLSIVLALMAGSKVVILDEPSSGMDPVSRRATWDILQ--HYKH 342
Cdd:TIGR02142 105 PSERRISFERVIELLGIGHLLGRL---PGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLErlHAEF 181
|
170 180 190
....*....|....*....|....*....|....
gi 525313703 343 NRTILLTTHYMDEADVLGDRVAIMVRGTLHCCGS 376
Cdd:TIGR02142 182 GIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGP 215
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1017-1221 |
7.95e-14 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 74.74 E-value: 7.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1017 KAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTRTPRKIRsRIGYCPQTESVLNHMTGRES 1096
Cdd:PRK10851 16 QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDR-KVGFVFQHYALFRHMTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1097 ----LVMYARLWGVLEQDINEYVEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIALMGKSSVVFLDEPSIGMDpvAQhL 1172
Cdd:PRK10851 95 iafgLTVLPRRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALD--AQ-V 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 525313703 1173 LWETITWICKTGKAIIITS----HRMEECEALCTRLAIMVKGRFTCLGTPQHV 1221
Cdd:PRK10851 172 RKELRRWLRQLHEELKFTSvfvtHDQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
160-377 |
8.11e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 73.16 E-value: 8.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 160 LEAG------IHIMHLHKEFKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYING---YNISD- 229
Cdd:PRK14246 1 MEAGksaedvFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGkvlYFGKDi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 230 ---NMIEVRKDLGFCPQHDLLFDDLTLSEHLFFYCMVKGIPQNINCEEI-DRMLSAFNL-QENYHTLSGSAS---GGVRR 301
Cdd:PRK14246 81 fqiDAIKLRKEVGMVFQQPNPFPHLSIYDNIAYPLKSHGIKEKREIKKIvEECLRKVGLwKEVYDRLNSPASqlsGGQQQ 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 525313703 302 KLSIVLALMAGSKVVILDEPSSGMDPVSRRATWDILQHYKHNRTILLTTHYMDEADVLGDRVAIMVRGTLHCCGSS 377
Cdd:PRK14246 161 RLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSS 236
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
164-394 |
8.64e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 72.64 E-value: 8.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 164 IHIMHLHKEFKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTgRF------AATRGEAYINGYNISD-NMIEVRK 236
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFN-RLielypeARVSGEVYLDGQDIFKmDVIELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 237 DLGFCPQHDLLFDDLTLSEHLFFYCMVKGIPQNiNCEEIDRMLSAFN-------LQENYHTLSGSASGGVRRKLSIVLAL 309
Cdd:PRK14247 83 RVQMVFQIPNPIPNLSIFENVALGLKLNRLVKS-KKELQERVRWALEkaqlwdeVKDRLDAPAGKLSGGQQQRLCIARAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 310 MAGSKVVILDEPSSGMDPVSRRATWDILQHYKHNRTILLTTHYMDEADVLGDRVAIMVRGTLHCCGSSvflKQIYGAGYH 389
Cdd:PRK14247 162 AFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPT---REVFTNPRH 238
|
....*
gi 525313703 390 IVMEK 394
Cdd:PRK14247 239 ELTEK 243
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
154-371 |
8.83e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 75.47 E-value: 8.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 154 EAEPPNLeagIHIMHLHKEFKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISDNMIE 233
Cdd:PRK15439 5 DTTAPPL---LCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 234 VRKDLG--FCPQHDLLFDDLTLSEHLFFycmvkGIPQNINCEE-IDRMLSAFNLQENYHTLSGSASGGVRRKLSIVLALM 310
Cdd:PRK15439 82 KAHQLGiyLVPQEPLLFPNLSVKENILF-----GLPKRQASMQkMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLM 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 525313703 311 AGSKVVILDEPSSGMDPVSRRATWDILQHY-KHNRTILLTTHYMDEADVLGDRVAIMVRGTL 371
Cdd:PRK15439 157 RDSRILILDEPTASLTPAETERLFSRIRELlAQGVGIVFISHKLPEIRQLADRISVMRDGTI 218
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1005-1221 |
9.68e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 73.10 E-value: 9.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1005 EVTKIYFKCPVVK--AVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTR-TPRKIRSRIGYC 1081
Cdd:PRK13632 9 KVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKeNLKEIRKKIGII 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1082 PQTESvlNHMTGR--ESLVMYArlwgvLE------QDINEYVEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIALMGKS 1153
Cdd:PRK13632 89 FQNPD--NQFIGAtvEDDIAFG-----LEnkkvppKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 525313703 1154 SVVFLDEPSIGMDPVAQHLLWETITWICKTG-KAIIITSHRMEECeALCTRLAIMVKGRFTCLGTPQHV 1221
Cdd:PRK13632 162 EIIIFDESTSMLDPKGKREIKKIMVDLRKTRkKTLISITHDMDEA-ILADKVIVFSEGKLIAQGKPKEI 229
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
172-351 |
1.13e-13 |
|
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: 72.19 E-value: 1.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 172 EFKN-------KPAV---NNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTgRF-AATRGEAYINGYNISD-NMIEVRKDLG 239
Cdd:cd03249 2 EFKNvsfrypsRPDVpilKGLSLTIPPGKTVALVGSSGCGKSTVVSLLE-RFyDPTSGEILLDGVDIRDlNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 240 FCPQHDLLFdDLTLSEHLFFycmvkGIPQNINCEEIDRMLSAF------NLQENYHTLSGSA----SGGVRRKLSIVLAL 309
Cdd:cd03249 81 LVSQEPVLF-DGTIAENIRY-----GKPDATDEEVEEAAKKANihdfimSLPDGYDTLVGERgsqlSGGQKQRIAIARAL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 525313703 310 MAGSKVVILDEPSSGMDPVSRRATWDILQHYKHNRTILLTTH 351
Cdd:cd03249 155 LRNPKILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAH 196
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
177-366 |
1.19e-13 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 70.73 E-value: 1.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 177 PAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGynisdnmievRKDLGFCPQHDLLFDDL--TLS 254
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG----------GARVAYVPQRSEVPDSLplTVR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 255 EhlffyCMVKGIPQNINC---------EEIDRMLSAFNLQENYHTLSGSASGGVRRKLSIVLALMAGSKVVILDEPSSGM 325
Cdd:NF040873 76 D-----LVAMGRWARRGLwrrltrddrAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 525313703 326 DPVSRRATWDILQHYKH-NRTILLTTHymDEADVLG-DRVAIM 366
Cdd:NF040873 151 DAESRERIIALLAEEHArGATVVVVTH--DLELVRRaDPCVLL 191
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
177-376 |
1.27e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 75.25 E-value: 1.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 177 PAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISD-NMIEVRKDLGFCPQHDLLFDDlTLSE 255
Cdd:PRK11160 354 PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADySEAALRQAISVVSQRVHLFSA-TLRD 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 256 HLFFYCmvkgipQNINCEEIDRMLSAFNLQ---ENYHTLS------GSA-SGGVRRKLSIVLALMAGSKVVILDEPSSGM 325
Cdd:PRK11160 433 NLLLAA------PNASDEALIEVLQQVGLEkllEDDKGLNawlgegGRQlSGGEQRRLGIARALLHDAPLLLLDEPTEGL 506
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 525313703 326 DPVSRRATWDILQHYKHNRTILLTTHYMDEADVLgDRVAIMVRGTLHCCGS 376
Cdd:PRK11160 507 DAETERQILELLAEHAQNKTVLMITHRLTGLEQF-DRICVMDNGQIIEQGT 556
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1017-1221 |
1.36e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 72.84 E-value: 1.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1017 KAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTRTPRK-----IRSRIGYCPQ-TESVLNH 1090
Cdd:PRK13643 20 RALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQkeikpVRKKVGVVFQfPESQLFE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1091 MTGRESLVMYARLWGVLEQDINEYVEAFLHSVHL-EPIADQFIHTYSAGSKRRLSTAIALMGKSSVVFLDEPSIGMDPVA 1169
Cdd:PRK13643 100 ETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLaDEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKA 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 525313703 1170 QHLLWETITWICKTGKAIIITSHRMEECEALCTRLAIMVKGRFTCLGTPQHV 1221
Cdd:PRK13643 180 RIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDV 231
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1017-1213 |
1.42e-13 |
|
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: 70.42 E-value: 1.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1017 KAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTRTPRKIRSRIGycpqtesvlnhmtgres 1096
Cdd:cd03247 16 QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLIS----------------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1097 lvmyarlwgVLEQdineyvEAFLHSVHL-EPIADQFihtySAGSKRRLSTAIALMGKSSVVFLDEPSIGMDPVAQHLLWE 1175
Cdd:cd03247 79 ---------VLNQ------RPYLFDTTLrNNLGRRF----SGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLS 139
|
170 180 190
....*....|....*....|....*....|....*...
gi 525313703 1176 TITWICKtGKAIIITSHRMEECEALcTRLAIMVKGRFT 1213
Cdd:cd03247 140 LIFEVLK-DKTLIWITHHLTGIEHM-DKILFLENGKII 175
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
160-371 |
1.48e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 72.18 E-value: 1.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 160 LEAGIHIMHLHKEFKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLT-----GRFAATRGEAYINGYNISD---NM 231
Cdd:PRK14267 1 MKFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNrllelNEEARVEGEVRLFGRNIYSpdvDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 232 IEVRKDLGFCPQHDLLFDDLTLSEHLFFYCMVKGIPQNIncEEIDRML------SAF--NLQENYHTLSGSASGGVRRKL 303
Cdd:PRK14267 81 IEVRREVGMVFQYPNPFPHLTIYDNVAIGVKLNGLVKSK--KELDERVewalkkAALwdEVKDRLNDYPSNLSGGQRQRL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 525313703 304 SIVLALMAGSKVVILDEPSSGMDPVSRRATWDILQHYKHNRTILLTTHYMDEADVLGDRVAIMVRGTL 371
Cdd:PRK14267 159 VIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARVSDYVAFLYLGKL 226
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
164-356 |
2.38e-13 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 71.65 E-value: 2.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 164 IHIMHLHKEFKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISDNMIEvrkdLGFCPQ 243
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAE----RGVVFQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 244 HDLLFDDLTLSEHLFFYCMVKGIPQNINCEEIDRMLSAFNLQENYHTLSGSASGGVRRKLSIVLALMAGSKVVILDEPSS 323
Cdd:PRK11248 78 NEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFG 157
|
170 180 190
....*....|....*....|....*....|....*
gi 525313703 324 GMDPVSRRATWDILQHYKHN--RTILLTTHYMDEA 356
Cdd:PRK11248 158 ALDAFTREQMQTLLLKLWQEtgKQVLLITHDIEEA 192
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
1020-1225 |
2.43e-13 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 74.70 E-value: 2.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1020 KNISLVVKKSECFGLLGLNGAGKTT-----TFKMLTGEETitSGIAFIDGNSVTRtpRKIRSRIGYCPQTESVLNHMTGR 1094
Cdd:TIGR00955 42 KNVSGVAKPGELLAVMGSSGAGKTTlmnalAFRSPKGVKG--SGSVLLNGMPIDA--KEMRAISAYVQQDDLFIPTLTVR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1095 ESLVMYA--RLWGVLEQDIN-EYVEAFLHSVHLEPIADQFIHT------YSAGSKRRLSTAIALMGKSSVVFLDEPSIGM 1165
Cdd:TIGR00955 118 EHLMFQAhlRMPRRVTKKEKrERVDEVLQALGLRKCANTRIGVpgrvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGL 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 525313703 1166 DPVAQHLLWETITWICKTGKAIIITSHR-MEECEALCTRLAIMVKGRFTCLGTPQHVRKRF 1225
Cdd:TIGR00955 198 DSFMAYSVVQVLKGLAQKGKTIICTIHQpSSELFELFDKIILMAEGRVAYLGSPDQAVPFF 258
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
181-372 |
2.50e-13 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 70.94 E-value: 2.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 181 NLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISDNMIEVRKdlgfcpqHDLLFDDLTLSEHLFFY 260
Cdd:COG3840 17 RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERP-------VSMLFQENNLFPHLTVA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 261 cmvkgipQNI----------NCEE---IDRMLSAFNLQENYHTLSGSASGGVRRKLSIVLALMAGSKVVILDEPSSGMDP 327
Cdd:COG3840 90 -------QNIglglrpglklTAEQraqVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDP 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 525313703 328 VSRRATWDILQ--HYKHNRTILLTTHYMDEADVLGDRVAIMVRGTLH 372
Cdd:COG3840 163 ALRQEMLDLVDelCRERGLTVLMVTHDPEDAARIADRVLLVADGRIA 209
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
164-377 |
2.53e-13 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 71.58 E-value: 2.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 164 IHIMHLHKEFKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATR---------GEAYINGYNISDNMIEV 234
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagshiellGRTVQREGRLARDIRKS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 235 RKDLGFCPQHDLLFDDLTLSEHLFFYCMvKGIPQNINC---------EEIDRMLSAFNLQENYHTLSGSASGGVRRKLSI 305
Cdd:PRK09984 85 RANTGYIFQQFNLVNRLSVLENVLIGAL-GSTPFWRTCfswftreqkQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAI 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 525313703 306 VLALMAGSKVVILDEPSSGMDPVSRRATWDILQHYKHNR--TILLTTHYMDEADVLGDRVAIMVRGTLHCCGSS 377
Cdd:PRK09984 164 ARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDgiTVVVTLHQVDYALRYCERIVALRQGHVFYDGSS 237
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
172-376 |
2.84e-13 |
|
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: 70.60 E-value: 2.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 172 EFKN---------KPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISDnmI---EVRKDLG 239
Cdd:cd03244 4 EFKNvslryrpnlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISK--IglhDLRSRIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 240 FCPQHDLLFDDlTLSEHLFFYC-----MVKGIPQNINCEEIdrmLSAFNLQENYHTLSGSA--SGGVRRKLSIVLALMAG 312
Cdd:cd03244 82 IIPQDPVLFSG-TIRSNLDPFGeysdeELWQALERVGLKEF---VESLPGGLDTVVEEGGEnlSVGQRQLLCLARALLRK 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 525313703 313 SKVVILDEPSSGMDPVSRRATWDILQHYKHNRTILLTTHYMDE-ADVlgDRVAIMVRGTLHCCGS 376
Cdd:cd03244 158 SKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTiIDS--DRILVLDKGRVVEFDS 220
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
171-371 |
2.85e-13 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 70.89 E-value: 2.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 171 KEFKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISDNMI---EVRKDLGFCPQHDLL 247
Cdd:PRK09493 9 KHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVderLIRQEAGMVFQQFYL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 248 FDDLTLSEHLFFYCM-VKGIPQNINCEEIDRMLSAFNLQENYHTLSGSASGGVRRKLSIVLALMAGSKVVILDEPSSGMD 326
Cdd:PRK09493 89 FPHLTALENVMFGPLrVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALD 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 525313703 327 PVSRRATWDILQHY-KHNRTILLTTHYMDEADVLGDRVAIMVRGTL 371
Cdd:PRK09493 169 PELRHEVLKVMQDLaEEGMTMVIVTHEIGFAEKVASRLIFIDKGRI 214
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
164-371 |
3.92e-13 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 72.14 E-value: 3.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 164 IHIMHLHKEF----KNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNI----SDNMIEVR 235
Cdd:PRK11153 2 IELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLtalsEKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 236 KDLGFCPQH-DLL-----FDDLTLSEHLffycmvkgipQNINCEEIDR----MLSAFNLQENYHTLSGSASGGVRRKLSI 305
Cdd:PRK11153 82 RQIGMIFQHfNLLssrtvFDNVALPLEL----------AGTPKAEIKArvteLLELVGLSDKADRYPAQLSGGQKQRVAI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 306 VLALMAGSKVVILDEPSSGMDPVSRRATWDILQhyKHNR----TILLTTHYMDEADVLGDRVAIMVRGTL 371
Cdd:PRK11153 152 ARALASNPKVLLCDEATSALDPATTRSILELLK--DINRelglTIVLITHEMDVVKRICDRVAVIDAGRL 219
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
178-364 |
4.45e-13 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 70.97 E-value: 4.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 178 AVNNLSLNIYEGQVTVLLGHNGAGKTTTLSV------LTGRFAAtRGEAYINGYNISDNMI---EVRKDLGFCPQHDLLF 248
Cdd:PRK14243 25 AVKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrlndLIPGFRV-EGKVTFHGKNLYAPDVdpvEVRRRIGMVFQKPNPF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 249 DDlTLSEHLFFYCMVKGIPQNINcEEIDRMLSAFNL----QENYHTLSGSASGGVRRKLSIVLALMAGSKVVILDEPSSG 324
Cdd:PRK14243 104 PK-SIYDNIAYGARINGYKGDMD-ELVERSLRQAALwdevKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSA 181
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 525313703 325 MDPVSRRATWDILQHYKHNRTILLTTHYMDEADVLGDRVA 364
Cdd:PRK14243 182 LDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTA 221
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
164-370 |
4.67e-13 |
|
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: 70.16 E-value: 4.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 164 IHIMHLHKEF-------KNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYIN-GYNISD------ 229
Cdd:COG4778 5 LEVENLSKTFtlhlqggKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhDGGWVDlaqasp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 230 -NMIEVRKD-LGFCPQhdllfddltlsehlFFYCM--------------VKGIPQNINCEEIDRMLSAFNLQENYHTLSG 293
Cdd:COG4778 85 rEILALRRRtIGYVSQ--------------FLRVIprvsaldvvaepllERGVDREEARARARELLARLNLPERLWDLPP 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 525313703 294 SA-SGGVRRKLSIVLALMAGSKVVILDEPSSGMDPVSRRATWDILQHYKHNRTILLT-THYMDEADVLGDRVAIMVRGT 370
Cdd:COG4778 151 ATfSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGiFHDEEVREAVADRVVDVTPFS 229
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
176-366 |
4.72e-13 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 70.66 E-value: 4.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 176 KPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGynisdnmIEVRK---DLGFCPQHDLLFDDLT 252
Cdd:COG4525 20 QPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDG-------VPVTGpgaDRGVVFQKDALLPWLN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 253 LSEHLFFYCMVKGIPQnINCEEI-DRMLSAFNLQENYHTLSGSASGGVRRKLSIVLALMAGSKVVILDEPSSGMDPVSR- 330
Cdd:COG4525 93 VLDNVAFGLRLRGVPK-AERRARaEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTRe 171
|
170 180 190
....*....|....*....|....*....|....*..
gi 525313703 331 RATWDILQHYKH-NRTILLTTHYMDEADVLGDRVAIM 366
Cdd:COG4525 172 QMQELLLDVWQRtGKGVFLITHSVEEALFLATRLVVM 208
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1019-1211 |
4.92e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 73.11 E-value: 4.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1019 VKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSV-TRTPRK-IRSRIGYCPQTE---------SV 1087
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVvTRSPQDgLANGIVYISEDRkrdglvlgmSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1088 LNHMTgRESLVMYARLWGVLE-QDINEYVEAFLHSVHLE-PIADQFIHTYSAGSKRRLSTAIALMGKSSVVFLDEPSIGM 1165
Cdd:PRK10762 348 KENMS-LTALRYFSRAGGSLKhADEQQAVSDFIRLFNIKtPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGV 426
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 525313703 1166 DPVAQHLLWETITWICKTGKAIIITSHRMEECEALCTRLAIMVKGR 1211
Cdd:PRK10762 427 DVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGR 472
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
171-369 |
5.06e-13 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 69.21 E-value: 5.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 171 KEFKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGR---FAATRGEAYINGYNISDNMIEVRKDLGFCPQHDLL 247
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRtegNVSVEGDIHYNGIPYKEFAEKYPGEIIYVSEEDVH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 248 FDDLTLSEHLFFYCMVKGipqninceeiDRMLSAFnlqenyhtlsgsaSGGVRRKLSIVLALMAGSKVVILDEPSSGMDP 327
Cdd:cd03233 95 FPTLTVRETLDFALRCKG----------NEFVRGI-------------SGGERKRVSIAEALVSRASVLCWDNSTRGLDS 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 525313703 328 VSrraTWDILQHYKHNRTILLTTHYM------DEADVLGDRVAIMVRG 369
Cdd:cd03233 152 ST---ALEILKCIRTMADVLKTTTFVslyqasDEIYDLFDKVLVLYEG 196
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
163-371 |
5.58e-13 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 70.04 E-value: 5.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 163 GIHIMHLHKEFKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGY------NISDN-MIEVR 235
Cdd:COG4161 2 SIQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfdfsqKPSEKaIRLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 236 KDLGFCPQHDLLFDDLTLSEHLFFY-CMVKGIPQNINCEEIDRMLSAFNLQENYHTLSGSASGGVRRKLSIVLALMAGSK 314
Cdd:COG4161 82 QKVGMVFQQYNLWPHLTVMENLIEApCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 525313703 315 VVILDEPSSGMDPVSRRATWDILQHYKHNR-TILLTTHYMDEADVLGDRVAIMVRGTL 371
Cdd:COG4161 162 VLLFDEPTAALDPEITAQVVEIIRELSQTGiTQVIVTHEVEFARKVASQVVYMEKGRI 219
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
176-371 |
6.18e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 73.34 E-value: 6.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 176 KPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGrFAATRGEAYINGYNISD-NMIEVRKDLGFCPQHDLLF-----D 249
Cdd:PRK11174 363 KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLG-FLPYQGSLKINGIELRElDPESWRKHLSWVGQNPQLPhgtlrD 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 250 DLTLSEHlffycmvkgipqNINCEEIDRMLSAFNLQENYHTL-----------SGSASGGVRRKLSIVLALMAGSKVVIL 318
Cdd:PRK11174 442 NVLLGNP------------DASDEQLQQALENAWVSEFLPLLpqgldtpigdqAAGLSVGQAQRLALARALLQPCQLLLL 509
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 525313703 319 DEPSSGMDPVSRRATWDILQHYKHNRTILLTTHYMDE-ADVlgDRVAIMVRGTL 371
Cdd:PRK11174 510 DEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDlAQW--DQIWVMQDGQI 561
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1018-1192 |
6.45e-13 |
|
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: 68.92 E-value: 6.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1018 AVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTRTPRKIRSRIGYCPQTESVLNHMTGRESL 1097
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPELSALENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1098 VMYARLWGVLEQDINEYVEAflhsVHLEPIADQFIHTYSAGSKRRLSTAIALMGKSSVVFLDEPSIGMDPVAQHLLWETI 1177
Cdd:TIGR01189 95 HFWAAIHGGAQRTIEDALAA----VGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGLL 170
|
170
....*....|....*
gi 525313703 1178 TWICKTGKAIIITSH 1192
Cdd:TIGR01189 171 RAHLARGGIVLLTTH 185
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
166-369 |
6.72e-13 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 70.10 E-value: 6.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 166 IMHLHKEFKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGR--FAATRGEAYINGYNISDNMIEVRKDLGFcpq 243
Cdd:COG0396 3 IKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEDILELSPDERARAGI--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 244 hdllfddltlsehlfFYCM-----VKGIP---------QNINCEEIDRMLSAFNLQENYHTLSGSA-----------SGG 298
Cdd:COG0396 80 ---------------FLAFqypveIPGVSvsnflrtalNARRGEELSAREFLKLLKEKMKELGLDEdfldryvnegfSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 299 VRRKLSIVLALMAGSKVVILDEPSSGMD-----PVSrratwDILQHYKH-NRTILLTTHY---MDEADVlgDRVAIMVRG 369
Cdd:COG0396 145 EKKRNEILQMLLLEPKLAILDETDSGLDidalrIVA-----EGVNKLRSpDRGILIITHYqriLDYIKP--DFVHVLVDG 217
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
154-371 |
6.74e-13 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 70.07 E-value: 6.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 154 EAEPPNLEAGIHIMHLHKEFKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVL-----TGRFAATRGEAYINGYNIS 228
Cdd:COG1117 2 TAPASTLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrmndLIPGARVEGEILLDGEDIY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 229 D---NMIEVRKDLGfcpqhdllfddltlsehlffycMV--------KGIPQNI-------------NCEEI--------- 275
Cdd:COG1117 82 DpdvDVVELRRRVG----------------------MVfqkpnpfpKSIYDNVayglrlhgiksksELDEIveeslrkaa 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 276 ------DRmL--SAFNLqenyhtlsgsaSGGVRRKLSIVLALMAGSKVVILDEPSSGMDPVSRRATWDILQHYKHNRTIL 347
Cdd:COG1117 140 lwdevkDR-LkkSALGL-----------SGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIV 207
|
250 260
....*....|....*....|....
gi 525313703 348 LTTHYMDEADVLGDRVAIMVRGTL 371
Cdd:COG1117 208 IVTHNMQQAARVSDYTAFFYLGEL 231
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
178-382 |
7.87e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 71.03 E-value: 7.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 178 AVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISD-----------------NMIEVRKDLGF 240
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDkknnhelitnpyskkikNFKELRRRVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 241 C---PQHDLLFDdlTLSEHLFFYCMVKGIPQNINCEEIDRMLSAFNLQENYHTLSG-SASGGVRRKLSIVLALMAGSKVV 316
Cdd:PRK13631 121 VfqfPEYQLFKD--TIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDSYLERSPfGLSGGQKRRVAIAGILAIQPEIL 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 525313703 317 ILDEPSSGMDPVSRRATWD-ILQHYKHNRTILLTTHYMDEADVLGDRVAIMVRGTLHCCGS--SVFLKQ 382
Cdd:PRK13631 199 IFDEPTAGLDPKGEHEMMQlILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTpyEIFTDQ 267
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
181-351 |
9.58e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 68.68 E-value: 9.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 181 NLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISdnmiEVRKDLgfcpQHDLLF--------DDLT 252
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIR----RQRDEY----HQDLLYlghqpgikTELT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 253 LSEHLFFYCmvkGIPQNINCEEIDRMLSAFNLQENYHTLSGSASGGVRRKlsIVLA--LMAGSKVVILDEP-----SSGM 325
Cdd:PRK13538 91 ALENLRFYQ---RLHGPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRR--VALArlWLTRAPLWILDEPftaidKQGV 165
|
170 180
....*....|....*....|....*.
gi 525313703 326 DPVSRRatwdILQHYKHNRTILLTTH 351
Cdd:PRK13538 166 ARLEAL----LAQHAEQGGMVILTTH 187
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
164-355 |
1.32e-12 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 68.59 E-value: 1.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 164 IHIMHLHKEFKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISDNMIEV-RKDLGFCP 242
Cdd:PRK10247 8 LQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIyRQQVSYCA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 243 QHDLLFDDlTLSEHLFFYCMVKGipQNINCEEIDRMLSAFNLQENYHTLSGSA-SGGVRRKLSIVLALMAGSKVVILDEP 321
Cdd:PRK10247 88 QTPTLFGD-TVYDNLIFPWQIRN--QQPDPAIFLDDLERFALPDTILTKNIAElSGGEKQRISLIRNLQFMPKVLLLDEI 164
|
170 180 190
....*....|....*....|....*....|....*.
gi 525313703 322 SSGMDPVSRRATWDILQHY--KHNRTILLTTHYMDE 355
Cdd:PRK10247 165 TSALDESNKHNVNEIIHRYvrEQNIAVLWVTHDKDE 200
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
189-359 |
1.35e-12 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 72.83 E-value: 1.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 189 GQVTVLLGHNGAGKTTTLSVLTGRFAA---TRGEAYINGYNISDNMievRKDLGFCPQHDLLFDDLTLSEHLFFYCMVKg 265
Cdd:TIGR00956 789 GTLTALMGASGAGKTTLLNVLAERVTTgviTGGDRLVNGRPLDSSF---QRSIGYVQQQDLHLPTSTVRESLRFSAYLR- 864
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 266 IPQNINCEE----IDRMLSAFNLQENYHTLSGSASGGV----RRKLSIVLALMAGSKVVI-LDEPSSGMDPvsrRATWDI 336
Cdd:TIGR00956 865 QPKSVSKSEkmeyVEEVIKLLEMESYADAVVGVPGEGLnveqRKRLTIGVELVAKPKLLLfLDEPTSGLDS---QTAWSI 941
|
170 180 190
....*....|....*....|....*....|..
gi 525313703 337 LQHYK----HNRTILLTTH-----YMDEADVL 359
Cdd:TIGR00956 942 CKLMRkladHGQAILCTIHqpsaiLFEEFDRL 973
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1022-1211 |
1.54e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 71.48 E-value: 1.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1022 ISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVT-RTPRK-IRSRIGYCPQ---TESVLNHMTGRES 1096
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDiRSPRDaIRAGIMLCPEdrkAEGIIPVHSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1097 LVMYAR----LWGVLeqdINEYVEAFLHSVHLE------PIADQFIHTYSAGSK------RRLSTAIalmgksSVVFLDE 1160
Cdd:PRK11288 352 INISARrhhlRAGCL---INNRWEAENADRFIRslniktPSREQLIMNLSGGNQqkailgRWLSEDM------KVILLDE 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 525313703 1161 PSIGMDPVAQHLLWETITWICKTGKAIIITSHRMEECEALCTRLAIMVKGR 1211
Cdd:PRK11288 423 PTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGR 473
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
155-351 |
2.32e-12 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 71.53 E-value: 2.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 155 AEPPNLEAGIHIMHLHKEFKNK-PAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISD-NMI 232
Cdd:PRK13657 326 IDLGRVKGAVEFDDVSFSYDNSrQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTvTRA 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 233 EVRKDLGFCPQHDLLFDdltlsehlffycmvKGIPQNINC-------EEIDRMLSAFNLQE-------NYHTLSG----S 294
Cdd:PRK13657 406 SLRRNIAVVFQDAGLFN--------------RSIEDNIRVgrpdatdEEMRAAAERAQAHDfierkpdGYDTVVGergrQ 471
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 525313703 295 ASGGVRRKLSIVLALMAGSKVVILDEPSSGMDPVSRRATWDILQHYKHNRTILLTTH 351
Cdd:PRK13657 472 LSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAH 528
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
175-351 |
2.46e-12 |
|
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: 68.03 E-value: 2.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 175 NKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISD-NMIEVRKDLGFCPQHDLLFDDlTL 253
Cdd:cd03253 13 GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREvTLDSLRRAIGVVPQDTVLFND-TI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 254 SEHLFFycmvkGIPqNINCEEIDRMLSA-------FNLQENYHTLSGSA----SGGVRRKLSIVLALMAGSKVVILDEPS 322
Cdd:cd03253 92 GYNIRY-----GRP-DATDEEVIEAAKAaqihdkiMRFPDGYDTIVGERglklSGGEKQRVAIARAILKNPPILLLDEAT 165
|
170 180
....*....|....*....|....*....
gi 525313703 323 SGMDPVSRRATWDILQHYKHNRTILLTTH 351
Cdd:cd03253 166 SALDTHTEREIQAALRDVSKGRTTIVIAH 194
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1003-1211 |
2.48e-12 |
|
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: 67.52 E-value: 2.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1003 LNEVTKIYFKCPVvkavkNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTRTPRKIRSrIGYCP 1082
Cdd:cd03298 3 LDKIRFSYGEQPM-----HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRP-VSMLF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1083 QTESVLNHMTgRESLVMYARLWGV-LEQDINEYVEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIALMGKSSVVFLDEP 1161
Cdd:cd03298 77 QENNLFAHLT-VEQNVGLGLSPGLkLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 525313703 1162 SIGMDPVAQHLLWETITWICK-TGKAIIITSHRMEECEALCTRLAIMVKGR 1211
Cdd:cd03298 156 FAALDPALRAEMLDLVLDLHAeTKMTVLMVTHQPEDAKRLAQRVVFLDNGR 206
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
1034-1193 |
2.73e-12 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 71.80 E-value: 2.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1034 LLGLNGAGKTTTFKMLTGEETitsGiAFIDGN-SVTRTPRKIRS--RI-GYCPQTESVLNHMTGRESLVMYARLW---GV 1106
Cdd:PLN03140 911 LMGVSGAGKTTLMDVLAGRKT---G-GYIEGDiRISGFPKKQETfaRIsGYCEQNDIHSPQVTVRESLIYSAFLRlpkEV 986
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1107 LEQDINEYVEAFLHSVHLEPIADQF-----IHTYSAGSKRRLSTAIALMGKSSVVFLDEPSIGMDPVAQHLLWETITWIC 1181
Cdd:PLN03140 987 SKEEKMMFVDEVMELVELDNLKDAIvglpgVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTV 1066
|
170
....*....|..
gi 525313703 1182 KTGKAIIITSHR 1193
Cdd:PLN03140 1067 DTGRTVVCTIHQ 1078
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
167-381 |
2.80e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 68.68 E-value: 2.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 167 MHL-------HKEFKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNIS-DNMIEVRKDL 238
Cdd:PRK13652 1 MHLietrdlcYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITkENIREVRKFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 239 GFCPQH--DLLFDDlTLSEHLFFYCMVKGIPQNINCEEIDRMLSAFNLQENYHTLSGSASGGVRRKLSIVLALMAGSKVV 316
Cdd:PRK13652 81 GLVFQNpdDQIFSP-TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 525313703 317 ILDEPSSGMDPVSRRATWDILQHY--KHNRTILLTTHYMDEADVLGDRVAIMVRGTLHCCGS--SVFLK 381
Cdd:PRK13652 160 VLDEPTAGLDPQGVKELIDFLNDLpeTYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTveEIFLQ 228
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
171-329 |
3.80e-12 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 70.68 E-value: 3.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 171 KEFKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAAT--RGEAYINGYNISDnmiEVRKDLGFCPQHDLLF 248
Cdd:PLN03211 76 RQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPTK---QILKRTGFVTQDDILY 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 249 DDLTLSEHLFFyCMVKGIPQNINCEE----IDRMLSAFNLQENYHTLSGSA-----SGGVRRKLSIVLALMAGSKVVILD 319
Cdd:PLN03211 153 PHLTVRETLVF-CSLLRLPKSLTKQEkilvAESVISELGLTKCENTIIGNSfirgiSGGERKRVSIAHEMLINPSLLILD 231
|
170
....*....|
gi 525313703 320 EPSSGMDPVS 329
Cdd:PLN03211 232 EPTSGLDATA 241
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
175-329 |
4.14e-12 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 68.25 E-value: 4.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 175 NKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNI----SDNMIEVRKDLGFCPQHDLLFDD 250
Cdd:PRK11831 19 NRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamsRSRLYTVRKRMSMLFQSGALFTD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 251 LT--------LSEHlffycmvKGIPQNINCEEIDRMLSAFNLQENYHTLSGSASGGVRRKLSIVLALMAGSKVVILDEPS 322
Cdd:PRK11831 99 MNvfdnvaypLREH-------TQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPF 171
|
....*..
gi 525313703 323 SGMDPVS 329
Cdd:PRK11831 172 VGQDPIT 178
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1018-1210 |
4.52e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 67.99 E-value: 4.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1018 AVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTRTPRKirSRIGYCPQTESV-LNHMTGRES 1096
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQK--NLVAYVPQSEEVdWSFPVLVED 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1097 LVMYARL--WGVL----EQDiNEYVEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIALMGKSSVVFLDEPSIGMDPVAQ 1170
Cdd:PRK15056 100 VVMMGRYghMGWLrrakKRD-RQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTE 178
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 525313703 1171 HLLWETITWICKTGKAIIITSHRMEECEALCTrLAIMVKG 1210
Cdd:PRK15056 179 ARIISLLRELRDEGKTMLVSTHNLGSVTEFCD-YTVMVKG 217
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1018-1226 |
4.93e-12 |
|
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: 67.25 E-value: 4.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1018 AVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTRTPRK-IRSRIGYCPQtESVLNHMTGRES 1096
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKsLRSMIGVVLQ-DTFLFSGTIMEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1097 LvmyaRLWGVLEQDinEYVEAFLHSVHlepiADQFI---------------HTYSAGSKRRLSTAIALMGKSSVVFLDEP 1161
Cdd:cd03254 97 I----RLGRPNATD--EEVIEAAKEAG----AHDFImklpngydtvlgengGNLSQGERQLLAIARAMLRDPKILILDEA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1162 SIGMDPVAQHLLWETITWICKtGKAIIITSHRmeeceaLCT-RLA--IMV--KGRFTCLGTPQHVRKRFG 1226
Cdd:cd03254 167 TSNIDTETEKLIQEALEKLMK-GRTSIIIAHR------LSTiKNAdkILVldDGKIIEEGTHDELLAKKG 229
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1018-1195 |
5.21e-12 |
|
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: 66.75 E-value: 5.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1018 AVKNISLVVKKSECFGLLGLNGAGKTTT----FKMLTgeetITSGIAFIDGNSVTRTP-RKIRSRIGYCPQtESVLNHMT 1092
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLllalFRLVE----LSSGSILIDGVDISKIGlHDLRSRISIIPQ-DPVLFSGT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1093 GRESLVMY-----ARLWGVLEQ-DINEYVEAFlhsvhlePIADQFIHT-----YSAGSKRRLSTAIALMGKSSVVFLDEP 1161
Cdd:cd03244 94 IRSNLDPFgeysdEELWQALERvGLKEFVESL-------PGGLDTVVEeggenLSVGQRQLLCLARALLRKSKILVLDEA 166
|
170 180 190
....*....|....*....|....*....|....
gi 525313703 1162 SIGMDPVAQHLLWETITWICKtGKAIIITSHRME 1195
Cdd:cd03244 167 TASVDPETDALIQKTIREAFK-DCTVLTIAHRLD 199
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1018-1221 |
5.24e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 68.09 E-value: 5.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1018 AVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSG---IAFIDGNSVTRTP--RKIRSRIGYCPQTESVlnHMT 1092
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGkvlVSGIDTGDFSKLQgiRKLVGIVFQNPETQFV--GRT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1093 GRESLVMYARLWGVLEQDINEYVEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIALMGKSSVVFLDEPSIGMDPVAQHL 1172
Cdd:PRK13644 95 VEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIA 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 525313703 1173 LWETITWICKTGKAIIITSHRMEECEAlCTRLAIMVKGRFTCLGTPQHV 1221
Cdd:PRK13644 175 VLERIKKLHEKGKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGEPENV 222
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
181-363 |
5.48e-12 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 67.15 E-value: 5.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 181 NLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNI----SDNMIEVR-KDLGFCPQHDLLFDDLTLSE 255
Cdd:PRK11629 27 NVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMsklsSAAKAELRnQKLGFIYQFHHLLPDFTALE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 256 HLFFYCMVKGIPQNINCEEIDRMLSAFNLQENYHTLSGSASGGVRRKLSIVLALMAGSKVVILDEPSSGMDPVSRRATWD 335
Cdd:PRK11629 107 NVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQ 186
|
170 180 190
....*....|....*....|....*....|
gi 525313703 336 ILQ--HYKHNRTILLTTHYMDEADVLGDRV 363
Cdd:PRK11629 187 LLGelNRLQGTAFLVVTHDLQLAKRMSRQL 216
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
176-379 |
5.94e-12 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 67.42 E-value: 5.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 176 KPAVNNLSLNIYEGQVTVLLGHNGAGKTTT----LSVLTGRFAATRGEAYINGYNISDNMIEVRK--------DLGFCPQ 243
Cdd:PRK10418 16 QPLVHGVSLTLQRGRVLALVGGSGSGKSLTcaaaLGILPAGVRQTAGRVLLDGKPVAPCALRGRKiatimqnpRSAFNPL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 244 HdllfddlTLSEHLFFYCMVKGIPQN----------INCEEIDRMLSAFNLQenyhtlsgsASGGVRRKLSIVLALMAGS 313
Cdd:PRK10418 96 H-------TMHTHARETCLALGKPADdatltaaleaVGLENAARVLKLYPFE---------MSGGMLQRMMIALALLCEA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 314 KVVILDEPSSGMDPVSRRATWDILQHYKHNRT--ILLTTHYMDEADVLGDRVAIMVRGTLHCCGS--SVF 379
Cdd:PRK10418 160 PFIIADEPTTDLDVVAQARILDLLESIVQKRAlgMLLVTHDMGVVARLADDVAVMSHGRIVEQGDveTLF 229
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
164-369 |
6.82e-12 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 67.08 E-value: 6.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 164 IHIMHLHKEFKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVL-------TGRFAAtrGEAYING---YNISDNMI- 232
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCInlleqpeAGTIRV--GDITIDTarsLSQQKGLIr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 233 EVRKDLGFCPQHDLLFDDLTLSEHLF-FYCMVKGIPQNINCEEIDRMLSAFNLQENYHTLSGSASGGVRRKLSIVLALMA 311
Cdd:PRK11264 82 QLRQHVGFVFQNFNLFPHRTVLENIIeGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 312 GSKVVILDEPSSGMDP--VSRRATwDILQHYKHNRTILLTTHYMDEADVLGDRVAIMVRG 369
Cdd:PRK11264 162 RPEVILFDEPTSALDPelVGEVLN-TIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQG 220
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
997-1221 |
7.11e-12 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 67.51 E-value: 7.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 997 QNTPLLLNEVTkiyFKCPVVKAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTRTPRKIRS 1076
Cdd:PRK10575 8 SDTTFALRNVS---FRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1077 R-IGYCPQTESVLNHMTGREsLVMYARL-W----GVLEQDINEYVEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIALM 1150
Cdd:PRK10575 85 RkVAYLPQQLPAAEGMTVRE-LVAIGRYpWhgalGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 525313703 1151 GKSSVVFLDEPSIGMDPVAQHLLWETITWICKT-GKAIIITSHRMEECEALCTRLAIMVKGRFTCLGTPQHV 1221
Cdd:PRK10575 164 QDSRCLLLDEPTSALDIAHQVDVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
998-1213 |
7.89e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 69.43 E-value: 7.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 998 NTPLLLNEVTKIYFKCPVV-----KAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVT-RTP 1071
Cdd:PRK09700 253 MKENVSNLAHETVFEVRNVtsrdrKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISpRSP 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1072 -RKIRSRIGYCPQTE---------SVLNHMTGRESLVM--YARLWGVL----EQDINEYVEAFL----HSVhlepiaDQF 1131
Cdd:PRK09700 333 lDAVKKGMAYITESRrdngffpnfSIAQNMAISRSLKDggYKGAMGLFhevdEQRTAENQRELLalkcHSV------NQN 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1132 IHTYSAGSKRRLSTAIALMGKSSVVFLDEPSIGMDPVAQHLLWETITWICKTGKAIIITSHRMEECEALCTRLAIMVKGR 1211
Cdd:PRK09700 407 ITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGR 486
|
..
gi 525313703 1212 FT 1213
Cdd:PRK09700 487 LT 488
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
993-1210 |
9.10e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 69.31 E-value: 9.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 993 LLRLQNTPLLLNEVTKIYFKCPVVKAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTR-TP 1071
Cdd:PRK15439 1 MQTSDTTAPPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARlTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1072 RKIRSR-IGYCPQTESVLNHMTGRES-LVMYARlwgvlEQDINEYVEAFLH--SVHLEP--------IADQFIHTYSAGs 1139
Cdd:PRK15439 81 AKAHQLgIYLVPQEPLLFPNLSVKENiLFGLPK-----RQASMQKMKQLLAalGCQLDLdssagsleVADRQIVEILRG- 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 525313703 1140 krrlstaiaLMGKSSVVFLDEPSIGMDPVAQHLLWETITWICKTGKAIIITSHRMEECEALCTRLAIMVKG 1210
Cdd:PRK15439 155 ---------LMRDSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDG 216
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
164-351 |
1.03e-11 |
|
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: 64.01 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 164 IHIMHLHKEFKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEayingynisdnmIEVRKDLGFCpq 243
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGI------------VTWGSTVKIG-- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 244 hdlLFDDLtlsehlffycmvkgipqninceeidrmlsafnlqenyhtlsgsaSGGVRRKLSIVLALMAGSKVVILDEPSS 323
Cdd:cd03221 67 ---YFEQL--------------------------------------------SGGEKMRLALAKLLLENPNLLLLDEPTN 99
|
170 180
....*....|....*....|....*...
gi 525313703 324 GMDPVSRRATWDILQHYKhnRTILLTTH 351
Cdd:cd03221 100 HLDLESIEALEEALKEYP--GTVILVSH 125
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
168-351 |
1.16e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 68.94 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 168 HLHKEFKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEayingynisdnmIEVRKDL--GFCPQHD 245
Cdd:COG0488 3 NLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGE------------VSIPKGLriGYLPQEP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 246 LLFDDLTLSEHLF-----FYCMVKGIPQ-----NINCEEIDRM----------------------LSAFNLQENYHTLS- 292
Cdd:COG0488 71 PLDDDLTVLDTVLdgdaeLRALEAELEEleaklAEPDEDLERLaelqeefealggweaearaeeiLSGLGFPEEDLDRPv 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 525313703 293 GSASGGVRRKLSIVLALMAGSKVVILDEPSSGMDPVSRRatW--DILQHYKHnrTILLTTH 351
Cdd:COG0488 151 SELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIE--WleEFLKNYPG--TVLVVSH 207
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
182-351 |
1.17e-11 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 65.21 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 182 LSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISDNMIEVRKDLGFCPQHDLLFDDLTLSEHLFFYC 261
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENLRFWH 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 262 MVKGIPQninCEE-IDRM-LSAFNlqenyHTLSGSASGGVRRKLSIVLALMAGSKVVILDEPSSGMDPVS-RRATWDILQ 338
Cdd:cd03231 99 ADHSDEQ---VEEaLARVgLNGFE-----DRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGvARFAEAMAG 170
|
170
....*....|...
gi 525313703 339 HYKHNRTILLTTH 351
Cdd:cd03231 171 HCARGGMVVLTTH 183
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1017-1221 |
1.28e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 66.69 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1017 KAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTRTP-----RKIRSRIGYCPQ-TESVLNH 1090
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSknkdiKQIRKKVGLVFQfPESQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1091 MTGRESLVMYARLWGVLEQDINEYVEAFLHSVHL-EPIADQFIHTYSAGSKRRLSTAIALMGKSSVVFLDEPSIGMDPVA 1169
Cdd:PRK13649 101 ETVLKDVAFGPQNFGVSQEEAEALAREKLALVGIsESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKG 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 525313703 1170 QHLLWETITWICKTGKAIIITSHRMEECEALCTRLAIMVKGRFTCLGTPQHV 1221
Cdd:PRK13649 181 RKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDI 232
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
168-366 |
1.29e-11 |
|
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: 67.39 E-value: 1.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 168 HLHKEFKNK----PAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTG---RFAATRGEAYINGYNISD----NMIEVR- 235
Cdd:COG0444 6 NLKVYFPTRrgvvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGllpPPGITSGEILFDGEDLLKlsekELRKIRg 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 236 KDLGFCPQhdllfDDLT-----------LSEHLFFYCMVKGIPQNincEEIDRMLSAFNLQE------NY-HTLSGsasg 297
Cdd:COG0444 86 REIQMIFQ-----DPMTslnpvmtvgdqIAEPLRIHGGLSKAEAR---ERAIELLERVGLPDperrldRYpHELSG---- 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 525313703 298 GVRRKLSIVLALMAGSKVVILDEPSSGMDpVSRRAtwDILQHYK-----HNRTILLTTHYMDEADVLGDRVAIM 366
Cdd:COG0444 154 GMRQRVMIARALALEPKLLIADEPTTALD-VTIQA--QILNLLKdlqreLGLAILFITHDLGVVAEIADRVAVM 224
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1020-1211 |
1.37e-11 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 65.18 E-value: 1.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1020 KNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGiafidgnSVTrtprkIRSRIGYCPQTESVLNhMTGRESLvm 1099
Cdd:cd03250 22 KDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSG-------SVS-----VPGSIAYVSQEPWIQN-GTIRENI-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1100 yarLWGvLEQDiNEYVEAFLHSVHLEPIADQFIH-----------TYSAGSKRRLSTAIALMGKSSVVFLDEPSIGMDP- 1167
Cdd:cd03250 87 ---LFG-KPFD-EERYEKVIKACALEPDLEILPDgdlteigekgiNLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAh 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 525313703 1168 VAQHLLWETITWICKTGKAIIITSHRMEECEAlCTRLAIMVKGR 1211
Cdd:cd03250 162 VGRHIFENCILGLLLNNKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
170-376 |
1.53e-11 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 65.87 E-value: 1.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 170 HKEFKnkpAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGyNISdNMIEVRkdLGFCPqhdllfd 249
Cdd:COG1134 36 REEFW---ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG-RVS-ALLELG--AGFHP------- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 250 DLTLSEHLFFYCMVKGIPQnincEEIDRMLS---AF-NLQE-------NYhtlsgsaSGGVRRKLSIVLALMAGSKVVIL 318
Cdd:COG1134 102 ELTGRENIYLNGRLLGLSR----KEIDEKFDeivEFaELGDfidqpvkTY-------SSGMRARLAFAVATAVDPDILLV 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 525313703 319 DEPSSGMDPV-SRRATWDILQHYKHNRTILLTTHYMDEADVLGDRVAIMVRGTLHCCGS 376
Cdd:COG1134 171 DEVLAVGDAAfQKKCLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGD 229
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
164-371 |
1.94e-11 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 67.03 E-value: 1.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 164 IHIMHLHKEFKNK----PAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISD----NMIEVR 235
Cdd:COG1135 2 IELENLSKTFPTKggpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTAlserELRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 236 KDLGFCPQHDLLFDDLTLSEhlffycmvkgipqNI---------NCEEIDR----MLSAFNLQE---NY-HTLsgsaSGG 298
Cdd:COG1135 82 RKIGMIFQHFNLLSSRTVAE-------------NValpleiagvPKAEIRKrvaeLLELVGLSDkadAYpSQL----SGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 299 VRRKLSIVLALMAGSKVVILDEPSSGMDPvsrRATWDILQ-----HYKHNRTILLTTHymdEADV---LGDRVAIMVRGT 370
Cdd:COG1135 145 QKQRVGIARALANNPKVLLCDEATSALDP---ETTRSILDllkdiNRELGLTIVLITH---EMDVvrrICDRVAVLENGR 218
|
.
gi 525313703 371 L 371
Cdd:COG1135 219 I 219
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
163-364 |
2.28e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 65.83 E-value: 2.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 163 GIHIMHLHKEFKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTgRFAATRGEAYING---------YNISDNMIE 233
Cdd:PRK14258 7 AIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLN-RMNELESEVRVEGrveffnqniYERRVNLNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 234 VRKDLGFC-PQHDLLfdDLTLSEHLFFYCMVKGIPQNINCEEI-DRMLSAFNL-QENYHTLSGSA---SGGVRRKLSIVL 307
Cdd:PRK14258 86 LRRQVSMVhPKPNLF--PMSVYDNVAYGVKIVGWRPKLEIDDIvESALKDADLwDEIKHKIHKSAldlSGGQQQRLCIAR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 525313703 308 ALMAGSKVVILDEPSSGMDPVSRRATWDILQHY--KHNRTILLTTHYMDEADVLGDRVA 364
Cdd:PRK14258 164 ALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLrlRSELTMVIVSHNLHQVSRLSDFTA 222
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1017-1193 |
2.44e-11 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 67.88 E-value: 2.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1017 KAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTR-TPRKIRSRIGYCPQtESVLNHMTGRE 1095
Cdd:COG1132 354 PVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDlTLESLRRQIGVVPQ-DTFLFSGTIRE 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1096 SLvmyarLWGVLEQDiNEYVEAFLHSVHlepiADQFIHT----Y-----------SAGSKRRLSTAIALMGKSSVVFLDE 1160
Cdd:COG1132 433 NI-----RYGRPDAT-DEEVEEAAKAAQ----AHEFIEAlpdgYdtvvgergvnlSGGQRQRIAIARALLKDPPILILDE 502
|
170 180 190
....*....|....*....|....*....|...
gi 525313703 1161 PSIGMDPVAQHLLWETITWICKtGKAIIITSHR 1193
Cdd:COG1132 503 ATSALDTETEALIQEALERLMK-GRTTIVIAHR 534
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1018-1231 |
2.86e-11 |
|
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: 65.20 E-value: 2.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1018 AVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSV-TRTPRKIRSRIGYCPQTESVLNHMT---- 1092
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLaLADPAWLRRQVGVVLQENVLFNRSIrdni 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1093 -------GRESLVMYARLWGVLEQdINEYVEAFlhsvhlEPIADQFIHTYSAGSKRRLSTAIALMGKSSVVFLDEPSIGM 1165
Cdd:cd03252 97 aladpgmSMERVIEAAKLAGAHDF-ISELPEGY------DTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSAL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 525313703 1166 DPVAQHLLWETITWICKtGKAIIITSHRMEECEAlCTRLAIMVKGRFTCLGTPQHVRKRFGHVYTL 1231
Cdd:cd03252 170 DYESEHAIMRNMHDICA-GRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLAENGLYAYL 233
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1022-1192 |
2.95e-11 |
|
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: 64.05 E-value: 2.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1022 ISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTRTPRKIRSRIGYCPQTESVLNHMTGRESLVMYA 1101
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENLRFWH 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1102 RLWGvleqdiNEYVEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIALMGKSSVVFLDEPSIGMDPVAQHLLWETITWIC 1181
Cdd:cd03231 99 ADHS------DEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGHC 172
|
170
....*....|.
gi 525313703 1182 KTGKAIIITSH 1192
Cdd:cd03231 173 ARGGMVVLTTH 183
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
157-351 |
3.88e-11 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 64.41 E-value: 3.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 157 PPNLEAGIHIMHLHKEFKNKPAVN---NLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISDNMIE 233
Cdd:cd03248 5 PDHLKGIVKFQNVTFAYPTRPDTLvlqDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 234 -VRKDLGFCPQHDLLFDDlTLSEHLFFycmvkGIPQnINCEEIDRMLSAFN-------LQENYHTLSGSA----SGGVRR 301
Cdd:cd03248 85 yLHSKVSLVGQEPVLFAR-SLQDNIAY-----GLQS-CSFECVKEAAQKAHahsfiseLASGYDTEVGEKgsqlSGGQKQ 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 525313703 302 KLSIVLALMAGSKVVILDEPSSGMDPVSRRATWDILQHYKHNRTILLTTH 351
Cdd:cd03248 158 RVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAH 207
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1017-1195 |
4.43e-11 |
|
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: 66.93 E-value: 4.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1017 KAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTRTPRK-IRSRIGYCPQTESVLNHmTGRE 1095
Cdd:TIGR02857 336 PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADsWRDQIAWVPQHPFLFAG-TIAE 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1096 SLVMYARlwGVLEQDINEYVE-AFLHSvhLEPIADQFIHT--------YSAGSKRRLSTAIALMGKSSVVFLDEPSIGMD 1166
Cdd:TIGR02857 415 NIRLARP--DASDAEIREALErAGLDE--FVAALPQGLDTpigeggagLSGGQAQRLALARAFLRDAPLLLLDEPTAHLD 490
|
170 180
....*....|....*....|....*....
gi 525313703 1167 PVAQHLLWETITWICKtGKAIIITSHRME 1195
Cdd:TIGR02857 491 AETEAEVLEALRALAQ-GRTVLLVTHRLA 518
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1020-1192 |
4.45e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 63.74 E-value: 4.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1020 KNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSG-IAFIDGNSvtrTPRKIRSRIGYCPQTESVLNHMTGRESLV 1098
Cdd:PRK13539 19 SGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGtIKLDGGDI---DDPDVAEACHYLGHRNAMKPALTVAENLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1099 MYARLWGVLEQDINEYVEAFlhsvHLEPIADQFIHTYSAGSKRRLSTAIALMGKSSVVFLDEPSIGMDPVAQHLLWETIT 1178
Cdd:PRK13539 96 FWAAFLGGEELDIAAALEAV----GLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELIR 171
|
170
....*....|....
gi 525313703 1179 WICKTGKAIIITSH 1192
Cdd:PRK13539 172 AHLAQGGIVIAATH 185
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
164-407 |
4.68e-11 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 64.65 E-value: 4.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 164 IHIMHLHKEFKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISD-NMIEVRKDLGFCP 242
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMlSSRQLARRLALLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 243 QHDLLFDDLTL--------SEHLFFYCMVKGIPQNInceeIDRMLSAFNLQENYHTLSGSASGGVRRKLSIVLALMAGSK 314
Cdd:PRK11231 83 QHHLTPEGITVrelvaygrSPWLSLWGRLSAEDNAR----VNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 315 VVILDEPSSGMDpVSRRAT-WDILQHYKHN-RTILLTTHYMDEADVLGDRVAIMVRGTLHCCGSSvflkqiygagyHIVM 392
Cdd:PRK11231 159 VVLLDEPTTYLD-INHQVElMRLMRELNTQgKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTP-----------EEVM 226
|
250
....*....|....*
gi 525313703 393 EKQQYCDVDNIIAMI 407
Cdd:PRK11231 227 TPGLLRTVFDVEAEI 241
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
173-369 |
5.34e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 65.03 E-value: 5.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 173 FKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNIS---DNMIEVRKDLGFC---PQHDL 246
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDyskRGLLALRQQVATVfqdPEQQI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 247 LFDDLtlSEHLFFYCMVKGIPQNINCEEIDRMLSAFNLQENYHTLSGSASGGVRRKLSIVLALMAGSKVVILDEPSSGMD 326
Cdd:PRK13638 91 FYTDI--DSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLD 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 525313703 327 PVSRRATWDILQH-YKHNRTILLTTHYMDEADVLGDRVAIMVRG 369
Cdd:PRK13638 169 PAGRTQMIAIIRRiVAQGNHVIISSHDIDLIYEISDAVYVLRQG 212
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
181-351 |
6.87e-11 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 66.67 E-value: 6.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 181 NLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNIS----DNMIEVRKD-LGFCPQHDLLFDDLTLSE 255
Cdd:PRK10535 26 GISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVAtldaDALAQLRREhFGFIFQRYHLLSHLTAAQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 256 HLFFYCMVKGIPQNINCEEIDRMLSAFNLQENYHTLSGSASGGVRRKLSIVLALMAGSKVVILDEPSSGMDPVSRRATWD 335
Cdd:PRK10535 106 NVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMA 185
|
170
....*....|....*..
gi 525313703 336 IL-QHYKHNRTILLTTH 351
Cdd:PRK10535 186 ILhQLRDRGHTVIIVTH 202
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1017-1221 |
7.43e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 64.47 E-value: 7.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1017 KAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVT-----RTPRKIRSRIGYCPQ-TESVLNH 1090
Cdd:PRK13641 21 KGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgnKNLKKLRKKVSLVFQfPEAQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1091 MTGRESLVMYARLWGVLEQDINEYVEAFLHSVHL-EPIADQFIHTYSAGSKRRLSTAIALMGKSSVVFLDEPSIGMDPVA 1169
Cdd:PRK13641 101 NTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEG 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 525313703 1170 QHLLWETITWICKTGKAIIITSHRMEECEALCTRLAIMVKGRFTCLGTPQHV 1221
Cdd:PRK13641 181 RKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEI 232
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1019-1231 |
8.03e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 64.37 E-value: 8.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1019 VKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVT-RTPRKIRSRIGYCPQTESvlNHMTGR--E 1095
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTeENVWDIRHKIGMVFQNPD--NQFVGAtvE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1096 SLVMYA-RLWGVLEQDINEYVEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIALMGKSSVVFLDEPSIGMDPVAQHLLW 1174
Cdd:PRK13650 101 DDVAFGlENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELI 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 525313703 1175 ETITWICKT-GKAIIITSHRMEECeALCTRLAIMVKGRFTCLGTPQHVRKRFGHVYTL 1231
Cdd:PRK13650 181 KTIKGIRDDyQMTVISITHDLDEV-ALSDRVLVMKNGQVESTSTPRELFSRGNDLLQL 237
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
178-357 |
8.07e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 66.69 E-value: 8.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 178 AVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISDNmiEVRKDLG----FCPQhDL---LFDD 250
Cdd:NF033858 16 ALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADA--RHRRAVCpriaYMPQ-GLgknLYPT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 251 LTLSEHLFFYCMVKGIPQnincEE----IDRMLSAFNLQENYHTLSGSASGGVRRKLSIVLALMAGSKVVILDEPSSGMD 326
Cdd:NF033858 93 LSVFENLDFFGRLFGQDA----AErrrrIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVD 168
|
170 180 190
....*....|....*....|....*....|....
gi 525313703 327 PVSRRATWDILQHYKHNR---TILLTTHYMDEAD 357
Cdd:NF033858 169 PLSRRQFWELIDRIRAERpgmSVLVATAYMEEAE 202
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
170-375 |
8.82e-11 |
|
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: 63.32 E-value: 8.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 170 HKEFKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGyNISdNMIEVrkDLGFCPqhdllfd 249
Cdd:cd03220 29 KGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG-RVS-SLLGL--GGGFNP------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 250 DLTLSEHLFFYCMVKGIPQnincEEIDRML---SAFN-LQENYHTLSGSASGGVRRKLSIVLALMAGSKVVILDEPSSGM 325
Cdd:cd03220 98 ELTGRENIYLNGRLLGLSR----KEIDEKIdeiIEFSeLGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 525313703 326 DPVSRRATWDILQHY-KHNRTILLTTHYMDEADVLGDRVAIMVRGTLHCCG 375
Cdd:cd03220 174 DAAFQEKCQRRLRELlKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
164-327 |
9.14e-11 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 63.49 E-value: 9.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 164 IHIMHLHKEFKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYI--NGYNISDN-----MIEVRK 236
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIagNHFDFSKTpsdkaIRELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 237 DLGFCPQHDLLFDDLTLSEHLFFY-CMVKGIPQNINCEEIDRMLSAFNLQENYHTLSGSASGGVRRKLSIVLALMAGSKV 315
Cdd:PRK11124 83 NVGMVFQQYNLWPHLTVQQNLIEApCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQV 162
|
170
....*....|..
gi 525313703 316 VILDEPSSGMDP 327
Cdd:PRK11124 163 LLFDEPTAALDP 174
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1019-1225 |
1.12e-10 |
|
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: 65.92 E-value: 1.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1019 VKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTR-TPRKIRSRIGYCPQTESVLNhmtG--RE 1095
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQwDREELGRHIGYLPQDVELFD---GtiAE 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1096 SLvmyARLWGVLEQDIneyVEAF-LHSVHlEPIA------DQFI----HTYSAGSKRRLSTAIALMGKSSVVFLDEPSIG 1164
Cdd:COG4618 425 NI---ARFGDADPEKV---VAAAkLAGVH-EMILrlpdgyDTRIgeggARLSGGQRQRIGLARALYGDPRLVVLDEPNSN 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 525313703 1165 MDPVAQHLLWETITWICKTGKAIIITSHRMeecEAL--CTRLAIMVKGRFTCLGTPQHVRKRF 1225
Cdd:COG4618 498 LDDEGEAALAAAIRALKARGATVVVITHRP---SLLaaVDKLLVLRDGRVQAFGPRDEVLARL 557
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
996-1221 |
1.21e-10 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 63.45 E-value: 1.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 996 LQNTPLLLNEVTKIYFKCPVVKAVkniSLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVT------- 1068
Cdd:PRK10619 1 MSENKLNVIDLHKRYGEHEVLKGV---SLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdg 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1069 -------RTPRKIRSRIGYCPQTESVLNHMTGRESlVMYA--RLWGVLEQDINEYVEAFLHSVHLEPIA-DQFIHTYSAG 1138
Cdd:PRK10619 78 qlkvadkNQLRLLRTRLTMVFQHFNLWSHMTVLEN-VMEApiQVLGLSKQEARERAVKYLAKVGIDERAqGKYPVHLSGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1139 SKRRLSTAIALMGKSSVVFLDEPSIGMDPVAQHLLWETITWICKTGKAIIITSHRMEECEALCTRLAIMVKGRFTCLGTP 1218
Cdd:PRK10619 157 QQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAP 236
|
...
gi 525313703 1219 QHV 1221
Cdd:PRK10619 237 EQL 239
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1019-1218 |
1.90e-10 |
|
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: 61.77 E-value: 1.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1019 VKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEE--TITSGIAFIDGNSVTRTPRKIRSRIG------YCPQTESVlnh 1090
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEERARLGiflafqYPPEIPGV--- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1091 mtgreSLVMYARlwgvleqDINEyveaflhsvhlepiadqfihTYSAGSKRRLSTAIALMGKSSVVFLDEPSIGMDPVAQ 1170
Cdd:cd03217 93 -----KNADFLR-------YVNE--------------------GFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDAL 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 525313703 1171 HLLWETITWICKTGKAIIITSHRMEECEAL-CTRLAIMVKGRFTCLGTP 1218
Cdd:cd03217 141 RLVAEVINKLREEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGDK 189
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
998-1166 |
1.96e-10 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 62.53 E-value: 1.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 998 NTPLLL-NEVTKIYFKCPVVKAV-KNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSV----TRTP 1071
Cdd:PRK11629 2 NKILLQcDNLCKRYQEGSVQTDVlHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMsklsSAAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1072 RKIRSR-IGYCPQTESVLNHMTGRESLVMYARLWGVLEQDINEYVEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIALM 1150
Cdd:PRK11629 82 AELRNQkLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALV 161
|
170
....*....|....*.
gi 525313703 1151 GKSSVVFLDEPSIGMD 1166
Cdd:PRK11629 162 NNPRLVLADEPTGNLD 177
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1001-1218 |
2.07e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 63.49 E-value: 2.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1001 LLLNEVTKIYFK-CPV-VKAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTG------EETITSGIAFIDGNSVTRTPR 1072
Cdd:PRK13645 7 IILDNVSYTYAKkTPFeFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGliisetGQTIVGDYAIPANLKKIKEVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1073 KIRSRIGYCPQ-TESVLNHMTGRESLVMYARLWGVLEQDINEYVEAFLHSVHL-EPIADQFIHTYSAGSKRRLSTA--IA 1148
Cdd:PRK13645 87 RLRKEIGLVFQfPEYQLFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAgiIA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 525313703 1149 LMGKSSVvfLDEPSIGMDPVAQHLLWETITWICKT-GKAIIITSHRMEECEALCTRLAIMVKGRFTCLGTP 1218
Cdd:PRK13645 167 MDGNTLV--LDEPTGGLDPKGEEDFINLFERLNKEyKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSP 235
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
171-370 |
2.17e-10 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 61.72 E-value: 2.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 171 KEFKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGynisdnmievrkDLGFCPQHDLLFDD 250
Cdd:cd03250 13 GEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG------------SIAYVSQEPWIQNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 251 lTLSEHLFFycmvkGIPqnINCEEIDRMLSAFNLQENYHTLSG-----------SASGGVRRKLSIVLALMAGSKVVILD 319
Cdd:cd03250 81 -TIRENILF-----GKP--FDEERYEKVIKACALEPDLEILPDgdlteigekgiNLSGGQKQRISLARAVYSDADIYLLD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 525313703 320 EPSSGMDPVSRRATWD--ILQHYKHNRTILLTTH---YMDEAdvlgDRVAIMVRGT 370
Cdd:cd03250 153 DPLSAVDAHVGRHIFEncILGLLLNNKTRILVTHqlqLLPHA----DQIVVLDNGR 204
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1003-1192 |
2.34e-10 |
|
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: 60.15 E-value: 2.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1003 LNEVTKIYFKCPVVKavkNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIafidgnsVTRTPrkiRSRIGYCP 1082
Cdd:cd03221 3 LENLSKTYGGKLLLK---DISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGI-------VTWGS---TVKIGYFE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1083 QtesvlnhmtgreslvmyarlwgvleqdineyveaflhsvhlepiadqfihtYSAGSKRRLSTAIALMGKSSVVFLDEPS 1162
Cdd:cd03221 70 Q---------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPT 98
|
170 180 190
....*....|....*....|....*....|
gi 525313703 1163 IGMDPVAQHLLWETITwicKTGKAIIITSH 1192
Cdd:cd03221 99 NHLDLESIEALEEALK---EYPGTVILVSH 125
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1005-1213 |
2.40e-10 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 61.81 E-value: 2.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1005 EVTKIYFKCPvvKAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTRTPRK----IRSRIGY 1080
Cdd:PRK10908 6 HVSKAYLGGR--QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNRevpfLRRQIGM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1081 CPQTESVLNHMTGRESLVMYARLWGVLEQDINEYVEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIALMGKSSVVFLDE 1160
Cdd:PRK10908 84 IFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 525313703 1161 PSIGMDPVAQHLLWETITWICKTGKAIIITSHRMEECEALCTRLAIMVKGRFT 1213
Cdd:PRK10908 164 PTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
171-365 |
2.50e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 64.55 E-value: 2.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 171 KEFKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYING----YNISDNMIE-----VRKDLGFC 241
Cdd:PRK11288 12 KTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGqemrFASTTAALAagvaiIYQELHLV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 242 PqhdllfdDLTLSEHLffycMVKGIPQN---IN----CEEIDRMLSAFNLQENYHTLSGSASGGVRRKLSIVLALMAGSK 314
Cdd:PRK11288 92 P-------EMTVAENL----YLGQLPHKggiVNrrllNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNAR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 525313703 315 VVILDEPSSGMdpvSRRATwDIL-----QHYKHNRTILLTTHYMDEADVLGDRVAI 365
Cdd:PRK11288 161 VIAFDEPTSSL---SAREI-EQLfrvirELRAEGRVILYVSHRMEEIFALCDAITV 212
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
1018-1193 |
2.60e-10 |
|
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: 64.69 E-value: 2.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1018 AVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTRTPR-KIRSRIGYCPQtESVLNHMTGRES 1096
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQdEVRRRVSVCAQ-DAHLFDTTVREN 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1097 LvMYAR-------LWGVLEQ-DINEYVEAFLHSVHLEPIADQfiHTYSAGSKRRLSTAIALMGKSSVVFLDEPSIGMDPV 1168
Cdd:TIGR02868 429 L-RLARpdatdeeLWAALERvGLADWLRALPDGLDTVLGEGG--ARLSGGERQRLALARALLADAPILLLDEPTEHLDAE 505
|
170 180
....*....|....*....|....*
gi 525313703 1169 AQHLLWETItWICKTGKAIIITSHR 1193
Cdd:TIGR02868 506 TADELLEDL-LAALSGRTVVLITHH 529
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1014-1231 |
2.60e-10 |
|
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: 62.17 E-value: 2.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1014 PVVKAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSV-TRTPRKIRSRIGYCPQtESVLNHMT 1092
Cdd:cd03249 14 PDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIrDLNLRWLRSQIGLVSQ-EPVLFDGT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1093 GRESLVmYARLWGVLEQDINEYVEAFLHSvhlepiadqFI----HTY-----------SAGSKRRLSTAIALMGKSSVVF 1157
Cdd:cd03249 93 IAENIR-YGKPDATDEEVEEAAKKANIHD---------FImslpDGYdtlvgergsqlSGGQKQRIAIARALLRNPKILL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 525313703 1158 LDEPSIGMDPVAQHLLWETITWICKtGKAIIITSHRmeeceaLCT-----RLAIMVKGRFTCLGTPQHVRKRFGHVYTL 1231
Cdd:cd03249 163 LDEATSALDAESEKLVQEALDRAMK-GRTTIVIAHR------LSTirnadLIAVLQNGQVVEQGTHDELMAQKGVYAKL 234
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1020-1221 |
2.65e-10 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 62.70 E-value: 2.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1020 KNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTR-TPRKIRSRIGYCPQTESVLNHMTGREsLV 1098
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHyASKEVARRIGLLAQNATTPGDITVQE-LV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1099 MYAR-----LWGVLEQDINEYVEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIALMGKSSVVFLDEPSIGMDPVAQHLL 1173
Cdd:PRK10253 103 ARGRyphqpLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDL 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 525313703 1174 WETITWICKT-GKAIIITSHRMEECEALCTRLAIMVKGRFTCLGTPQHV 1221
Cdd:PRK10253 183 LELLSELNREkGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
1030-1193 |
4.54e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 64.13 E-value: 4.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1030 ECFGLLGLNGAGKTTTFKMLTG--EETITSGIAFIDGNSVTRtprKIRSRIGYCPQTESVLNHMTGRESLVMYA--RLWG 1105
Cdd:PLN03211 95 EILAVLGPSGSGKSTLLNALAGriQGNNFTGTILANNRKPTK---QILKRTGFVTQDDILYPHLTVRETLVFCSllRLPK 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1106 VLEQDINEYV-EAFLHSVHLEP-----IADQFIHTYSAGSKRRLSTAIALMGKSSVVFLDEPSIGMDPVAQHLLWETITW 1179
Cdd:PLN03211 172 SLTKQEKILVaESVISELGLTKcentiIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGS 251
|
170
....*....|....
gi 525313703 1180 ICKTGKAIIITSHR 1193
Cdd:PLN03211 252 LAQKGKTIVTSMHQ 265
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
177-371 |
4.64e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 63.87 E-value: 4.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 177 PAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNIS--------DNMI----EVRKdlgfcpqH 244
Cdd:PRK10762 266 PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVtrspqdglANGIvyisEDRK-------R 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 245 DLLFDDLTLSEHL-------FFYCMVKgIPQNINCEEIDRMLSAFNLQenyhTLS-----GSASGGVRRKLSIVLALMAG 312
Cdd:PRK10762 339 DGLVLGMSVKENMsltalryFSRAGGS-LKHADEQQAVSDFIRLFNIK----TPSmeqaiGLLSGGNQQKVAIARGLMTR 413
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 525313703 313 SKVVILDEPSSGMDPVSRRATWDILQHYKHN-RTILLTTHYMDEadVLG--DRVAIMVRGTL 371
Cdd:PRK10762 414 PKVLILDEPTRGVDVGAKKEIYQLINQFKAEgLSIILVSSEMPE--VLGmsDRILVMHEGRI 473
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1026-1173 |
4.69e-10 |
|
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: 61.66 E-value: 4.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1026 VKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTrtprkirsrigYCPQTESVLNHMTGRESLvmYARLWG 1105
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS-----------YKPQYIKADYEGTVRDLL--SSITKD 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 525313703 1106 VLEQdiNEYVEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIALMGKSSVVFLDEPSIGMDpVAQHLL 1173
Cdd:cd03237 89 FYTH--PYFKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLD-VEQRLM 153
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
171-415 |
4.98e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 63.79 E-value: 4.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 171 KEFKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRF--AATRGEAYING-----YNISDNMievRKDLGFCPQ 243
Cdd:PRK13549 13 KTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYphGTYEGEIIFEGeelqaSNIRDTE---RAGIAIIHQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 244 HDLLFDDLTLSEHLFFYC-MVKG--IPQNINCEEIDRMLSAFNLQENYHTLSGSASGGVRRKLSIVLALMAGSKVVILDE 320
Cdd:PRK13549 90 ELALVKELSVLENIFLGNeITPGgiMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 321 PSSGMDPVSRRATWDILQHYK-HNRTILLTTHYMDEADVLGDRVAImVRGtlhccgssvflkqiygaGYHIVMEKQQYCD 399
Cdd:PRK13549 170 PTASLTESETAVLLDIIRDLKaHGIACIYISHKLNEVKAISDTICV-IRD-----------------GRHIGTRPAAGMT 231
|
250 260
....*....|....*....|....*..
gi 525313703 400 VDNIIAMI-----------QQHVPGAV 415
Cdd:PRK13549 232 EDDIITMMvgreltalyprEPHTIGEV 258
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
157-363 |
5.21e-10 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 61.62 E-value: 5.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 157 PPNLEAGIHIM--HLHKEFKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEaYINGyniSDNMIEV 234
Cdd:PRK11247 4 TARLNQGTPLLlnAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGE-LLAG---TAPLAEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 235 RKDLgfcpqhDLLFDDLTLSEHlffycmvKGIPQNINC-------EEIDRMLSAFNLQENYHTLSGSASGGVRRKLSIVL 307
Cdd:PRK11247 80 REDT------RLMFQDARLLPW-------KKVIDNVGLglkgqwrDAALQALAAVGLADRANEWPAALSGGQKQRVALAR 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 525313703 308 ALMAGSKVVILDEPSSGMDPVSRRATWDILQHY--KHNRTILLTTHYMDEADVLGDRV 363
Cdd:PRK11247 147 ALIHRPGLLLLDEPLGALDALTRIEMQDLIESLwqQHGFTVLLVTHDVSEAVAMADRV 204
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
135-351 |
5.23e-10 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 63.58 E-value: 5.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 135 KIRKTTEEAkctPIVHNCYEAEPPnlEAG---IHIMHLHKEFKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTG 211
Cdd:PRK10789 289 RIRAMLAEA---PVVKDGSEPVPE--GRGeldVNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQR 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 212 RFAATRGEAYINGYNISD-NMIEVRKDLGFCPQHDLLFDDlTLSEHLFFYCmVKGIPQNIncEEIDRMLSA----FNLQE 286
Cdd:PRK10789 364 HFDVSEGDIRFHDIPLTKlQLDSWRSRLAVVSQTPFLFSD-TVANNIALGR-PDATQQEI--EHVARLASVhddiLRLPQ 439
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 525313703 287 NYHTLSGSA----SGGVRRKLSIVLALMAGSKVVILDEPSSGMDPVSRRATWDILQHYKHNRTILLTTH 351
Cdd:PRK10789 440 GYDTEVGERgvmlSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAH 508
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1014-1211 |
6.23e-10 |
|
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: 63.31 E-value: 6.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1014 PVVKAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGE-ETITSGIAFIDGNSV-TRTPRK-IRSRIGYCPQ------- 1083
Cdd:TIGR02633 271 PHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPVdIRNPAQaIRAGIAMVPEdrkrhgi 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1084 ----------TESVLNHMTGReslvmyARLWGVLEQDIneyVEAFLHSVHLEPIA-DQFIHTYSAGSKRRLSTAIALMGK 1152
Cdd:TIGR02633 351 vpilgvgkniTLSVLKSFCFK------MRIDAAAELQI---IGSAIQRLKVKTASpFLPIGRLSGGNQQKAVLAKMLLTN 421
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 525313703 1153 SSVVFLDEPSIGMDPVAQHLLWETITWICKTGKAIIITSHRMEECEALCTRLAIMVKGR 1211
Cdd:TIGR02633 422 PRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGK 480
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
161-375 |
8.89e-10 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 61.05 E-value: 8.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 161 EAGIHIMHLHKEFKN-KPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISDNMievRKDL- 238
Cdd:PRK15056 4 QAGIVVNDVTVTWRNgHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQAL---QKNLv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 239 GFCPQHD-------LLFDDLTLSEHLFFYCMVKgIPQNINCEEIDRMLSAFNLQENYHTLSGSASGGVRRKLSIVLALMA 311
Cdd:PRK15056 81 AYVPQSEevdwsfpVLVEDVVMMGRYGHMGWLR-RAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQ 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 525313703 312 GSKVVILDEPSSGMDPVSRRATWDILQHYK-HNRTILLTTHYMDEADVLGDrVAIMVRGTLHCCG 375
Cdd:PRK15056 160 QGQVILLDEPFTGVDVKTEARIISLLRELRdEGKTMLVSTHNLGSVTEFCD-YTVMVKGTVLASG 223
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1016-1211 |
8.96e-10 |
|
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: 62.92 E-value: 8.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1016 VKAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTG--------EETITSGiAFIDGNSVTRTPRK----IRSRIGYCPQ 1083
Cdd:TIGR02633 14 VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGvyphgtwdGEIYWSG-SPLKASNIRDTERAgiviIHQELTLVPE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1084 TESVLNHMTGRESLVMYARLwgvleqDINEYV---EAFLHSVHLEPIAD-QFIHTYSAGSKRRLSTAIALMGKSSVVFLD 1159
Cdd:TIGR02633 93 LSVAENIFLGNEITLPGGRM------AYNAMYlraKNLLRELQLDADNVtRPVGDYGGGQQQLVEIAKALNKQARLLILD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 525313703 1160 EPSIGMDPVAQHLLWETITWICKTGKAIIITSHRMEECEALCTRLAIMVKGR 1211
Cdd:TIGR02633 167 EPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
168-407 |
9.12e-10 |
|
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: 62.92 E-value: 9.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 168 HLHKEFKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRF--AATRGEAYING-----YNISDNMievRKDLGF 240
Cdd:TIGR02633 6 GIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphGTWDGEIYWSGsplkaSNIRDTE---RAGIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 241 CPQHDLLFDDLTLSEHLFF--YCMVKGIPQNIN-----CEEIDRMLSAFNLqeNYHTLSGSASGGVRRKLSIVLALMAGS 313
Cdd:TIGR02633 83 IHQELTLVPELSVAENIFLgnEITLPGGRMAYNamylrAKNLLRELQLDAD--NVTRPVGDYGGGQQQLVEIAKALNKQA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 314 KVVILDEPSSGMDPVSRRATWDILQHYK-HNRTILLTTHYMDEADVLGDRVAImVRGtlhccgssvflkqiygaGYHIVM 392
Cdd:TIGR02633 161 RLLILDEPSSSLTEKETEILLDIIRDLKaHGVACVYISHKLNEVKAVCDTICV-IRD-----------------GQHVAT 222
|
250
....*....|....*
gi 525313703 393 EKQQYCDVDNIIAMI 407
Cdd:TIGR02633 223 KDMSTMSEDDIITMM 237
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
168-372 |
9.14e-10 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 60.37 E-value: 9.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 168 HLHKEFknkpavnnlSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISDNMIEVRkdlgfcPQhDLL 247
Cdd:PRK10771 13 HLPMRF---------DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRR------PV-SML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 248 FDDLTLSEHLffycmvkGIPQNINC-------------EEIDRMLSAFNLQENYHTLSGSASGGVRRKLSIVLALMAGSK 314
Cdd:PRK10771 77 FQENNLFSHL-------TVAQNIGLglnpglklnaaqrEKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 315 VVILDEPSSGMDPVSRRATWDILQHYKHNR--TILLTTHYMDEADVLGDRVAIMVRGTLH 372
Cdd:PRK10771 150 ILLLDEPFSALDPALRQEMLTLVSQVCQERqlTLLMVSHSLEDAARIAPRSLVVADGRIA 209
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
178-369 |
9.43e-10 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 61.66 E-value: 9.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 178 AVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAA---TRGEAYINGYNISdNMIEVRKDLGFCPQHDLLFDD---- 250
Cdd:PRK09473 31 AVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREIL-NLPEKELNKLRAEQISMIFQDpmts 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 251 ----LTLSEHLFFYCMV-KGIPQNINCEEIDRMLSAFNLQENYHTLS---GSASGGVRRKLSIVLALMAGSKVVILDEPS 322
Cdd:PRK09473 110 lnpyMRVGEQLMEVLMLhKGMSKAEAFEESVRMLDAVKMPEARKRMKmypHEFSGGMRQRVMIAMALLCRPKLLIADEPT 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 525313703 323 SGMDPVSRRATWDILQHYKH--NRTILLTTHymDEADVLG--DRVAIMVRG 369
Cdd:PRK09473 190 TALDVTVQAQIMTLLNELKRefNTAIIMITH--DLGVVAGicDKVLVMYAG 238
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1014-1211 |
1.14e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 62.64 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1014 PVVKAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGE-ETITSGIAFIDGNSVT-RTPRK-IRSRIGYCPQ------- 1083
Cdd:PRK13549 273 PHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAyPGRWEGEIFIDGKPVKiRNPQQaIAQGIAMVPEdrkrdgi 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1084 ----------TESVLNHMTGReslvmyARLWGVLEQDIneyVEAFLHSVHLE-PIADQFIHTYSAGSKRRLSTAIALMGK 1152
Cdd:PRK13549 353 vpvmgvgkniTLAALDRFTGG------SRIDDAAELKT---ILESIQRLKVKtASPELAIARLSGGNQQKAVLAKCLLLN 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 525313703 1153 SSVVFLDEPSIGMDPVAQHLLWETITWICKTGKAIIITSHRMEECEALCTRLAIMVKGR 1211
Cdd:PRK13549 424 PKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGK 482
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
181-351 |
1.40e-09 |
|
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: 63.01 E-value: 1.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 181 NLSLNIYEGQVTVLLGHNGAGKTTTLSVLTgRFAATRGEAYINGynISDNMIEV---RKDLGFCPQHDLLFDDlTLSEHL 257
Cdd:TIGR01271 1237 DLSFSVEGGQRVGLLGRTGSGKSTLLSALL-RLLSTEGEIQIDG--VSWNSVTLqtwRKAFGVIPQKVFIFSG-TFRKNL 1312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 258 FFYcmvkgipQNINCEEIDR---------MLSAFNLQENYHTLSGSA--SGGVRRKLSIVLALMAGSKVVILDEPSSGMD 326
Cdd:TIGR01271 1313 DPY-------EQWSDEEIWKvaeevglksVIEQFPDKLDFVLVDGGYvlSNGHKQLMCLARSILSKAKILLLDEPSAHLD 1385
|
170 180
....*....|....*....|....*
gi 525313703 327 PVSRRATWDILQHYKHNRTILLTTH 351
Cdd:TIGR01271 1386 PVTLQIIRKTLKQSFSNCTVILSEH 1410
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1018-1232 |
1.86e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 60.15 E-value: 1.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1018 AVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVT-RTPRKIRSRIGYCPQTESvlNHMTGreS 1096
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITdDNFEKLRKHIGIVFQNPD--NQFVG--S 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1097 LVMYARLWG-----VLEQDINEYVEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIALMGKSSVVFLDEPSIGMDPVAQH 1171
Cdd:PRK13648 100 IVKYDVAFGlenhaVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQ 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 525313703 1172 LLWETITWIcKTGKAIIITSHRMEECEAL-CTRLAIMVKGRFTCLGTPQHVrkrFGHVYTLT 1232
Cdd:PRK13648 180 NLLDLVRKV-KSEHNITIISITHDLSEAMeADHVIVMNKGTVYKEGTPTEI---FDHAEELT 237
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
998-1212 |
1.91e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 61.94 E-value: 1.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 998 NTPLL-LNEVTKIYfkcPVVKAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVT-RTPRK-- 1073
Cdd:PRK10762 1 MQALLqLKGIDKAF---PGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfNGPKSsq 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1074 ------IRSRIGYCPQTESVLNHMTGREslvMYARLWGVLEQDINEYVEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAI 1147
Cdd:PRK10762 78 eagigiIHQELNLIPQLTIAENIFLGRE---FVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAK 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 525313703 1148 ALMGKSSVVFLDEPSIGMDPVAQHLLWETITWICKTGKAIIITSHRMEECEALCTRLAIMVKGRF 1212
Cdd:PRK10762 155 VLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQF 219
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1017-1218 |
2.13e-09 |
|
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: 58.96 E-value: 2.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1017 KAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTRTP-RKIRSRIGYCPQtESVLNHMTGRE 1095
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPlEDLRSSLTIIPQ-DPTLFSGTIRS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1096 SLVMYarlwgvleqdiNEYVEAFLH-SVHLEPIADQFihtySAGSKRRLSTAIALMGKSSVVFLDEPSIGMDPVAQHLLW 1174
Cdd:cd03369 101 NLDPF-----------DEYSDEEIYgALRVSEGGLNL----SQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQ 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 525313703 1175 ETITWICkTGKAIIITSHRMEECeALCTRLAIMVKGRFTCLGTP 1218
Cdd:cd03369 166 KTIREEF-TNSTILTIAHRLRTI-IDYDKILVMDAGEVKEYDHP 207
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1019-1221 |
2.56e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 59.47 E-value: 2.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1019 VKNISLVVKKSECFGLLGLNGAGKTT---TFKMLT--GEETITSGIAFIDGNSVTRT---PRKIRSRIGYCPQTESVLNH 1090
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTllrTFNRLLelNEEARVEGEVRLFGRNIYSPdvdPIEVRREVGMVFQYPNPFPH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1091 MTGRESLVMYARLWGVL--EQDINEYVEAFLHSVHL-EPIADQ---FIHTYSAGSKRRLSTAIALMGKSSVVFLDEPSIG 1164
Cdd:PRK14267 100 LTIYDNVAIGVKLNGLVksKKELDERVEWALKKAALwDEVKDRlndYPSNLSGGQRQRLVIARALAMKPKILLMDEPTAN 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 525313703 1165 MDPVA----QHLLWETitwicKTGKAIIITSHRMEECEALCTRLAIMVKGRFTCLGTPQHV 1221
Cdd:PRK14267 180 IDPVGtakiEELLFEL-----KKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKV 235
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1006-1221 |
3.13e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 59.29 E-value: 3.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1006 VTKIYFKCPVVKAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTRTPR-------KIRSRI 1078
Cdd:PRK14246 13 ISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDifqidaiKLRKEV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1079 GYCPQTESVLNHMTGRESLVMYARLWGVLEQ-DINEYVEAFLHSVHL-EPIADQF---IHTYSAGSKRRLSTAIALMGKS 1153
Cdd:PRK14246 93 GMVFQQPNPFPHLSIYDNIAYPLKSHGIKEKrEIKKIVEECLRKVGLwKEVYDRLnspASQLSGGQQQRLTIARALALKP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 525313703 1154 SVVFLDEPSIGMDPVAQHLLWETITWIcKTGKAIIITSHRMEECEALCTRLAIMVKGRFTCLGTPQHV 1221
Cdd:PRK14246 173 KVLLMDEPTSMIDIVNSQAIEKLITEL-KNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEI 239
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1005-1192 |
3.48e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 59.71 E-value: 3.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1005 EVTKIY-FKCP-VVKAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSG---IAFIDGNSVTRTPRK------ 1073
Cdd:PRK13651 7 NIVKIFnKKLPtELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGtieWIFKDEKNKKKTKEKekvlek 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1074 ----------------IRSRIGYCPQ-TESVLNHMTGRESLVMYARLWGVLEQDINEYVEAFLHSVHL-EPIADQFIHTY 1135
Cdd:PRK13651 87 lviqktrfkkikkikeIRRRVGVVFQfAEYQLFEQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLdESYLQRSPFEL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 525313703 1136 SAGSKRRLSTAIALMGKSSVVFLDEPSIGMDPVAQHLLWETITWICKTGKAIIITSH 1192
Cdd:PRK13651 167 SGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTH 223
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1004-1226 |
3.59e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 59.41 E-value: 3.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1004 NEVTKIYFK-CPV-VKAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVT-----RTPRKIRS 1076
Cdd:PRK13646 6 DNVSYTYQKgTPYeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIThktkdKYIRPVRK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1077 RIGYCPQ-TESVLNHMTGRESLVMYARLWGVLEQDINEYVEAFLHSVHLE-PIADQFIHTYSAGSKRRLSTAIALMGKSS 1154
Cdd:PRK13646 86 RIGMVFQfPESQLFEDTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFSrDVMSQSPFQMSGGQMRKIAIVSILAMNPD 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 525313703 1155 VVFLDEPSIGMDPVAQHLLWETITWI-CKTGKAIIITSHRMEECEALCTRLAIMVKGRFTCLGTPqhvRKRFG 1226
Cdd:PRK13646 166 IIVLDEPTAGLDPQSKRQVMRLLKSLqTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSP---KELFK 235
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1019-1166 |
3.80e-09 |
|
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: 58.04 E-value: 3.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1019 VKNISLVVKKSECFGLLGLNGAGKTTTFKMLTG--EETI-TSGIAFIDGNSVTRTPRKIRSRIGYCPQTESVLNHMTGRE 1095
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANrtEGNVsVEGDIHYNGIPYKEFAEKYPGEIIYVSEEDVHFPTLTVRE 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 525313703 1096 SLVMYARLWGvleqdineyveaflhsvhlepiaDQFIHTYSAGSKRRLSTAIALMGKSSVVFLDEPSIGMD 1166
Cdd:cd03233 103 TLDFALRCKG-----------------------NEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1017-1194 |
4.68e-09 |
|
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: 58.40 E-value: 4.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1017 KAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSV-TRTPRKIRSRIGYCPQtESVLNHMTGRE 1095
Cdd:cd03251 16 PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVrDYTLASLRRQIGLVSQ-DVFLFNDTVAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1096 SlVMYARLWGVLEQdineyVEAFLHSVHlepiADQFI-------HT--------YSAGSKRRLSTAIALMGKSSVVFLDE 1160
Cdd:cd03251 95 N-IAYGRPGATREE-----VEEAARAAN----AHEFImelpegyDTvigergvkLSGGQRQRIAIARALLKDPPILILDE 164
|
170 180 190
....*....|....*....|....*....|....
gi 525313703 1161 PSIGMDPVAQHLLWETITWICKTGKAIIItSHRM 1194
Cdd:cd03251 165 ATSALDTESERLVQAALERLMKNRTTFVI-AHRL 197
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1019-1224 |
5.11e-09 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 58.61 E-value: 5.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1019 VKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIA-----FIDG----NSVTRTPRKIRSRIGYCPQTESVLN 1089
Cdd:PRK11264 19 LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgdiTIDTarslSQQKGLIRQLRQHVGFVFQNFNLFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1090 HMTGRESLVM-YARLWGVLEQDINEYVEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIALMGKSSVVFLDEPSIGMDPV 1168
Cdd:PRK11264 99 HRTVLENIIEgPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPE 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 525313703 1169 AQHLLWETITWICKTGKAIIITSHRMEECEALCTRLAIMVKGRF-------TCLGTPQHVRKR 1224
Cdd:PRK11264 179 LVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIveqgpakALFADPQQPRTR 241
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
993-1221 |
6.98e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 59.09 E-value: 6.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 993 LLRLQNTPLLLNEVTKiyfkcPVVKAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGeeTITSGIAFI---------- 1062
Cdd:PRK13631 21 ILRVKNLYCVFDEKQE-----NELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNG--LIKSKYGTIqvgdiyigdk 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1063 ---DGNSVTRTPRKI------RSRIGYCPQTESVLNHMTGRESLVMYARL-WGVLEQDINEYVEAFLHSVHL-EPIADQF 1131
Cdd:PRK13631 94 knnHELITNPYSKKIknfkelRRRVSMVFQFPEYQLFKDTIEKDIMFGPVaLGVKKSEAKKLAKFYLNKMGLdDSYLERS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1132 IHTYSAGSKRRLSTAIALMGKSSVVFLDEPSIGMDPVAQHLLWETITWICKTGKAIIITSHRMEECEALCTRLAIMVKGR 1211
Cdd:PRK13631 174 PFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGK 253
|
250
....*....|
gi 525313703 1212 FTCLGTPQHV 1221
Cdd:PRK13631 254 ILKTGTPYEI 263
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
181-351 |
7.01e-09 |
|
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: 58.33 E-value: 7.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 181 NLSLNIYEGQVTVLLGHNGAGKTTTLSVLTgRFAATRGEAYINGYNI-SDNMIEVRKDLGFCPQHDLLFDDlTLSEHLFF 259
Cdd:cd03289 22 NISFSISPGQRVGLLGRTGSGKSTLLSAFL-RLLNTEGDIQIDGVSWnSVPLQKWRKAFGVIPQKVFIFSG-TFRKNLDP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 260 YcmvkgipQNINCEEIDR---------MLSAFNLQENYHTLSGSA--SGGVRRKLSIVLALMAGSKVVILDEPSSGMDPV 328
Cdd:cd03289 100 Y-------GKWSDEEIWKvaeevglksVIEQFPGQLDFVLVDGGCvlSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPI 172
|
170 180
....*....|....*....|...
gi 525313703 329 SRRATWDILQHYKHNRTILLTTH 351
Cdd:cd03289 173 TYQVIRKTLKQAFADCTVILSEH 195
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1016-1213 |
7.53e-09 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 59.66 E-value: 7.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1016 VKAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTR-TPRKIRSR-IGYCP---QTESVLNH 1090
Cdd:COG3845 271 VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGlSPRERRRLgVAYIPedrLGRGLVPD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1091 MTGRESLVM-------YARlWGVLEQD-INEYVEAflhsvhlepIADQF-IHTYSAGSK-RRLS------TAIA--LMGK 1152
Cdd:COG3845 351 MSVAENLILgryrrppFSR-GGFLDRKaIRAFAEE---------LIEEFdVRTPGPDTPaRSLSggnqqkVILAreLSRD 420
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 525313703 1153 SSVVFLDEPSIGMDPVAQHLLWETITWICKTGKAIIITSHRMEECEALCTRLAIMVKGRFT 1213
Cdd:COG3845 421 PKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRIV 481
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
176-371 |
7.56e-09 |
|
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: 58.28 E-value: 7.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 176 KPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNIS----DNMIEVRKDLgfcpqhDLLFDDL 251
Cdd:TIGR02769 24 APVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYqldrKQRRAFRRDV------QLVFQDS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 252 ------------TLSEHLFFYCMVKGIPQNincEEIDRMLSAFNLQ-ENYHTLSGSASGGVRRKLSIVLALMAGSKVVIL 318
Cdd:TIGR02769 98 psavnprmtvrqIIGEPLRHLTSLDESEQK---ARIAELLDMVGLRsEDADKLPRQLSGGQLQRINIARALAVKPKLIVL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 525313703 319 DEPSSGMDPVSRRATWDILQHYKHNRTI--LLTTHYMDEADVLGDRVAIMVRGTL 371
Cdd:TIGR02769 175 DEAVSNLDMVLQAVILELLRKLQQAFGTayLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
181-371 |
7.68e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 59.68 E-value: 7.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 181 NLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISDNMIEVRKDLG--FCP----QHDLLFD----- 249
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGlvYLPedrqSSGLYLDaplaw 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 250 ---DLTLSEHLFF------------YCMVKGIpqniNCEEIDRMLsafnlqenyHTLSGsasgGVRRKLSIVLALMAGSK 314
Cdd:PRK15439 361 nvcALTHNRRGFWikparenavlerYRRALNI----KFNHAEQAA---------RTLSG----GNQQKVLIAKCLEASPQ 423
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 525313703 315 VVILDEPSSGMDpVSRRAtwDILQHYKH----NRTILLTTHYMDEADVLGDRVAIMVRGTL 371
Cdd:PRK15439 424 LLIVDEPTRGVD-VSARN--DIYQLIRSiaaqNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
1018-1203 |
7.70e-09 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 59.90 E-value: 7.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1018 AVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSvtrTPRKIRSRIGycpqtesvlNHMTGRESL 1097
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSA---ALIAISSGLN---------GQLTGIENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1098 VMYARLWGVLEQDINEYVEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIALMGKSSVVFLDEP-SIGMDPVAQHLLwET 1176
Cdd:PRK13545 107 ELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEAlSVGDQTFTKKCL-DK 185
|
170 180
....*....|....*....|....*..
gi 525313703 1177 ITWICKTGKAIIITSHRMEECEALCTR 1203
Cdd:PRK13545 186 MNEFKEQGKTIFFISHSLSQVKSFCTK 212
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
182-385 |
8.71e-09 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 58.26 E-value: 8.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 182 LSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISD-NMIEVRKDLGFCPQHDLLFDDLTLSEHL--- 257
Cdd:PRK10575 30 LSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESwSSKAFARKVAYLPQQLPAAEGMTVRELVaig 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 258 -FFYCMVKGIPQNINCEEIDRMLSAFNLQENYHTLSGSASGGVRRKLSIVLALMAGSKVVILDEPSSGMDPVSRRATWDI 336
Cdd:PRK10575 110 rYPWHGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLAL 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 525313703 337 LQHYKHNR--TILLTTHYMDEADVLGDRVAIMVRGTLHCCGS------SVFLKQIYG 385
Cdd:PRK10575 190 VHRLSQERglTVIAVLHDINMAARYCDYLVALRGGEMIAQGTpaelmrGETLEQIYG 246
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
161-371 |
9.17e-09 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 58.06 E-value: 9.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 161 EAGIHIMHLHKEFKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNI-----SDNMIEV- 234
Cdd:PRK10619 3 ENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlvrdKDGQLKVa 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 235 --------RKDLGFCPQHDLLFDDLTLSEHLFFY-CMVKGIPQNINCEEIDRMLSAFNLQENYH-TLSGSASGGVRRKLS 304
Cdd:PRK10619 83 dknqlrllRTRLTMVFQHFNLWSHMTVLENVMEApIQVLGLSKQEARERAVKYLAKVGIDERAQgKYPVHLSGGQQQRVS 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 525313703 305 IVLALMAGSKVVILDEPSSGMDPVSRRATWDILQHY-KHNRTILLTTHYMDEADVLGDRVAIMVRGTL 371
Cdd:PRK10619 163 IARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLaEEGKTMVVVTHEMGFARHVSSHVIFLHQGKI 230
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1019-1193 |
9.70e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 56.88 E-value: 9.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1019 VKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTRTPRKIRSRIGYCPQTESVLNHMTGRESlV 1098
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGHRSGINPYLTLREN-C 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1099 MYARLWGVLEQDINEYVEAFlhsvHLEPIADQFIHTYSAGSKRRLSTAIALMGKSSVVFLDEPSIGMDPVAQHLLWETIT 1178
Cdd:PRK13540 96 LYDIHFSPGAVGITELCRLF----SLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQ 171
|
170
....*....|....*
gi 525313703 1179 WICKTGKAIIITSHR 1193
Cdd:PRK13540 172 EHRAKGGAVLLTSHQ 186
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
172-356 |
1.12e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 58.17 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 172 EFKnkpAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISD---------------------- 229
Cdd:PRK13651 19 ELK---ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNkkktkekekvleklviqktrfk 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 230 ---NMIEVRKDLGFCPQHD--LLFDDlTLSEHLFFYCMVKGIPQNINCEEIDRMLSAFNLQENYhtLSGSA---SGGVRR 301
Cdd:PRK13651 96 kikKIKEIRRRVGVVFQFAeyQLFEQ-TIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDESY--LQRSPfelSGGQKR 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 525313703 302 KLSIVLALMAGSKVVILDEPSSGMDPVSRRATWDILQH-YKHNRTILLTTHYMDEA 356
Cdd:PRK13651 173 RVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNlNKQGKTIILVTHDLDNV 228
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1017-1221 |
1.19e-08 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 57.43 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1017 KAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGiafidgnSVTRTPrkiRSRIGYCPQTESVLNHMTGRES 1096
Cdd:PRK09544 18 RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEG-------VIKRNG---KLRIGYVPQKLYLDTTLPLTVN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1097 LVMYARLwGVLEQDIneyvEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIALMGKSSVVFLDEPSIGMDPVAQHLLWET 1176
Cdd:PRK09544 88 RFLRLRP-GTKKEDI----LPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 525313703 1177 ITWICKT-GKAIIITSHRM-----EECEALCtrlaimVKGRFTCLGTPQHV 1221
Cdd:PRK09544 163 IDQLRRElDCAVLMVSHDLhlvmaKTDEVLC------LNHHICCSGTPEVV 207
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1016-1225 |
1.29e-08 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 59.05 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1016 VKAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETI--TSG-IAFidgnSVTRTPR----KIRSRIGY-CPQTESV 1087
Cdd:TIGR03269 13 KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYepTSGrIIY----HVALCEKcgyvERPSKVGEpCPVCGGT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1088 LNHMT--------------GRESLVMYAR---LWG---VLEQDINEYVEA-------------FLHSVHLEPIADQFIHT 1134
Cdd:TIGR03269 89 LEPEEvdfwnlsdklrrriRKRIAIMLQRtfaLYGddtVLDNVLEALEEIgyegkeavgravdLIEMVQLSHRITHIARD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1135 YSAGSKRRLSTAIALMGKSSVVFLDEPSIGMDPVAQHLLWETITWICK-TGKAIIITSHRMEECEALCTRLAIMVKGRFT 1213
Cdd:TIGR03269 169 LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKaSGISMVLTSHWPEVIEDLSDKAIWLENGEIK 248
|
250
....*....|..
gi 525313703 1214 CLGTPQHVRKRF 1225
Cdd:TIGR03269 249 EEGTPDEVVAVF 260
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
177-351 |
1.37e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 56.78 E-value: 1.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 177 PAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISDNmiEVRKDLGFCPQHDLLFDDLTLSEH 256
Cdd:PRK13543 25 PVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRG--DRSRFMAYLGHLPGLKADLSTLEN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 257 LFFYCMVKG-----IPQNinceeidrMLSAFNLQENYHTLSGSASGGVRRKLSIVLALMAGSKVVILDEPSSGMDP---- 327
Cdd:PRK13543 103 LHFLCGLHGrrakqMPGS--------ALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLegit 174
|
170 180
....*....|....*....|....*
gi 525313703 328 -VSRRatwdILQHYKHNRTILLTTH 351
Cdd:PRK13543 175 lVNRM----ISAHLRGGGAALVTTH 195
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
166-388 |
1.43e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 57.34 E-value: 1.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 166 IMHLHKEFKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGR--FAATRGEAYINGYNISDNMIEVRKDLG---- 239
Cdd:CHL00131 10 IKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLEPEERAHLGifla 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 240 FcpQH----------DLL---------FDDLTLSEHLFFYCMVKGIPQNINceeidrMLSAF---NLQENYhtlsgsaSG 297
Cdd:CHL00131 90 F--QYpieipgvsnaDFLrlaynskrkFQGLPELDPLEFLEIINEKLKLVG------MDPSFlsrNVNEGF-------SG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 298 GVRRKLSIVLALMAGSKVVILDEPSSGMDpvsrratWDILQHYKH--------NRTILLTTHYMDEAD-VLGDRVAIMVR 368
Cdd:CHL00131 155 GEKKRNEILQMALLDSELAILDETDSGLD-------IDALKIIAEginklmtsENSIILITHYQRLLDyIKPDYVHVMQN 227
|
250 260
....*....|....*....|
gi 525313703 369 GTLHCCGSSVFLKQIYGAGY 388
Cdd:CHL00131 228 GKIIKTGDAELAKELEKKGY 247
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
998-1211 |
1.70e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 58.79 E-value: 1.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 998 NTPLL-LNEVTKIYfkcPVVKAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTG--EETITSGIAFIDG-----NSVTR 1069
Cdd:PRK13549 2 MEYLLeMKNITKTF---GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGvyPHGTYEGEIIFEGeelqaSNIRD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1070 TPRK----IRSRIGYCPQTeSVL-NHMTGRESL--------VMYARLWGVLEQ---DINEYveaflhsvhlEPIADqfih 1133
Cdd:PRK13549 79 TERAgiaiIHQELALVKEL-SVLeNIFLGNEITpggimdydAMYLRAQKLLAQlklDINPA----------TPVGN---- 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 525313703 1134 tYSAGSKRRLSTAIALMGKSSVVFLDEPSIGMDPVAQHLLWETITWICKTGKAIIITSHRMEECEALCTRLAIMVKGR 1211
Cdd:PRK13549 144 -LGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
189-351 |
2.06e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 59.09 E-value: 2.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 189 GQVTVLLGHNGAGKTTTLSVLTGRFAA--TRGEAYINGYniSDNMIEVRKDLGFCPQHDLLFDDLTLSEHLFFYCMVKgI 266
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLMDVLAGRKTGgyIEGDIRISGF--PKKQETFARISGYCEQNDIHSPQVTVRESLIYSAFLR-L 982
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 267 PQNINCEE----IDRMLSAF---NLQENYHTLSG--SASGGVRRKLSIVLALMAGSKVVILDEPSSGMDPvsrRATWDIL 337
Cdd:PLN03140 983 PKEVSKEEkmmfVDEVMELVeldNLKDAIVGLPGvtGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDA---RAAAIVM 1059
|
170
....*....|....*...
gi 525313703 338 QHYKHN----RTILLTTH 351
Cdd:PLN03140 1060 RTVRNTvdtgRTVVCTIH 1077
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
162-366 |
2.63e-08 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 57.73 E-value: 2.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 162 AGIHIMHLHKEFKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISDnMIEVRKDLGFC 241
Cdd:PRK11000 2 ASVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMND-VPPAERGVGMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 242 PQHDLLFDDLTLSEHLFFYCMVKGIPQNinceEIDRMLS--AFNLQENyHTLS---GSASGGVRRKLSIVLALMAGSKVV 316
Cdd:PRK11000 81 FQSYALYPHLSVAENMSFGLKLAGAKKE----EINQRVNqvAEVLQLA-HLLDrkpKALSGGQRQRVAIGRTLVAEPSVF 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 525313703 317 ILDEPSSGMDP---VSRRATWDILqHYKHNRTILLTTHYMDEADVLGDRVAIM 366
Cdd:PRK11000 156 LLDEPLSNLDAalrVQMRIEISRL-HKRLGRTMIYVTHDQVEAMTLADKIVVL 207
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1017-1210 |
3.43e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 55.94 E-value: 3.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1017 KAVKNISLVVKKSECFGLLGLNGAGKTTTFKM------LTGEETITSGIAFiDGNSVTrTPR----KIRSRIGYCPQTES 1086
Cdd:PRK14239 19 KALNSVSLDFYPNEITALIGPSGSGKSTLLRSinrmndLNPEVTITGSIVY-NGHNIY-SPRtdtvDLRKEIGMVFQQPN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1087 VLNhMTGRESLVMYARLWGVLEQDI-NEYVEAFLHSVHL-EPIADQfIHT----YSAGSKRRLSTAIALMGKSSVVFLDE 1160
Cdd:PRK14239 97 PFP-MSIYENVVYGLRLKGIKDKQVlDEAVEKSLKGASIwDEVKDR-LHDsalgLSGGQQQRVCIARVLATSPKIILLDE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 525313703 1161 PSIGMDPVAQHLLWETITWIcKTGKAIIITSHRMEECEALCTRLAIMVKG 1210
Cdd:PRK14239 175 PTSALDPISAGKIEETLLGL-KDDYTMLLVTRSMQQASRISDRTGFFLDG 223
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
173-371 |
3.47e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 56.26 E-value: 3.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 173 FKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTT---TLSVLTGRFAATR--GEAYINGYNISD--NMIEVRKDLGFCPQHD 245
Cdd:PRK14271 31 FAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTflrTLNRMNDKVSGYRysGDVLLGGRSIFNyrDVLEFRRRVGMLFQRP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 246 LLFDDLTLSEHLFFYCMVKGIPQNINCEEIDRMLSAFNLQENYHT-LSGSA---SGGVRRKLSIVLALMAGSKVVILDEP 321
Cdd:PRK14271 111 NPFPMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDrLSDSPfrlSGGQQQLLCLARTLAVNPEVLLLDEP 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 525313703 322 SSGMDPVSRRATWDILQHYKHNRTILLTTHYMDEADVLGDRVAIMVRGTL 371
Cdd:PRK14271 191 TSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARISDRAALFFDGRL 240
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
1036-1192 |
3.91e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 55.24 E-value: 3.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1036 GLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTRTPRkirSR-IGYCPQTESVLNHMTGRESLVMYARLWGVLEQDINEY 1114
Cdd:PRK13543 44 GDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDR---SRfMAYLGHLPGLKADLSTLENLHFLCGLHGRRAKQMPGS 120
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 525313703 1115 VEAFlhsVHLEPIADQFIHTYSAGSKRRLSTAIALMGKSSVVFLDEPSIGMDPVAQHLLWETITWICKTGKAIIITSH 1192
Cdd:PRK13543 121 ALAI---VGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMISAHLRGGGAALVTTH 195
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1020-1213 |
4.05e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 57.37 E-value: 4.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1020 KNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTRTPRKIRSRIG--YCPQ-------------- 1083
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGlvYLPEdrqssglyldapla 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1084 --TESVLNHM------TGRESLVM--YARLWGVleqdineyveAFLHsvhlepiADQFIHTYSAGSKRRLSTAIALMGKS 1153
Cdd:PRK15439 360 wnVCALTHNRrgfwikPARENAVLerYRRALNI----------KFNH-------AEQAARTLSGGNQQKVLIAKCLEASP 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1154 SVVFLDEPSIGMDPVAQHLLWETITWICKTGKAIIITSHRMEECEALCTRLAIMVKGRFT 1213
Cdd:PRK15439 423 QLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEIS 482
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1019-1198 |
4.23e-08 |
|
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: 58.00 E-value: 4.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1019 VKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETiTSGIAFIDG---NSVTRtpRKIRSRIGYCPQTESVLNHmTGRE 1095
Cdd:TIGR01271 1235 LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGvswNSVTL--QTWRKAFGVIPQKVFIFSG-TFRK 1310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1096 SLVMYAR-----LWGVLEQ-DINEYVEAFLHSVHLEPIADQFIhtYSAGSKRRLSTAIALMGKSSVVFLDEPSIGMDPVA 1169
Cdd:TIGR01271 1311 NLDPYEQwsdeeIWKVAEEvGLKSVIEQFPDKLDFVLVDGGYV--LSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVT 1388
|
170 180 190
....*....|....*....|....*....|....*
gi 525313703 1170 QHLLWETITWI---CktgkAIIITSHRME---ECE 1198
Cdd:TIGR01271 1389 LQIIRKTLKQSfsnC----TVILSEHRVEallECQ 1419
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1005-1210 |
4.88e-08 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 55.48 E-value: 4.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1005 EVTKIYFKCPVVKAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTrTPRKIRsriGYCPQT 1084
Cdd:PRK11248 3 QISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVE-GPGAER---GVVFQN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1085 ESVLNHMTGRESLVMYARLWGVLEQDINEYVEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIALMGKSSVVFLDEPSIG 1164
Cdd:PRK11248 79 EGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 525313703 1165 MDPVA----QHLL---WEtitwicKTGKAIIITSHRMEECEALCTRLAIMVKG 1210
Cdd:PRK11248 159 LDAFTreqmQTLLlklWQ------ETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
175-357 |
5.23e-08 |
|
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: 55.03 E-value: 5.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 175 NKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISDNMIEV-----RKDLGFCPQHDLLFd 249
Cdd:cd03290 13 GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEAtrsrnRYSVAYAAQKPWLL- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 250 DLTLSEHLFFycmvkGIPqnINCEEIDRMLSAFNLQENYHTLSG-----------SASGGVRRKLSIVLALMAGSKVVIL 318
Cdd:cd03290 92 NATVEENITF-----GSP--FNKQRYKAVTDACSLQPDIDLLPFgdqteigergiNLSGGQRQRICVARALYQNTNIVFL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 525313703 319 DEPSSGM-----DPVSRRATWDILQHYKhnRTILLTTH---YMDEAD 357
Cdd:cd03290 165 DDPFSALdihlsDHLMQEGILKFLQDDK--RTLVLVTHklqYLPHAD 209
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1026-1166 |
5.39e-08 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 57.10 E-value: 5.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1026 VKKSECFGLLGLNGAGKTTTFKMLTGEETITSGiaFIDGNsvtrtprkirSRIGYCPQtesvlnhmtgreslvmYarlwg 1105
Cdd:COG1245 363 IREGEVLGIVGPNGIGKTTFAKILAGVLKPDEG--EVDED----------LKISYKPQ----------------Y----- 409
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 525313703 1106 vLEQDINEYVEAFLHSVH------------------LEPIADQFIHTYSAGSKRRLSTAIALMGKSSVVFLDEPSIGMD 1166
Cdd:COG1245 410 -ISPDYDGTVEEFLRSANtddfgssyykteiikplgLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 487
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1017-1235 |
6.47e-08 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 57.14 E-value: 6.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1017 KAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTRTPRK-IRSRIGYCPQTESVLNHmTGRE 1095
Cdd:PRK11160 354 PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAaLRQAISVVSQRVHLFSA-TLRD 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1096 SLVMYA------RLWGVLEQdineyveaflhsVHLEPIADQF--IHTY--------SAGSKRRLSTAIALMGKSSVVFLD 1159
Cdd:PRK11160 433 NLLLAApnasdeALIEVLQQ------------VGLEKLLEDDkgLNAWlgeggrqlSGGEQRRLGIARALLHDAPLLLLD 500
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 525313703 1160 EPSIGMDPVAQHLLWETITWICKtGKAIIITSHR---MEECEALCtrlaIMVKGRFTCLGTPQHVRKRFGHVYTLTVRI 1235
Cdd:PRK11160 501 EPTEGLDAETERQILELLAEHAQ-NKTVLMITHRltgLEQFDRIC----VMDNGQIIEQGTHQELLAQQGRYYQLKQRL 574
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
169-369 |
9.30e-08 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 54.93 E-value: 9.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 169 LHKEFKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAyinGYNISDN-------MIE------VR 235
Cdd:PRK11701 12 LTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEV---HYRMRDGqlrdlyaLSEaerrrlLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 236 KDLGFCPQHDLlfDDLTLS--------EHLffycMVKG------IPQ---------NINCEEIDRMLSAFnlqenyhtls 292
Cdd:PRK11701 89 TEWGFVHQHPR--DGLRMQvsaggnigERL----MAVGarhygdIRAtagdwlervEIDAARIDDLPTTF---------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 293 gsaSGGVRRKLSIVLALMAGSKVVILDEPSSGMDpVSRRATW-DILQHYKH--NRTILLTTHYMDEADVLGDRVAIMVRG 369
Cdd:PRK11701 153 ---SGGMQQRLQIARNLVTHPRLVFMDEPTGGLD-VSVQARLlDLLRGLVRelGLAVVIVTHDLAVARLLAHRLLVMKQG 228
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
176-367 |
1.04e-07 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 54.19 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 176 KPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYIngyNISDNMIEvrkdlgfcpqhdllfDDLTLSE 255
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCV---DVPDNQFG---------------REASLID 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 256 HLffycmvkGIPQNINceEIDRMLSAFNLQEN------YHTLsgsaSGGVRRKLSIVLALMAGSKVVILDEPSSGMDPVS 329
Cdd:COG2401 105 AI-------GRKGDFK--DAVELLNAVGLSDAvlwlrrFKEL----STGQKFRFRLALLLAERPKLLVIDEFCSHLDRQT 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 525313703 330 RRATWDILQHY--KHNRTILLTTHYMDEADVLGDRVAIMV 367
Cdd:COG2401 172 AKRVARNLQKLarRAGITLVVATHHYDVIDDLQPDLLIFV 211
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
176-371 |
1.23e-07 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 55.79 E-value: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 176 KPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYING--YNISDNMIEVRKDLGFCP---QHDLLFDD 250
Cdd:COG1129 265 GGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGkpVRIRSPRDAIRAGIAYVPedrKGEGLVLD 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 251 LTLSE-----HLFFYCMVKGIPQNINCEEIDRMLSAFNLQ-ENYHTLSGSASGGVRRKlsIVLA--LMAGSKVVILDEPS 322
Cdd:COG1129 345 LSIREnitlaSLDRLSRGGLLDRRRERALAEEYIKRLRIKtPSPEQPVGNLSGGNQQK--VVLAkwLATDPKVLILDEPT 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 525313703 323 SGMDPVSRRATWDILQHYKHN-RTILLTTHYMDEadVLG--DRVAIMVRGTL 371
Cdd:COG1129 423 RGIDVGAKAEIYRLIRELAAEgKAVIVISSELPE--LLGlsDRILVMREGRI 472
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1020-1161 |
1.46e-07 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 55.42 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1020 KNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTRTPRKIRSrIGYCPQTESVLNHMTGRESLVM 1099
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERG-VGMVFQSYALYPHLSVAENMSF 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 525313703 1100 YARLWGVLEQDINEYVEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIALMGKSSVVFLDEP 1161
Cdd:PRK11000 99 GLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEP 160
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
189-351 |
1.51e-07 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 53.63 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 189 GQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISDNMIEVR-----KDLGFCPQHDLLFDDLTLSEHLFFYCMV 263
Cdd:PRK10584 36 GETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARaklraKHVGFVFQSFMLIPTLNALENVELPALL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 264 KGIPQNINCEEIDRMLSAFNLQENYHTLSGSASGGVRRKLSIVLALMAGSKVVILDEPSSGMDPVSRRATWDIL--QHYK 341
Cdd:PRK10584 116 RGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLfsLNRE 195
|
170
....*....|
gi 525313703 342 HNRTILLTTH 351
Cdd:PRK10584 196 HGTTLILVTH 205
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
172-351 |
2.22e-07 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 53.58 E-value: 2.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 172 EFKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGeayingynisdnMIEVRKDL--GFCPQHdlLFD 249
Cdd:PRK09544 13 SFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEG------------VIKRNGKLriGYVPQK--LYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 250 DLTLSEHLFFYCMVK-GIPQNINCEEIDRMLSAFNLQENYHTLSGsasGGVRRKLsIVLALMAGSKVVILDEPSSGMDPV 328
Cdd:PRK09544 79 DTTLPLTVNRFLRLRpGTKKEDILPALKRVQAGHLIDAPMQKLSG---GETQRVL-LARALLNRPQLLVLDEPTQGVDVN 154
|
170 180
....*....|....*....|....*
gi 525313703 329 SRRATWDILQHYKH--NRTILLTTH 351
Cdd:PRK09544 155 GQVALYDLIDQLRRelDCAVLMVSH 179
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
155-357 |
2.51e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 55.37 E-value: 2.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 155 AEPPNLEAGIHIMHLHKEF------KNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAatrgeayingyNIS 228
Cdd:PLN03232 603 AQNPPLQPGAPAISIKNGYfswdskTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELS-----------HAE 671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 229 DNMIEVRKDLGFCPQHDLLFdDLTLSEHLFFycmvkgiPQNINCEEIDRMLSAFNLQENYHTLSG-----------SASG 297
Cdd:PLN03232 672 TSSVVIRGSVAYVPQVSWIF-NATVRENILF-------GSDFESERYWRAIDVTALQHDLDLLPGrdlteigergvNISG 743
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 525313703 298 GVRRKLSIVLALMAGSKVVILDEPSSGMDP-VSRRATWDILQHYKHNRTILLTT---HYMDEAD 357
Cdd:PLN03232 744 GQKQRVSMARAVYSNSDIYIFDDPLSALDAhVAHQVFDSCMKDELKGKTRVLVTnqlHFLPLMD 807
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
176-372 |
2.84e-07 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 52.95 E-value: 2.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 176 KPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNIS----DNMIEVRKDLGFCPQHDLLFDDL 251
Cdd:PRK10908 15 RQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITrlknREVPFLRRQIGMIFQDHHLLMDR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 252 TLSEHLFFYCMVKGipqnINCEEIDRMLSA----FNLQENYHTLSGSASGGVRRKLSIVLALMAGSKVVILDEPSSGMDP 327
Cdd:PRK10908 95 TVYDNVAIPLIIAG----ASGDDIRRRVSAaldkVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 525313703 328 VsrrATWDILQHYKH-NR---TILLTTHYMDEADVLGDRVAIMVRGTLH 372
Cdd:PRK10908 171 A---LSEGILRLFEEfNRvgvTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1019-1198 |
2.94e-07 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 53.70 E-value: 2.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1019 VKNISLVVKKSECFGLLGLNGAGKTTTF----KMLTGEETITsgiafIDGNSVTRTP-RKIRSRIGYCPQTESVLNHmTG 1093
Cdd:cd03289 20 LENISFSISPGQRVGLLGRTGSGKSTLLsaflRLLNTEGDIQ-----IDGVSWNSVPlQKWRKAFGVIPQKVFIFSG-TF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1094 RESLVMYAR-----LWGVLEQdineyveaflhsVHLEPIADQFI-----------HTYSAGSKRRLSTAIALMGKSSVVF 1157
Cdd:cd03289 94 RKNLDPYGKwsdeeIWKVAEE------------VGLKSVIEQFPgqldfvlvdggCVLSHGHKQLMCLARSVLSKAKILL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 525313703 1158 LDEPSIGMDPVAQHLLWETITWiCKTGKAIIITSHRME---ECE 1198
Cdd:cd03289 162 LDEPSAHLDPITYQVIRKTLKQ-AFADCTVILSEHRIEamlECQ 204
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1017-1221 |
3.16e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 53.49 E-value: 3.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1017 KAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTG-----EETITSGIAFIDGNSVTRTPRKIRSRIGYCPQ-TESVLNH 1090
Cdd:PRK13634 21 RALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGllqptSGTVTIGERVITAGKKNKKLKPLRKKVGIVFQfPEHQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1091 MTGRESLVMYARLWGVLEQDINEYVEAFLHSVHL-EPIADQFIHTYSAGSKRRLSTAIALMGKSSVVFLDEPSIGMDPVA 1169
Cdd:PRK13634 101 ETVEKDICFGPMNFGVSEEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKG 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 525313703 1170 QHLLWETITWICKT-GKAIIITSHRMEECEALCTRLAIMVKGRFTCLGTPQHV 1221
Cdd:PRK13634 181 RKEMMEMFYKLHKEkGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREI 233
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1022-1166 |
3.21e-07 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 52.86 E-value: 3.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1022 ISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTRTPRKIRSR-----IGYCPQTESVLNHMTGRES 1096
Cdd:PRK10584 29 VELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKlrakhVGFVFQSFMLIPTLNALEN 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1097 LVMYARLWGVLEQDINEYVEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIALMGKSSVVFLDEPSIGMD 1166
Cdd:PRK10584 109 VELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLD 178
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
178-359 |
3.40e-07 |
|
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: 54.42 E-value: 3.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 178 AVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISDNMIEVRKDLgFCPqhdlLFDDLTLSEHL 257
Cdd:COG4615 347 TLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQL-FSA----VFSDFHLFDRL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 258 FfycmvkGIPQNINCEEIDRMLSAFNLQE-------NYHTLSGSAsgGVRRKLSIVLALMAGSKVVILDEPSSGMDPVSR 330
Cdd:COG4615 422 L------GLDGEADPARARELLERLELDHkvsvedgRFSTTDLSQ--GQRKRLALLVALLEDRPILVFDEWAADQDPEFR 493
|
170 180 190
....*....|....*....|....*....|....*.
gi 525313703 331 RatW---DILQHYK-HNRTILLTTH---YMDEADVL 359
Cdd:COG4615 494 R--VfytELLPELKaRGKTVIAISHddrYFDLADRV 527
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1003-1223 |
4.64e-07 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 52.85 E-value: 4.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1003 LNEVTKIYFKCPVVKAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTRTPR----KIRSRI 1078
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRsrlyTVRKRM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1079 GYCPQTESVLNHMTGRESLVMYARLWGVL-EQDINEYVEAFLHSVHLEPIADQFIHTYSAGSKRR--LSTAIALmgKSSV 1155
Cdd:PRK11831 87 SMLFQSGALFTDMNVFDNVAYPLREHTQLpAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRaaLARAIAL--EPDL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 525313703 1156 VFLDEPSIGMDPVAQHLLWETITWICKT-GKAIIITSHRMEECEALCTRLAIMVKGRFTCLGTPQHVRK 1223
Cdd:PRK11831 165 IMFDEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQA 233
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
173-361 |
4.74e-07 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 50.82 E-value: 4.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 173 FKNKPAVNNLSLNiyEGQVTVLLGHNGAGKTTTLS----VLTGRFAATRGEAYIngynisdnmievrkdlgfcpqhdllf 248
Cdd:cd03227 7 FPSYFVPNDVTFG--EGSLTIITGPNGSGKSTILDaiglALGGAQSATRRRSGV-------------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 249 ddltlsehlffycmvkGIPQNINCEEIDRMLSafnlqenYHTLSGSASggVRRKLSIVLALMA--GSKVVILDEPSSGMD 326
Cdd:cd03227 59 ----------------KAGCIVAAVSAELIFT-------RLQLSGGEK--ELSALALILALASlkPRPLYILDEIDRGLD 113
|
170 180 190
....*....|....*....|....*....|....*....
gi 525313703 327 PVSRRA-TWDILQHYKHNRTILLTTHY---MDEADVLGD 361
Cdd:cd03227 114 PRDGQAlAEAILEHLVKGAQVIVITHLpelAELADKLIH 152
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
168-224 |
5.37e-07 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 52.91 E-value: 5.37e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 525313703 168 HLHKEFKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRF--------AATRGEAYING 224
Cdd:PRK13547 6 HLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLtgggaprgARVTGDVTLNG 70
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1010-1221 |
5.37e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 52.79 E-value: 5.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1010 YFKCPVVKAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVT-RTPRKIRSRIGYCPQTESvl 1088
Cdd:PRK13642 14 YEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTaENVWNLRRKIGMVFQNPD-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1089 NHMTG---RESLVMYARLWGVLEQDINEYVEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIALMGKSSVVFLDEPSIGM 1165
Cdd:PRK13642 92 NQFVGatvEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSML 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 525313703 1166 DPVAQHLLWETITWIC-KTGKAIIITSHRMEECeALCTRLAIMVKGRFTCLGTPQHV 1221
Cdd:PRK13642 172 DPTGRQEIMRVIHEIKeKYQLTVLSITHDLDEA-ASSDRILVMKAGEIIKEAAPSEL 227
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1014-1208 |
5.43e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 54.04 E-value: 5.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1014 PVVKAVKNISLVV-----KKSECFGLLGLNGAGKTTTFKMLTGEETITSGiafidgnSVTRTPrkirsRIGYCPQtesvl 1088
Cdd:PRK13409 345 DLTKKLGDFSLEVeggeiYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEG-------EVDPEL-----KISYKPQ----- 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1089 nhmtgreslvmYarlwgvLEQDINEYVEAFLHSV-----------------HLEPIADQFIHTYSAGSKRRLSTAIALMG 1151
Cdd:PRK13409 408 -----------Y------IKPDYDGTVEDLLRSItddlgssyykseiikplQLERLLDKNVKDLSGGELQRVAIAACLSR 470
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 525313703 1152 KSSVVFLDEPSIGMDpVAQHLlwetitwicKTGKAIiitSHRMEECEAlctrlAIMV 1208
Cdd:PRK13409 471 DADLYLLDEPSAHLD-VEQRL---------AVAKAI---RRIAEEREA-----TALV 509
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1033-1221 |
6.11e-07 |
|
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: 53.18 E-value: 6.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1033 GLLGLNGAGKTTTFKMLTGEETITSG-IAF-----IDGNSVTRTPRKIRsRIGYCPQTESVLNHMTGRESLvMYARLWGV 1106
Cdd:COG4148 29 ALFGPSGSGKTTLLRAIAGLERPDSGrIRLggevlQDSARGIFLPPHRR-RIGYVFQEARLFPHLSVRGNL-LYGRKRAP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1107 LEQ---DINEYVEAFlhsvHLEPIADQFIHTYSAGSKRRLSTAIALMGKSSVVFLDEPSIGMDP------------VAQH 1171
Cdd:COG4148 107 RAErriSFDEVVELL----GIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLarkaeilpylerLRDE 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 525313703 1172 LlwetitwicktGKAIIITSHRMEECEALCTRLAIMVKGRFTCLGTPQHV 1221
Cdd:COG4148 183 L-----------DIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEV 221
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
997-1166 |
7.79e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 52.66 E-value: 7.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 997 QNTPLLL-NEVTKIY------FKCP-VVKAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVT 1068
Cdd:PRK11308 1 SQQPLLQaIDLKKHYpvkrglFKPErLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1069 RTPR----KIRSRIgycpqtESVLNHMTGreSLVMYARLWGVLEQ--DIN---------EYVEAFLHSVHLEP-IADQFI 1132
Cdd:PRK11308 81 KADPeaqkLLRQKI------QIVFQNPYG--SLNPRKKVGQILEEplLINtslsaaerrEKALAMMAKVGLRPeHYDRYP 152
|
170 180 190
....*....|....*....|....*....|....
gi 525313703 1133 HTYSAGSKRRLSTAIALMGKSSVVFLDEPSIGMD 1166
Cdd:PRK11308 153 HMFSGGQRQRIAIARALMLDPDVVVADEPVSALD 186
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
166-395 |
7.84e-07 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 52.10 E-value: 7.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 166 IMHLHKEFKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGR--FAATRGEAYINGYNISDNMIEVRKDLGFCPQ 243
Cdd:PRK09580 4 IKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSPEDRAGEGIFMA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 244 HDLLFDDLTLSEHLFFYCMVKGIPQNINCEEIDRM---------LSAFNLQENYHTLSGSA--SGGVRRKLSIVLALMAG 312
Cdd:PRK09580 84 FQYPVEIPGVSNQFFLQTALNAVRSYRGQEPLDRFdfqdlmeekIALLKMPEDLLTRSVNVgfSGGEKKRNDILQMAVLE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 313 SKVVILDEPSSGMDPVSRRATWDILQHYKH-NRTILLTTHYMDEAD-VLGDRVAIMVRGTLHCCGSSVFLKQIYGAGYHI 390
Cdd:PRK09580 164 PELCILDESDSGLDIDALKIVADGVNSLRDgKRSFIIVTHYQRILDyIKPDYVHVLYQGRIVKSGDFTLVKQLEEQGYGW 243
|
....*
gi 525313703 391 VMEKQ 395
Cdd:PRK09580 244 LTEQQ 248
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
178-371 |
9.74e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 53.05 E-value: 9.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 178 AVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNIS-DNMIEVRKdlgfcpqhdlLFDDLTLSEH 256
Cdd:PRK10522 338 SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTaEQPEDYRK----------LFSAVFTDFH 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 257 LFFYcMVKGIPQNINCEEIDRMLSAFNLQ-----ENYHTLSGSASGGVRRKLSIVLALMAGSKVVILDEPSSGMDPVSRR 331
Cdd:PRK10522 408 LFDQ-LLGPEGKPANPALVEKWLERLKMAhklelEDGRISNLKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRR 486
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 525313703 332 ATWDIL--QHYKHNRTILLTTH---YMDEAdvlgDRVAIMVRGTL 371
Cdd:PRK10522 487 EFYQVLlpLLQEMGKTIFAISHddhYFIHA----DRLLEMRNGQL 527
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
173-326 |
1.11e-06 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 51.53 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 173 FKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISDNMI-EVRKDLGFCPQHDLLFDDL 251
Cdd:PRK10253 17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASkEVARRIGLLAQNATTPGDI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 252 TLSE--------HLFFYCMVKGIPQnincEEIDRMLSAFNLQENYHTLSGSASGGVRRKLSIVLALMAGSKVVILDEPSS 323
Cdd:PRK10253 97 TVQElvargrypHQPLFTRWRKEDE----EAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTT 172
|
...
gi 525313703 324 GMD 326
Cdd:PRK10253 173 WLD 175
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
179-350 |
1.38e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 52.86 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 179 VNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEayingynisdnmIEVRK--DLGFCPQHDLLF--DDLTLS 254
Cdd:PRK10636 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGE------------IGLAKgiKLGYFAQHQLEFlrADESPL 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 255 EHLffycmVKGIPQNINcEEIDRMLSAFNLQENYHT-LSGSASGGVRRKLsiVLALMAGSK--VVILDEPSSGMDPVSRR 331
Cdd:PRK10636 396 QHL-----ARLAPQELE-QKLRDYLGGFGFQGDKVTeETRRFSGGEKARL--VLALIVWQRpnLLLLDEPTNHLDLDMRQ 467
|
170 180
....*....|....*....|....*.
gi 525313703 332 ATWDILQHYK-------HNRTILLTT 350
Cdd:PRK10636 468 ALTEALIDFEgalvvvsHDRHLLRST 493
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
177-326 |
2.14e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 52.67 E-value: 2.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 177 PAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISD-NMIEVRKDLGFCPQHDLLFDDLT--- 252
Cdd:PLN03232 1250 PVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKfGLTDLRRVLSIIPQSPVLFSGTVrfn 1329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 253 ---LSEH----LFfycmvKGIPQNINCEEIDRmlSAFNLQENYHTLSGSASGGVRRKLSIVLALMAGSKVVILDEPSSGM 325
Cdd:PLN03232 1330 idpFSEHndadLW-----EALERAHIKDVIDR--NPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASV 1402
|
.
gi 525313703 326 D 326
Cdd:PLN03232 1403 D 1403
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1016-1166 |
2.15e-06 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 50.94 E-value: 2.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1016 VKAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTRTPRKIRS-RIGYCPQTESvlNHMTGR 1094
Cdd:PRK15112 26 VEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSqRIRMIFQDPS--TSLNPR 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 525313703 1095 ES----LVMYARLWGVLE-QDINEYVEAFLHSVHLEPI-ADQFIHTYSAGSKRRLSTAIALMGKSSVVFLDEPSIGMD 1166
Cdd:PRK15112 104 QRisqiLDFPLRLNTDLEpEQREKQIIETLRQVGLLPDhASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLD 181
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
999-1192 |
2.32e-06 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 52.03 E-value: 2.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 999 TPLL-LNEVTKIYfkcP----VVKAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTRT--- 1070
Cdd:PRK10535 2 TALLeLKDIRRSY---PsgeeQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLdad 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1071 --PRKIRSRIGYCPQTESVLNHMTGRESLVMYARLWGVLEQDINEYVEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIA 1148
Cdd:PRK10535 79 alAQLRREHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 525313703 1149 LMGKSSVVFLDEPSIGMDPVAQHLLWETITWICKTGKAIIITSH 1192
Cdd:PRK10535 159 LMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTH 202
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
1022-1234 |
2.37e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 52.29 E-value: 2.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1022 ISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTRTP-RKIRSRIGYCPQTeSVLNHMTGRESLVMY 1100
Cdd:PLN03232 1255 LSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGlTDLRRVLSIIPQS-PVLFSGTVRFNIDPF 1333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1101 -----ARLWGVLEQ-DINEYVEAflHSVHLEPIADQFIHTYSAGSKRRLSTAIALMGKSSVVFLDEPSIGMDPVAQHLLW 1174
Cdd:PLN03232 1334 sehndADLWEALERaHIKDVIDR--NPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQ 1411
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1175 ETITWICKTGKAIIItSHRMEECeALCTRLAIMVKGRFTCLGTPQHVRKRFGHVYTLTVR 1234
Cdd:PLN03232 1412 RTIREEFKSCTMLVI-AHRLNTI-IDCDKILVLSSGQVLEYDSPQELLSRDTSAFFRMVH 1469
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1018-1192 |
2.40e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 51.90 E-value: 2.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1018 AVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVT-RTPRKIRSRIGYCPQTESVLNHMTGRES 1096
Cdd:PRK10522 338 SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTaEQPEDYRKLFSAVFTDFHLFDQLLGPEG 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1097 lvmyarlwgvlEQDINEYVEAFL------HSVHLEpiaDQFIHT--YSAGSKRRLSTAIALMGKSSVVFLDEPSIGMDPV 1168
Cdd:PRK10522 418 -----------KPANPALVEKWLerlkmaHKLELE---DGRISNlkLSKGQKKRLALLLALAEERDILLLDEWAADQDPH 483
|
170 180
....*....|....*....|....*
gi 525313703 1169 AQHLLW-ETITWICKTGKAIIITSH 1192
Cdd:PRK10522 484 FRREFYqVLLPLLQEMGKTIFAISH 508
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
178-369 |
2.67e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 51.78 E-value: 2.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 178 AVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNI---SDNMIE-VRKDLGFCPQ--HDLLFDDL 251
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIdtlSPGKLQaLRRDIQFIFQdpYASLDPRQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 252 TLSEHLFFYCMVKGIPQ-NINCEEIDRMLSAFNLQ-ENYHTLSGSASGGVRRKLSIVLALMAGSKVVILDEPSSGMDPVS 329
Cdd:PRK10261 419 TVGDSIMEPLRVHGLLPgKAAAARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSI 498
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 525313703 330 RRATWDILQHYKHNRTI--LLTTHYMDEADVLGDRVAIMVRG 369
Cdd:PRK10261 499 RGQIINLLLDLQRDFGIayLFISHDMAVVERISHRVAVMYLG 540
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1023-1211 |
2.70e-06 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 49.97 E-value: 2.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1023 SLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTRTPRKIRsrigycP-----QTESVLNHMTGRESL 1097
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRR------PvsmlfQENNLFSHLTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1098 VMyarlwGV-----LEQDINEYVEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIALMGKSSVVFLDEPSIGMDPVAQHL 1172
Cdd:PRK10771 93 GL-----GLnpglkLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQE 167
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 525313703 1173 LWETITWICKTGK-AIIITSHRMEECEALCTRLAIMVKGR 1211
Cdd:PRK10771 168 MLTLVSQVCQERQlTLLMVSHSLEDAARIAPRSLVVADGR 207
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
151-378 |
2.97e-06 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 51.36 E-value: 2.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 151 NCYEAEPPNLEAGI----HIMHLHKEFKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRF-AATRGEAYINGY 225
Cdd:TIGR02633 244 SLYPHEPHEIGDVIlearNLTCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYpGKFEGNVFINGK 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 226 NISDN-----------MI-EVRKDLGFCPQHDLlFDDLTLSEhLFFYCMVKGIPQNINCEEIDRMLSAFNLQENYHTLS- 292
Cdd:TIGR02633 324 PVDIRnpaqairagiaMVpEDRKRHGIVPILGV-GKNITLSV-LKSFCFKMRIDAAAELQIIGSAIQRLKVKTASPFLPi 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 293 GSASGGVRRKLSIVLALMAGSKVVILDEPSSGMDPVSRRATWDIL-QHYKHNRTILLTTHYMDEADVLGDRVAIMVRGTL 371
Cdd:TIGR02633 402 GRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLInQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
....*..
gi 525313703 372 hcCGSSV 378
Cdd:TIGR02633 482 --KGDFV 486
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1017-1213 |
3.02e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 51.33 E-value: 3.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1017 KAVKNISLVVKKSECFGLLGLNGAGKTTtFKM-LTGEE--TITSGIAFIDGNSV-TRT-PRKIRSRIGYCpqTESV---- 1087
Cdd:NF040905 274 KVVDDVSLNVRRGEIVGIAGLMGAGRTE-LAMsVFGRSygRNISGTVFKDGKEVdVSTvSDAIDAGLAYV--TEDRkgyg 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1088 LNHM-TGRESLVMyARL-----WGVLeQDINEYVEA--FLHSVHLE-PIADQFIHTYSAGSKRRLSTAIALMGKSSVVFL 1158
Cdd:NF040905 351 LNLIdDIKRNITL-ANLgkvsrRGVI-DENEEIKVAeeYRKKMNIKtPSVFQKVGNLSGGNQQKVVLSKWLFTDPDVLIL 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 525313703 1159 DEPSIGMDPVAQHLLWETITWICKTGKAIIITSHRMEECEALCTRLAIMVKGRFT 1213
Cdd:NF040905 429 DEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMNEGRIT 483
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1019-1166 |
3.11e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 52.03 E-value: 3.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1019 VKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGE-----ETITSGIAFiDGNSVTRTPRKIRSRIGYCPQTESVLNHMTG 1093
Cdd:TIGR00956 77 LKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNtdgfhIGVEGVITY-DGITPEEIKKHYRGDVVYNAETDVHFPHLTV 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1094 RESLVMYARLW-------GVLEQD----INEYVEAFLHSVHLE--PIADQFIHTYSAGSKRRLSTAIALMGKSSVVFLDE 1160
Cdd:TIGR00956 156 GETLDFAARCKtpqnrpdGVSREEyakhIADVYMATYGLSHTRntKVGNDFVRGVSGGERKRVSIAEASLGGAKIQCWDN 235
|
....*.
gi 525313703 1161 PSIGMD 1166
Cdd:TIGR00956 236 ATRGLD 241
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1002-1230 |
3.66e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 51.39 E-value: 3.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1002 LLNEVTKiyfkcpVVKAVKNISLVVKKSECFGLLGLNGAGKTTTFKML-----TGEETITSGIAFIDGNSVTRTpRKIRS 1076
Cdd:PRK10261 329 LLNRVTR------EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALlrlveSQGGEIIFNGQRIDTLSPGKL-QALRR 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1077 RIGYCPQT--ESVLNHMTGRESLVMYARLWGVLEQD-INEYVEAFLHSVHLEPI-ADQFIHTYSAGSKRRLSTAIALMGK 1152
Cdd:PRK10261 402 DIQFIFQDpyASLDPRQTVGDSIMEPLRVHGLLPGKaAAARVAWLLERVGLLPEhAWRYPHEFSGGQRQRICIARALALN 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 525313703 1153 SSVVFLDEPSIGMD-PVAQHLLWETITWICKTGKAIIITSHRMEECEALCTRLAIMVKGRFTCLGTPQHVRKRFGHVYT 1230
Cdd:PRK10261 482 PKVIIADEAVSALDvSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYT 560
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
167-389 |
4.05e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 51.39 E-value: 4.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 167 MHLHKEFKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNI---SDNMIEVRKDLGFCPQ 243
Cdd:PRK10261 20 IAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLrrrSRQVIELSEQSAAQMR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 244 H------DLLFDDLTLSEHLFFYC---------MVKGIPQNINCEEIDRMLSAFNLQENYHTLS---GSASGGVRRKLSI 305
Cdd:PRK10261 100 HvrgadmAMIFQEPMTSLNPVFTVgeqiaesirLHQGASREEAMVEAKRMLDQVRIPEAQTILSrypHQLSGGMRQRVMI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 306 VLALMAGSKVVILDEPSSGMDpVSRRAtwDILQHYK-----HNRTILLTTHYMDEADVLGDRVAIMVRGTLHCCGSsvfL 380
Cdd:PRK10261 180 AMALSCRPAVLIADEPTTALD-VTIQA--QILQLIKvlqkeMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGS---V 253
|
....*....
gi 525313703 381 KQIYGAGYH 389
Cdd:PRK10261 254 EQIFHAPQH 262
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
175-351 |
6.13e-06 |
|
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: 50.59 E-value: 6.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 175 NKPAVNNLSLNIYEGQVTVLLGHNGAGKTTtLSVLTGRF-AATRGEAYINGYNISD-NMIEVRKDLGFCPQHDLLFDDlT 252
Cdd:COG5265 370 ERPILKGVSFEVPAGKTVAIVGPSGAGKST-LARLLFRFyDVTSGRILIDGQDIRDvTQASLRAAIGIVPQDTVLFND-T 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 253 LsehlfFYcmvkgipqNI-------NCEEIDR-----MLSAF--NLQENYHTLSGSA----SGGVRRKLSIVLALMAGSK 314
Cdd:COG5265 448 I-----AY--------NIaygrpdaSEEEVEAaaraaQIHDFieSLPDGYDTRVGERglklSGGEKQRVAIARTLLKNPP 514
|
170 180 190
....*....|....*....|....*....|....*..
gi 525313703 315 VVILDEPSSGMDPVSRRATWDILQHYKHNRTILLTTH 351
Cdd:COG5265 515 ILIFDEATSALDSRTERAIQAALREVARGRTTLVIAH 551
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1016-1161 |
6.72e-06 |
|
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: 50.45 E-value: 6.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1016 VKAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETiTSGIAFIDGNSVTRTPRK----IRSRIG------Ycpqte 1085
Cdd:COG4172 299 VKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSRRalrpLRRRMQvvfqdpF----- 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1086 SVLN-HMT-GR---ESLVMYARlwGVLEQDINEYVEAFLHSVHLEP-IADQFIHTYSAGSKRRLSTAIALMGKSSVVFLD 1159
Cdd:COG4172 373 GSLSpRMTvGQiiaEGLRVHGP--GLSAAERRARVAEALEEVGLDPaARHRYPHEFSGGQRQRIAIARALILEPKLLVLD 450
|
..
gi 525313703 1160 EP 1161
Cdd:COG4172 451 EP 452
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1005-1196 |
6.77e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 49.26 E-value: 6.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1005 EVTKIYFKCPVVKAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLT------GEETITSGIAFIDGNSVTR--TPRKIRS 1076
Cdd:PRK14258 9 KVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNrmneleSEVRVEGRVEFFNQNIYERrvNLNRLRR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1077 RIGYC-PQTEsvLNHMTGRESLVMYARLWGVLEQ-DINEYVEAFLHSVHLEPIADQFIHT----YSAGSKRRLSTAIALM 1150
Cdd:PRK14258 89 QVSMVhPKPN--LFPMSVYDNVAYGVKIVGWRPKlEIDDIVESALKDADLWDEIKHKIHKsaldLSGGQQQRLCIARALA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 525313703 1151 GKSSVVFLDEPSIGMDPVAQHLLWETI-TWICKTGKAIIITSHRMEE 1196
Cdd:PRK14258 167 VKPKVLLMDEPCFGLDPIASMKVESLIqSLRLRSELTMVIVSHNLHQ 213
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1019-1221 |
6.78e-06 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 49.44 E-value: 6.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1019 VKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGE---------ETITSGIAfIDGNSVTRT-PRKIRSRIGYCPQTESVL 1088
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDltgggaprgARVTGDVT-LNGEPLAAIdAPRLARLRAVLPQAAQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1089 NHMTGRESLVM----YARLWGVLEQDINEYVEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIAL---------MGKSSV 1155
Cdd:PRK13547 96 FAFSAREIVLLgrypHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpphdaAQPPRY 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 525313703 1156 VFLDEPSIGMDPVAQHLLWETITWICKTGK-AIIITSHRMEECEALCTRLAIMVKGRFTCLGTPQHV 1221
Cdd:PRK13547 176 LLLDEPTAALDLAHQHRLLDTVRRLARDWNlGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADV 242
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
1018-1225 |
6.92e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 49.04 E-value: 6.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1018 AVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGN-SVtrtprkIRSRIGYCPQtesvlnhMTGRES 1096
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEvSV------IAISAGLSGQ-------LTGIEN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1097 LVMYARLWGVLEQDINEYVEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIALMGKSSVVFLDEP-SIGMDPVAQHLLwE 1175
Cdd:PRK13546 106 IEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEAlSVGDQTFAQKCL-D 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 525313703 1176 TITWICKTGKAIIITSHRMEECEALCTRLAIMVKGRFTCLGTPQHVRKRF 1225
Cdd:PRK13546 185 KIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPKY 234
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
166-369 |
7.69e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 50.09 E-value: 7.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 166 IMHLHKEFKN----KPAVNNLSLNIYEGQVTVLLGHNGAGKT-TTLSVL-----------TG--RFAAT----------R 217
Cdd:PRK15134 8 IENLSVAFRQqqtvRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILrllpsppvvypSGdiRFHGEsllhaseqtlR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 218 GeayINGYNISdnMIEVRKDLGFCPQHDL---LFDDLTLseHlffycmvKGIPQNINCEEIDRML-------SAFNLQEN 287
Cdd:PRK15134 88 G---VRGNKIA--MIFQEPMVSLNPLHTLekqLYEVLSL--H-------RGMRREAARGEILNCLdrvgirqAAKRLTDY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 288 YHTLSGsasgGVRRKLSIVLALMAGSKVVILDEPSSGMDpVSRRAtwDILQHYKH-----NRTILLTTHYMDEADVLGDR 362
Cdd:PRK15134 154 PHQLSG----GERQRVMIAMALLTRPELLIADEPTTALD-VSVQA--QILQLLRElqqelNMGLLFITHNLSIVRKLADR 226
|
....*..
gi 525313703 363 VAIMVRG 369
Cdd:PRK15134 227 VAVMQNG 233
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1003-1193 |
7.99e-06 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 50.32 E-value: 7.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1003 LNEVTKIYfkcPVVKAV-KNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNsvtrtprkirSRIGYC 1081
Cdd:TIGR03719 7 MNRVSKVV---PPKKEIlKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPG----------IKVGYL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1082 PQ------TESVL-NHMTG-RESLVMYARLWGVLE-------------------QDINEYVEAFLHSVHLE--------P 1126
Cdd:TIGR03719 74 PQepqldpTKTVReNVEEGvAEIKDALDRFNEISAkyaepdadfdklaaeqaelQEIIDAADAWDLDSQLEiamdalrcP 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 525313703 1127 IADQFIHTYSAGSKRRLSTAIALMGKSSVVFLDEPSigmdpvaQHLLWETITWICK-----TGKAIIITSHR 1193
Cdd:TIGR03719 154 PWDADVTKLSGGERRRVALCRLLLSKPDMLLLDEPT-------NHLDAESVAWLERhlqeyPGTVVAVTHDR 218
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1016-1230 |
9.86e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 48.76 E-value: 9.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1016 VKAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTG-----EETITSGIAFIDGNSVTRTP-RKIRSRIGYCPQTESVLN 1089
Cdd:PRK14247 16 VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRlielyPEARVSGEVYLDGQDIFKMDvIELRRRVQMVFQIPNPIP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1090 HMTGRESLVMYARLWGVL--EQDINEYVEAFLHSVHL-EPIADQF---IHTYSAGSKRRLSTAIALMGKSSVVFLDEPSI 1163
Cdd:PRK14247 96 NLSIFENVALGLKLNRLVksKKELQERVRWALEKAQLwDEVKDRLdapAGKLSGGQQQRLCIARALAFQPEVLLADEPTA 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 525313703 1164 GMDPVAQHLLwETITWICKTGKAIIITSHRMEECEALCTRLAIMVKGRFTCLGTPQHVRKRFGHVYT 1230
Cdd:PRK14247 176 NLDPENTAKI-ESLFLELKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRHELT 241
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1018-1211 |
9.91e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 49.73 E-value: 9.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1018 AVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTRTPRKIRSRIGYCPQTESvlnhmtgRESL 1097
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAINHGFALVTEE-------RRST 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1098 VMYARL---WGVLEQDINEYVEAF--LHSVHLE--------------PIADQFIHTYSAGSKRRLSTAIALMGKSSVVFL 1158
Cdd:PRK10982 336 GIYAYLdigFNSLISNIRNYKNKVglLDNSRMKsdtqwvidsmrvktPGHRTQIGSLSGGNQQKVIIGRWLLTQPEILML 415
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 525313703 1159 DEPSIGMDPVAQHLLWETITWICKTGKAIIITSHRMEECEALCTRLAIMVKGR 1211
Cdd:PRK10982 416 DEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGL 468
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
174-370 |
1.00e-05 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 50.10 E-value: 1.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 174 KNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISDNMIEV-RKDLGFCPQH-----DLL 247
Cdd:PRK10790 352 DDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVlRQGVAMVQQDpvvlaDTF 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 248 FDDLTLSehlffycmvkgipQNINCEEIDRMLSAFNLQE-------NYHTLSG----SASGGVRRKLSIVLALMAGSKVV 316
Cdd:PRK10790 432 LANVTLG-------------RDISEEQVWQALETVQLAElarslpdGLYTPLGeqgnNLSVGQKQLLALARVLVQTPQIL 498
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 317 ILDEPSSGMDPVSRRATWDILQHYKHNRTILLTTHYMD---EAD---VLgDRVAIMVRGT 370
Cdd:PRK10790 499 ILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLStivEADtilVL-HRGQAVEQGT 557
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1018-1230 |
1.01e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 49.70 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1018 AVKNISLVVKKSECFGLLGLNGAGKTTT----FKMLTGEETITsgiafIDGNSVTRTPRK----IRSRIGYCPQT-ESVL 1088
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTglalLRLINSQGEIW-----FDGQPLHNLNRRqllpVRHRIQVVFQDpNSSL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1089 NHMTG-----RESLVMYARLWGVLEQDinEYVEAFLHSVHLEPIADQ-FIHTYSAGSKRRLSTAIALMGKSSVVFLDEPS 1162
Cdd:PRK15134 376 NPRLNvlqiiEEGLRVHQPTLSAAQRE--QQVIAVMEEVGLDPETRHrYPAEFSGGQRQRIAIARALILKPSLIILDEPT 453
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 525313703 1163 IGMDPVAQHLLWETITWICKTGK-AIIITSHRMEECEALCTRLAIMVKGRFTCLGTPQHVRKRFGHVYT 1230
Cdd:PRK15134 454 SSLDKTVQAQILALLKSLQQKHQlAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEYT 522
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
181-362 |
1.02e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 50.41 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 181 NLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYIN-GYNISD-NMIEVRKDLGFCPQHDLLFD--------- 249
Cdd:PTZ00265 403 DLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINdSHNLKDiNLKWWRSKIGVVSQDPLLFSnsiknniky 482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 250 ------DL-TLSEHL-------------FFYCMVKG------IPQNINCEEIDRMLSAFN-------------------- 283
Cdd:PTZ00265 483 slyslkDLeALSNYYnedgndsqenknkRNSCRAKCagdlndMSNTTDSNELIEMRKNYQtikdsevvdvskkvlihdfv 562
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 284 --LQENYHTLSGS----ASGGVRRKLSIVLALMAGSKVVILDEPSSGMDPVSRRATWDILQHYKHNR---TILL-----T 349
Cdd:PTZ00265 563 saLPDKYETLVGSnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNEnriTIIIahrlsT 642
|
250
....*....|...
gi 525313703 350 THYMDEADVLGDR 362
Cdd:PTZ00265 643 IRYANTIFVLSNR 655
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
998-1192 |
1.07e-05 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 48.48 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 998 NTPLLlnEVTKIYFKCPVVKAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEE--TITSGIAFIDGNSVTRTPRKIR 1075
Cdd:CHL00131 4 NKPIL--EIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPayKILEGDILFKGESILDLEPEER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1076 SRIG------YCPQTESVLNHMTGRESLVMYARLWGVLEQDINEYVEAF---LHSVHLEPIadqFIHTY-----SAGSKR 1141
Cdd:CHL00131 82 AHLGiflafqYPIEIPGVSNADFLRLAYNSKRKFQGLPELDPLEFLEIInekLKLVGMDPS---FLSRNvnegfSGGEKK 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 525313703 1142 R---LSTAIAlmgKSSVVFLDEPSIGMDPVAQHLLWETITWICKTGKAIIITSH 1192
Cdd:CHL00131 159 RneiLQMALL---DSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITH 209
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1019-1211 |
1.22e-05 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 48.53 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1019 VKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTR------------------------TPRKI 1074
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKlnraqrkafrrdiqmvfqdsisavNPRKT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1075 RSRIGYCPqtesvLNHMTGRESLVMYARlwgvleqdineyVEAFLHSVHLEP-IADQFIHTYSAGSKRRLSTAIALMGKS 1153
Cdd:PRK10419 108 VREIIREP-----LRHLLSLDKAERLAR------------ASEMLRAVDLDDsVLDKRPPQLSGGQLQRVCLARALAVEP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 525313703 1154 SVVFLDEPSIGMDPVAQHLLWETITWI-CKTGKAIIITSHRMEECEALCTRLAIMVKGR 1211
Cdd:PRK10419 171 KLLILDEAVSNLDLVLQAGVIRLLKKLqQQFGTACLFITHDLRLVERFCQRVMVMDNGQ 229
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1019-1166 |
1.36e-05 |
|
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: 49.55 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1019 VKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGiAFIDGNSVtrtprkirsRIGYCPQTesvlnhmtgRESLV 1098
Cdd:TIGR03719 338 IDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSG-TIEIGETV---------KLAYVDQS---------RDALD 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1099 MYARLWGVLE--QDINE----------YVEAFLHSVhlepiADQ--FIHTYSAGSKRRLSTAIALMGKSSVVFLDEPSIG 1164
Cdd:TIGR03719 399 PNKTVWEEISggLDIIKlgkreipsraYVGRFNFKG-----SDQqkKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTND 473
|
..
gi 525313703 1165 MD 1166
Cdd:TIGR03719 474 LD 475
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
169-326 |
1.61e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 49.12 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 169 LHKEFKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEayingYNISDNmievrKDLGFCPQ-HDLL 247
Cdd:PRK15064 325 LTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGT-----VKWSEN-----ANIGYYAQdHAYD 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 248 FD-DLTLSEHLFFYC-------MVKGIpqninceeIDRML-SAFNLQENYHTLSGSASGgvrR----KLsivlaLMAGSK 314
Cdd:PRK15064 395 FEnDLTLFDWMSQWRqegddeqAVRGT--------LGRLLfSQDDIKKSVKVLSGGEKG---RmlfgKL-----MMQKPN 458
|
170
....*....|..
gi 525313703 315 VVILDEPSSGMD 326
Cdd:PRK15064 459 VLVMDEPTNHMD 470
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1011-1195 |
1.93e-05 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 49.52 E-value: 1.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1011 FKCPVVKAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGiafidgnsvtrtprKIR--SRIGYCPQTESVL 1088
Cdd:TIGR01271 434 FSLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEG--------------KIKhsGRISFSPQTSWIM 499
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1089 NHmTGRESLvmyarLWGV---------------LEQDINEYVEAflhsvHLEPIADQFIhTYSAGSKRRLSTAIALMGKS 1153
Cdd:TIGR01271 500 PG-TIKDNI-----IFGLsydeyrytsvikacqLEEDIALFPEK-----DKTVLGEGGI-TLSGGQRARISLARAVYKDA 567
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 525313703 1154 SVVFLDEPSIGMDPVAQHLLWETItwICK--TGKAIIITSHRME 1195
Cdd:TIGR01271 568 DLYLLDSPFTHLDVVTEKEIFESC--LCKlmSNKTRILVTSKLE 609
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1020-1166 |
2.00e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 49.09 E-value: 2.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1020 KNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFidgnsvtrtpRKIRSRIGYCPQtesvlNHMTGRE---- 1095
Cdd:PLN03073 526 KNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVF----------RSAKVRMAVFSQ-----HHVDGLDlssn 590
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 525313703 1096 SLVMYARLW-GVLEQDINEYVEAFLHSVHLepiADQFIHTYSAGSKRRLSTAIALMGKSSVVFLDEPSIGMD 1166
Cdd:PLN03073 591 PLLYMMRCFpGVPEQKLRAHLGSFGVTGNL---ALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD 659
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1003-1226 |
2.52e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 48.97 E-value: 2.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1003 LNEVTKIYFKcpvVKAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSG-IAFIDGN-SVTRTPRKIRSRIGY 1080
Cdd:NF033858 4 LEGVSHRYGK---TVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGrVEVLGGDmADARHRRAVCPRIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1081 CPQ--------TESVlnhmtgRESLVMYARLWGvleQDINE---YVEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIAL 1149
Cdd:NF033858 81 MPQglgknlypTLSV------FENLDFFGRLFG---QDAAErrrRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 525313703 1150 MGKSSVVFLDEPSIGMDPVAQHLLWETITWICKT--GKAIIITSHRMEECEAlCTRLAIMVKGRFTCLGTPQHVRKRFG 1226
Cdd:NF033858 152 IHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAErpGMSVLVATAYMEEAER-FDWLVAMDAGRVLATGTPAELLARTG 229
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1033-1166 |
2.98e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 48.24 E-value: 2.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1033 GLLGLNGAGKTTTFKMLTGEETITSG-IAFIDGnsvtrtprkirSRIGYCPQ--------TESVLNHMtgreslvmyARL 1103
Cdd:PRK10636 342 GLLGRNGAGKSTLIKLLAGELAPVSGeIGLAKG-----------IKLGYFAQhqleflraDESPLQHL---------ARL 401
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 525313703 1104 W-GVLEQDINEYVEAF-LHSVHLEPIADQFihtySAGSKRRLSTAIALMGKSSVVFLDEPSIGMD 1166
Cdd:PRK10636 402 ApQELEQKLRDYLGGFgFQGDKVTEETRRF----SGGEKARLVLALIVWQRPNLLLLDEPTNHLD 462
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1014-1212 |
3.00e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 48.19 E-value: 3.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1014 PVVKAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTRTPRK--IRSRIGYCPQ------TE 1085
Cdd:PRK10982 9 PGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKeaLENGISMVHQelnlvlQR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1086 SVLNHM-TGRESLvmyaRLWGVLEQDINEYVEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIALMGKSSVVFLDEPSIG 1164
Cdd:PRK10982 89 SVMDNMwLGRYPT----KGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSS 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 525313703 1165 MDPVAQHLLWETITWICKTGKAIIITSHRMEECEALCTRLAIMVKGRF 1212
Cdd:PRK10982 165 LTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQW 212
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
174-371 |
3.12e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 47.12 E-value: 3.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 174 KNKP--AVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGyniSDNMIEVRKDLGfcpqhdllfDDL 251
Cdd:PRK13546 33 KNKTffALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG---EVSVIAISAGLS---------GQL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 252 TLSEHLFFYCMVKGIPQNINCEEIDRMLSAFNLQENYHTLSGSASGGVRRKLSIVLALMAGSKVVILDEPSSGMDPVSRR 331
Cdd:PRK13546 101 TGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQ 180
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 525313703 332 ATWDILQHYK-HNRTILLTTHYMDEADVLGDRVAIMVRGTL 371
Cdd:PRK13546 181 KCLDKIYEFKeQNKTIFFVSHNLGQVRQFCTKIAWIEGGKL 221
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
164-375 |
3.36e-05 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 47.91 E-value: 3.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 164 IHIMHLHKEFKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISD-NMIEVRKDLGFCP 242
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEAlSARAASRRVASVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 243 QHDLL---FDDLTLSE-----HLFFYCMVKGIPQNINCEEIDRMLSAFNLQENYHTLsgsaSGGVRRKLSIVLALMAGSK 314
Cdd:PRK09536 84 QDTSLsfeFDVRQVVEmgrtpHRSRFDTWTETDRAAVERAMERTGVAQFADRPVTSL----SGGERQRVLLARALAQATP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 525313703 315 VVILDEPSSGMDPVSRRATWDILQHY-KHNRTILLTTHYMDEADVLGDRVAIMVRGTLHCCG 375
Cdd:PRK09536 160 VLLLDEPTASLDINHQVRTLELVRRLvDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAG 221
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
1022-1234 |
4.21e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 48.20 E-value: 4.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1022 ISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTRTP-RKIRSRIGYCPQTeSVLNHMTGRESLVMY 1100
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGlMDLRKVLGIIPQA-PVLFSGTVRFNLDPF 1336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1101 -----ARLWGVLEQdineyveAFL------HSVHLEPIADQFIHTYSAGSKRRLSTAIALMGKSSVVFLDEPSIGMDPVA 1169
Cdd:PLN03130 1337 nehndADLWESLER-------AHLkdvirrNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRT 1409
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 525313703 1170 QHLLWETITWICKTGKAIIItSHRMEECeALCTRLAIMVKGRFTCLGTPQHVRKRFGHVYTLTVR 1234
Cdd:PLN03130 1410 DALIQKTIREEFKSCTMLII-AHRLNTI-IDCDRILVLDAGRVVEFDTPENLLSNEGSAFSKMVQ 1472
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1018-1196 |
5.10e-05 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 46.70 E-value: 5.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1018 AVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSG------IAFIDGNSVTR--TPRKIRSRIGYC-----PQT 1084
Cdd:PRK14243 25 AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPGfrvegkVTFHGKNLYAPdvDPVEVRRRIGMVfqkpnPFP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1085 ESVlnhmtgRESLVMYARLWGvLEQDINEYVEAFLHSVHL-EPIADQFIHT---YSAGSKRRLSTAIALMGKSSVVFLDE 1160
Cdd:PRK14243 105 KSI------YDNIAYGARING-YKGDMDELVERSLRQAALwDEVKDKLKQSglsLSGGQQQRLCIARAIAVQPEVILMDE 177
|
170 180 190
....*....|....*....|....*....|....*.
gi 525313703 1161 PSIGMDPVAQHLLWETITWIcKTGKAIIITSHRMEE 1196
Cdd:PRK14243 178 PCSALDPISTLRIEELMHEL-KEQYTIIIVTHNMQQ 212
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1016-1230 |
5.19e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 47.54 E-value: 5.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1016 VKAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTRTPRKIrsrIGYCPQTESVLNHMTG-- 1093
Cdd:PRK10261 29 IAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRQV---IELSEQSAAQMRHVRGad 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1094 -----RESLVMYARLWGVLEQdINEYV---------EAFLHSVHL---------EPIADQFIHTYSAGSKRRLSTAIALM 1150
Cdd:PRK10261 106 mamifQEPMTSLNPVFTVGEQ-IAESIrlhqgasreEAMVEAKRMldqvripeaQTILSRYPHQLSGGMRQRVMIAMALS 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1151 GKSSVVFLDEPSIGMDPVAQHLLWETITWICK-TGKAIIITSHRMEECEALCTRLAIMVKGRFTCLGTPQHVRKRFGHVY 1229
Cdd:PRK10261 185 CRPAVLIADEPTTALDVTIQAQILQLIKVLQKeMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAPQHPY 264
|
.
gi 525313703 1230 T 1230
Cdd:PRK10261 265 T 265
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
997-1196 |
5.53e-05 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 45.86 E-value: 5.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 997 QNTPLLlnEVTKIYFKCPVVKAVKNISLVVKKSEcFGLL-GLNGAGKTTTFKMLTGEETITSGIAFIDGNSV-TRTPRKI 1074
Cdd:PRK10247 3 ENSPLL--QLQNVGYLAGDAKILNNISFSLRAGE-FKLItGPSGCGKSTLLKIVASLISPTSGTLLFEGEDIsTLKPEIY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1075 RSRIGYCPQTESVLNHmTGRESLVMyarLWGVLEQDINE-YVEAFLHSVHL-EPIADQFIHTYSAGSKRRLSTAIALMGK 1152
Cdd:PRK10247 80 RQQVSYCAQTPTLFGD-TVYDNLIF---PWQIRNQQPDPaIFLDDLERFALpDTILTKNIAELSGGEKQRISLIRNLQFM 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 525313703 1153 SSVVFLDEPSIGMDPVAQHLLWETIT-WICKTGKAIIITSHRMEE 1196
Cdd:PRK10247 156 PKVLLLDEITSALDESNKHNVNEIIHrYVREQNIAVLWVTHDKDE 200
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
176-357 |
5.90e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 47.81 E-value: 5.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 176 KPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATrgeayingyniSDNMIEVRKDLGFCPQHDLLFDdLTLSE 255
Cdd:PLN03130 630 RPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPR-----------SDASVVIRGTVAYVPQVSWIFN-ATVRD 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 256 HLFFycmvkGIPqnINCEEIDRMLSAFNLQENYHTLSG-----------SASGGVRRKLSIVLALMAGSKVVILDEPSSG 324
Cdd:PLN03130 698 NILF-----GSP--FDPERYERAIDVTALQHDLDLLPGgdlteigergvNISGGQKQRVSMARAVYSNSDVYIFDDPLSA 770
|
170 180 190
....*....|....*....|....*....|....*..
gi 525313703 325 MDPVSRRATWD--ILQHYKHNRTILLTT--HYMDEAD 357
Cdd:PLN03130 771 LDAHVGRQVFDkcIKDELRGKTRVLVTNqlHFLSQVD 807
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1036-1192 |
6.79e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 45.25 E-value: 6.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1036 GLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTRTPRKIRSRIGYcpqTESVLNHMTGRESLVMYARLWgvleqDINEYV 1115
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYCTYIGH---NLGLKLEMTVFENLKFWSEIY-----NSAETL 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 525313703 1116 EAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIALMGKSSVVFLDEPSIGMDPVAQHLLWETITWICKTGKAIIITSH 1192
Cdd:PRK13541 105 YAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVMKANSGGIVLLSSH 181
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1033-1162 |
7.76e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 47.04 E-value: 7.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1033 GLLGLNGAGKTTTFKMLTGEETITSGiAFIDGNSVtrtprkirsRIGYCPQTesvlnhmtgRESLVMYARLWGVL--EQD 1110
Cdd:PRK11819 354 GIIGPNGAGKSTLFKMITGQEQPDSG-TIKIGETV---------KLAYVDQS---------RDALDPNKTVWEEIsgGLD 414
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 525313703 1111 INE----------YVEAFLHSVhlepiADQ--FIHTYSAGSKRRLSTAIALMGKSSVVFLDEPS 1162
Cdd:PRK11819 415 IIKvgnreipsraYVGRFNFKG-----GDQqkKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPT 473
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
178-332 |
9.13e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 46.11 E-value: 9.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 178 AVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISDNMIEVRKDLGFCPQhdLLFDD------- 250
Cdd:PRK11308 30 ALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLLRQKIQ--IVFQNpygslnp 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 251 -----LTLSEhlffycmvkgiPQNINC--------EEIDRMLSAFNLQ-ENYHTLSGSASGGVRRKLSIVLALMAGSKVV 316
Cdd:PRK11308 108 rkkvgQILEE-----------PLLINTslsaaerrEKALAMMAKVGLRpEHYDRYPHMFSGGQRQRIAIARALMLDPDVV 176
|
170
....*....|....*.
gi 525313703 317 ILDEPSSGMDpVSRRA 332
Cdd:PRK11308 177 VADEPVSALD-VSVQA 191
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
171-369 |
9.81e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 46.65 E-value: 9.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 171 KEFKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNIS--------DNMIE-VRKDLGFC 241
Cdd:PRK10982 6 KSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfksskealENGISmVHQELNLV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 242 PQHDLLfDDLTLS---------EHLFFYCMVKGIPQNInceEIDrmlsaFNLQENYHTLSGSAsggvRRKLSIVLALMAG 312
Cdd:PRK10982 86 LQRSVM-DNMWLGryptkgmfvDQDKMYRDTKAIFDEL---DID-----IDPRAKVATLSVSQ----MQMIEIAKAFSYN 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 525313703 313 SKVVILDEPSSGMDPVSRRATWDILQHYKHNRT-ILLTTHYMDEADVLGDRVAIMVRG 369
Cdd:PRK10982 153 AKIVIMDEPTSSLTEKEVNHLFTIIRKLKERGCgIVYISHKMEEIFQLCDEITILRDG 210
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1021-1192 |
1.02e-04 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 44.79 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1021 NISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVtrtpRKIRSR-------IGYCPQTESVLnhmTG 1093
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPI----RRQRDEyhqdllyLGHQPGIKTEL---TA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1094 RESLVMYARLWGVLEQDIneyVEAFLHSVHLEPIADQFIHTYSAGSKRRLSTAIALMGKSSVVFLDEP--SI---GMDPV 1168
Cdd:PRK13538 92 LENLRFYQRLHGPGDDEA---LWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPftAIdkqGVARL 168
|
170 180
....*....|....*....|....
gi 525313703 1169 AQHLLWEtitwiCKTGKAIIITSH 1192
Cdd:PRK13538 169 EALLAQH-----AEQGGMVILTTH 187
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1019-1195 |
1.48e-04 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 45.23 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1019 VKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGiafidgnsvtrtprKIR--SRIGYCPQTESVLNHmTGRES 1096
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEG--------------KIKhsGRISFSSQFSWIMPG-TIKEN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1097 LVmyarlWGV---------------LEQDINEYVEAflhsvHLEPIADQFIhTYSAGSKRRLSTAIALMGKSSVVFLDEP 1161
Cdd:cd03291 118 II-----FGVsydeyryksvvkacqLEEDITKFPEK-----DNTVLGEGGI-TLSGGQRARISLARAVYKDADLYLLDSP 186
|
170 180 190
....*....|....*....|....*....|....*.
gi 525313703 1162 SIGMDPVAQHLLWETItwICK--TGKAIIITSHRME 1195
Cdd:cd03291 187 FGYLDVFTEKEIFESC--VCKlmANKTRILVTSKME 220
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
164-351 |
3.27e-04 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 44.93 E-value: 3.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 164 IHIMHLHKEFKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEayingYNISDNMievrkDLGFCPQ 243
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGT-----IEIGETV-----KLAYVDQ 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 244 -HDLLFDDLTLSEHL---FFYCMVKG--IPQNINCeeidrmlSAFNL----QENyhtLSGSASGGVRRKLSIVLALMAGS 313
Cdd:TIGR03719 393 sRDALDPNKTVWEEIsggLDIIKLGKreIPSRAYV-------GRFNFkgsdQQK---KVGQLSGGERNRVHLAKTLKSGG 462
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 525313703 314 KVVILDEPSSGMDPVSRRATWDILQHY-------KHNRTIL--LTTH 351
Cdd:TIGR03719 463 NVLLLDEPTNDLDVETLRALEEALLNFagcavviSHDRWFLdrIATH 509
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1001-1161 |
3.41e-04 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 44.45 E-value: 3.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1001 LLLNEVTKIYFKcpVVKAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTRtpRKIRSR-IG 1079
Cdd:PRK11650 4 LKLQAVRKSYDG--KTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNE--LEPADRdIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1080 YCPQTESVLNHMTGRESLVmYA-RLWGVLEQDINEYVEAFLHSVHLEPIADQFIHTYSAGSKRRLStaialMGKSSV--- 1155
Cdd:PRK11650 80 MVFQNYALYPHMSVRENMA-YGlKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVA-----MGRAIVrep 153
|
....*...
gi 525313703 1156 -VFL-DEP 1161
Cdd:PRK11650 154 aVFLfDEP 161
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1005-1195 |
3.49e-04 |
|
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: 43.47 E-value: 3.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1005 EVTKIYFK-CPVVKAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAF-----IDGNSVTRTPRKIRSRI 1078
Cdd:cd03290 2 QVTNGYFSwGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwsnknESEPSFEATRSRNRYSV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1079 GYCPQTESVLNhMTGRESLVmyarlwgvLEQDIN-EYVEAFLHSVHLEPIADQFIH-----------TYSAGSKRRLSTA 1146
Cdd:cd03290 82 AYAAQKPWLLN-ATVEENIT--------FGSPFNkQRYKAVTDACSLQPDIDLLPFgdqteigergiNLSGGQRQRICVA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 525313703 1147 IALMGKSSVVFLDEPSIGMD-PVAQHLLWETITWICKTGK-AIIITSHRME 1195
Cdd:cd03290 153 RALYQNTNIVFLDDPFSALDiHLSDHLMQEGILKFLQDDKrTLVLVTHKLQ 203
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
174-371 |
4.59e-04 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 44.25 E-value: 4.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 174 KNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISDNMIEVRKDLGFC-----PQHDLLF 248
Cdd:COG3845 269 RGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLGVAyipedRLGRGLV 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 249 DDLTLSEHLFF-----YCMVKGIpqNINCEEI----DRMLSAFNLQ-ENYHTLSGSASGGVRRKLsiVLA--LMAGSKVV 316
Cdd:COG3845 349 PDMSVAENLILgryrrPPFSRGG--FLDRKAIrafaEELIEEFDVRtPGPDTPARSLSGGNQQKV--ILAreLSRDPKLL 424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 525313703 317 ILDEPSSGMDPVSRRATWD-ILQHYKHNRTILLTTHYMDEADVLGDRVAIMVRGTL 371
Cdd:COG3845 425 IAAQPTRGLDVGAIEFIHQrLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRI 480
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
1025-1074 |
4.62e-04 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 42.56 E-value: 4.62e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 525313703 1025 VVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSVTRTPRKI 1074
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVYKPQYI 70
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1021-1193 |
5.99e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 44.01 E-value: 5.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1021 NISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSV-----TRTPRKIRSRIGYC-------PQTESVL 1088
Cdd:PRK10636 19 NATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQlawvnQETPALPQPALEYVidgdreyRQLEAQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1089 NHMTGRESLVMYARLWGVLEQ----DINEYVEAFLHSVHL-EPIADQFIHTYSAGSKRRLSTAIALMGKSSVVFLDEPSi 1163
Cdd:PRK10636 99 HDANERNDGHAIATIHGKLDAidawTIRSRAASLLHGLGFsNEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPT- 177
|
170 180 190
....*....|....*....|....*....|....*
gi 525313703 1164 gmdpvaQHLLWETITWICK-----TGKAIIITSHR 1193
Cdd:PRK10636 178 ------NHLDLDAVIWLEKwlksyQGTLILISHDR 206
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
177-326 |
6.58e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 44.34 E-value: 6.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 177 PAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISD-NMIEVRKDLGFCPQHDLLF------- 248
Cdd:PLN03130 1253 PVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKfGLMDLRKVLGIIPQAPVLFsgtvrfn 1332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 249 -------DDLTLSEHL---FFYCMVKGIPQNINCEeidrmlsAFNLQENYhtlsgsaSGGVRRKLSIVLALMAGSKVVIL 318
Cdd:PLN03130 1333 ldpfnehNDADLWESLeraHLKDVIRRNSLGLDAE-------VSEAGENF-------SVGQRQLLSLARALLRRSKILVL 1398
|
....*...
gi 525313703 319 DEPSSGMD 326
Cdd:PLN03130 1399 DEATAAVD 1406
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
164-211 |
7.02e-04 |
|
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: 44.02 E-value: 7.02e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 525313703 164 IHIMHLHKEFKNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTG 211
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRG 48
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1020-1166 |
7.74e-04 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 43.94 E-value: 7.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1020 KNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNSV-TRTPRKIRSRIGYCPQTESVL------NHMT 1092
Cdd:PRK10790 358 QNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLsSLSHSVLRQGVAMVQQDPVVLadtflaNVTL 437
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 525313703 1093 GREslVMYARLWGVLEQ-DINEYVEAFLHSVHlEPIADQFiHTYSAGSKRRLSTAIALMGKSSVVFLDEPSIGMD 1166
Cdd:PRK10790 438 GRD--ISEEQVWQALETvQLAELARSLPDGLY-TPLGEQG-NNLSVGQKQLLALARVLVQTPQILILDEATANID 508
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
178-228 |
1.03e-03 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 42.47 E-value: 1.03e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 525313703 178 AVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNIS 228
Cdd:PRK15112 28 AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLH 78
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
177-376 |
1.29e-03 |
|
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: 43.36 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 177 PAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGyNISdnmievrkdlgFCPQHDLLFDDlTLSEH 256
Cdd:TIGR01271 440 PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-RIS-----------FSPQTSWIMPG-TIKDN 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 257 LFF--------YCMVkgipqnINCEEIDRMLSAFNLQENYHTLSG--SASGGVRRKLSIVLALMAGSKVVILDEPSSGMD 326
Cdd:TIGR01271 507 IIFglsydeyrYTSV------IKACQLEEDIALFPEKDKTVLGEGgiTLSGGQRARISLARAVYKDADLYLLDSPFTHLD 580
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 525313703 327 PVSRRATWD-ILQHYKHNRTILLTTHYMDEADvLGDRVAIMVRGTLHCCGS 376
Cdd:TIGR01271 581 VVTEKEIFEsCLCKLMSNKTRILVTSKLEHLK-KADKILLLHEGVCYFYGT 630
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
186-365 |
1.57e-03 |
|
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: 41.02 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 186 IYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISdnmievrkdlgfcpqhdllfddltlsehlffycmVKg 265
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPV----------------------------------YK- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 266 iPQNInceeidrmlsafnlqenyhtlsgSASGGVRRKLSIVLALMAGSKVVILDEPSSGMDPVSRRATWDILQHY--KHN 343
Cdd:cd03222 67 -PQYI-----------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLseEGK 122
|
170 180
....*....|....*....|..
gi 525313703 344 RTILLTTHYMDEADVLGDRVAI 365
Cdd:cd03222 123 KTALVVEHDLAVLDYLSDRIHV 144
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
1019-1231 |
1.58e-03 |
|
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: 43.01 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1019 VKNISLVVKKSECFGLLGLNGAGKTTT----FKMLTGEEtitsGIAFIDGNSVTRTP-RKIRSRIGYCPQtESVLNHMTG 1093
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLtlglFRINESAE----GEIIIDGLNIAKIGlHDLRFKITIIPQ-DPVLFSGSL 1376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1094 RESLVMYAR-----LWGVLE-QDINEYVEAFLHSVHLEpiADQFIHTYSAGSKRRLSTAIALMGKSSVVFLDEPSIGMDP 1167
Cdd:TIGR00957 1377 RMNLDPFSQysdeeVWWALElAHLKTFVSALPDKLDHE--CAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDL 1454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 525313703 1168 VAQHLLWETITWICKTGKAIIItSHRMEECEALcTRLAIMVKGRFTCLGTPQHVRKRFGHVYTL 1231
Cdd:TIGR00957 1455 ETDNLIQSTIRTQFEDCTVLTI-AHRLNTIMDY-TRVIVLDKGEVAEFGAPSNLLQQRGIFYSM 1516
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
174-369 |
1.84e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 42.41 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 174 KNKPAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISDN------------MIEVRKDLGFC 241
Cdd:PRK10982 259 LRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHnaneainhgfalVTEERRSTGIY 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 242 PQHDLLFDDLTlsEHLFFYCMVKGIPQNINCEE-----IDRMlsafNLQE-NYHTLSGSASGGVRRKLSIVLALMAGSKV 315
Cdd:PRK10982 339 AYLDIGFNSLI--SNIRNYKNKVGLLDNSRMKSdtqwvIDSM----RVKTpGHRTQIGSLSGGNQQKVIIGRWLLTQPEI 412
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 525313703 316 VILDEPSSGMDPVSRRATWD-ILQHYKHNRTILLTTHYMDEADVLGDRVAIMVRG 369
Cdd:PRK10982 413 LMLDEPTRGIDVGAKFEIYQlIAELAKKDKGIIIISSEMPELLGITDRILVMSNG 467
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1014-1051 |
2.08e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 42.47 E-value: 2.08e-03
10 20 30
....*....|....*....|....*....|....*...
gi 525313703 1014 PVVKAVKNISLVVKKSECFGLLGLNGAGKTTTFKMLTG 1051
Cdd:NF040905 12 PGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSG 49
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
183-369 |
2.14e-03 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 42.21 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 183 SLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISDN----------MI--EVRKDLGFCPQHDLLfDD 250
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRsprdairagiMLcpEDRKAEGIIPVHSVA-DN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 251 LTLS---EHLFFYCMVKGIPQNINCEE-IDRMlsafNLQE-NYHTLSGSASGGVRRKlsIVLA--LMAGSKVVILDEPSS 323
Cdd:PRK11288 352 INISarrHHLRAGCLINNRWEAENADRfIRSL----NIKTpSREQLIMNLSGGNQQK--AILGrwLSEDMKVILLDEPTR 425
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 525313703 324 GMDPVSRRATWDILqhY---KHNRTILLTTHymDEADVLG--DRVAIMVRG 369
Cdd:PRK11288 426 GIDVGAKHEIYNVI--YelaAQGVAVLFVSS--DLPEVLGvaDRIVVMREG 472
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
1091-1195 |
2.50e-03 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 40.04 E-value: 2.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1091 MTGReSLVMYARLWGVLEQDINEYVEAFLHS------VHLEPIadQFIHTYSAGSKRRLSTAIAL----MGKSSVVFLDE 1160
Cdd:cd03227 31 GSGK-STILDAIGLALGGAQSATRRRSGVKAgcivaaVSAELI--FTRLQLSGGEKELSALALILalasLKPRPLYILDE 107
|
90 100 110
....*....|....*....|....*....|....*
gi 525313703 1161 PSIGMDPVAQHLLWETITWICKTGKAIIITSHRME 1195
Cdd:cd03227 108 IDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPE 142
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
995-1166 |
3.14e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 41.80 E-value: 3.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 995 RLQNTPLLLNEVTKIYFKCPVVKavkNISLVVKKSECFGLLGLNGAGKTTTFKMLTGEETITSGIAFIDGNsvtrtprki 1074
Cdd:PRK15064 314 KLHRNALEVENLTKGFDNGPLFK---NLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSEN--------- 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1075 rSRIGYCPQ--------TESVLNHMT-----GRESLVMYARLWGVL--EQDINEYVEAFlhsvhlepiadqfihtySAGS 1139
Cdd:PRK15064 382 -ANIGYYAQdhaydfenDLTLFDWMSqwrqeGDDEQAVRGTLGRLLfsQDDIKKSVKVL-----------------SGGE 443
|
170 180
....*....|....*....|....*..
gi 525313703 1140 KRRLSTAIALMGKSSVVFLDEPSIGMD 1166
Cdd:PRK15064 444 KGRMLFGKLMMQKPNVLVMDEPTNHMD 470
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
181-351 |
3.88e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 40.24 E-value: 3.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 181 NLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGYNISDnmieVRKDLGFCPQHDL-LFDDLTLSEHLFF 259
Cdd:PRK13541 18 DLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINN----IAKPYCTYIGHNLgLKLEMTVFENLKF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 260 YCMVKGipqniNCEEIDRMLSAFNLQENYHTLSGSASGGVRRKLSIVLALMAGSKVVILDEPSSGMDPVSRRATWD-ILQ 338
Cdd:PRK13541 94 WSEIYN-----SAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNlIVM 168
|
170
....*....|...
gi 525313703 339 HYKHNRTILLTTH 351
Cdd:PRK13541 169 KANSGGIVLLSSH 181
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
998-1161 |
4.69e-03 |
|
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: 41.21 E-value: 4.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 998 NTPLLlnEVT--KIYFK--CPVVKAVKNISLVVKKSECFGLLGLNGAGKTTTF----KMLTGEETITSGIAFIDGNSVTR 1069
Cdd:COG4172 3 SMPLL--SVEdlSVAFGqgGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTAlsilRLLPDPAAHPSGSILFDGQDLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 1070 TP----RKIR-SRIGYC---PQTEsvLN-HMT-GR---ESLVMYARLWGvleQDINEYVEAFLHSVHL-EP--IADQFIH 1133
Cdd:COG4172 81 LSerelRRIRgNRIAMIfqePMTS--LNpLHTiGKqiaEVLRLHRGLSG---AAARARALELLERVGIpDPerRLDAYPH 155
|
170 180
....*....|....*....|....*...
gi 525313703 1134 TYSAGSKRRLSTAIALMGKSSVVFLDEP 1161
Cdd:COG4172 156 QLSGGQRQRVMIAMALANEPDLLIADEP 183
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
177-370 |
8.49e-03 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 39.84 E-value: 8.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 177 PAVNNLSLNIYEGQVTVLLGHNGAGKTTTLSVLTGRFAATRGEAYINGyNISdnmievrkdlgFCPQHDLLFDDlTLSEH 256
Cdd:cd03291 51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-RIS-----------FSSQFSWIMPG-TIKEN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313703 257 LFFycmvkGIPQN-------INCEEIDRMLSAFNLQENYHTLSG--SASGGVRRKLSIVLALMAGSKVVILDEPSSGMDP 327
Cdd:cd03291 118 IIF-----GVSYDeyryksvVKACQLEEDITKFPEKDNTVLGEGgiTLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 192
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 525313703 328 VSRRATWD-ILQHYKHNRTILLTTHYMDEADVlGDRVAIMVRGT 370
Cdd:cd03291 193 FTEKEIFEsCVCKLMANKTRILVTSKMEHLKK-ADKILILHEGS 235
|
|
| |
