|
Name |
Accession |
Description |
Interval |
E-value |
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1-2272 |
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: 4924.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1 MGFVRQIQLLLWKNWTLRKRQKIRFVVELVWPLSLFLVLIWLRNANPLYSHHECHFPNKAMPSAGMLPWLQGIFCNVNNP 80
Cdd:TIGR01257 1 MGFLRQIQLLLWKNWTLRKRQKIRFVVELVWPLSLFLVLIWLRNANPLYSQHECHFPNKAMPSAGMLPWLQGIFCNVNNP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 81 CFQSPTPGESPGIVSNYNNSILARVYRDFQELLMNAPESQHLGRIWTELHILSQFMDTLRTHPERIAGRGIRIRDILKDE 160
Cdd:TIGR01257 81 CFQSPTPGESPGIVSNYNNSILARVYRDFQELLMDAPESQHLGQVWAELRTLSQFMDTLRTHPERIAGRGIRIRDILKDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 161 ETLTLFLIKNIGLSDSVVYLLINSQVRPEQFAHGVPDLALKDIACSEALLERFIIFSQRRGAKTVRYALCSLSQGTLQWI 240
Cdd:TIGR01257 161 EALTLFLMKNIGLSDSVVYLLVNSQVRPEQFAYGVPDLELKDIACSEALLERFIIFSQRRGAQTVRDALCSLSQGTLQWI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 241 EDTLYANVDFFKLFRVLPTLLDSRSQGINLRSWGGILSDMSPRIQEFIHRPSMQDLLWVTRPLMQNGGPETFTKLMGILS 320
Cdd:TIGR01257 241 EDTLYANVDFFKLFHVLPTLLDSRSQGINLRSWGGILSDMSPRIQEFIHRPSVQDLLWVTRPLLQNGGPETFTQLMGILS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 321 DLLCGYPEGGGSRVLSFNWYEDNNYKAFLGIDSTRKDPIYSYDRRTTSFCNALIQSLESNPLTKIAWRAAKPLLMGKILY 400
Cdd:TIGR01257 321 DLLCGYPEGGGSRVFSFNWYEDNNYKAFLGIDSTRKDPIYSYDKRTTSFCNALIQSLESNPLTKIAWRAAKPLLMGKILF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 401 TPDSPAARRILKNANSTFEELEHVRKLVKAWEEVGPQIWYFFDNSTQMNMIRDTLGNPTVKDFLNRQLGEEGITAEAILN 480
Cdd:TIGR01257 401 TPDSPAARRILKNANSTFEELERVRKLVKAWEEVGPQIWYFFDKSTQMTMIRDTLQNPTVKDFINRQLGEEGITAEAVLN 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 481 FLYKGPRESQADDMANFDWRDIFNITDRTLRLVNQYLECLVLDKFESYNDETQLTQRALSLLEENMFWAGVVFPDMYPWT 560
Cdd:TIGR01257 481 FLYNGPREKQADDMTNFDWRDIFNITDRFLRLANQYLECLVLDKFESYDDEVQLTQRALSLLEENRFWAGVVFPDMYPWT 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 561 SSLPPHVKYKIRMDIDVVEKTNKIKDRYWDSGPRADPVEDFRYIWGGFAYLQDMVEQGITRSQVQAEAPVGIYLQQMPYP 640
Cdd:TIGR01257 561 SSLPPHVKYKIRMDIDVVEKTNKIKDRYWDSGPRADPVEDFRYIWGGFAYLQDMVEQGITRSQMQAEPPVGIYLQQMPYP 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 641 CFVDDSFMIILNRCFPIFMVLAWIYSVSMTVKSIVLEKELRLKETLKNQGVSNAVIWCTWFLDSFSIMSMSIFLLTIFIM 720
Cdd:TIGR01257 641 CFVDDSFMIILNRCFPIFMVLAWIYSVSMTVKSIVLEKELRLKETLKNQGVSNAVIWCTWFLDSFSIMSMSIFLLTIFIM 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 721 HGRILHYSDPFILFLFLLAFSTATIMLCFLLSTFFSKASLAAACSGVIYFTLYLPHILCFAWQDRMTAELKKAVSLLSPV 800
Cdd:TIGR01257 721 HGRILHYSDPFILFLFLLAFSTATIMQCFLLSTFFSKASLAAACSGVIYFTLYLPHILCFAWQDRMTADLKTAVSLLSPV 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 801 AFGFGTEYLVRFEEQGLGLQWSNIGNSPTEGDEFSFLLSMQMMLLDAAVYGLLAWYLDQVFPGDYGTPLPWYFLLQESYW 880
Cdd:TIGR01257 801 AFGFGTEYLVRFEEQGLGLQWSNIGNSPLEGDEFSFLLSMKMMLLDAALYGLLAWYLDQVFPGDYGTPLPWYFLLQESYW 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 881 LGGEGCSTREERALEKTEPLTEETEDPEHPEGIHDSFFEREHPGWVPGVCVKNLVKIFEPCGRPAVDRLNITFYENQITA 960
Cdd:TIGR01257 881 LGGEGCSTREERALEKTEPLTEEMEDPEHPEGINDSFFERELPGLVPGVCVKNLVKIFEPSGRPAVDRLNITFYENQITA 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 961 FLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIETSLDAVRQSLGMCPQHNILFHHLTVAEHMLFYAQLKGKSQEEAQL 1040
Cdd:TIGR01257 961 FLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQL 1040
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1041 EMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHM 1120
Cdd:TIGR01257 1041 EMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHM 1120
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1121 DEADLLGDRIAIIAQGRLYCSGTPLFLKNCFGTGLYLTLVRKMKNIQSQRKGSEGTCSCSSKGFSTTCPAHVDDLTPEQV 1200
Cdd:TIGR01257 1121 DEADLLGDRIAIISQGRLYCSGTPLFLKNCFGTGFYLTLVRKMKNIQSQRGGCEGTCSCTSKGFSTRCPARVDEITPEQV 1200
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1201 LDGDVNELMDVVLHHVPEAKLVECIGQELIFLLPNKNFKHRAYASLFRELEETLADLGLSSFGISDTPLEEIFLKVTEDS 1280
Cdd:TIGR01257 1201 LDGDVNELMDLVYHHVPEAKLVECIGQELIFLLPNKNFKQRAYASLFRELEETLADLGLSSFGISDTPLEEIFLKVTEDA 1280
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1281 DSGPLFAGGAQQKRENVNPRHPCLGPREKAGQTPQDSNVCSPGAPAAHPEGQPPPEPECPGPQLNTGTQLVLQHVQALLV 1360
Cdd:TIGR01257 1281 DSGSLFAGGAQQKRENANLRHPCSGPTEKAGQTPQASHTCSPGQPAAHPEGQPPPEPEDPGVPLNTGARLILQHVQALLV 1360
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1361 KRFQHTIRSHKDFLAQIVLPATFVFLALMLSIVIPPFGEYPALTLHPWIYGQQYTFFSMDEPGSEQFTVLADVLLNKPGF 1440
Cdd:TIGR01257 1361 KRFQHTIRSHKDFLAQIVLPATFVFLALMLSIIIPPFGEYPALTLHPWMYGQQYTFFSMDEPNSEHLEVLADVLLNKPGF 1440
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1441 GNRCLKEGWLPEYPCGNSTPWKTPSVSPNITQLFQKQKWTQVNPSPSCRCSTREKLTMLPECPEGAGGLPPPQRTQRSTE 1520
Cdd:TIGR01257 1441 GNRCLKEEWLPEYPCGNSTPWKTPSVSPNITHLFQKQKWTAAHPSPSCRCSTREKLTMLPECPEGAGGLPPPQRTQRSTE 1520
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1521 ILQDLTDRNISDFLVKTYPALIRSSLKSKFWVNEQRYGGISIGGKLPVVPITGEALVGFLSDLGRIMNVSGGPITREASK 1600
Cdd:TIGR01257 1521 ILQDLTDRNISDFLVKTYPALIRSSLKSKFWVNEQRYGGISIGGKLPAIPITGEALVGFLSDLGQMMNVSGGPVTREASK 1600
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1601 EIPDFLKHLETEDNIKVWFNNKGWHALVSFLNVAHNAILRASLPKDRSPEEYGITVISQPLNLTKEQLSEITVLTTSVDA 1680
Cdd:TIGR01257 1601 EMPDFLKHLETEDNIKVWFNNKGWHALVSFLNVAHNAILRASLPKDRDPEEYGITVISQPLNLTKEQLSEITVLTTSVDA 1680
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1681 VVAICVIFSMSFVPASFVLYLIQERVNKSKHLQFISGVSPTTYWVTNFLWDIMNYSVSAGLVVGIFIGFQKKAYTSPENL 1760
Cdd:TIGR01257 1681 VVAICVIFAMSFVPASFVLYLIQERVNKAKHLQFISGVSPTTYWLTNFLWDIMNYAVSAGLVVGIFIGFQKKAYTSPENL 1760
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1761 PALVALLLLYGWAVIPMMYPASFLFDVPSTAYVALSCANLFIGINSSAITFILELFENNRTLLRFNAVLRKLLIVFPHFC 1840
Cdd:TIGR01257 1761 PALVALLMLYGWAVIPMMYPASFLFDVPSTAYVALSCANLFIGINSSAITFVLELFENNRTLLRFNAMLRKLLIVFPHFC 1840
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1841 LGRGLIDLALSQAVTDVYARFGEEHSANPFHWDLIGKNLFAMVVEGVVYFLLTLLVQRHFFLSQWIAEPTKEPIVDEDDD 1920
Cdd:TIGR01257 1841 LGRGLIDLALSQAVTDVYAQFGEEHSANPFQWDLIGKNLVAMAVEGVVYFLLTLLIQHHFFLSRWIAEPAKEPIFDEDDD 1920
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1921 VAEERQRIITGGNKTDILRLHELTKIYPGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAG 2000
Cdd:TIGR01257 1921 VAEERQRIISGGNKTDILRLNELTKVYSGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAG 2000
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2001 KSILTNISEVHQNMGYCPQFDAIDELLTGREHLYLYARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLS 2080
Cdd:TIGR01257 2001 KSILTNISDVHQNMGYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLS 2080
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2081 TAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFRCMGTIQHLKSK 2160
Cdd:TIGR01257 2081 TAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSK 2160
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2161 FGDGYIVTMKIKSPKDDLLPDLNPVEQFFQGNFPGSVQRERHYNMLQFQVSSSSLARIFQLLLSHKDSLLIEEYSVTQTT 2240
Cdd:TIGR01257 2161 FGDGYIVTMKIKSPKDDLLPDLNPVEQFFQGNFPGSVQRERHYNMLQFQVSSSSLARIFQLLISHKDSLLIEEYSVTQTT 2240
|
2250 2260 2270
....*....|....*....|....*....|..
gi 105990541 2241 LDQVFVNFAKQQTESHDLPLHPRAAGASRQAQ 2272
Cdd:TIGR01257 2241 LDQVFVNFAKQQTETYDLPLHPRAAGASRQAK 2272
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1938-2158 |
4.44e-118 |
|
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: 372.61 E-value: 4.44e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1938 LRLHELTKIYPGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISEVHQNMGYC 2017
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2018 PQFDAIDELLTGREHLYLYARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEP 2097
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 105990541 2098 TTGMDPQARRMLWNVIVSiIREGRAVVLTSHSMEECEALCTRLAIMVKGAFRCMGTIQHLK 2158
Cdd:cd03263 161 TSGLDPASRRAIWDLILE-VRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
929-1148 |
5.10e-113 |
|
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: 357.97 E-value: 5.10e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 929 VCVKNLVKIFEPCGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIETSLDAVRQSLGMC 1008
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1009 PQHNILFHHLTVAEHMLFYAQLKGKSQEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEP 1088
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1089 TSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIIAQGRLYCSGTPLFLK 1148
Cdd:cd03263 161 TSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
931-1144 |
4.09e-85 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 278.49 E-value: 4.09e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 931 VKNLVKIFEpcGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIETSLDAVRQSLGMCPQ 1010
Cdd:COG1131 3 VRGLTKRYG--DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1011 HNILFHHLTVAEHMLFYAQLKGKSQEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTS 1090
Cdd:COG1131 81 EPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 105990541 1091 GVDPYSRRSIWDLLLKYRS-GRTIIMSTHHMDEADLLGDRIAIIAQGRLYCSGTP 1144
Cdd:COG1131 161 GLDPEARRELWELLRELAAeGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTP 215
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
1938-2161 |
8.21e-81 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 266.16 E-value: 8.21e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1938 LRLHELTKIYPGTssPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISEVHQNMGYC 2017
Cdd:COG1131 1 IEVRGLTKRYGDK--TALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2018 PQFDAIDELLTGREHLYLYARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEP 2097
Cdd:COG1131 79 PQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 105990541 2098 TTGMDPQARRMLWNVIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFRCMGTIQHLKSKF 2161
Cdd:COG1131 159 TSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARL 222
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
931-1138 |
1.74e-65 |
|
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: 219.58 E-value: 1.74e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 931 VKNLVKIFEpcGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIETSLDAVRQSLGMCPQ 1010
Cdd:cd03230 3 VRNLSKRYG--KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1011 HNILFHHLTVAEHMlfyaqlkgksqeeaqlemeamledtglhhkrneeaqDLSGGMQRKLSVAIAFVGDAKVVILDEPTS 1090
Cdd:cd03230 81 EPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTS 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 105990541 1091 GVDPYSRRSIWDLLLKYRS-GRTIIMSTHHMDEADLLGDRIAIIAQGRL 1138
Cdd:cd03230 125 GLDPESRREFWELLRELKKeGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1942-2158 |
1.82e-64 |
|
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: 218.78 E-value: 1.82e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1942 ELTKIYPGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISEVHQNMGYCPQFD 2021
Cdd:cd03265 5 NLVKKYGDFE--AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIVFQDL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2022 AIDELLTGREHLYLYARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGM 2101
Cdd:cd03265 83 SVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 105990541 2102 DPQARRMLWNVIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFRCMGTIQHLK 2158
Cdd:cd03265 163 DPQTRAHVWEYIEKLKEEfGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
931-1152 |
3.75e-63 |
|
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: 215.88 E-value: 3.75e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 931 VKNLVKIFEpcGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIETSLDAVRQSLGMCPQ 1010
Cdd:COG4555 4 VENLSKKYG--KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGVLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1011 HNILFHHLTVAEHMLFYAQLKGKSQEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTS 1090
Cdd:COG4555 82 ERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 105990541 1091 GVDPYSRRSIWDLLLKYR-SGRTIIMSTHHMDEADLLGDRIAIIAQGRLYCSGTPLFLKNCFG 1152
Cdd:COG4555 162 GLDVMARRLLREILRALKkEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
944-1277 |
3.01e-62 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 215.72 E-value: 3.01e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 944 PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIETSLDAVRQSLGMCPQHNILFHHLTVAEH 1023
Cdd:TIGR01188 7 KAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVRRSIGIVPQYASVDEDLTGREN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1024 MLFYAQLKGKSQEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTSGVDPYSRRSIWDL 1103
Cdd:TIGR01188 87 LEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRAIWDY 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1104 LLKYR-SGRTIIMSTHHMDEADLLGDRIAIIAQGRLYCSGTPLFLKNCFGTGLYLTLVRKMKNIQSQRkgSEGTCSCSSK 1182
Cdd:TIGR01188 167 IRALKeEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKRRLGKDTLESRPRDIQSLKVEV--SMLIAELGET 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1183 GFSTTCpAHVDDltpeqvldgdvnelmDVVLHHVPEAKlvecigqelifllpnknfkhRAYASLFRELEETlaDLGLSSF 1262
Cdd:TIGR01188 245 GLGLLA-VTVDS---------------DRIKILVPDGD--------------------ETVPEIVEAAIRN--GIRIRSI 286
|
330
....*....|....*
gi 105990541 1263 GISDTPLEEIFLKVT 1277
Cdd:TIGR01188 287 STERPSLDDVFLKLT 301
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1938-2146 |
1.40e-58 |
|
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: 199.93 E-value: 1.40e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1938 LRLHELTKIYPGTssPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISEVHQNMGYC 2017
Cdd:cd03230 1 IEVRNLSKRYGKK--TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2018 PQFDAIDELLTGREHLYlyarlrgvpaeeiekvanwsikslgltvyadclagtYSGGNKRKLSTAIALIGCPPLVLLDEP 2097
Cdd:cd03230 79 PEEPSLYENLTVRENLK------------------------------------LSGGMKQRLALAQALLHDPELLILDEP 122
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 105990541 2098 TTGMDPQARRMLWNVIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
Cdd:cd03230 123 TSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNG 171
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
931-1156 |
3.74e-57 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 200.72 E-value: 3.74e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 931 VKNLVKIFEpcGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIEtslDAVRQSLGMCPQ 1010
Cdd:COG4152 4 LKGLTKRFG--DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD---PEDRRRIGYLPE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1011 HNILFHHLTVAEHMLFYAQLKGKSQEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTS 1090
Cdd:COG4152 79 ERGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 105990541 1091 GVDPYSRRSIWDLLLKYR-SGRTIIMSTHHMDEADLLGDRIAIIAQGRLYCSGTPLFLKNCFGTGLY 1156
Cdd:COG4152 159 GLDPVNVELLKDVIRELAaKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQFGRNTL 225
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
931-1148 |
8.21e-57 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 196.82 E-value: 8.21e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 931 VKNLVKIFEpcGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIETSLDAVRQSLGMCPQ 1010
Cdd:cd03265 3 VENLVKKYG--DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1011 HNILFHHLTVAEHMLFYAQLKGKSQEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTS 1090
Cdd:cd03265 81 DLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1091 GVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIIAQGRLYCSGTPLFLK 1148
Cdd:cd03265 161 GLDPQTRAHVWEYIekLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1938-2163 |
2.84e-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: 193.15 E-value: 2.84e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1938 LRLHELTKIYPgtSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISEVHQNMGYC 2017
Cdd:COG4555 2 IEVENLSKKYG--KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2018 PQFDAIDELLTGREHLYLYARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEP 2097
Cdd:COG4555 80 PDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 105990541 2098 TTGMDPQARRMLWNVIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFRCMGTIQHLKSKFGD 2163
Cdd:COG4555 160 TNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGE 225
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
931-1144 |
2.00e-54 |
|
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: 190.24 E-value: 2.00e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 931 VKNLVKIFEPcGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDI-ETSLDAVRQSLGMCP 1009
Cdd:COG1122 3 LENLSFSYPG-GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDItKKNLRELRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1010 QH--NILFhHLTVAEHMLFYAQLKGKSQEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDE 1087
Cdd:COG1122 82 QNpdDQLF-APTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 105990541 1088 PTSGVDPYSRRSIWDLLLKY-RSGRTIIMSTHHMDEADLLGDRIAIIAQGRLYCSGTP 1144
Cdd:COG1122 161 PTAGLDPRGRRELLELLKRLnKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTP 218
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
931-1137 |
1.05e-51 |
|
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: 181.90 E-value: 1.05e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 931 VKNLVKIFEPCGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDI-ETSLDAVRQSLGMCP 1009
Cdd:cd03225 2 LKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLtKLSLKELRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1010 QH--NILFHHlTVAEHMLFYAQLKGKSQEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDE 1087
Cdd:cd03225 82 QNpdDQFFGP-TVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 105990541 1088 PTSGVDPYSRRSIWDLLLKY-RSGRTIIMSTHHMDEADLLGDRIAIIAQGR 1137
Cdd:cd03225 161 PTAGLDPAGRRELLELLKKLkAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
931-1142 |
3.06e-51 |
|
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: 180.47 E-value: 3.06e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 931 VKNLVKIFEpcGRPAVDRLNITFyENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIETSLDAVRQSLGMCPQ 1010
Cdd:cd03264 3 LENLTKRYG--KKRALDGVSLTL-GPGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1011 HNILFHHLTVAEHMLFYAQLKGKSQEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTS 1090
Cdd:cd03264 80 EFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 105990541 1091 GVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIIAQGRLYCSG 1142
Cdd:cd03264 160 GLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
931-1137 |
1.17e-49 |
|
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: 175.93 E-value: 1.17e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 931 VKNLVKIFEPcgRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIEtslDAVRQSLGMCPQ 1010
Cdd:cd03269 3 VENVTKRFGR--VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD---IAARNRIGYLPE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1011 HNILFHHLTVAEHMLFYAQLKGKSQEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTS 1090
Cdd:cd03269 78 ERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFS 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 105990541 1091 GVDPYSRRSIWDLLLKY-RSGRTIIMSTHHMDEADLLGDRIAIIAQGR 1137
Cdd:cd03269 158 GLDPVNVELLKDVIRELaRAGKTVILSTHQMELVEELCDRVLLLNKGR 205
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1935-2146 |
3.71e-48 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 175.38 E-value: 3.71e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1935 TDILRLHELTKIYPGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISEVHQNM 2014
Cdd:PRK13537 5 VAPIDFRNVEKRYGDKL--VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2015 GYCPQFDAIDELLTGREHLYLYARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLL 2094
Cdd:PRK13537 83 GVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 105990541 2095 DEPTTGMDPQARRMLWNVIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
Cdd:PRK13537 163 DEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEG 214
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1937-2152 |
1.26e-47 |
|
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: 170.24 E-value: 1.26e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1937 ILRLHELTKIYPGTSSP--AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISEVHQNM 2014
Cdd:cd03266 1 MITADALTKRFRDVKKTvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2015 GYCPQFDAIDELLTGREHLYLYARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLL 2094
Cdd:cd03266 81 GFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 105990541 2095 DEPTTGMDPQARRMLWNVIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFRCMG 2152
Cdd:cd03266 161 DEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
931-1144 |
1.77e-47 |
|
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: 170.70 E-value: 1.77e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 931 VKNLVKIFEpcGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIeTSLDA---VRQSLGM 1007
Cdd:cd03219 3 VRGLTKRFG--GLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDI-TGLPPheiARLGIGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1008 CPQHNILFHHLTVAEHMLFYAQLKGKS--------QEEAQLEMEAM--LEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFV 1077
Cdd:cd03219 80 TFQIPRLFPELTVLENVMVAAQARTGSglllararREEREARERAEelLERVGLADLADRPAGELSYGQQRRLEIARALA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 105990541 1078 GDAKVVILDEPTSGVDPYSRRSIWDLLLKYR-SGRTIIMSTHHMDEADLLGDRIAIIAQGRLYCSGTP 1144
Cdd:cd03219 160 TDPKLLLLDEPAAGLNPEETEELAELIRELReRGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTP 227
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
931-1130 |
3.42e-47 |
|
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: 168.81 E-value: 3.42e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 931 VKNLVKIFEpcGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIETSLDAVRQSLGMCPQ 1010
Cdd:COG4133 5 AENLSCRRG--ERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYLGH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1011 HNILFHHLTVAEHMLFYAQLKGKSQEEAQLemEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTS 1090
Cdd:COG4133 83 ADGLKPELTVRENLRFWAALYGLRADREAI--DEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFT 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 105990541 1091 GVDPYSRRSIWDLLLKYR-SGRTIIMSTHhmDEADLLGDRI 1130
Cdd:COG4133 161 ALDAAGVALLAELIAAHLaRGGAVLLTTH--QPLELAAARV 199
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
931-1144 |
3.51e-47 |
|
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: 170.60 E-value: 3.51e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 931 VKNLVKIFEpcGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIeTSLDA---VRQSLGM 1007
Cdd:COG0411 7 VRGLTKRFG--GLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDI-TGLPPhriARLGIAR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1008 CPQHNILFHHLTVAEHMLFYAQLKGKS-------------QEEAQLEMEAM--LEDTGLHHKRNEEAQDLSGGMQRKLSV 1072
Cdd:COG0411 84 TFQNPRLFPELTVLENVLVAAHARLGRgllaallrlprarREEREARERAEelLERVGLADRADEPAGNLSYGQQRRLEI 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 105990541 1073 AIAFVGDAKVVILDEPTSGVDPYSRRSIWDLLLKYR--SGRTIIMSTHHMDEADLLGDRIAIIAQGRLYCSGTP 1144
Cdd:COG0411 164 ARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRdeRGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTP 237
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
931-1138 |
3.94e-47 |
|
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: 168.85 E-value: 3.94e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 931 VKNLVKIFEpcGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIeTSLDAVRQSLGMCPQ 1010
Cdd:cd03259 3 LKGLSKTYG--SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV-TGVPPERRNIGMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1011 HNILFHHLTVAEHMLFYAQLKGKSQEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTS 1090
Cdd:cd03259 80 DYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 105990541 1091 GVDPYSRRSIWDLLLKY--RSGRTIIMSTHHMDEADLLGDRIAIIAQGRL 1138
Cdd:cd03259 160 ALDAKLREELREELKELqrELGITTIYVTHDQEEALALADRIAVMNEGRI 209
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1932-2146 |
1.46e-45 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 168.86 E-value: 1.46e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1932 GNKTDI-LRLHELTKIYPGtsSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISEV 2010
Cdd:PRK13536 35 GSMSTVaIDLAGVSKSYGD--KAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2011 HQNMGYCPQFDAIDELLTGREHLYLYARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPP 2090
Cdd:PRK13536 113 RARIGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQ 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 105990541 2091 LVLLDEPTTGMDPQARRMLWNVIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
Cdd:PRK13536 193 LLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAG 248
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
931-1144 |
2.06e-45 |
|
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: 164.60 E-value: 2.06e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 931 VKNLVKIFEpcGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDI----ETSLDAVRQSLG 1006
Cdd:cd03261 3 LRGLTKSFG--GRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDIsglsEAELYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1007 MCPQHNILFHHLTVAEHMLFYAQLKGKSQEEAQLEMEAM-LEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVIL 1085
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFPLREHTRLSEEEIREIVLEkLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLY 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 105990541 1086 DEPTSGVDPYSRRSIWDLLLKYR--SGRTIIMSTHHMDEADLLGDRIAIIAQGRLYCSGTP 1144
Cdd:cd03261 161 DEPTAGLDPIASGVIDDLIRSLKkeLGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTP 221
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
931-1138 |
2.10e-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: 163.54 E-value: 2.10e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 931 VKNLVKIFEpcGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIETSLDAVRQsLGMCPQ 1010
Cdd:cd03268 3 TNDLTKTYG--KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRR-IGALIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1011 HNILFHHLTVAEHMLFYAQLKGKSQEEAqlemEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTS 1090
Cdd:cd03268 80 APGFYPNLTARENLRLLARLLGIRKKRI----DEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTN 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 105990541 1091 GVDPYSRRSIWDLLLKYR-SGRTIIMSTHHMDEADLLGDRIAIIAQGRL 1138
Cdd:cd03268 156 GLDPDGIKELRELILSLRdQGITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
931-1144 |
3.96e-45 |
|
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: 164.00 E-value: 3.96e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 931 VKNLVKIFEpcGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDI----ETSLDAVRQSLG 1006
Cdd:COG1127 8 VRNLTKSFG--DRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDItglsEKELYELRRRIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1007 MCPQHNILFHHLTVAEHMLFY-AQLKGKSQEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVIL 1085
Cdd:COG1127 86 MLFQGGALFDSLTVFENVAFPlREHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILLY 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 105990541 1086 DEPTSGVDPYSRRSIWDLLLKYRS--GRTIIMSTHHMDEADLLGDRIAIIAQGRLYCSGTP 1144
Cdd:COG1127 166 DEPTAGLDPITSAVIDELIRELRDelGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTP 226
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
931-1142 |
5.69e-45 |
|
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: 162.92 E-value: 5.69e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 931 VKNLVKIFEPCGRP--AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIETSLDAVRQSLGMC 1008
Cdd:cd03266 4 ADALTKRFRDVKKTvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLGFV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1009 PQHNILFHHLTVAEHMLFYAQLKGKSQEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEP 1088
Cdd:cd03266 84 SDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 105990541 1089 TSGVDPYSRRSIWDLLLKYRS-GRTIIMSTHHMDEADLLGDRIAIIAQGRLYCSG 1142
Cdd:cd03266 164 TTGLDVMATRALREFIRQLRAlGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
931-1133 |
6.00e-45 |
|
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: 162.64 E-value: 6.00e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 931 VKNLVKIFEPCGRP--AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIEtsldAVRQSLGMC 1008
Cdd:cd03293 3 VRNVSKTYGGGGGAvtALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVT----GPGPDRGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1009 PQHNILFHHLTVAEHMLFYAQLKGKSQEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEP 1088
Cdd:cd03293 79 FQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEP 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 105990541 1089 TSGVDPYSRRSIWDLLLK--YRSGRTIIMSTHHMDEADLLGDRIAII 1133
Cdd:cd03293 159 FSALDALTREQLQEELLDiwRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
942-1144 |
2.14e-44 |
|
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: 162.52 E-value: 2.14e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 942 GRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIET-SLDAVRQSLGMCPQHNILFHHLTV 1020
Cdd:COG1120 13 GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASlSRRELARRIAYVPQEPPAPFGLTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1021 AE--------HMLFYAQLKGKSQEEAqlemEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTSGV 1092
Cdd:COG1120 93 RElvalgrypHLGLFGRPSAEDREAV----EEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 105990541 1093 DPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIIAQGRLYCSGTP 1144
Cdd:COG1120 169 DLAHQLEVLELLrrLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPP 222
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
1938-2146 |
6.30e-44 |
|
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: 159.30 E-value: 6.30e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1938 LRLHELTKIYPGtsSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNIsEVHQNMGYC 2017
Cdd:cd03268 1 LKTNDLTKTYGK--KRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNI-EALRRIGAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2018 PQFDAIDELLTGREHLYLYARLRGVPAEEIEKVanwsIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEP 2097
Cdd:cd03268 78 IEAPGFYPNLTARENLRLLARLLGIRKKRIDEV----LDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEP 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 105990541 2098 TTGMDPQARRMLWNVIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
Cdd:cd03268 154 TNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKG 202
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1937-2254 |
2.21e-43 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 161.04 E-value: 2.21e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1937 ILRLHELTKIYPGTssPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIltnISEVHQNMGY 2016
Cdd:COG4152 1 MLELKGLTKRFGDK--TAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPL---DPEDRRRIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2017 CPqfdaiDE--L---LTGREHLYLYARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPL 2091
Cdd:COG4152 76 LP-----EErgLypkMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPEL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2092 VLLDEPTTGMDPQARRMLWNVIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFRCMGTIQHLKSKFGdGYIVTMKI 2171
Cdd:COG4152 151 LILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQFG-RNTLRLEA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2172 KSPKDDLLpdlnpveqffqgNFPGSVQRERHYNMLQFQVSSSSLAR-IFQLLLSHKDsllIEEYSVTQTTLDQVFVNFAK 2250
Cdd:COG4152 230 DGDAGWLR------------ALPGVTVVEEDGDGAELKLEDGADAQeLLRALLARGP---VREFEEVRPSLNEIFIEVVG 294
|
....
gi 105990541 2251 QQTE 2254
Cdd:COG4152 295 EKAE 298
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
927-1132 |
3.16e-43 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 159.10 E-value: 3.16e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 927 PGVCVKNLVKIFEPCG--RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIEtsldAVRQS 1004
Cdd:COG1116 6 PALELRGVSKRFPTGGggVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVT----GPGPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1005 LGMCPQHNILFHHLTVAEHMLFYAQLKGKSQEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVI 1084
Cdd:COG1116 82 RGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 105990541 1085 LDEPTSGVDPYSRRSIWDLLLKY--RSGRTIIMSTHHMDEADLLGDRIAI 1132
Cdd:COG1116 162 MDEPFGALDALTRERLQDELLRLwqETGKTVLFVTHDVDEAVFLADRVVV 211
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
932-1144 |
5.57e-43 |
|
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: 157.85 E-value: 5.57e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 932 KNLVKIFePCGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIeTSLDAV--RQSLGMCP 1009
Cdd:cd03295 4 ENVTKRY-GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDI-REQDPVelRRKIGYVI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1010 QHNILFHHLTVAEHMLFYAQLKGKSQEEAQLEMEAMLEDTGL--HHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDE 1087
Cdd:cd03295 82 QQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLLMDE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 105990541 1088 PTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIIAQGRLYCSGTP 1144
Cdd:cd03295 162 PFGALDPITRDQLQEEFkrLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTP 220
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1938-2128 |
9.27e-43 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 156.10 E-value: 9.27e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1938 LRLHELTKIYPGTssPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISEVHQNMGYC 2017
Cdd:COG4133 3 LEAENLSCRRGER--LLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2018 PQFDAIDELLTGREHLYLYARLRGVPA--EEIEKVanwsIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLD 2095
Cdd:COG4133 81 GHADGLKPELTVRENLRFWAALYGLRAdrEAIDEA----LEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLD 156
|
170 180 190
....*....|....*....|....*....|...
gi 105990541 2096 EPTTGMDPQARRMLWNVIVSIIREGRAVVLTSH 2128
Cdd:COG4133 157 EPFTALDAAGVALLAELIAAHLARGGAVLLTTH 189
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
931-1138 |
2.53e-42 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 154.96 E-value: 2.53e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 931 VKNLVKIFEPCGR--PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDI----ETSLDAVR-Q 1003
Cdd:cd03255 3 LKNLSKTYGGGGEkvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDIsklsEKELAAFRrR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1004 SLGMCPQHNILFHHLTVAEHMLFYAQLKGKSQEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVV 1083
Cdd:cd03255 83 HIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPKII 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 105990541 1084 ILDEPTSGVDPYSRRSIWDLLLKYR--SGRTIIMSTHHMDEADlLGDRIAIIAQGRL 1138
Cdd:cd03255 163 LADEPTGNLDSETGKEVMELLRELNkeAGTTIVVVTHDPELAE-YADRIIELRDGKI 218
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
927-1144 |
9.42e-42 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 157.95 E-value: 9.42e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 927 PGVCVKNLVKIFEpcGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIeTSLDAVRQSLG 1006
Cdd:COG3842 4 PALELENVSKRYG--DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDV-TGLPPEKRNVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1007 MCPQHNILFHHLTVAEHMLFYAQLKGKSQEEAQLEMEAMLEDTGLHHKRNEEAQDLSGG-MQRklsVAIA--FVGDAKVV 1083
Cdd:COG3842 81 MVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGqQQR---VALAraLAPEPRVL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 105990541 1084 ILDEPTSGVDPYSRRSIWDLLLKY--RSGRTIIMSTHHMDEADLLGDRIAIIAQGRLYCSGTP 1144
Cdd:COG3842 158 LLDEPLSALDAKLREEMREELRRLqrELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTP 220
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
931-1144 |
1.47e-41 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 161.99 E-value: 1.47e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 931 VKNLVKIFEPCGR---PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIET----SLDAVRQ 1003
Cdd:COG1123 263 VRNLSKRYPVRGKggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKlsrrSLRELRR 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1004 SLGMCPQH--NILFHHLTVAEHMLF-YAQLKGKSQEEAQLEMEAMLEDTGLhhkrNEEAQD-----LSGGMQRKLSVAIA 1075
Cdd:COG1123 343 RVQMVFQDpySSLNPRMTVGDIIAEpLRLHGLLSRAERRERVAELLERVGL----PPDLADrypheLSGGQRQRVAIARA 418
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 105990541 1076 FVGDAKVVILDEPTSGVDPYSRRSIWDLLLKYR--SGRTIIMSTHHMDEADLLGDRIAIIAQGRLYCSGTP 1144
Cdd:COG1123 419 LALEPKLLILDEPTSALDVSVQAQILNLLRDLQreLGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPT 489
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
944-1144 |
1.65e-41 |
|
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: 152.97 E-value: 1.65e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 944 PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIeTSLDA---VRQSLGMCPQHNILFHHLTV 1020
Cdd:cd03224 14 QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDI-TGLPPherARAGIGYVPEGRRIFPELTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1021 AEHMLFYAQLKGKSQEEAQLE-MEAMLEDtgLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTSGVDPYSRRS 1099
Cdd:cd03224 93 EENLLLGAYARRRAKRKARLErVYELFPR--LKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEE 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 105990541 1100 IWDLLLKYR-SGRTIIMSTHHMDEADLLGDRIAIIAQGRLYCSGTP 1144
Cdd:cd03224 171 IFEAIRELRdEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTA 216
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1938-2149 |
1.77e-41 |
|
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: 152.35 E-value: 1.77e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1938 LRLHELTKIYPGTSspAVD----RLCVGVrpgecFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISEVHQN 2013
Cdd:cd03264 1 LQLENLTKRYGKKR--ALDgvslTLGPGM-----YGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2014 MGYCPQFDAIDELLTGREHLYLYARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVL 2093
Cdd:cd03264 74 IGYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILI 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 105990541 2094 LDEPTTGMDPQARRMLWNVIVSiIREGRAVVLTSHSMEECEALCTRLAIMVKGAFR 2149
Cdd:cd03264 154 VDEPTAGLDPEERIRFRNLLSE-LGEDRIVILSTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
930-1137 |
1.93e-41 |
|
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: 150.09 E-value: 1.93e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 930 CVKNLVKIFEpcGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIET-SLDAVRQSLGMC 1008
Cdd:cd00267 1 EIENLSFRYG--GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKlPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1009 PQhnilfhhltvaehmlfyaqlkgksqeeaqlemeamledtglhhkrneeaqdLSGGMQRKLSVAIAFVGDAKVVILDEP 1088
Cdd:cd00267 79 PQ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEP 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 105990541 1089 TSGVDPYSRRSIWDLLLKY-RSGRTIIMSTHHMDEADLLGDRIAIIAQGR 1137
Cdd:cd00267 108 TSGLDPASRERLLELLRELaEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
946-1090 |
4.27e-41 |
|
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: 148.95 E-value: 4.27e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 946 VDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDI-ETSLDAVRQSLGMCPQHNILFHHLTVAEHM 1024
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLtDDERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1025 LFYAQLKGKSQEEAQLEMEAMLEDTGLHHKRNEEAQD----LSGGMQRKLSVAIAFVGDAKVVILDEPTS 1090
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVGErpgtLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
892-1144 |
7.08e-41 |
|
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: 161.09 E-value: 7.08e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 892 RALEKTEPLTEETEDPEHPEGihdsfferehpgwVPGVCVKNLVKIFEPCGRPAVDRLNITFYENQITAFLGHNGAGKTT 971
Cdd:COG4987 310 NELLDAPPAVTEPAEPAPAPG-------------GPSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKST 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 972 TLSILTGLLPPTSGTVLVGGRDIET-SLDAVRQSLGMCPQHNILFHHlTVAEHMLFyAqlKGKSQEEaqlEMEAMLEDTG 1050
Cdd:COG4987 377 LLALLLRFLDPQSGSITLGGVDLRDlDEDDLRRRIAVVPQRPHLFDT-TLRENLRL-A--RPDATDE---ELWAALERVG 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1051 LHH----KRN-------EEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHH 1119
Cdd:COG4987 450 LGDwlaaLPDgldtwlgEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHR 529
|
250 260
....*....|....*....|....*
gi 105990541 1120 MDEADlLGDRIAIIAQGRLYCSGTP 1144
Cdd:COG4987 530 LAGLE-RMDRILVLEDGRIVEQGTH 553
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
931-1138 |
1.38e-40 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 150.58 E-value: 1.38e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 931 VKNLVKIFePCG---RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDI----ETSLDAVR- 1002
Cdd:COG1136 7 LRNLTKSY-GTGegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDIsslsERELARLRr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1003 QSLGMCPQ-HNiLFHHLTVAEHMLFYAQLKGKSQEEAQLEMEAMLEDTGLHHKRNEEAQDLSGG-MQRklsVAIA--FVG 1078
Cdd:COG1136 86 RHIGFVFQfFN-LLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGqQQR---VAIAraLVN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 105990541 1079 DAKVVILDEPTSGVDPYSRRSIWDLLLKY--RSGRTIIMSTHHMDEADlLGDRIAIIAQGRL 1138
Cdd:COG1136 162 RPKLILADEPTGNLDSKTGEEVLELLRELnrELGTTIVMVTHDPELAA-RADRVIRLRDGRI 222
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
942-1144 |
5.47e-40 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 149.47 E-value: 5.47e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 942 GRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIEtsldAVRQSLGMCPQHNILFHH--LT 1019
Cdd:COG1121 18 GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPR----RARRRIGYVPQRAEVDWDfpIT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1020 VAE--HMLFYAQ---LKGKSQEEAQLEMEAmLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTSGVDP 1094
Cdd:COG1121 94 VRDvvLMGRYGRrglFRRPSRADREAVDEA-LERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDA 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 105990541 1095 YSRRSIWDLLLKYRS-GRTIIMSTHHMDEADLLGDRIAIIAqGRLYCSGTP 1144
Cdd:COG1121 173 ATEEALYELLRELRReGKTILVVTHDLGAVREYFDRVLLLN-RGLVAHGPP 222
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1939-2146 |
9.90e-40 |
|
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: 147.61 E-value: 9.90e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1939 RLHELTKIYPGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIL-TNISEVHQNMGYC 2017
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTkLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2018 PQF--------DAIDELLTGREHLylyarlrGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCP 2089
Cdd:cd03225 81 FQNpddqffgpTVEEEVAFGLENL-------GLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 105990541 2090 PLVLLDEPTTGMDPQARRMLWNVIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
Cdd:cd03225 154 DILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
923-1144 |
1.02e-39 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 150.73 E-value: 1.02e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 923 PGWVPGVCVKNLVKIFEPcgRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIETSLDAVR 1002
Cdd:PRK13537 2 PMSVAPIDFRNVEKRYGD--KLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1003 QSLGMCPQHNILFHHLTVAEHMLFYAQLKGKSQEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKV 1082
Cdd:PRK13537 80 QRVGVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 105990541 1083 VILDEPTSGVDPYSRRSIWDLLlkyRS----GRTIIMSTHHMDEADLLGDRIAIIAQGRLYCSGTP 1144
Cdd:PRK13537 160 LVLDEPTTGLDPQARHLMWERL---RSllarGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAP 222
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
931-1137 |
1.41e-39 |
|
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: 145.79 E-value: 1.41e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 931 VKNLVKIFEpcGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIETSLDAV---RQSLGM 1007
Cdd:cd03229 3 LKNVSKRYG--QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELpplRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1008 CPQHNILFHHLTVAEHMLFyaqlkgksqeeaqlemeamledtglhhkrneeaqDLSGGMQRKLSVAIAFVGDAKVVILDE 1087
Cdd:cd03229 81 VFQDFALFPHLTVLENIAL----------------------------------GLSGGQQQRVALARALAMDPDVLLLDE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 105990541 1088 PTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIIAQGR 1137
Cdd:cd03229 127 PTSALDPITRREVRALLksLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1938-2146 |
1.73e-39 |
|
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: 146.66 E-value: 1.73e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1938 LRLHELTKIYpGTSSpAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTnisEVHQNMGYC 2017
Cdd:cd03269 1 LEVENVTKRF-GRVT-ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDI---AARNRIGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2018 PQFDAIDELLTGREHLYLYARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEP 2097
Cdd:cd03269 76 PEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEP 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 105990541 2098 TTGMDPQARRMLWNVIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
Cdd:cd03269 156 FSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKG 204
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
942-1144 |
2.10e-39 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 151.14 E-value: 2.10e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 942 GRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIETSLDAVRQSLGMCPQHNILFHHLTVA 1021
Cdd:PRK13536 53 DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARARIGVVPQFDNLDLEFTVR 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1022 EHMLFYAQLKGKSQEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTSGVDPYSRRSIW 1101
Cdd:PRK13536 133 ENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIW 212
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 105990541 1102 DLLlkyRS----GRTIIMSTHHMDEADLLGDRIAIIAQGRLYCSGTP 1144
Cdd:PRK13536 213 ERL---RSllarGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRP 256
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
929-1137 |
5.57e-39 |
|
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: 143.68 E-value: 5.57e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 929 VCVKNLVKIFEPCGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIET-SLDAVRQSLGM 1007
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDlDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1008 CPQHNILFhHLTVAEHMlfyaqlkgksqeeaqlemeamledtglhhkrneeaqdLSGGMQRKLSVAIAFVGDAKVVILDE 1087
Cdd:cd03228 81 VPQDPFLF-SGTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 105990541 1088 PTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADlLGDRIAIIAQGR 1137
Cdd:cd03228 123 ATSALDPETEALILEALRALAKGKTVIVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
931-1143 |
8.01e-39 |
|
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: 145.80 E-value: 8.01e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 931 VKNLVKIFEPCGR--PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDI----ETSLDAVRQS 1004
Cdd:cd03258 4 LKNVSKVFGDTGGkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLtllsGKELRKARRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1005 LGMCPQHNILFHHLTVAEHMLFYAQLKGKSQEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVI 1084
Cdd:cd03258 84 IGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 105990541 1085 LDEPTSGVDPYSRRSIWDLLLKY--RSGRTIIMSTHHMDEADLLGDRIAIIAQGRLYCSGT 1143
Cdd:cd03258 164 CDEATSALDPETTQSILALLRDInrELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGT 224
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
942-1142 |
2.37e-38 |
|
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: 142.19 E-value: 2.37e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 942 GRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIETsldavrqslgmcpqhnilFHHLTVA 1021
Cdd:cd03214 11 GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLAS------------------LSPKELA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1022 EHMLFYAQlkgksqeeaqlemeaMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTSGVDPYSRRSIW 1101
Cdd:cd03214 73 RKIAYVPQ---------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELL 137
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 105990541 1102 DLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIIAQGRLYCSG 1142
Cdd:cd03214 138 ELLrrLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
903-1144 |
3.34e-38 |
|
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: 152.99 E-value: 3.34e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 903 ETEDPEHPEGIHDSFFEREhpgwvPGVCVKNLVkIFEPCGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPP 982
Cdd:COG4988 316 DAPEPAAPAGTAPLPAAGP-----PSIELEDVS-FSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPP 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 983 TSGTVLVGGRDIET-SLDAVRQSLGMCPQHNILFHhLTVAEHMLFYAQLKGKSQ-----EEAQL-EMEAMLEDtGLHHKR 1055
Cdd:COG4988 390 YSGSILINGVDLSDlDPASWRRQIAWVPQNPYLFA-GTIRENLRLGRPDASDEEleaalEAAGLdEFVAALPD-GLDTPL 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1056 NEEAQDLSGG-MQRkLSVAIAFVGDAKVVILDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADlLGDRIAIIA 1134
Cdd:COG4988 468 GEGGRGLSGGqAQR-LALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLA-QADRILVLD 545
|
250
....*....|
gi 105990541 1135 QGRLYCSGTP 1144
Cdd:COG4988 546 DGRIVEQGTH 555
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
931-1144 |
3.91e-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: 143.45 E-value: 3.91e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 931 VKNLVKIFEpcGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIETSLDAVRQSLGMC-- 1008
Cdd:cd03218 3 AENLSKRYG--KRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLGIGyl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1009 PQHNILFHHLTVAEHMLFYAQLKGKSQEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEP 1088
Cdd:cd03218 81 PQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 105990541 1089 TSGVDPYSRRSIWDLLLKYR-SGRTIIMSTHHMDEADLLGDRIAIIAQGRLYCSGTP 1144
Cdd:cd03218 161 FAGVDPIAVQDIQKIIKILKdRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTP 217
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
929-1145 |
5.45e-38 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 147.14 E-value: 5.45e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 929 VCVKNLVKIFEpcGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIeTSLDAVRQSLGMC 1008
Cdd:COG3839 4 LELENVSKSYG--GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDV-TDLPPKDRNIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1009 PQHNILFHHLTVAEHMLFYAQLKGKSQEEAQLEMEAMLEDTGLHHKRNEEAQDLSGG-MQRklsVAI--AFVGDAKVVIL 1085
Cdd:COG3839 81 FQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGqRQR---VALgrALVREPKVFLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 105990541 1086 DEPTSGVDPYSRRSIWDLLLKY--RSGRTIIMSTHHMDEADLLGDRIAIIAQGRLYCSGTPL 1145
Cdd:COG3839 158 DEPLSNLDAKLRVEMRAEIKRLhrRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPE 219
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
931-1144 |
8.39e-38 |
|
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: 143.94 E-value: 8.39e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 931 VKNLVKIFEPCGRPAVDRL--------------------NITF--YENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVL 988
Cdd:cd03294 3 IKGLYKIFGKNPQKAFKLLakgkskeeilkktgqtvgvnDVSLdvREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 989 VGGRDI----ETSLDAVR-QSLGMCPQHNILFHHLTVAEHMLFYAQLKG-KSQEEAQLEMEAmLEDTGLHHKRNEEAQDL 1062
Cdd:cd03294 83 IDGQDIaamsRKELRELRrKKISMVFQSFALLPHRTVLENVAFGLEVQGvPRAEREERAAEA-LELVGLEGWEHKYPDEL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1063 SGGMQRKLSVAIAFVGDAKVVILDEPTSGVDPYSRRSIWDLLLKYRS--GRTIIMSTHHMDEADLLGDRIAIIAQGRLYC 1140
Cdd:cd03294 162 SGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAelQKTIVFITHDLDEALRLGDRIAIMKDGRLVQ 241
|
....
gi 105990541 1141 SGTP 1144
Cdd:cd03294 242 VGTP 245
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
931-1144 |
9.24e-38 |
|
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: 142.38 E-value: 9.24e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 931 VKNLVKIFEpcGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIeTSLDAVRQSLGMCPQ 1010
Cdd:cd03300 3 LENVSKFYG--GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI-TNLPPHKRPVNTVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1011 HNILFHHLTVAEHMLFYAQLKGKSQEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTS 1090
Cdd:cd03300 80 NYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLG 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 105990541 1091 GVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIIAQGRLYCSGTP 1144
Cdd:cd03300 160 ALDLKLRKDMQLELkrLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTP 215
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
945-1138 |
2.18e-37 |
|
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: 141.16 E-value: 2.18e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLP-----PTSGTVLVGGRDI---ETSLDAVRQSLGMCPQHNILFH 1016
Cdd:cd03260 15 ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIydlDVDVLELRRRVGMVFQKPNPFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1017 hLTVAEHMLFYAQLKG-KSQEEAQLEMEAMLEDTGLHH--KRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTSGVD 1093
Cdd:cd03260 95 -GSIYDNVAYGLRLHGiKLKEELDERVEEALRKAALWDevKDRLHALGLSGGQQQRLCLARALANEPEVLLLDEPTSALD 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 105990541 1094 PYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIIAQGRL 1138
Cdd:cd03260 174 PISTAKIEELIAELKKEYTIVIVTHNMQQAARVADRTAFLLNGRL 218
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
931-1144 |
3.11e-37 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 141.32 E-value: 3.11e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 931 VKNLVKIFEpcGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIeTSLD----AvRQSLG 1006
Cdd:COG1137 6 AENLVKSYG--KRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDI-THLPmhkrA-RLGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1007 MCPQHNILFHHLTVAEHMLFYAQLKGKSQEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILD 1086
Cdd:COG1137 82 YLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 105990541 1087 EPTSGVDPYSRRSIWDLL--LKYRsGRTIIMSTHHMDEAdlLG--DRIAIIAQGRLYCSGTP 1144
Cdd:COG1137 162 EPFAGVDPIAVADIQKIIrhLKER-GIGVLITDHNVRET--LGicDRAYIISEGKVLAEGTP 220
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1938-2146 |
4.31e-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: 140.55 E-value: 4.31e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1938 LRLHELTKIYPGtSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIL-TNISEVHQNMGY 2016
Cdd:COG1122 1 IELENLSFSYPG-GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITkKNLRELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2017 CPQ------FDAI--DELLTGREHLylyarlrGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGC 2088
Cdd:COG1122 80 VFQnpddqlFAPTveEDVAFGPENL-------GLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAME 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 105990541 2089 PPLVLLDEPTTGMDPQARRMLWNVIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
Cdd:COG1122 153 PEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDG 210
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
927-1144 |
5.33e-37 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 148.13 E-value: 5.33e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 927 PGVCVKNLVKIFEPCGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPT---SGTVLVGGRDIETSLDAVR- 1002
Cdd:COG1123 3 PLLEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1003 QSLGMCPQH-NILFHHLTVAEHMLFYAQLKGKSQEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAK 1081
Cdd:COG1123 83 RRIGMVFQDpMTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 105990541 1082 VVILDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIIAQGRLYCSGTP 1144
Cdd:COG1123 163 LLIADEPTTALDVTTQAEILDLLreLQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPP 227
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
932-1138 |
7.47e-37 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 139.42 E-value: 7.47e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 932 KNLVKIFEPcGRPAVDRLNITFYENQItAFL-GHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIET----SLDAVRQSLG 1006
Cdd:COG2884 5 ENVSKRYPG-GREALSDVSLEIEKGEF-VFLtGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRlkrrEIPYLRRRIG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1007 MCPQHNILFHHLTVAEHMLFYAQLKGKSQEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILD 1086
Cdd:COG2884 83 VVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLAD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 105990541 1087 EPTSGVDPYSRRSIWDLLLKY-RSGRTIIMSTHHMDEADLLGDRIAIIAQGRL 1138
Cdd:COG2884 163 EPTGNLDPETSWEIMELLEEInRRGTTVLIATHDLELVDRMPKRVLELEDGRL 215
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
931-1144 |
2.21e-36 |
|
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: 138.95 E-value: 2.21e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 931 VKNLVKIFEpcGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIeTSL---DAVRQSLGM 1007
Cdd:TIGR04406 4 AENLIKSYK--KRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDI-THLpmhERARLGIGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1008 CPQHNILFHHLTVAEHMLFYAQLKGK-SQEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILD 1086
Cdd:TIGR04406 81 LPQEASIFRKLTVEENIMAVLEIRKDlDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 105990541 1087 EPTSGVDPYSRRSIWDLLLKYRS-GRTIIMSTHHMDEADLLGDRIAIIAQGRLYCSGTP 1144
Cdd:TIGR04406 161 EPFAGVDPIAVGDIKKIIKHLKErGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTP 219
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
938-1138 |
6.66e-36 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 136.48 E-value: 6.66e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 938 FEPCGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIET-SLDAVRQSLGMCPQHNILFH 1016
Cdd:COG4619 8 FRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAmPPPEWRRQVAYVPQEPALWG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1017 HlTVAEHMLFYAQLKGKSQEEAqlEMEAMLEDTGLHHK-RNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTSGVDPY 1095
Cdd:COG4619 88 G-TVRDNLPFPFQLRERKFDRE--RALELLERLGLPPDiLDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPE 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 105990541 1096 SRRSIWDLLLKYR--SGRTIIMSTHHMDEADLLGDRIAIIAQGRL 1138
Cdd:COG4619 165 NTRRVEELLREYLaeEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
931-1136 |
6.94e-36 |
|
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: 136.23 E-value: 6.94e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 931 VKNLVKIFEPCGRpAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIetSLDAVRQSLGMCPQ 1010
Cdd:cd03226 2 IENISFSYKKGTE-ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI--KAKERRKSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1011 HniLFHHL---TVAEHMLFYAQLKGKSQEEAqlemEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDE 1087
Cdd:cd03226 79 D--VDYQLftdSVREELLLGLKELDAGNEQA----ETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 105990541 1088 PTSGVDPYSRRSIWDLLLK-YRSGRTIIMSTHHMDEADLLGDRIAIIAQG 1136
Cdd:cd03226 153 PTSGLDYKNMERVGELIRElAAQGKAVIVITHDYEFLAKVCDRVLLLANG 202
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
942-1142 |
1.22e-35 |
|
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: 135.74 E-value: 1.22e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 942 GRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIETSldavRQSLGMCPQH-NILFHH-LT 1019
Cdd:cd03235 11 GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE----RKRIGYVPQRrSIDRDFpIS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1020 VAE--------HMLFyaqLKGKSQEEAQLEMEAmLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTSG 1091
Cdd:cd03235 87 VRDvvlmglygHKGL---FRRLSKADKAKVDEA-LERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAG 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 105990541 1092 VDPYSRRSIWDLLLKYRS-GRTIIMSTHHMDEADLLGDRIAIIAqGRLYCSG 1142
Cdd:cd03235 163 VDPKTQEDIYELLRELRReGMTILVVTHDLGLVLEYFDRVLLLN-RTVVASG 213
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
931-1144 |
4.95e-35 |
|
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: 135.00 E-value: 4.95e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 931 VKNLVKIFePCGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIET----SLDAVRQSLG 1006
Cdd:cd03256 3 VENLSKTY-PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKlkgkALRQLRRQIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1007 MCPQHNILFHHLTVAEHML---------FYAQLKGKSQEEAQLEMEAmLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFV 1077
Cdd:cd03256 82 MIFQQFNLIERLSVLENVLsgrlgrrstWRSLFGLFPKEEKQRALAA-LERVGLLDKAYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 105990541 1078 GDAKVVILDEPTSGVDPYSRRSIWDLLLKYRS--GRTIIMSTHHMDEADLLGDRIAIIAQGRLYCSGTP 1144
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQVMDLLKRINReeGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPP 229
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
945-1144 |
4.96e-35 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 146.42 E-value: 4.96e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVL-----VGGRDIETsldavRQSLGMCPQHNILFHHLT 1019
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWlfgqpVDAGDIAT-----RRRVGYMSQAFSLYGELT 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1020 VAEHMLFYAQLKGKSQEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTSGVDPYSRRS 1099
Cdd:NF033858 356 VRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDM 435
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 105990541 1100 IWDLL--LKYRSGRTIIMSTHHMDEAdLLGDRIAIIAQGRLYCSGTP 1144
Cdd:NF033858 436 FWRLLieLSREDGVTIFISTHFMNEA-ERCDRISLMHAGRVLASDTP 481
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
931-1138 |
8.71e-35 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 133.79 E-value: 8.71e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 931 VKNLVKIFEPCGRP--AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIeTSLDAVRQSL--- 1005
Cdd:cd03257 4 VKNLSVSFPTGGGSvkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDL-LKLSRRLRKIrrk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1006 --GMCPQH--NILFHHLTVAEHML--FYAQLKGKSQEEAQLEMEAMLEDTGLHHKR-NEEAQDLSGGMQRKLSVAIAFVG 1078
Cdd:cd03257 83 eiQMVFQDpmSSLNPRMTIGEQIAepLRIHGKLSKKEARKEAVLLLLVGVGLPEEVlNRYPHELSGGQRQRVAIARALAL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 105990541 1079 DAKVVILDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIIAQGRL 1138
Cdd:cd03257 163 NPKLLIADEPTSALDVSVQAQILDLLkkLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1939-2146 |
8.93e-35 |
|
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: 131.21 E-value: 8.93e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1939 RLHELTKIYPGtsSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTN-ISEVHQNMGYC 2017
Cdd:cd00267 1 EIENLSFRYGG--RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLpLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2018 PQFdaidelltgrehlylyarlrgvpaeeiekvanwsikslgltvyadclagtySGGNKRKLSTAIALIGCPPLVLLDEP 2097
Cdd:cd00267 79 PQL---------------------------------------------------SGGQRQRVALARALLLNPDLLLLDEP 107
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 105990541 2098 TTGMDPQARRMLWNVIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
Cdd:cd00267 108 TSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
931-1144 |
2.08e-34 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 136.43 E-value: 2.08e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 931 VKNLVKIFEpcGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIETSLDAVRQSLGMCPQ 1010
Cdd:COG1118 5 VRNISKRFG--SFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLPPRERRVGFVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1011 HNILFHHLTVAEHMLFYAQLKGKSQEEAQLEMEAMLED---TGLHHKRneEAQdLSGGM-QRklsVAIA--FVGDAKVVI 1084
Cdd:COG1118 83 HYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELvqlEGLADRY--PSQ-LSGGQrQR---VALAraLAVEPEVLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 105990541 1085 LDEPTSGVDPYSRRSIWDLLLKY--RSGRTIIMSTHHMDEADLLGDRIAIIAQGRLYCSGTP 1144
Cdd:COG1118 157 LDEPFGALDAKVRKELRRWLRRLhdELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTP 218
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
932-1138 |
2.56e-34 |
|
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: 132.15 E-value: 2.56e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 932 KNLVKIFePCGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDI----ETSLDAVRQSLGM 1007
Cdd:cd03292 4 INVTKTY-PNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVsdlrGRAIPYLRRKIGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1008 CPQHNILFHHLTVAEHMLFYAQLKGKSQEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDE 1087
Cdd:cd03292 83 VFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 105990541 1088 PTSGVDPYSRRSIWDLLLKY-RSGRTIIMSTHHMDEADLLGDRIAIIAQGRL 1138
Cdd:cd03292 163 PTGNLDPDTTWEIMNLLKKInKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
949-1140 |
3.30e-34 |
|
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: 132.01 E-value: 3.30e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPP---TSGTVLVGGRdiETSLDAVRQSLGMCPQHNILFHHLTVAEHML 1025
Cdd:cd03234 26 VSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQ--PRKPDQFQKCVAYVRQDDILLPGLTVRETLT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1026 FYAQLK-GKSQEEAQLEMEA---MLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTSGVDPYSRRSIW 1101
Cdd:cd03234 104 YTAILRlPRKSSDAIRKKRVedvLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLV 183
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 105990541 1102 DLLLKY-RSGRTIIMSTHHmDEADL--LGDRIAIIAQGRL-YC 1140
Cdd:cd03234 184 STLSQLaRRNRIVILTIHQ-PRSDLfrLFDRILLLSSGEIvYS 225
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
940-1148 |
5.49e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 133.61 E-value: 5.49e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 940 PCGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDI-----ETSLDAVRQSLGMC---PQH 1011
Cdd:PRK13634 17 PFERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkkNKKLKPLRKKVGIVfqfPEH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1012 NiLFHHlTVAEHMLFYAQLKGKSQEEAQLEMEAMLEDTGLHHKRNEEAQ-DLSGGMQRKlsVAIAFV--GDAKVVILDEP 1088
Cdd:PRK13634 97 Q-LFEE-TVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEELLARSPfELSGGQMRR--VAIAGVlaMEPEVLVLDEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 105990541 1089 TSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIIAQGRLYCSGTP--LFLK 1148
Cdd:PRK13634 173 TAGLDPKGRKEMMEMFykLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPreIFAD 236
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1938-2153 |
1.43e-33 |
|
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: 130.63 E-value: 1.43e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1938 LRLHELTKIYPGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT---------NIS 2008
Cdd:cd03219 1 LEVRGLTKRFGGLV--ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGlppheiarlGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2009 EVHQNMGYCPQFDAIDELLTG----REHLYLYARLRGVPAEEIEKVANWsIKSLGLTVYADCLAGTYSGGNKRKLSTAIA 2084
Cdd:cd03219 79 RTFQIPRLFPELTVLENVMVAaqarTGSGLLLARARREEREARERAEEL-LERVGLADLADRPAGELSYGQQRRLEIARA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 105990541 2085 LIGCPPLVLLDEPTTGMDPQARRMLWNVIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFRCMGT 2153
Cdd:cd03219 158 LATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGT 226
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
929-1138 |
1.51e-33 |
|
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: 129.68 E-value: 1.51e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 929 VCVKNLVKIFEpcGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIeTSLDAVRQSLGMC 1008
Cdd:cd03301 1 VELENVTKRFG--NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDV-TDLPPKDRDIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1009 PQHNILFHHLTVAEHMLFYAQLKGKSQEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEP 1088
Cdd:cd03301 78 FQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 105990541 1089 TSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIIAQGRL 1138
Cdd:cd03301 158 LSNLDAKLRVQMRAELkrLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
944-1144 |
1.62e-33 |
|
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: 130.49 E-value: 1.62e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 944 PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIeTSLDA---VRQSLGMCPQHNILFHHLTV 1020
Cdd:COG0410 17 HVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDI-TGLPPhriARLGIGYVPEGRRIFPSLTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1021 AEHMLFYAQLKGKSQEEAQlEMEAMLE---DtgLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTSGVDPYSR 1097
Cdd:COG0410 96 EENLLLGAYARRDRAEVRA-DLERVYElfpR--LKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIV 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 105990541 1098 RSIWDLL--LKyRSGRTIIMSTHHMDEADLLGDRIAIIAQGRLYCSGTP 1144
Cdd:COG0410 173 EEIFEIIrrLN-REGVTILLVEQNARFALEIADRAYVLERGRIVLEGTA 220
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
893-1161 |
3.28e-33 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 139.58 E-value: 3.28e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 893 ALEKTEPLTEEteDPEHPEGIHDSFFEREHPGwvpgVCVKNLVKIFEPCGRPAVDRLNITFYENQITAFLGHNGAGKTTT 972
Cdd:COG2274 444 ALERLDDILDL--PPEREEGRSKLSLPRLKGD----IELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTL 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 973 LSILTGLLPPTSGTVLVGGRDIET-SLDAVRQSLGMCPQHNILFHHlTVAEHMLFYAQlkGKSQEEAQ--LEMEAMLEDT 1049
Cdd:COG2274 518 LKLLLGLYEPTSGRILIDGIDLRQiDPASLRRQIGVVLQDVFLFSG-TIRENITLGDP--DATDEEIIeaARLAGLHDFI 594
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1050 -----GLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEAD 1124
Cdd:COG2274 595 ealpmGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIR 674
|
250 260 270
....*....|....*....|....*....|....*....
gi 105990541 1125 LLgDRIAIIAQGRLYCSGTP--LFLKNcfgtGLYLTLVR 1161
Cdd:COG2274 675 LA-DRIIVLDKGRIVEDGTHeeLLARK----GLYAELVQ 708
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1933-2156 |
4.25e-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: 4.25e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1933 NKTDILRLHELTKIYPGTssPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKsiltNISEVHQ 2012
Cdd:COG1121 2 MMMPAIELENLTVSYGGR--PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGK----PPRRARR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2013 NMGYCPQFDAIDEL--LTGRE--HLYLYAR---LRGVPAEEIEKVANWsIKSLGLTVYADCLAGTYSGGNKRKLSTAIAL 2085
Cdd:COG1121 76 RIGYVPQRAEVDWDfpITVRDvvLMGRYGRrglFRRPSRADREAVDEA-LERVGLEDLADRPIGELSGGQQQRVLLARAL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 105990541 2086 IGCPPLVLLDEPTTGMDPQARRMLWNVIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFrCMGTIQH 2156
Cdd:COG1121 155 AQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLV-AHGPPEE 224
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
942-1138 |
5.85e-33 |
|
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: 127.28 E-value: 5.85e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 942 GRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPP--TSGTVLVGGRDIetSLDAVRQSLGMCPQHNILFHHLT 1019
Cdd:cd03213 21 GKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRPL--DKRSFRKIIGYVPQDDILHPTLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1020 VAEHMLFYAQLKGksqeeaqlemeamledtglhhkrneeaqdLSGGMQRKLSVAIAFVGDAKVVILDEPTSGVDPYSRRS 1099
Cdd:cd03213 99 VRETLMFAAKLRG-----------------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQ 149
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 105990541 1100 IWDLLLKYRS-GRTIIMSTHHM-DEADLLGDRIAIIAQGRL 1138
Cdd:cd03213 150 VMSLLRRLADtGRTIICSIHQPsSEIFELFDKLLLLSQGRV 190
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
948-1142 |
7.39e-33 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 127.61 E-value: 7.39e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 948 RLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIeTSLDAVRQSLGMCPQHNILFHHLTVAEHMLFY 1027
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDV-TAAPPADRPVSMLFQENNLFAHLTVEQNVGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1028 AQLKGKSQEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTSGVDPYSRRSIWDLLLKY 1107
Cdd:cd03298 95 LSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDL 174
|
170 180 190
....*....|....*....|....*....|....*..
gi 105990541 1108 R--SGRTIIMSTHHMDEADLLGDRIAIIAQGRLYCSG 1142
Cdd:cd03298 175 HaeTKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
942-1144 |
1.10e-32 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes 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 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. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 131.90 E-value: 1.10e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 942 GRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIeTSLDAV------RQSLGMCPQHNILF 1015
Cdd:TIGR01186 5 GKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENI-MKQSPVelrevrRKKIGMVFQQFALF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1016 HHLTVAEHMLFYAQLKGKSQEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTSGVDPY 1095
Cdd:TIGR01186 84 PHMTILQNTSLGPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSALDPL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 105990541 1096 SRRSIWDLLLKYRS--GRTIIMSTHHMDEADLLGDRIAIIAQGRLYCSGTP 1144
Cdd:TIGR01186 164 IRDSMQDELKKLQAtlQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTP 214
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1938-2146 |
1.22e-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: 127.25 E-value: 1.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1938 LRLHELTKIYPGTssPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIlTNISEVHQNMGYC 2017
Cdd:cd03259 1 LELKGLSKTYGSV--RALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV-TGVPPERRNIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2018 PQFDAIDELLTGREHLYLYARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEP 2097
Cdd:cd03259 78 FQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 105990541 2098 TTGMDPQARRMLWNVIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKG 2146
Cdd:cd03259 158 LSALDAKLREELREELKELQRElGITTIYVTHDQEEALALADRIAVMNEG 207
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
931-1143 |
1.58e-32 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 130.97 E-value: 1.58e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 931 VKNLVKIFEPCGRP--AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIeTSLD-----AVRQ 1003
Cdd:COG1135 4 LENLSKTFPTKGGPvtALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDL-TALSerelrAARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1004 SLGMCPQH-NiLFHHLTVAEHMLFYAQLKGKSQEEAQLEMEAMLEDTGLHHKRNE-EAQdLSGGM-QRklsVAIA--FVG 1078
Cdd:COG1135 83 KIGMIFQHfN-LLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAyPSQ-LSGGQkQR---VGIAraLAN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 105990541 1079 DAKVVILDEPTSGVDPYSRRSIWDLLLKYRS--GRTIIMSTHHMDEADLLGDRIAIIAQGRLYCSGT 1143
Cdd:COG1135 158 NPKVLLCDEATSALDPETTRSILDLLKDINRelGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGP 224
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
942-1161 |
2.01e-32 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 135.68 E-value: 2.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 942 GRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDI-ETSLDAVRQSLGMCPQHNILFhHLTV 1020
Cdd:COG1132 352 DRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIrDLTLESLRRQIGVVPQDTFLF-SGTI 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1021 AEHMLFyaqlkGK---SQEE-------AQL-EMEAMLEDtGLHHKRNEEAQDLSGGmQR-KLSVAIAFVGDAKVVILDEP 1088
Cdd:COG1132 431 RENIRY-----GRpdaTDEEveeaakaAQAhEFIEALPD-GYDTVVGERGVNLSGG-QRqRIAIARALLKDPPILILDEA 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1089 TSGVDPYSRRSIWDLLLKYRSGRTIIMSTH------HMdeadllgDRIAIIAQGRLYCSGTP--LfLKNCfgtGLYLTLV 1160
Cdd:COG1132 504 TSALDTETEALIQEALERLMKGRTTIVIAHrlstirNA-------DRILVLDDGRIVEQGTHeeL-LARG---GLYARLY 572
|
.
gi 105990541 1161 R 1161
Cdd:COG1132 573 R 573
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
931-1138 |
2.39e-32 |
|
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: 126.11 E-value: 2.39e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 931 VKNLVKIFEpcGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDI---ETSLDAVRQSLGM 1007
Cdd:cd03262 3 IKNLHKSFG--DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtddKKNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1008 CPQHNILFHHLTVAEH-MLFYAQLKGKSQEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILD 1086
Cdd:cd03262 81 VFQQFNLFPHLTVLENiTLAPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 105990541 1087 EPTSGVDPYSRRSIWDLLLKY-RSGRTIIMSTHHMDEADLLGDRIAIIAQGRL 1138
Cdd:cd03262 161 EPTSALDPELVGEVLDVMKDLaEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
931-1138 |
2.49e-31 |
|
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: 124.53 E-value: 2.49e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 931 VKNLVKIFEPCGR--PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIETSLD-AVRQSLGM 1007
Cdd:COG1124 4 VRNLSVSYGQGGRrvPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRkAFRRRVQM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1008 CPQHNIL-FH-HLTVAEHMLFYAQLKGKSQEEAQLEmeAMLEDTGLH----HKRNEEaqdLSGG-MQRklsVAI--AFVG 1078
Cdd:COG1124 84 VFQDPYAsLHpRHTVDRILAEPLRIHGLPDREERIA--ELLEQVGLPpsflDRYPHQ---LSGGqRQR---VAIarALIL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 105990541 1079 DAKVVILDEPTSGVDPYSRRSIWDLLLKYR--SGRTIIMSTHHMDEADLLGDRIAIIAQGRL 1138
Cdd:COG1124 156 EPELLLLDEPTSALDVSVQAEILNLLKDLReeRGLTYLFVSHDLAVVAHLCDRVAVMQNGRI 217
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
893-1124 |
3.69e-31 |
|
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: 130.87 E-value: 3.69e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 893 ALEKTEPLTEETEDPEHPEGihDSFferehPGWVPGVCVKNLVKIFePCGRPAVDRLNITFYENQITAFLGHNGAGKTTT 972
Cdd:TIGR02857 293 AAEALFAVLDAAPRPLAGKA--PVT-----AAPASSLEFSGVSVAY-PGRRPALRPVSFTVPPGERVALVGPSGAGKSTL 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 973 LSILTGLLPPTSGTVLVGGRDI-ETSLDAVRQSLGMCPQHNILFHHlTVAEHMLFY------AQLKGKSQEEAQLEMEAM 1045
Cdd:TIGR02857 365 LNLLLGFVDPTEGSIAVNGVPLaDADADSWRDQIAWVPQHPFLFAG-TIAENIRLArpdasdAEIREALERAGLDEFVAA 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1046 LEDtGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTH---HMDE 1122
Cdd:TIGR02857 444 LPQ-GLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHrlaLAAL 522
|
..
gi 105990541 1123 AD 1124
Cdd:TIGR02857 523 AD 524
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
960-1144 |
4.21e-31 |
|
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: 123.60 E-value: 4.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 960 AFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIeTSLDAVRQSLGMCPQHNILFHHLTVAEHMLFYAQLKGKSQEEAQ 1039
Cdd:cd03299 29 VILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDI-TNLPPEKRDISYVPQNYALFPHMTVYKNIAYGLKKRKVDKKEIE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1040 LEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTSGVDPYSRRSIWDLLLKYR--SGRTIIMST 1117
Cdd:cd03299 108 RKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRkeFGVTVLHVT 187
|
170 180
....*....|....*....|....*..
gi 105990541 1118 HHMDEADLLGDRIAIIAQGRLYCSGTP 1144
Cdd:cd03299 188 HDFEEAWALADKVAIMLNGKLIQVGKP 214
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
928-1144 |
6.92e-31 |
|
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: 122.83 E-value: 6.92e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 928 GVCVKNLVKIFEpcGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIeTSLDAVRQSLGM 1007
Cdd:cd03296 2 SIEVRNVSKRFG--DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDA-TDVPVQERNVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1008 CPQHNILFHHLTVAEHMLFYAQLKGKSQEEAQLEMEA----MLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVV 1083
Cdd:cd03296 79 VFQHYALFRHMTVFDNVAFGLRVKPRSERPPEAEIRAkvheLLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 105990541 1084 ILDEPTSGVDPYSRRSI--WDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIIAQGRLYCSGTP 1144
Cdd:cd03296 159 LLDEPFGALDAKVRKELrrWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTP 221
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
929-1138 |
1.23e-30 |
|
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: 119.46 E-value: 1.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 929 VCVKNLVKIFEpcGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIE--TSLDAVRQSLG 1006
Cdd:cd03216 1 LELRGITKRFG--GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSfaSPRDARRAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1007 MCPQhnilfhhltvaehmlfyaqlkgksqeeaqlemeamledtglhhkrneeaqdLSGGMQRKLSVAIAFVGDAKVVILD 1086
Cdd:cd03216 79 MVYQ---------------------------------------------------LSVGERQMVEIARALARNARLLILD 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 105990541 1087 EPTSGVDPYSRRSIWDLLLKYRS-GRTIIMSTHHMDEADLLGDRIAIIAQGRL 1138
Cdd:cd03216 108 EPTAALTPAEVERLFKVIRRLRAqGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1937-2147 |
2.58e-30 |
|
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: 121.68 E-value: 2.58e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1937 ILRLHELTKIYPGTssPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIlTNISeVH----- 2011
Cdd:COG0411 4 LLEVRGLTKRFGGL--VAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDI-TGLP-PHriarl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2012 ------QNMGYCPQFDAIDELLTGREH------LYLYARLRGVPAEE---IEKVANWsIKSLGLTVYADCLAGTYSGGNK 2076
Cdd:COG0411 80 giartfQNPRLFPELTVLENVLVAAHArlgrglLAALLRLPRARREEreaRERAEEL-LERVGLADRADEPAGNLSYGQQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 105990541 2077 RKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGA 2147
Cdd:COG0411 159 RRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErGITILLIEHDMDLVMGLADRIVVLDFGR 230
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
927-1138 |
5.57e-30 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 126.68 E-value: 5.57e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 927 PGVCVKNLVKIFepcgrPAV---DRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGR--DIETSLDAV 1001
Cdd:COG3845 4 PALELRGITKRF-----GGVvanDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKpvRIRSPRDAI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1002 RQSLGMCPQHNILFHHLTVAEH-MLFYAQLKGK--SQEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKlsVAI--AF 1076
Cdd:COG3845 79 ALGIGMVHQHFMLVPNLTVAENiVLGLEPTKGGrlDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQR--VEIlkAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 105990541 1077 VGDAKVVILDEPTSGVDPYSRRSIWDLLLKYRS-GRTIIMSTHHMDEADLLGDRIAIIAQGRL 1138
Cdd:COG3845 157 YRGARILILDEPTAVLTPQEADELFEILRRLAAeGKSIIFITHKLREVMAIADRVTVLRRGKV 219
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
940-1144 |
6.04e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 121.49 E-value: 6.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 940 PCGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIETS---LDAVRQSLGMCPQH--NIL 1014
Cdd:PRK13636 16 SDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSrkgLMKLRESVGMVFQDpdNQL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1015 FhHLTVAEHMLFYAQLKGKSQEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTSGVDP 1094
Cdd:PRK13636 96 F-SASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDP 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 105990541 1095 YSRRSIWDLLLKYRS--GRTIIMSTHHMDEADLLGDRIAIIAQGRLYCSGTP 1144
Cdd:PRK13636 175 MGVSEIMKLLVEMQKelGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNP 226
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
931-1144 |
8.93e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 120.95 E-value: 8.93e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 931 VKNLVKIFePCGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIE---TSLDAVRQSLGM 1007
Cdd:PRK13639 4 TRDLKYSY-PDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKydkKSLLEVRKTVGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1008 CPQH--NILFHHlTVAEHMLFYAQLKGKSQEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVIL 1085
Cdd:PRK13639 83 VFQNpdDQLFAP-TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1086 DEPTSGVDPYSRRSIWDLLLKY-RSGRTIIMSTHHMDEADLLGDRIAIIAQGRLYCSGTP 1144
Cdd:PRK13639 162 DEPTSGLDPMGASQIMKLLYDLnKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTP 221
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
911-1138 |
1.06e-29 |
|
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: 119.36 E-value: 1.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 911 EGIHDSFFEREHPGWVPGvcvkNLVKIFEPCGR--PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVL 988
Cdd:cd03267 4 SNLSKSYRVYSKEPGLIG----SLKSLFKRKYRevEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 989 VGGRDIETSLDAVRQSLG-MCPQHNILFHHLTVAEHMLFYAQLKGKSQEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQ 1067
Cdd:cd03267 80 VAGLVPWKRRKKFLRRIGvVFGQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 105990541 1068 RKLSVAIAFVGDAKVVILDEPTSGVDPYSRRSIWDLLLKYRSGR--TIIMSTHHMDEADLLGDRIAIIAQGRL 1138
Cdd:cd03267 160 MRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
932-1144 |
1.06e-29 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 119.61 E-value: 1.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 932 KNLVKIFEpcGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIetSL----DAVRQSLGM 1007
Cdd:PRK10895 7 KNLAKAYK--GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDI--SLlplhARARRGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1008 CPQHNILFHHLTVAEHMLFYAQLKGK-SQEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILD 1086
Cdd:PRK10895 83 LPQEASIFRRLSVYDNLMAVLQIRDDlSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 105990541 1087 EPTSGVDPYSRRSIWDLLLKYR-SGRTIIMSTHHMDEADLLGDRIAIIAQGRLYCSGTP 1144
Cdd:PRK10895 163 EPFAGVDPISVIDIKRIIEHLRdSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTP 221
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
931-1144 |
1.16e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 120.92 E-value: 1.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 931 VKNLVKIFEPcGRP----AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDI---ETSLDAVRQ 1003
Cdd:PRK13637 5 IENLTHIYME-GTPfekkALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdkKVKLSDIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1004 SLGMC---PQHNiLFHHlTVAEHMLFYAQLKGKSQEEAQLEMEAMLEDTGLHHK--RNEEAQDLSGGMQRKLSVAIAFVG 1078
Cdd:PRK13637 84 KVGLVfqyPEYQ-LFEE-TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDYEdyKDKSPFELSGGQKRRVAIAGVVAM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 105990541 1079 DAKVVILDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIIAQGRLYCSGTP 1144
Cdd:PRK13637 162 EPKILILDEPTAGLDPKGRDEILNKIkeLHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTP 229
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
940-1144 |
1.31e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 120.62 E-value: 1.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 940 PCGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIETS-----LDAVRQSLGMCPQ--HN 1012
Cdd:PRK13649 17 PFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTsknkdIKQIRKKVGLVFQfpES 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1013 ILFHHlTVAEHMLFYAQLKGKSQEEAQLEMEAMLEDTGLHHK-RNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTSG 1091
Cdd:PRK13649 97 QLFEE-TVLKDVAFGPQNFGVSQEEAEALAREKLALVGISESlFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 105990541 1092 VDPYSRRSIWDLLLK-YRSGRTIIMSTHHMDEADLLGDRIAIIAQGRLYCSGTP 1144
Cdd:PRK13649 176 LDPKGRKELMTLFKKlHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKP 229
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
932-1138 |
2.88e-29 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 121.45 E-value: 2.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 932 KNLVKIFEPCGRP--AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIeTSLD-----AVRQS 1004
Cdd:PRK11153 5 KNISKVFPQGGRTihALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDL-TALSekelrKARRQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1005 LGMCPQHNILFHHLTVAEHMLFYAQLKGKSQEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGM-QRklsVAIA--FVGDAK 1081
Cdd:PRK11153 84 IGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQkQR---VAIAraLASNPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 105990541 1082 VVILDEPTSGVDPYSRRSIWDLLLKY--RSGRTIIMSTHHMDEADLLGDRIAIIAQGRL 1138
Cdd:PRK11153 161 VLLCDEATSALDPATTRSILELLKDInrELGLTIVLITHEMDVVKRICDRVAVIDAGRL 219
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1937-2153 |
3.21e-29 |
|
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: 118.61 E-value: 3.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1937 ILRLHELTKIYPGTssPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIlTNIS--EVHQNM 2014
Cdd:COG1120 1 MLEAENLSVGYGGR--PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDL-ASLSrrELARRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2015 GYCPQFDAIDELLTGREhLYLYAR------LRGVPAEEIEKVAnWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGC 2088
Cdd:COG1120 78 AYVPQEPPAPFGLTVRE-LVALGRyphlglFGRPSAEDREAVE-EALERTGLEHLADRPVDELSGGERQRVLIARALAQE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 105990541 2089 PPLVLLDEPTTGMDPQARRMLWNVIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFRCMGT 2153
Cdd:COG1120 156 PPLLLLDEPTSHLDLAHQLEVLELLRRLARErGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGP 221
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1938-2146 |
3.74e-29 |
|
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: 117.64 E-value: 3.74e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1938 LRLHELTKIYPGTssPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIlTNIsEVHQ----N 2013
Cdd:cd03218 1 LRAENLSKRYGKR--KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDI-TKL-PMHKrarlG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2014 MGYCPQFDAIDELLTGREHLYLYARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVL 2093
Cdd:cd03218 77 IGYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 105990541 2094 LDEPTTGMDPQARRMLWNVIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
Cdd:cd03218 157 LDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEG 209
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
942-1149 |
4.27e-29 |
|
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: 117.33 E-value: 4.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 942 GRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIET-SLDAVRQSLGMCPQHNILFHHlTV 1020
Cdd:cd03254 15 KKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDiSRKSLRSMIGVVLQDTFLFSG-TI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1021 AEHMLfYAQLKGKSQEEAQLEMEAMLED------TGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTSGVDP 1094
Cdd:cd03254 94 MENIR-LGRPNATDEEVIEAAKEAGAHDfimklpNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDT 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1095 YSRRSIWDLLLKYRSGRTIIMSTHHMD---EAdllgDRIAIIAQGRLYCSGTP--LFLKN 1149
Cdd:cd03254 173 ETEKLIQEALEKLMKGRTSIIIAHRLStikNA----DKILVLDDGKIIEEGTHdeLLAKK 228
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1954-2143 |
4.53e-29 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 127.16 E-value: 4.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1954 AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISEVHQNMGYCPQ-FDAIDElLTGREH 2032
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIATRRRVGYMSQaFSLYGE-LTVRQN 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2033 LYLYARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNV 2112
Cdd:NF033858 360 LELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRL 439
|
170 180 190
....*....|....*....|....*....|..
gi 105990541 2113 IVSIIREGRAVVLTS-HSMEECEaLCTRLAIM 2143
Cdd:NF033858 440 LIELSREDGVTIFIStHFMNEAE-RCDRISLM 470
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
948-1139 |
7.32e-29 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 116.78 E-value: 7.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 948 RLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIeTSLDAVRQSLGMCPQHNILFHHLTVAEHMLFY 1027
Cdd:COG3840 17 RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDL-TALPPAERPVSMLFQENNLFPHLTVAQNIGLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1028 AQLKGKSQEEAQLEMEAMLEDTGLHHKRNEEAQDLSGG-MQRklsVAIA--FVGDAKVVILDEPTSGVDPYSRRSIWDLL 1104
Cdd:COG3840 96 LRPGLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGqRQR---VALArcLVRKRPILLLDEPFSALDPALRQEMLDLV 172
|
170 180 190
....*....|....*....|....*....|....*..
gi 105990541 1105 --LKYRSGRTIIMSTHHMDEADLLGDRIAIIAQGRLY 1139
Cdd:COG3840 173 deLCRERGLTVLMVTHDPEDAARIADRVLLVADGRIA 209
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1962-2099 |
8.01e-29 |
|
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: 113.90 E-value: 8.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIL-TNISEVHQNMGYCPQFDAIDELLTGREHLYLYARLR 2040
Cdd:pfam00005 8 LNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTdDERKSLRKEIGYVFQDPQLFPRLTVRENLRLGLLLK 87
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 105990541 2041 GVPAEEIEKVANWSIKSLGLTVYAD----CLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTT 2099
Cdd:pfam00005 88 GLSKREKDARAEEALEKLGLGDLADrpvgERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1937-2146 |
1.04e-28 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 116.67 E-value: 1.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1937 ILRLHELTKIYPGTssPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIlTNISeVHQ---- 2012
Cdd:COG1137 3 TLEAENLVKSYGKR--TVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDI-THLP-MHKrarl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2013 NMGYCPQFDAIDELLTGREHLYLYARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLV 2092
Cdd:COG1137 79 GIGYLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFI 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2093 LLDEPTTGMDPQArrmlwnV--IVSIIRE----GRAVVLTSHSMEECEALCTRLAIMVKG 2146
Cdd:COG1137 159 LLDEPFAGVDPIA------VadIQKIIRHlkerGIGVLITDHNVRETLGICDRAYIISEG 212
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
942-1144 |
1.93e-28 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 116.41 E-value: 1.93e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 942 GRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIE-TSLDAVRQSLGMCPQHNILFHHLTV 1020
Cdd:PRK13548 14 GRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLAdWSPAELARRRAVLPQHSSLSFPFTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1021 AE--HMLFYAqLKGKSQEEAQLEMEAMlEDTGLHHKRNEEAQDLSGG-MQRklsVAIAFV--------GDAKVVILDEPT 1089
Cdd:PRK13548 94 EEvvAMGRAP-HGLSRAEDDALVAAAL-AQVDLAHLAGRDYPQLSGGeQQR---VQLARVlaqlwepdGPPRWLLLDEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 105990541 1090 SGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIIAQGRLYCSGTP 1144
Cdd:PRK13548 169 SALDLAHQHHVLRLArqLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTP 225
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
931-1145 |
1.95e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 117.01 E-value: 1.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 931 VKNLVKIFEPCGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIET-SLDAVRQSLGmcp 1009
Cdd:PRK13632 10 VENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKeNLKEIRKKIG--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1010 qhnILFHH-------LTVAEHMLFYAQLKGKSQEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGM-QRklsVAIAFV--GD 1079
Cdd:PRK13632 87 ---IIFQNpdnqfigATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQkQR---VAIASVlaLN 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 105990541 1080 AKVVILDEPTSGVDPYSRRSIWDLLLKYRSGR--TIIMSTHHMDEAdLLGDRIAIIAQGRLYCSGTPL 1145
Cdd:PRK13632 161 PEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkkTLISITHDMDEA-ILADKVIVFSEGKLIAQGKPK 227
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
931-1138 |
2.50e-28 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 121.66 E-value: 2.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 931 VKNLVKIFePcGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIE--TSLDAVRQSLGMC 1008
Cdd:COG1129 7 MRGISKSF-G-GVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRfrSPRDAQAAGIAII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1009 PQHNILFHHLTVAEHMLFYAQLKGK---SQEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGmQRKLsVAI--AFVGDAKVV 1083
Cdd:COG1129 85 HQELNLVPNLSVAENIFLGREPRRGgliDWRAMRRRARELLARLGLDIDPDTPVGDLSVA-QQQL-VEIarALSRDARVL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 105990541 1084 ILDEPTSGVDPYSRRSIWDLLLKYRS-GRTIIMSTHHMDEADLLGDRIAIIAQGRL 1138
Cdd:COG1129 163 ILDEPTASLTEREVERLFRIIRRLKAqGVAIIYISHRLDEVFEIADRVTVLRDGRL 218
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1935-2157 |
6.59e-28 |
|
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: 120.78 E-value: 6.59e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1935 TDILRLHELTKIYPGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTG---DTTVTSGDATVAGKSILT-NISEV 2010
Cdd:COG1123 2 TPLLEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGllpHGGRISGEVLLDGRDLLElSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2011 HQNMGYCPQfDAIDEL--LTGREHLYLYARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGC 2088
Cdd:COG1123 82 GRRIGMVFQ-DPMTQLnpVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2089 PPLVLLDEPTTGMDPQARRMLWNVIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFRCMGTIQHL 2157
Cdd:COG1123 161 PDLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
931-1144 |
7.91e-28 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 115.50 E-value: 7.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 931 VKNLVKIFEPCGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGR--DIETSLDaVRQSLGMC 1008
Cdd:PRK13635 8 VEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMvlSEETVWD-VRRQVGMV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1009 PQH-NILFHHLTVAEHMLFYAQLKGKSQEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGmqRKLSVAIAFVGDA--KVVIL 1085
Cdd:PRK13635 87 FQNpDNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGG--QKQRVAIAGVLALqpDIIIL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 105990541 1086 DEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEAdLLGDRIAIIAQGRLYCSGTP 1144
Cdd:PRK13635 165 DEATSMLDPRGRREVLETVrqLKEQKGITVLSITHDLDEA-AQADRVIVMNKGEILEEGTP 224
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1954-2244 |
1.84e-27 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 115.57 E-value: 1.84e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1954 AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAG-------KSILTNISEVhqnMGycpQ-----FD 2021
Cdd:COG4586 37 AVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGyvpfkrrKEFARRIGVV---FG---QrsqlwWD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2022 aidelLTGREHLYLYARLRGVPAEEIEKVANWSIKSLGLtvyADCLagtysggNK--RKLS--------TAIALIGCPPL 2091
Cdd:COG4586 111 -----LPAIDSFRLLKAIYRIPDAEYKKRLDELVELLDL---GELL-------DTpvRQLSlgqrmrceLAAALLHRPKI 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2092 VLLDEPTTGMDPQARRMLWNVIVSIIREGRA-VVLTSHSMEECEALCTRLAIMVKGafRCM--GTIQHLKSKFGDGYIVT 2168
Cdd:COG4586 176 LFLDEPTIGLDVVSKEAIREFLKEYNRERGTtILLTSHDMDDIEALCDRVIVIDHG--RIIydGSLEELKERFGPYKTIV 253
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 105990541 2169 MKIKSPKDDL-LPDLNPVEqffqgnfpgsvqrERHYNMLQFQVSS-SSLARIFQLLLSHKDsllIEEYSVTQTTLDQV 2244
Cdd:COG4586 254 LELAEPVPPLeLPRGGEVI-------------EREGNRVRLEVDPrESLAEVLARLLARYP---VRDLTIEEPPIEEV 315
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1938-2146 |
1.90e-27 |
|
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: 112.20 E-value: 1.90e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1938 LRLHELTKIYP--GTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIlTNISEV----- 2010
Cdd:cd03255 1 IELKNLSKTYGggGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDI-SKLSEKelaaf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2011 -HQNMGYCPQFDAIDELLTGREHLYLYARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCP 2089
Cdd:cd03255 80 rRRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 105990541 2090 PLVLLDEPTTGMDPQARRMLWNVIVSIIRE-GRAVVLTSHSMEEcEALCTRLAIMVKG 2146
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHDPEL-AEYADRIIELRDG 216
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
942-1123 |
2.23e-27 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 111.17 E-value: 2.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 942 GRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDietsldavrqSLGMCPQHNILFHHL--T 1019
Cdd:NF040873 4 GRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGA----------RVAYVPQRSEVPDSLplT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1020 VAE--HMLFYAQ--LKGKSQEEAQLEMEAMLEDTGLHHKRNEEAQDLSGG-MQRKLsVAIAFVGDAKVVILDEPTSGVDP 1094
Cdd:NF040873 74 VRDlvAMGRWARrgLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGqRQRAL-LAQGLAQEADLLLLDEPTTGLDA 152
|
170 180 190
....*....|....*....|....*....|
gi 105990541 1095 YSRRSIWDLLLKYRS-GRTIIMSTHHMDEA 1123
Cdd:NF040873 153 ESRERIIALLAEEHArGATVVVVTHDLELV 182
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1962-2146 |
2.33e-27 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 112.14 E-value: 2.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIlTNISE---VHQNMGYCPQFDAIDELLTGREHLYL--Y 2036
Cdd:cd03224 23 VPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDI-TGLPPherARAGIGYVPEGRRIFPELTVEENLLLgaY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2037 ARLRGVPAEEIEKVanwsikslgltvYA---------DCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARR 2107
Cdd:cd03224 102 ARRRAKRKARLERV------------YElfprlkerrKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVE 169
|
170 180 190
....*....|....*....|....*....|....*....
gi 105990541 2108 MLWNVIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
Cdd:cd03224 170 EIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERG 208
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1938-2143 |
4.14e-27 |
|
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: 111.41 E-value: 4.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1938 LRLHELTKIYPGTSSP--AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIltniSEVHQNMG 2015
Cdd:cd03293 1 LEVRNVSKTYGGGGGAvtALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPV----TGPGPDRG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2016 YCPQFDAIDELLTGREHLYLYARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLD 2095
Cdd:cd03293 77 YVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLD 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 105990541 2096 EPTTGMDPQARRMLWNVIVSIIRE-GRAVVLTSHSMEECEALCTRLAIM 2143
Cdd:cd03293 157 EPFSALDALTREQLQEELLDIWREtGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
942-1144 |
5.10e-27 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 112.52 E-value: 5.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 942 GRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIET-SLDAVRQSLGMCPQHNILFHHLTV 1020
Cdd:COG4559 13 GRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAwSPWELARRRAVLPQHSSLAFPFTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1021 AEHMLF--YAQLKGKSQEEAQLEmeAMLEDTGLHHKRNEEAQDLSGG-MQRklsVAIAFV---------GDAKVVILDEP 1088
Cdd:COG4559 93 EEVVALgrAPHGSSAAQDRQIVR--EALALVGLAHLAGRSYQTLSGGeQQR---VQLARVlaqlwepvdGGPRWLFLDEP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 105990541 1089 TSGVDPYSRRSIWDLLLKY-RSGRTIIMSTHHMDEADLLGDRIAIIAQGRLYCSGTP 1144
Cdd:COG4559 168 TSALDLAHQHAVLRLARQLaRRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTP 224
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
943-1130 |
6.20e-27 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 112.26 E-value: 6.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 943 RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIETSlDAVRqslGMCPQHNILFHHLTVAE 1022
Cdd:COG4525 20 QPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGP-GADR---GVVFQKDALLPWLNVLD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1023 HMLFYAQLKGKSQEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTSGVDPYSRRSIWD 1102
Cdd:COG4525 96 NVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQE 175
|
170 180 190
....*....|....*....|....*....|
gi 105990541 1103 LLLKY--RSGRTIIMSTHHMDEADLLGDRI 1130
Cdd:COG4525 176 LLLDVwqRTGKGVFLITHSVEEALFLATRL 205
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1939-2143 |
6.70e-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: 110.70 E-value: 6.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1939 RLHELTKIYPGTssPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKsiltNISEVHQNMGYCP 2018
Cdd:cd03235 1 EVEDLTVSYGGH--PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGK----PLEKERKRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2019 QFDAIDEL--LTGRE--HLYLYAR---LRGVPAEEIEKVANwSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPL 2091
Cdd:cd03235 75 QRRSIDRDfpISVRDvvLMGLYGHkglFRRLSKADKAKVDE-ALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 105990541 2092 VLLDEPTTGMDPQARRMLWNVIVSIIREGRAVVLTSHSMEECEALCTRLAIM 2143
Cdd:cd03235 154 LLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
902-1119 |
6.81e-27 |
|
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: 117.85 E-value: 6.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 902 EETEDPEHPEGIHDSFFEREHPGWVPGVCVKNLvKIFEPCGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLP 981
Cdd:TIGR02868 308 VEVLDAAGPVAEGSAPAAGAVGLGKPTLELRDL-SAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLD 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 982 PTSGTVLVGGRDIET-SLDAVRQSLGMCPQHNILFHHlTVAEHMLFyaqLKGKSQEEaqlEMEAMLE-----------DT 1049
Cdd:TIGR02868 387 PLQGEVTLDGVPVSSlDQDEVRRRVSVCAQDAHLFDT-TVRENLRL---ARPDATDE---ELWAALErvgladwlralPD 459
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1050 GLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHH 1119
Cdd:TIGR02868 460 GLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHH 529
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
1603-1895 |
9.32e-27 |
|
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: 114.02 E-value: 9.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1603 PDFLKHLETEDN--IKVWFNNKGWHALVSFLNVAHNaiLRASLPKDRSPEEYGITVISQPLNLTKEQLSEitVLTTSVDA 1680
Cdd:pfam12698 87 KGFSKDLLKGESatVTVYINSSNLLVSKLILNALQS--LLQQLNASALVLLLEALSTSAPIPVESTPLFN--PQSGYAYY 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1681 VVAICVIFSMSFVPASFVLYLIQERVNKSKHLQFISGVSPTTYWVTNFLWDIMNYSVSAGLVVGIFIGFqkkaYTSPENL 1760
Cdd:pfam12698 163 LVGLILMIIILIGAAIIAVSIVEEKESRIKERLLVSGVSPLQYWLGKILGDFLVGLLQLLIILLLLFGI----GIPFGNL 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1761 PALVALLLLYGWAVIPMMYPASFLFDVPSTAYVALSCANLFIGInSSAITFILELFENnrtllrfnaVLRKLLIVFPHFC 1840
Cdd:pfam12698 239 GLLLLLFLLYGLAYIALGYLLGSLFKNSEDAQSIIGIVILLLSG-FFGGLFPLEDPPS---------FLQWIFSIIPFFS 308
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 105990541 1841 LGRGLIDLALSQAVTDvyarfgeehsanpfhwdlIGKNLFAMVVEGVVYFLLTLL 1895
Cdd:pfam12698 309 PIDGLLRLIYGDSLWE------------------IAPSLIILLLFAVVLLLLALL 345
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
945-1144 |
1.14e-26 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 119.46 E-value: 1.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIETSldAVRQSLG-----McPQ---HNiLFH 1016
Cdd:NF033858 16 ALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADA--RHRRAVCpriayM-PQglgKN-LYP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1017 HLTVAEHMLFYAQLKGKSQEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTSGVDPYS 1096
Cdd:NF033858 92 TLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLS 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 105990541 1097 RRSIWDLLLKYRSGR---TIIMSTHHMDEADLLgDRIAIIAQGRLYCSGTP 1144
Cdd:NF033858 172 RRQFWELIDRIRAERpgmSVLVATAYMEEAERF-DWLVAMDAGRVLATGTP 221
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
942-1142 |
1.29e-26 |
|
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: 110.94 E-value: 1.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 942 GRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSG-TVLVGGRDI-ETSLDAVRQSLGMC-PQ-HNILFHH 1017
Cdd:COG1119 15 GKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRgGEDVWELRKRIGLVsPAlQLRFPRD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1018 LTVAEHML--FYAQLkGKSQE--EAQLEM-EAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTSGV 1092
Cdd:COG1119 95 ETVLDVVLsgFFDSI-GLYREptDEQRERaRELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 105990541 1093 DPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIIAQGRLYCSG 1142
Cdd:COG1119 174 DLGARELLLALLdkLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAG 225
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
943-1144 |
1.62e-26 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 110.87 E-value: 1.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 943 RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIETSLD-AVRQSLGMCPQHNILFHHLTVA 1021
Cdd:PRK11231 15 KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSrQLARRLALLPQHHLTPEGITVR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1022 EHMLF----YAQLKGK-SQEEAQLEMEAMlEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTSGVDPYS 1096
Cdd:PRK11231 95 ELVAYgrspWLSLWGRlSAEDNARVNQAM-EQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINH 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 105990541 1097 RRSIWDLLLKYRS-GRTIIMSTHHMDEADLLGDRIAIIAQGRLYCSGTP 1144
Cdd:PRK11231 174 QVELMRLMRELNTqGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTP 222
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
943-1138 |
1.62e-26 |
|
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: 109.60 E-value: 1.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 943 RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIETsLDAV--RQSLGMCPQHNilfhhltv 1020
Cdd:cd03245 17 IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQ-LDPAdlRRNIGYVPQDV-------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1021 aehMLFYAQLK-----GKSQEEAQLEMEAMlEDTGLH-----HKR------NEEAQDLSGGMQRKLSVAIAFVGDAKVVI 1084
Cdd:cd03245 88 ---TLFYGTLRdnitlGAPLADDERILRAA-ELAGVTdfvnkHPNgldlqiGERGRGLSGGQRQAVALARALLNDPPILL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 105990541 1085 LDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLgDRIAIIAQGRL 1138
Cdd:cd03245 164 LDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLV-DRIIVMDSGRI 216
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
931-1138 |
2.05e-26 |
|
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: 108.29 E-value: 2.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 931 VKNLvkifepCGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIE--TSLDAVRQSLGMC 1008
Cdd:cd03215 7 VRGL------SVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTrrSPRDAIRAGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1009 P---QHNILFHHLTVAEHMLFyaqlkgksqeeaqlemeamledtglhhkrneeAQDLSGGMQRKLSVAIAFVGDAKVVIL 1085
Cdd:cd03215 81 PedrKREGLVLDLSVAENIAL--------------------------------SSLLSGGNQQKVVLARWLARDPRVLIL 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 105990541 1086 DEPTSGVDPYSRRSIWDLLLKYRS-GRTIIMSTHHMDEADLLGDRIAIIAQGRL 1138
Cdd:cd03215 129 DEPTRGVDVGAKAEIYRLIRELADaGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
949-1138 |
3.31e-26 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 108.54 E-value: 3.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 949 LNITF-YENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGrdieTSLDAVRQSLGMCP---------QHNILFHHL 1018
Cdd:cd03297 15 LKIDFdLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNG----TVLFDSRKKINLPPqqrkiglvfQQYALFPHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1019 TVAEHMLFyaQLKGKSQEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTSGVDPYSRR 1098
Cdd:cd03297 91 NVRENLAF--GLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 105990541 1099 SIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIIAQGRL 1138
Cdd:cd03297 169 QLLPELkqIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRL 210
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1938-2165 |
3.39e-26 |
|
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: 109.51 E-value: 3.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1938 LRLHELTKIYP--GTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNIS-EVHQNM 2014
Cdd:COG1124 2 LEVRNLSVSYGqgGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRkAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2015 GYCPQ--FDAIDELLTGREHLYLYARLRGVPAEEiEKVANWsIKSLGLTV-YADCLAGTYSGGNKRKLSTAIALIGCPPL 2091
Cdd:COG1124 82 QMVFQdpYASLHPRHTVDRILAEPLRIHGLPDRE-ERIAEL-LEQVGLPPsFLDRYPHQLSGGQRQRVAIARALILEPEL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 105990541 2092 VLLDEPTTGMDP--QARrmLWNVIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFRCMGTIQHLKSKFGDGY 2165
Cdd:COG1124 160 LLLDEPTSALDVsvQAE--ILNLLKDLREErGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKHPY 234
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
945-1138 |
4.90e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 111.33 E-value: 4.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDI---ETSLdaVRQ-SLGMcPQHNILFHHLTV 1020
Cdd:COG4586 37 AVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPfkrRKEF--ARRiGVVF-GQRSQLWWDLPA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1021 AEHMLFYAQLKGKSQEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGmQR-KLSVAIAFVGDAKVVILDEPTSGVDPYSRRS 1099
Cdd:COG4586 114 IDSFRLLKAIYRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLG-QRmRCELAAALLHRPKILFLDEPTIGLDVVSKEA 192
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 105990541 1100 IWDLLLKY--RSGRTIIMSTHHMDEADLLGDRIAIIAQGRL 1138
Cdd:COG4586 193 IREFLKEYnrERGTTILLTSHDMDDIEALCDRVIVIDHGRI 233
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
943-1166 |
8.85e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 109.41 E-value: 8.85e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 943 RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDI--ETSLDAVRQSLGMC---PQHNILfhH 1017
Cdd:PRK13633 23 KLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTsdEENLWDIRNKAGMVfqnPDNQIV--A 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1018 LTVAEHMLFYAQLKGKSQEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTSGVDPYSR 1097
Cdd:PRK13633 101 TIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGR 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 105990541 1098 RSIWDLL--LKYRSGRTIIMSTHHMDEAdLLGDRIAIIAQGRLYCSGTPlflKNCFGTglyltlVRKMKNI 1166
Cdd:PRK13633 181 REVVNTIkeLNKKYGITIILITHYMEEA-VEADRIIVMDSGKVVMEGTP---KEIFKE------VEMMKKI 241
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1937-2146 |
9.37e-26 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 114.23 E-value: 9.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1937 ILRLHELTKIYPGTSS---PAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT----NISE 2009
Cdd:COG1123 260 LLEVRNLSKRYPVRGKggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKlsrrSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2010 VHQNMGYCPQ--FDAIDELLTGREHLYLYARLRGV-PAEEIEKVANWSIKSLGLTV-YADCLAGTYSGGNKRKLSTAIAL 2085
Cdd:COG1123 340 LRRRVQMVFQdpYSSLNPRMTVGDIIAEPLRLHGLlSRAERRERVAELLERVGLPPdLADRYPHELSGGQRQRVAIARAL 419
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 105990541 2086 IGCPPLVLLDEPTTGMDPQARRMLWNVIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKG 2146
Cdd:COG1123 420 ALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDG 481
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
931-1144 |
1.13e-25 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 111.47 E-value: 1.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 931 VKNLVKIFEpcGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIeTSLDAVRQSLGMCPQ 1010
Cdd:PRK11607 22 IRNLTKSFD--GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDL-SHVPPYQRPINMMFQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1011 HNILFHHLTVAEHMLFYAQLKGKSQEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTS 1090
Cdd:PRK11607 99 SYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMG 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 105990541 1091 GVDPYSRR----SIWDLLlkYRSGRTIIMSTHHMDEADLLGDRIAIIAQGRLYCSGTP 1144
Cdd:PRK11607 179 ALDKKLRDrmqlEVVDIL--ERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEP 234
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
940-1144 |
1.18e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 109.44 E-value: 1.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 940 PCGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGgrDI-------ETSLDAVRQSLGMCPQ-- 1010
Cdd:PRK13643 16 PFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVG--DIvvsstskQKEIKPVRKKVGVVFQfp 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1011 HNILFHHlTVAEHMLFYAQLKGKSQEEAQLEMEAMLEDTGLHHKRNEEAQ-DLSGGMQRKLSVAIAFVGDAKVVILDEPT 1089
Cdd:PRK13643 94 ESQLFEE-TVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPfELSGGQMRRVAIAGILAMEPEVLVLDEPT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 105990541 1090 SGVDPYSRRSIWDLLLK-YRSGRTIIMSTHHMDEADLLGDRIAIIAQGRLYCSGTP 1144
Cdd:PRK13643 173 AGLDPKARIEMMQLFESiHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTP 228
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1953-2146 |
1.88e-25 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 107.03 E-value: 1.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1953 PAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAG-------KSILTNISEVhqnMGYCPQ--FDai 2023
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGlvpwkrrKKFLRRIGVV---FGQKTQlwWD-- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2024 delLTGREHLYLYARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDP 2103
Cdd:cd03267 110 ---LPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDV 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 105990541 2104 QARRMLWNVIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKG 2146
Cdd:cd03267 187 VAQENIRNFLKEYNRErGTTVLLTSHYMKDIEALARRVLVIDKG 230
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1937-2146 |
1.88e-25 |
|
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: 106.82 E-value: 1.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1937 ILRLHELTKIYP--GTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTN----ISEV 2010
Cdd:cd03257 1 LLEVKNLSVSFPtgGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLsrrlRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2011 HQNMGYCPQ--FDAIDELLTGREHLY--LYARLRGVPAEEIEKVANWSIKSLGL-TVYADCLAGTYSGGNKRKLSTAIAL 2085
Cdd:cd03257 81 RKEIQMVFQdpMSSLNPRMTIGEQIAepLRIHGKLSKKEARKEAVLLLLVGVGLpEEVLNRYPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 105990541 2086 IGCPPLVLLDEPTTGMDPQARRMLWNVIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKG 2146
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAG 222
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1938-2153 |
1.89e-25 |
|
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: 106.94 E-value: 1.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1938 LRLHELTKIYPGTssPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT------NISEVH 2011
Cdd:cd03300 1 IELENVSKFYGGF--VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNlpphkrPVNTVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2012 QNMGYCPQFDAIDELLTGrehlylyARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPL 2091
Cdd:cd03300 79 QNYALFPHLTVFENIAFG-------LRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 105990541 2092 VLLDEPTTGMDPQARRMLWNVIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFRCMGT 2153
Cdd:cd03300 152 LLLDEPLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGT 214
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1938-2190 |
2.00e-25 |
|
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: 107.39 E-value: 2.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1938 LRLHELTKIYPGtSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIL-TNISEVHQNMGY 2016
Cdd:cd03295 1 IEFENVTKRYGG-GKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIReQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2017 CPQFDAIDELLTGREHLYLYARLRGVPAEEIEKVANWSIKSLGL--TVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLL 2094
Cdd:cd03295 80 VIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLLM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2095 DEPTTGMDPQARRMLWNVIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFRCMGTIQHLkskfgdgyivtmkIKS 2173
Cdd:cd03295 160 DEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEI-------------LRS 226
|
250
....*....|....*..
gi 105990541 2174 PKDDLlpdlnpVEQFFQ 2190
Cdd:cd03295 227 PANDF------VAEFVG 237
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
931-1142 |
2.15e-25 |
|
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: 105.09 E-value: 2.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 931 VKNLVKIFEPCGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIETSLDAVRQSLGMCPQ 1010
Cdd:cd03247 3 INNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVLNQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1011 HNILFhhltvaehmlfyaqlkgksqeeaqlemeamleDTGLhhkRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTS 1090
Cdd:cd03247 83 RPYLF--------------------------------DTTL---RNNLGRRFSGGERQRLALARILLQDAPIVLLDEPTV 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 105990541 1091 GVDPYSRRSIWDLLLKYRSGRTIIMSTHHmdeadLLG----DRIAIIAQGRLYCSG 1142
Cdd:cd03247 128 GLDPITERQLLSLIFEVLKDKTLIWITHH-----LTGiehmDKILFLENGKIIMQG 178
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
955-1144 |
2.23e-25 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 111.28 E-value: 2.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 955 ENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIETSLDAV-----RQSLGMCPQHNILFHHLTVAEHMLFYAQ 1029
Cdd:PRK10070 53 EGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAElrevrRKKIAMVFQSFALMPHMTVLDNTAFGME 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1030 LKGKSQEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTSGVDPYSRRSIWDLLLKYRS 1109
Cdd:PRK10070 133 LAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQA 212
|
170 180 190
....*....|....*....|....*....|....*..
gi 105990541 1110 G--RTIIMSTHHMDEADLLGDRIAIIAQGRLYCSGTP 1144
Cdd:PRK10070 213 KhqRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTP 249
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
931-1143 |
2.25e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 107.51 E-value: 2.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 931 VKNLVKIFEpcGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIetsldavrqsLGMcPQ 1010
Cdd:COG4674 13 VEDLTVSFD--GFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDL----------TGL-DE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1011 HNI-------------LFHHLTVAEHML--------FYAQLKGKSQEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRK 1069
Cdd:COG4674 80 HEIarlgigrkfqkptVFEELTVFENLElalkgdrgVFASLFARLTAEERDRIEEVLETIGLTDKADRLAGLLSHGQKQW 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 105990541 1070 LSVAIAFVGDAKVVILDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIIAQGRLYCSGT 1143
Cdd:COG4674 160 LEIGMLLAQDPKLLLLDEPVAGMTDAETERTAELLKSLAGKHSVVVVEHDMEFVRQIARKVTVLHQGSVLAEGS 233
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1937-2147 |
2.39e-25 |
|
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: 106.90 E-value: 2.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1937 ILRLHELTKIYPGTSS--PAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT----NISEV 2010
Cdd:cd03258 1 MIELKNVSKVFGDTGGkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLlsgkELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2011 HQNMGYCPQ-FDaideLLTGR---EHLYLYARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALI 2086
Cdd:cd03258 81 RRRIGMIFQhFN----LLSSRtvfENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 105990541 2087 GCPPLVLLDEPTTGMDPQARRMLWNVIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGA 2147
Cdd:cd03258 157 NNPKVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGE 218
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
942-1118 |
3.23e-25 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 105.73 E-value: 3.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 942 GRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIE-TSLDAVRQSLGmcpQHNILFHHLTV 1020
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDdPDVAEACHYLG---HRNAMKPALTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1021 AEHMLFYAQLKGksqeEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTSGVDPYSRRSI 1100
Cdd:PRK13539 91 AENLEFWAAFLG----GEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALF 166
|
170
....*....|....*....
gi 105990541 1101 WDLLLKYR-SGRTIIMSTH 1118
Cdd:PRK13539 167 AELIRAHLaQGGIVIAATH 185
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
932-1144 |
3.50e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 107.99 E-value: 3.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 932 KNLVKIFEPcGRP----AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDI--ETS---LDAVR 1002
Cdd:PRK13641 6 ENVDYIYSP-GTPmekkGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItpETGnknLKKLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1003 QSLGMCPQ--HNILFHHlTVAEHMLFYAQLKGKSQEEAQLEMEAMLEDTGLHHK-RNEEAQDLSGGMQRKLSVAIAFVGD 1079
Cdd:PRK13641 85 KKVSLVFQfpEAQLFEN-TVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDlISKSPFELSGGQMRRVAIAGVMAYE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 105990541 1080 AKVVILDEPTSGVDPYSRRSIWDLLLKY-RSGRTIIMSTHHMDEADLLGDRIAIIAQGRLYCSGTP 1144
Cdd:PRK13641 164 PEILCLDEPAAGLDPEGRKEMMQLFKDYqKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASP 229
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1962-2146 |
6.90e-25 |
|
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: 105.94 E-value: 6.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSG-DATVAGKSI-LTNISEVHQNMGYC-----PQFD----AIDELLTGr 2030
Cdd:COG1119 26 VKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRgGEDVWELRKRIGLVspalqLRFPrdetVLDVVLSG- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2031 ehlyLYA---RLRGVPAEEIEKVANWsIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARR 2107
Cdd:COG1119 105 ----FFDsigLYREPTDEQRERAREL-LELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARE 179
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 105990541 2108 MLWNVIVSIIREG-RAVVLTSHSMEECEALCTRLAIMVKG 2146
Cdd:COG1119 180 LLLALLDKLAAEGaPTLVLVTHHVEEIPPGITHVLLLKDG 219
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
943-1170 |
1.13e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 106.04 E-value: 1.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 943 RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDI-ETSLDAVRQSLGMCPQH--NILFHHlT 1019
Cdd:PRK13652 17 KEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPItKENIREVRKFVGLVFQNpdDQIFSP-T 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1020 VAEHMLFYAQLKGKSQEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTSGVDPYSRRS 1099
Cdd:PRK13652 96 VEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKE 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 105990541 1100 IWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIIAQGRLYCSGTP--LFLKNCFGTGLYLTLVRKMKNIQSQR 1170
Cdd:PRK13652 176 LIDFLndLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVeeIFLQPDLLARVHLDLPSLPKLIRSLQ 250
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
945-1158 |
1.40e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 106.02 E-value: 1.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDI-----ETSLDAVRQSLGMCPQ--HNILFHH 1017
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktkDKYIRPVRKRIGMVFQfpESQLFED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1018 lTVAEHMLFYAQLKGKSQEEAQLEMEAMLEDTGLhhKRNEEAQD---LSGGMQRKLSVAIAFVGDAKVVILDEPTSGVDP 1094
Cdd:PRK13646 102 -TVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGF--SRDVMSQSpfqMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDP 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 105990541 1095 YSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIIAQGRLYCSGTPlflKNCFGTGLYLT 1158
Cdd:PRK13646 179 QSKRQVMRLLksLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSP---KELFKDKKKLA 241
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
945-1144 |
1.74e-24 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 105.07 E-value: 1.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIE--TSLDAVRQSLGMCPQHNILFHHLTVAE 1022
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEglPGHQIARMGVVRTFQHVRLFREMTVIE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1023 HMLFyAQ--------LKG--KSQEEAQLEMEAM------LEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILD 1086
Cdd:PRK11300 100 NLLV-AQhqqlktglFSGllKTPAFRRAESEALdraatwLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLD 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1087 EPTSGVDPYSRRSIWDLLLKYRS--GRTIIMSTHHMDEADLLGDRIAIIAQGRLYCSGTP 1144
Cdd:PRK11300 179 EPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTP 238
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1937-2143 |
2.17e-24 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 104.79 E-value: 2.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1937 ILRLHELTKIYPGTSS--PAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIltniSEVHQNM 2014
Cdd:COG1116 7 ALELRGVSKRFPTGGGgvTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPV----TGPGPDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2015 GYCPQFDAideLL---TGREHLYLYARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPL 2091
Cdd:COG1116 83 GVVFQEPA---LLpwlTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 105990541 2092 VLLDEPTTGMDPQARRMLWNVIVSIIRE-GRAVVLTSHSMEECEALCTRLAIM 2143
Cdd:COG1116 160 LLMDEPFGALDALTRERLQDELLRLWQEtGKTVLFVTHDVDEAVFLADRVVVL 212
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
1937-2157 |
2.32e-24 |
|
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: 104.28 E-value: 2.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1937 ILRLHELTKIYpgTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIltniseVHQNM-- 2014
Cdd:TIGR04406 1 TLVAENLIKSY--KKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDI------THLPMhe 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2015 ------GYCPQFDAIDELLTGREHLYLYARLRG-VPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIG 2087
Cdd:TIGR04406 73 rarlgiGYLPQEASIFRKLTVEENIMAVLEIRKdLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALAT 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2088 CPPLVLLDEPTTGMDPQARRMLWNVIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFRCMGTIQHL 2157
Cdd:TIGR04406 153 NPKFILLDEPFAGVDPIAVGDIKKIIKHLKERGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEI 222
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
931-1137 |
4.42e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 104.01 E-value: 4.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 931 VKNLVKIFEPcG----RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIeTSLDA------ 1000
Cdd:COG1101 4 LKNLSKTFNP-GtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDV-TKLPEykraky 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1001 ---VRQ--SLGMCPqhnilfhHLTVAEHMLFyAQLKGKS---------------QEE-AQLEMeamledtGLHHKRNEEA 1059
Cdd:COG1101 82 igrVFQdpMMGTAP-------SMTIEENLAL-AYRRGKRrglrrgltkkrrelfRELlATLGL-------GLENRLDTKV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1060 QDLSGGmQRK-LSVAIAFVGDAKVVILDEPTSGVDPYSRRSIWDLLLKY--RSGRTIIMSTHHMDEADLLGDRIAIIAQG 1136
Cdd:COG1101 147 GLLSGG-QRQaLSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIveENNLTTLMVTHNMEQALDYGNRLIMMHEG 225
|
.
gi 105990541 1137 R 1137
Cdd:COG1101 226 R 226
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
1962-2148 |
4.83e-24 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 102.20 E-value: 4.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISEVHQNMGYCPQ----FDAidellTGREHLYLY 2036
Cdd:COG4619 23 LEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAmPPPEWRRQVAYVPQepalWGG-----TVRDNLPFP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2037 ARLRGVPAEEiEKVANWsIKSLGLTvyADCL---AGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVI 2113
Cdd:COG4619 98 FQLRERKFDR-ERALEL-LERLGLP--PDILdkpVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENTRRVEELL 173
|
170 180 190
....*....|....*....|....*....|....*.
gi 105990541 2114 VSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAF 2148
Cdd:COG4619 174 REYLAEeGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
932-1144 |
5.04e-24 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 103.25 E-value: 5.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 932 KNLVKIFEPCgrPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGG---RDIETSLDAVRQSLGMC 1008
Cdd:PRK09493 5 KNVSKHFGPT--QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGlkvNDPKVDERLIRQEAGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1009 PQHNILFHHLTVAEHMLFYA-QLKGKSQEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDE 1087
Cdd:PRK09493 83 FQQFYLFPHLTALENVMFGPlRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 105990541 1088 PTSGVDPYSR----RSIWDLLlkyRSGRTIIMSTHHMDEADLLGDRIAIIAQGRLYCSGTP 1144
Cdd:PRK09493 163 PTSALDPELRhevlKVMQDLA---EEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDP 220
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1935-2159 |
6.65e-24 |
|
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: 102.75 E-value: 6.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1935 TDILRLHELTKIYPGtsSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISE--VHQ 2012
Cdd:COG0410 1 MPMLEVENLHAGYGG--IHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHriARL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2013 NMGYCPQFDAIDELLTGREHLYLYARLRGVPAEEIEKVAnwsikslglTVYA---------DCLAGTYSGGNKRKLSTAI 2083
Cdd:COG0410 79 GIGYVPEGRRIFPSLTVEENLLLGAYARRDRAEVRADLE---------RVYElfprlkerrRQRAGTLSGGEQQMLAIGR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 105990541 2084 ALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFRCMGTIQHLKS 2159
Cdd:COG0410 150 ALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLA 225
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
953-1144 |
7.72e-24 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 108.98 E-value: 7.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 953 FYENQITAFLGHNGAGKTTTLSILTGLLPP---TSGTVLVGGRDIEtsLDAVRQSLGMCPQHNILFHHLTVAEHMLFYAQ 1029
Cdd:TIGR00955 48 AKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPID--AKEMRAISAYVQQDDLFIPTLTVREHLMFQAH 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1030 LKGK---SQEEAQLEMEAMLEDTGLHHKRNEEAQD------LSGGMQRKLSVAIAFVGDAKVVILDEPTSGVDPYSRRSI 1100
Cdd:TIGR00955 126 LRMPrrvTKKEKRERVDEVLQALGLRKCANTRIGVpgrvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSV 205
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 105990541 1101 WDLLLKY-RSGRTIIMSTHHmDEADL--LGDRIAIIAQGRLYCSGTP 1144
Cdd:TIGR00955 206 VQVLKGLaQKGKTIICTIHQ-PSSELfeLFDKIILMAEGRVAYLGSP 251
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1962-2128 |
1.62e-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: 101.19 E-value: 1.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1962 VRPGECFGLLGVNGAGKTTTFKMLTG---DTTVTSGDATVAGKSIltNISEVHQNMGYCPQFDAIDELLTGREHLYLYAR 2038
Cdd:cd03234 30 VESGQVMAILGSSGSGKTTLLDAISGrveGGGTTSGQILFNGQPR--KPDQFQKCVAYVRQDDILLPGLTVRETLTYTAI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2039 LRG---VPAEEIEK-VANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPqarrMLWNVIV 2114
Cdd:cd03234 108 LRLprkSSDAIRKKrVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDS----FTALNLV 183
|
170
....*....|....*...
gi 105990541 2115 SII----REGRAVVLTSH 2128
Cdd:cd03234 184 STLsqlaRRNRIVILTIH 201
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1937-2146 |
1.97e-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: 104.41 E-value: 1.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1937 ILRLHELTKIYPGTssPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIlTNISeVHQ-NMG 2015
Cdd:COG3842 5 ALELENVSKRYGDV--TALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDV-TGLP-PEKrNVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2016 YCPQFDAIDELLTGREHLYLYARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNK-RklsTAIA--LIGCPPLV 2092
Cdd:COG3842 81 MVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQqR---VALAraLAPEPRVL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 105990541 2093 LLDEPTTGMDPQARRMLWNVIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKG 2146
Cdd:COG3842 158 LLDEPLSALDAKLREEMREELRRLQRElGITFIYVTHDQEEALALADRIAVMNDG 212
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
927-1144 |
2.00e-23 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 104.64 E-value: 2.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 927 PGVCVKNLVKIFEpcGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIeTSLDAVRQSLG 1006
Cdd:PRK09452 13 PLVELRGISKSFD--GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDI-THVPAENRHVN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1007 MCPQHNILFHHLTVAEHMLFYAQLKGKSQEE-AQLEMEAM----LEDTGlhhkrNEEAQDLSGGMQRKLSVAIAFVGDAK 1081
Cdd:PRK09452 90 TVFQSYALFPHMTVFENVAFGLRMQKTPAAEiTPRVMEALrmvqLEEFA-----QRKPHQLSGGQQQRVAIARAVVNKPK 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 105990541 1082 VVILDEPTSGVDpYSRRSIWDLLLKY---RSGRTIIMSTHHMDEADLLGDRIAIIAQGRLYCSGTP 1144
Cdd:PRK09452 165 VLLLDESLSALD-YKLRKQMQNELKAlqrKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTP 229
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
931-1138 |
2.45e-23 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 101.37 E-value: 2.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 931 VKNLVKIFEpcGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIETS---------LDAV 1001
Cdd:PRK11264 6 VKNLVKKFH--GQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTArslsqqkglIRQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1002 RQSLGMCPQHNILFHHLTVAEHML-FYAQLKGKSQEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDA 1080
Cdd:PRK11264 84 RQHVGFVFQNFNLFPHRTVLENIIeGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 105990541 1081 KVVILDEPTSGVDPysrRSIWDLLLKYRS----GRTIIMSTHHMDEADLLGDRIAIIAQGRL 1138
Cdd:PRK11264 164 EVILFDEPTSALDP---ELVGEVLNTIRQlaqeKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
931-1149 |
2.52e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 102.12 E-value: 2.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 931 VKNLvKIFEPCGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDI-ETSLDAVRQSLGMCP 1009
Cdd:PRK13647 7 VEDL-HFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVnAENEKWVRSKVGLVF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1010 Q--HNILFhHLTVAEHMLFYAQLKGKSQEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDE 1087
Cdd:PRK13647 86 QdpDDQVF-SSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 105990541 1088 PTSGVDPYSRRSIWDLLLK-YRSGRTIIMSTHHMDEADLLGDRIAIIAQGRLYCSGTPLFLKN 1149
Cdd:PRK13647 165 PMAYLDPRGQETLMEILDRlHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTD 227
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
942-1119 |
3.06e-23 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 99.74 E-value: 3.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 942 GRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIETSLDAVRQSLGMCPQHNILFHHLTVA 1021
Cdd:TIGR01189 12 ERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPELSAL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1022 EHMLFYAQLKGksqeEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTSGVDPYSRRSIW 1101
Cdd:TIGR01189 92 ENLHFWAAIHG----GAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLA 167
|
170
....*....|....*....
gi 105990541 1102 DLLLKY-RSGRTIIMSTHH 1119
Cdd:TIGR01189 168 GLLRAHlARGGIVLLTTHQ 186
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1938-2152 |
3.46e-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: 100.02 E-value: 3.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1938 LRLHELTKIYPGTssPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT------NISEVH 2011
Cdd:cd03301 1 VELENVTKRFGNV--TALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDlppkdrDIAMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2012 QNMGYCPQfdaidelLTGREHLYLYARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPL 2091
Cdd:cd03301 79 QNYALYPH-------MTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 105990541 2092 VLLDEPTTGMDPQARRMLWNVIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFRCMG 2152
Cdd:cd03301 152 FLMDEPLSNLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1935-2154 |
3.58e-23 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 100.93 E-value: 3.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1935 TDILRLHELTKIYPGTSSP--------------------AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSG 1994
Cdd:COG1134 2 SSMIEVENVSKSYRLYHEPsrslkelllrrrrtrreefwALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1995 DATVAGK--SILtnisEVhqNMGYCPQfdaidelLTGREHLYLYARLRGVPAEEIEK----VANWSikslGLTVYADCLA 2068
Cdd:COG1134 82 RVEVNGRvsALL----EL--GAGFHPE-------LTGRENIYLNGRLLGLSRKEIDEkfdeIVEFA----ELGDFIDQPV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2069 GTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDP--QAR---RMLwnvivSIIREGRAVVLTSHSMEECEALCTRLAIM 2143
Cdd:COG1134 145 KTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAafQKKclaRIR-----ELRESGRTVIFVSHSMGAVRRLCDRAIWL 219
|
250
....*....|.
gi 105990541 2144 VKGAFRCMGTI 2154
Cdd:COG1134 220 EKGRLVMDGDP 230
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
927-1142 |
4.19e-23 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 106.02 E-value: 4.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 927 PGVCVKNLVKIFEPCgrPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIE--TSLDAVRQS 1004
Cdd:PRK09700 4 PYISMAGIGKSFGPV--HALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNklDHKLAAQLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1005 LGMCPQHNILFHHLTVAEHmLFYAQLKGKS--------QEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAF 1076
Cdd:PRK09700 82 IGIIYQELSVIDELTVLEN-LYIGRHLTKKvcgvniidWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 105990541 1077 VGDAKVVILDEPTSGVDPYSRRSIWDLLLKYRS-GRTIIMSTHHMDEADLLGDRIAIIAQGRLYCSG 1142
Cdd:PRK09700 161 MLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKeGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
1954-2162 |
4.75e-23 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 103.28 E-value: 4.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1954 AVDRLCVGVRPGECFGLLGVNGAGKTTTfkmlTGDTTVTSGDATVAGKSILT---NISEVHQNMG-YCPQFDAIDELLTG 2029
Cdd:NF000106 28 AVDGVDLDVREGTVLGVLGP*GAA**RG----ALPAHV*GPDAGRRPWRF*TwcaNRRALRRTIG*HRPVR*GRRESFSG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2030 REHLYLYARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRML 2109
Cdd:NF000106 104 RENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEV 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 105990541 2110 WNVIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFRCMGTIQHLKSKFG 2162
Cdd:NF000106 184 WDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVG 236
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1938-2153 |
6.14e-23 |
|
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: 97.50 E-value: 6.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1938 LRLHELTKIYPGTssPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIltnisevhqnmgyc 2017
Cdd:cd03216 1 LELRGITKRFGGV--KALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEV-------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2018 pQFDAIDElltgrehlylyARLRGVpaeeiekvanwsikslgLTVYadclagTYSGGNKRKLSTAIALIGCPPLVLLDEP 2097
Cdd:cd03216 65 -SFASPRD-----------ARRAGI-----------------AMVY------QLSVGERQMVEIARALARNARLLILDEP 109
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 105990541 2098 TTGMDPQARRMLWNVIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGafRCMGT 2153
Cdd:cd03216 110 TAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDG--RVVGT 163
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
942-1167 |
6.74e-23 |
|
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: 99.61 E-value: 6.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 942 GRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDI-ETSLDAVRQSLGMCPQHNILFHhlTV 1020
Cdd:cd03253 13 GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIrEVTLDSLRRAIGVVPQDTVLFN--DT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1021 AEHMLFYAQLKGKSQEEAQLEMEAMLEDT------GLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTSGVDP 1094
Cdd:cd03253 91 IGYNIRYGRPDATDEEVIEAAKAAQIHDKimrfpdGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLDEATSALDT 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 105990541 1095 YSRRSIWDLLLKYRSGRTIIMSTHHMDEAdLLGDRIAIIAQGRLYCSGTPLFL--KNcfgtGLYltlvRKMKNIQ 1167
Cdd:cd03253 171 HTEREIQAALRDVSKGRTTIVIAHRLSTI-VNADKIIVLKDGRIVERGTHEELlaKG----GLY----AEMWKAQ 236
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
943-1142 |
7.32e-23 |
|
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: 99.14 E-value: 7.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 943 RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDieTSLDAVrqSLGMCPQhnilfhhLTVAE 1022
Cdd:cd03220 35 FWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRV--SSLLGL--GGGFNPE-------LTGRE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1023 HMLFYAQLKGKSQEEAQLEMEAMLEDTGLhhkrnEEAQDL-----SGGMQRKL--SVAIAFVGDakVVILDEPTSGVDPY 1095
Cdd:cd03220 104 NIYLNGRLLGLSRKEIDEKIDEIIEFSEL-----GDFIDLpvktySSGMKARLafAIATALEPD--ILLIDEVLAVGDAA 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 105990541 1096 SRRSIWDLLLKYRS-GRTIIMSTHHMDEADLLGDRIAIIAQGRLYCSG 1142
Cdd:cd03220 177 FQEKCQRRLRELLKqGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
1913-2157 |
1.03e-22 |
|
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: 105.23 E-value: 1.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1913 PIVDEDDDVAEERQRIITggNKTDILRLHELTKIYPGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVT 1992
Cdd:COG4987 311 ELLDAPPAVTEPAEPAPA--PGGPSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQ 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1993 SGDATVAGKSILT-NISEVHQNMGYCPQ----FDAidellTGREHLyLYARlrgvPA---EEIEKV------ANWsIKSL 2058
Cdd:COG4987 389 SGSITLGGVDLRDlDEDDLRRRIAVVPQrphlFDT-----TLRENL-RLAR----PDatdEELWAAlervglGDW-LAAL 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2059 --GLtvyaDCLAGTY----SGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSiIREGRAVVLTSHSMEE 2132
Cdd:COG4987 458 pdGL----DTWLGEGgrrlSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLE-ALAGRTVLLITHRLAG 532
|
250 260
....*....|....*....|....*
gi 105990541 2133 CEAlCTRLAIMVKGAFRCMGTIQHL 2157
Cdd:COG4987 533 LER-MDRILVLEDGRIVEQGTHEEL 556
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1962-2146 |
1.17e-22 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 98.76 E-value: 1.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGK-SILTNIsevhqNMGYCPQfdaidelLTGREHLYLYARLR 2040
Cdd:cd03220 45 VPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRvSSLLGL-----GGGFNPE-------LTGRENIYLNGRLL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2041 GVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSIIREG 2120
Cdd:cd03220 113 GLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQG 192
|
170 180
....*....|....*....|....*.
gi 105990541 2121 RAVVLTSHSMEECEALCTRLAIMVKG 2146
Cdd:cd03220 193 KTVILVSHDPSSIKRLCDRALVLEKG 218
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
920-1165 |
1.55e-22 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 104.80 E-value: 1.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 920 REHPGWVPG-VCVKNLVKIFEPCGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDI-ETS 997
Cdd:TIGR02203 321 TRAIERARGdVEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLaDYT 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 998 LDAVRQSLGMCPQHNILFHHlTVAEHMLfYAQLKGKSQE--EAQLEMEAMLE-----DTGLHHKRNEEAQDLSGGMQRKL 1070
Cdd:TIGR02203 401 LASLRRQVALVSQDVVLFND-TIANNIA-YGRTEQADRAeiERALAAAYAQDfvdklPLGLDTPIGENGVLLSGGQRQRL 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1071 SVAIAFVGDAKVVILDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADlLGDRIAIIAQGRLYCSGT--PLFLK 1148
Cdd:TIGR02203 479 AIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIE-KADRIVVMDDGRIVERGThnELLAR 557
|
250
....*....|....*..
gi 105990541 1149 NcfgtGLYLTLvRKMKN 1165
Cdd:TIGR02203 558 N----GLYAQL-HNMQF 569
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
943-1165 |
1.60e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 99.87 E-value: 1.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 943 RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPP-----TSGTVLVGGRDIETSLDaVRQSLGMCPQH-NILFH 1016
Cdd:PRK13640 20 KPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnpnSKITVDGITLTAKTVWD-IREKVGIVFQNpDNQFV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1017 HLTVAEHMLFYAQLKGKSQEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTSGVDPYS 1096
Cdd:PRK13640 99 GATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAG 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 105990541 1097 RRSIWDLL--LKYRSGRTIIMSTHHMDEADlLGDRIAIIAQGRLYCSGTPL-------FLKNcfgTGLYLTLVRKMKN 1165
Cdd:PRK13640 179 KEQILKLIrkLKKKNNLTVISITHDIDEAN-MADQVLVLDDGKLLAQGSPVeifskveMLKE---IGLDIPFVYKLKN 252
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1939-2146 |
2.30e-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: 96.35 E-value: 2.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1939 RLHELTKIYPGTssPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISEVHQNMGYC 2017
Cdd:cd03214 1 EVENLSVGYGGR--TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASlSPKELARKIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2018 PQfdaidelltgrehlylyarlrgvpaeeiekvanwSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEP 2097
Cdd:cd03214 79 PQ----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEP 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 105990541 2098 TTGMDP--QARRMlwNVIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKG 2146
Cdd:cd03214 125 TSHLDIahQIELL--ELLRRLARErGKTVVMVLHDLNLAARYADRVILLKDG 174
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
931-1132 |
2.82e-22 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 100.13 E-value: 2.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 931 VKNLVKIFEPCGRP--AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPP---TSGTVLVGGRDI----ETSLDAV 1001
Cdd:COG0444 4 VRNLKVYFPTRRGVvkAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLlklsEKELRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1002 R-QSLGMCPQH-----NILFhhlTVAEHML-FYAQLKGKSQEEAQLEMEAMLEDTGLHHKrnEEAQD-----LSGGMQRK 1069
Cdd:COG0444 84 RgREIQMIFQDpmtslNPVM---TVGDQIAePLRIHGGLSKAEARERAIELLERVGLPDP--ERRLDrypheLSGGMRQR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 105990541 1070 LSVAIAFVGDAKVVILDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAI 1132
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDVTIQAQILNLLkdLQRELGLAILFITHDLGVVAEIADRVAV 223
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
942-1138 |
3.49e-22 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 98.19 E-value: 3.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 942 GRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGL--LPP---TSGTVLVGGRDI---ETSLDAVRQSLGMCPQHNI 1013
Cdd:COG1117 23 DKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndLIPgarVEGEILLDGEDIydpDVDVVELRRRVGMVFQKPN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1014 LFHHlTVAEHMLFYAQLKG-KSQEEAQLEMEAMLEDTGL----HHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEP 1088
Cdd:COG1117 103 PFPK-SIYDNVAYGLRLHGiKSKSELDEIVEESLRKAALwdevKDRLKKSALGLSGGQQQRLCIARALAVEPEVLLMDEP 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 105990541 1089 TSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIIAQGRL 1138
Cdd:COG1117 182 TSALDPISTAKIEELILELKKDYTIVIVTHNMQQAARVSDYTAFFYLGEL 231
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
1939-2148 |
4.65e-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: 96.56 E-value: 4.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1939 RLHELTKIYPGTSSpAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI-----LTNISEVHQN 2013
Cdd:cd03226 1 RIENISFSYKKGTE-ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIkakerRKSIGYVMQD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2014 MGYCPQFDaidellTGREHLYLYARLRGVPAEEIEKVanwsIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVL 2093
Cdd:cd03226 80 VDYQLFTD------SVREELLLGLKELDAGNEQAETV----LKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 105990541 2094 LDEPTTGMDPQARRMLWNVIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAF 2148
Cdd:cd03226 150 FDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
945-1145 |
5.55e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 98.54 E-value: 5.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIETSLDAV------RQSLGMC---PQHNiLF 1015
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKIkevkrlRKEIGLVfqfPEYQ-LF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1016 HHlTVAEHMLFYAQLKGKSQEEAQLEMEAMLEDTGLHHKRNEEAQ-DLSGGMQRKLSVAIAFVGDAKVVILDEPTSGVDP 1094
Cdd:PRK13645 105 QE-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDYVKRSPfELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDP 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 105990541 1095 YSRRSIWDLLLKYRS--GRTIIMSTHHMDEADLLGDRIAIIAQGRLYCSGTPL 1145
Cdd:PRK13645 184 KGEEDFINLFERLNKeyKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPF 236
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1953-2128 |
6.38e-22 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 95.89 E-value: 6.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1953 PAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISEVHQNMGYCPQFDAIDELLTGREH 2032
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPELSALEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2033 LYLYARLRGVPAEEIEKvanwSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNV 2112
Cdd:TIGR01189 94 LHFWAAIHGGAQRTIED----ALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGL 169
|
170
....*....|....*.
gi 105990541 2113 IVSIIREGRAVVLTSH 2128
Cdd:TIGR01189 170 LRAHLARGGIVLLTTH 185
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1937-2131 |
6.61e-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: 6.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1937 ILRLHELTKIYPGtSSPAVDRLCVGVRPGE-CFgLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSiLTNIS--EVH-- 2011
Cdd:COG2884 1 MIRFENVSKRYPG-GREALSDVSLEIEKGEfVF-LTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQD-LSRLKrrEIPyl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2012 -QNMGYCPQfdaiD-ELLTGR---EHLYLYARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALI 2086
Cdd:COG2884 78 rRRIGVVFQ----DfRLLPDRtvyENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALV 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 105990541 2087 GCPPLVLLDEPTTGMDPQARRMLWNVIVSIIREGRAVVLTSHSME 2131
Cdd:COG2884 154 NRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLE 198
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
931-1144 |
6.89e-22 |
|
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: 96.41 E-value: 6.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 931 VKNLVKIFEPCGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIET-SLDAVRQSLGMCP 1009
Cdd:cd03244 5 FKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKiGLHDLRSRISIIP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1010 QHNILFH---------HLTVAEHMLFYAqLkgksqEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGmQRKL-SVAIAFVGD 1079
Cdd:cd03244 85 QDPVLFSgtirsnldpFGEYSDEELWQA-L-----ERVGLKEFVESLPGGLDTVVEEGGENLSVG-QRQLlCLARALLRK 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 105990541 1080 AKVVILDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDE-ADLlgDRIAIIAQGRLYCSGTP 1144
Cdd:cd03244 158 SKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTiIDS--DRILVLDKGRVVEFDSP 221
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
931-1138 |
7.50e-22 |
|
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: 94.59 E-value: 7.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 931 VKNLVKIFEPCGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIET-SLDAVRQSLGMCP 1009
Cdd:cd03246 3 VENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQwDPNELGDHVGYLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1010 QHNILFHHlTVAEHMlfyaqlkgksqeeaqlemeamledtglhhkrneeaqdLSGGMQRKLSVAIAFVGDAKVVILDEPT 1089
Cdd:cd03246 83 QDDELFSG-SIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPN 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 105990541 1090 SGVDPYSRRSIWDLLLKYRS-GRTIIMSTHHMdEADLLGDRIAIIAQGRL 1138
Cdd:cd03246 125 SHLDVEGERALNQAIAALKAaGATRIVIAHRP-ETLASADRILVLEDGRV 173
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
944-1143 |
7.51e-22 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 102.60 E-value: 7.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 944 PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDI-ETSLDAVRQSLGMCPQHNILFHHlTVAE 1022
Cdd:PRK11160 354 PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIaDYSEAALRQAISVVSQRVHLFSA-TLRD 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1023 HMLFyaqLKGKSQEEaqlEMEAMLEDTGLH-HKRNEEAQD---------LSGGMQRKLSVAIAFVGDAKVVILDEPTSGV 1092
Cdd:PRK11160 433 NLLL---AAPNASDE---ALIEVLQQVGLEkLLEDDKGLNawlgeggrqLSGGEQRRLGIARALLHDAPLLLLDEPTEGL 506
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 105990541 1093 DPYSRRSIWDLLLKYRSGRTIIMSTH------HMdeadllgDRIAIIAQGRLYCSGT 1143
Cdd:PRK11160 507 DAETERQILELLAEHAQNKTVLMITHrltgleQF-------DRICVMDNGQIIEQGT 556
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
942-1136 |
7.63e-22 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 97.08 E-value: 7.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 942 GRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIETSlDAVRqslGMCPQHNILFHHLTVA 1021
Cdd:PRK11248 13 GKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGP-GAER---GVVFQNEGLLPWRNVQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1022 EHMLFYAQLKGKSQEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTSGVDPYSRRSIW 1101
Cdd:PRK11248 89 DNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQ 168
|
170 180 190
....*....|....*....|....*....|....*..
gi 105990541 1102 DLLLK--YRSGRTIIMSTHHMDEADLLGDRIAIIAQG 1136
Cdd:PRK11248 169 TLLLKlwQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
946-1136 |
8.23e-22 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 96.38 E-value: 8.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 946 VDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDI-ETSLD--AVRQSLGMCPQhnilfhhLTVAE 1022
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQItEPGPDrmVVFQNYSLLPW-------LTVRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1023 HMLFY--AQLKGKSQEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTSGVDPYSRRSI 1100
Cdd:TIGR01184 74 NIALAvdRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNL 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 105990541 1101 WDLLLKY--RSGRTIIMSTHHMDEADLLGDRIAIIAQG 1136
Cdd:TIGR01184 154 QEELMQIweEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1937-2153 |
8.31e-22 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 96.89 E-value: 8.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1937 ILRLHELTKIYPGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGK--SILTNISEVHQNM 2014
Cdd:PRK10895 3 TLTAKNLAKAYKGRR--VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEdiSLLPLHARARRGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2015 GYCPQFDAIDELLTGREHLYLYARLR-GVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVL 2093
Cdd:PRK10895 81 GYLPQEASIFRRLSVYDNLMAVLQIRdDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2094 LDEPTTGMDPQARRMLWNVIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFRCMGT 2153
Cdd:PRK10895 161 LDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGT 220
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
945-1144 |
8.38e-22 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 96.69 E-value: 8.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRdIeTSLDAVrqSLGMCPQhnilfhhLTVAEHM 1024
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR-V-SALLEL--GAGFHPE-------LTGRENI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1025 LFYAQLKGKSQEeaqlEMEAMLED----TGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTSGVDPY-SRRS 1099
Cdd:COG1134 110 YLNGRLLGLSRK----EIDEKFDEivefAELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAfQKKC 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 105990541 1100 IwDLLLKYR-SGRTIIMSTHHMDEADLLGDRIAIIAQGRLYCSGTP 1144
Cdd:COG1134 186 L-ARIRELReSGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDP 230
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
945-1138 |
1.67e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 96.00 E-value: 1.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILT--GLLPP---TSGTVLVGGRDI---ETSLDAVRQSLGMCPQHNILFH 1016
Cdd:PRK14239 20 ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDLNPevtITGSIVYNGHNIyspRTDTVDLRKEIGMVFQQPNPFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1017 hLTVAEHMLFYAQLKG-KSQE------EAQLEMEAMLEDTG--LHhkrnEEAQDLSGGMQRKLSVAIAFVGDAKVVILDE 1087
Cdd:PRK14239 100 -MSIYENVVYGLRLKGiKDKQvldeavEKSLKGASIWDEVKdrLH----DSALGLSGGQQQRVCIARVLATSPKIILLDE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 105990541 1088 PTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIIAQGRL 1138
Cdd:PRK14239 175 PTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRISDRTGFFLDGDL 225
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
940-1144 |
2.83e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 96.21 E-value: 2.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 940 PCGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDI--ETSLDAVRQSLGMCPQH-NILFH 1016
Cdd:PRK13644 12 PDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTgdFSKLQGIRKLVGIVFQNpETQFV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1017 HLTVAEHMLFYAQLKGKSQEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTSGVDPYS 1096
Cdd:PRK13644 92 GRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDS 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 105990541 1097 RRSIWDLLLK-YRSGRTIIMSTHHMDEADlLGDRIAIIAQGRLYCSGTP 1144
Cdd:PRK13644 172 GIAVLERIKKlHEKGKTIVYITHNLEELH-DADRIIVMDRGKIVLEGEP 219
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1937-2143 |
3.48e-21 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 99.71 E-value: 3.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1937 ILRLHELTKIYPGTssPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI-LTNISE------ 2009
Cdd:COG1129 4 LLEMRGISKSFGGV--KALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVrFRSPRDaqaagi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2010 --VHQNMGYCPQFDAIDELLTGRE----HLYLYARLRgvpaEEIEKVanwsIKSLGLTVYADCLAGTYSGGNKRKLSTAI 2083
Cdd:COG1129 82 aiIHQELNLVPNLSVAENIFLGREprrgGLIDWRAMR----RRAREL----LARLGLDIDPDTPVGDLSVAQQQLVEIAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2084 ALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSIIREGRAVVLTSHSMEECEALCTRLAIM 2143
Cdd:COG1129 154 ALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVL 213
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
945-1144 |
3.83e-21 |
|
nickel import ATP-binding protein NikD; This family represents the NikD 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. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 94.36 E-value: 3.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPP----TSGTVLVGGRDIETSldAVRQ-SLGMCPQH-----NIL 1014
Cdd:TIGR02770 1 LVQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPgltqTSGEILLDGRPLLPL--SIRGrHIATIMQNprtafNPL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1015 FhhlTVAEHMLFYAQLKGKSQEEAQLEMEAMLEDTGLHHKrnEEAQD-----LSGGMQRKLSVAIAFVGDAKVVILDEPT 1089
Cdd:TIGR02770 79 F---TMGNHAIETLRSLGKLSKQARALILEALEAVGLPDP--EEVLKkypfqLSGGMLQRVMIALALLLEPPFLIADEPT 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 105990541 1090 SGVDPYSRRSIWDLLLKYRS--GRTIIMSTHHMDEADLLGDRIAIIAQGRLYCSGTP 1144
Cdd:TIGR02770 154 TDLDVVNQARVLKLLRELRQlfGTGILLITHDLGVVARIADEVAVMDDGRIVERGTV 210
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
960-1138 |
4.00e-21 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 94.42 E-value: 4.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 960 AFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIeTSLD-----AVR-QSLGMCPQHnilFH---HLTVAEHMLFYAQL 1030
Cdd:COG4181 42 AIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDL-FALDedaraRLRaRHVGFVFQS---FQllpTLTALENVMLPLEL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1031 KGKSqeEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTSGVDPYSRRSIWDLL--LKYR 1108
Cdd:COG4181 118 AGRR--DARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLfeLNRE 195
|
170 180 190
....*....|....*....|....*....|.
gi 105990541 1109 SGRTIIMSTHhmDEADLL-GDRIAIIAQGRL 1138
Cdd:COG4181 196 RGTTLVLVTH--DPALAArCDRVLRLRAGRL 224
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1947-2146 |
4.47e-21 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 93.81 E-value: 4.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1947 YPGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI-LTNISEVHQNMGYCPQfDAidE 2025
Cdd:cd03245 12 YPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIrQLDPADLRRNIGYVPQ-DV--T 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2026 LLTG--REHLYLYARLrgVPAEEIEKVANWSikslGLTVYADCLAGTY-----------SGGNKRKLSTAIALIGCPPLV 2092
Cdd:cd03245 89 LFYGtlRDNITLGAPL--ADDERILRAAELA----GVTDFVNKHPNGLdlqigergrglSGGQRQAVALARALLNDPPIL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 105990541 2093 LLDEPTTGMDPQARRMLWNVIVSIIReGRAVVLTSH--SMEEceaLCTRLAIMVKG 2146
Cdd:cd03245 163 LLDEPTSAMDMNSEERLKERLRQLLG-DKTLIIITHrpSLLD---LVDRIIVMDSG 214
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
950-1127 |
5.46e-21 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 94.11 E-value: 5.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 950 NITFY--ENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIETSLDAVR-----QSLGMCPQhnilFHHL---- 1018
Cdd:PRK11629 27 NVSFSigEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKaelrnQKLGFIYQ----FHHLlpdf 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1019 TVAEHMLFYAQLKGKSQEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTSGVDPYSRR 1098
Cdd:PRK11629 103 TALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNAD 182
|
170 180 190
....*....|....*....|....*....|.
gi 105990541 1099 SIWDLL--LKYRSGRTIIMSTHHMDEADLLG 1127
Cdd:PRK11629 183 SIFQLLgeLNRLQGTAFLVVTHDLQLAKRMS 213
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
1962-2128 |
6.74e-21 |
|
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: 92.69 E-value: 6.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTT--VTSGDATVAGKSILTNISEVhqnMGYCPQFDAIDELLTGREHLYLYARL 2039
Cdd:cd03232 30 VKPGTLTALMGESGAGKTTLLDVLAGRKTagVITGEILINGRPLDKNFQRS---TGYVEQQDVHSPNLTVREALRFSALL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2040 RGVPAEEiekvanwsikslgltvyadclagtysggnKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSIIRE 2119
Cdd:cd03232 107 RGLSVEQ-----------------------------RKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADS 157
|
....*....
gi 105990541 2120 GRAVVLTSH 2128
Cdd:cd03232 158 GQAILCTIH 166
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1935-2131 |
7.12e-21 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 93.57 E-value: 7.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1935 TDILRLHELTKIYP--GTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIlTNISEV-- 2010
Cdd:COG1136 2 SPLLELRNLTKSYGtgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDI-SSLSERel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2011 ----HQNMGYCPQ-FDAIDELlTGREHLYLYARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIAL 2085
Cdd:COG1136 81 arlrRRHIGFVFQfFNLLPEL-TALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARAL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 105990541 2086 IGCPPLVLLDEPTTGMDPQARRMLWNVIVSIIRE-GRAVVLTSHSME 2131
Cdd:COG1136 160 VNRPKLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHDPE 206
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
945-1144 |
8.41e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 95.69 E-value: 8.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIETSLDAVRQSLGMCPQHNILFHHL------ 1018
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHELITNPYSKKIKNFKELrrrvsm 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1019 ------------TVAEHMLFYAQLKGKSQEEAQLEMEAMLEDTGLHHKRNEEAQ-DLSGGMQRKLSVAIAFVGDAKVVIL 1085
Cdd:PRK13631 121 vfqfpeyqlfkdTIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDSYLERSPfGLSGGQKRRVAIAGILAIQPEILIF 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1086 DEPTSGVDPYSRRSIWDLLLKYR-SGRTIIMSTHHMDEADLLGDRIAIIAQGRLYCSGTP 1144
Cdd:PRK13631 201 DEPTAGLDPKGEHEMMQLILDAKaNNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTP 260
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1962-2158 |
9.23e-21 |
|
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: 93.51 E-value: 9.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIlTNISE-----VHQNMGYCPQFDAideLLTG------- 2029
Cdd:COG1127 28 VPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDI-TGLSEkelyeLRRRIGMLFQGGA---LFDSltvfenv 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2030 ----REHlylyarlRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQA 2105
Cdd:COG1127 104 afplREH-------TDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILLYDEPTAGLDPIT 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 105990541 2106 RRmlwnVIVSIIRE-----GRAVVLTSHSMEECEALCTRLAIMVKGAFRCMGTIQHLK 2158
Cdd:COG1127 177 SA----VIDELIRElrdelGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELL 230
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
945-1144 |
1.00e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 94.43 E-value: 1.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIET-SLDAVRQSLGMCPQH-NILFHHLTVAE 1022
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDdNFEKLRKHIGIVFQNpDNQFVGSIVKY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1023 HMLFYAQLKGKSQEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTSGVDPYSRRSIWD 1102
Cdd:PRK13648 104 DVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLD 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 105990541 1103 LLLKYRSGR--TIIMSTHHMDEAdLLGDRIAIIAQGRLYCSGTP 1144
Cdd:PRK13648 184 LVRKVKSEHniTIISITHDLSEA-MEADHVIVMNKGTVYKEGTP 226
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
944-1144 |
1.11e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 94.30 E-value: 1.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 944 PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIETS---LDAVRQSLGMC---PQHNILFhh 1017
Cdd:PRK13638 15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSkrgLLALRQQVATVfqdPEQQIFY-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1018 LTVAEHMLFYAQLKGKSQEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTSGVDPYSR 1097
Cdd:PRK13638 93 TDIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGR 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 105990541 1098 RSIWDLLLK-YRSGRTIIMSTHHMDEADLLGDRIAIIAQGRLYCSGTP 1144
Cdd:PRK13638 173 TQMIAIIRRiVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAP 220
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1962-2158 |
1.27e-20 |
|
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: 92.95 E-value: 1.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNIS----EVHQNMGYCPQFDAIDELLTGREH--LYL 2035
Cdd:cd03261 23 VRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEaelyRLRRRMGMLFQSGALFDSLTVFENvaFPL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2036 YARLRGvPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARrmlwNVIVS 2115
Cdd:cd03261 103 REHTRL-SEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEPTAGLDPIAS----GVIDD 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 105990541 2116 IIRE-----GRAVVLTSHSMEECEALCTRLAIMVKGAFRCMGTIQHLK 2158
Cdd:cd03261 178 LIRSlkkelGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELR 225
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
943-1162 |
1.27e-20 |
|
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: 93.37 E-value: 1.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 943 RPAV---DRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIET-SLDAVRQSLGMCPQHNILFHhL 1018
Cdd:cd03249 13 RPDVpilKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDlNLRWLRSQIGLVSQEPVLFD-G 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1019 TVAEHMLFyaqlkGKSQEEAQLEMEAMLED------TGLHHKRNEEAQD----LSGGMQRKLSVAIAFVGDAKVVILDEP 1088
Cdd:cd03249 92 TIAENIRY-----GKPDATDEEVEEAAKKAnihdfiMSLPDGYDTLVGErgsqLSGGQKQRIAIARALLRNPKILLLDEA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 105990541 1089 TSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMD---EAdllgDRIAIIAQGRLYCSGTP--LFLKNcfgtGLYLTLVRK 1162
Cdd:cd03249 167 TSALDAESEKLVQEALDRAMKGRTTIVIAHRLStirNA----DLIAVLQNGQVVEQGTHdeLMAQK----GVYAKLVKA 237
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
933-1149 |
1.33e-20 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 94.06 E-value: 1.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 933 NLVKI----FEPCGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDI----ETSLDAVRQS 1004
Cdd:PRK11831 6 NLVDMrgvsFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamsRSRLYTVRKR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1005 LGMCPQHNILFHHLTVAEHMLFyaQLKGKSQ-EEAQLEMEAM--LEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAK 1081
Cdd:PRK11831 86 MSMLFQSGALFTDMNVFDNVAY--PLREHTQlPAPLLHSTVMmkLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPD 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1082 VVILDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIIAQGRLYCSGTPLFLKN 1149
Cdd:PRK11831 164 LIMFDEPFVGQDPITMGVLVKLIseLNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQA 233
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
949-1147 |
2.16e-20 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 95.48 E-value: 2.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGR---DIETSldavRQSLGMCPQHNILFHHLTVAEHML 1025
Cdd:PRK11000 22 INLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKrmnDVPPA----ERGVGMVFQSYALYPHLSVAENMS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1026 FYAQLKGKSQEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGmQRKlSVAIA--FVGDAKVVILDEPTSGVDPYSR---RSI 1100
Cdd:PRK11000 98 FGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGG-QRQ-RVAIGrtLVAEPSVFLLDEPLSNLDAALRvqmRIE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 105990541 1101 WDLLLKyRSGRTIIMSTHHMDEADLLGDRIAIIAQGRLYCSGTPLFL 1147
Cdd:PRK11000 176 ISRLHK-RLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
942-1139 |
2.20e-20 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 92.25 E-value: 2.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 942 GRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDI----ETSLDAVRQSLGMCPQHNILFHH 1017
Cdd:PRK10908 14 GRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItrlkNREVPFLRRQIGMIFQDHHLLMD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1018 LTVAEHMLFYAQLKGKSQEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTSGVDPYSR 1097
Cdd:PRK10908 94 RTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALS 173
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 105990541 1098 RSIWDLLLKY-RSGRTIIMSTHHMDEADLLGDRIAIIAQGRLY 1139
Cdd:PRK10908 174 EGILRLFEEFnRVGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1938-2146 |
2.78e-20 |
|
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: 90.32 E-value: 2.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1938 LRLHELTKIYPGTssPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILtnisevhqnmgyc 2017
Cdd:cd03229 1 LELKNVSKRYGQK--TVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLT------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2018 pqfDAIDELLTGREHL-YLYARLRGVPaeeiekvanwsikslGLTVYADCLAGtYSGGNKRKLSTAIALIGCPPLVLLDE 2096
Cdd:cd03229 66 ---DLEDELPPLRRRIgMVFQDFALFP---------------HLTVLENIALG-LSGGQQQRVALARALAMDPDVLLLDE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 105990541 2097 PTTGMDPQARRMLWNVIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKG 2146
Cdd:cd03229 127 PTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
950-1146 |
2.82e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 93.26 E-value: 2.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 950 NITFYENQ--ITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDI-ETSLDAVRQSLGMCPQH-NILFHHLTVAEHML 1025
Cdd:PRK13650 25 DVSFHVKQgeWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLtEENVWDIRHKIGMVFQNpDNQFVGATVEDDVA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1026 FYAQLKGKSQEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTSGVDPYSRRSIWDLLL 1105
Cdd:PRK13650 105 FGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIK 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 105990541 1106 KYRS--GRTIIMSTHHMDEAdLLGDRIAIIAQGRLYCSGTP--LF 1146
Cdd:PRK13650 185 GIRDdyQMTVISITHDLDEV-ALSDRVLVMKNGQVESTSTPreLF 228
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1954-2153 |
2.95e-20 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 92.75 E-value: 2.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1954 AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISEVHQNMGYCPQFD---------AID 2024
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGVVRTFQhvrlfremtVIE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2025 ELLTGrEHLYLYARL----------RGVPAEEIEKVANWsIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLL 2094
Cdd:PRK11300 100 NLLVA-QHQQLKTGLfsgllktpafRRAESEALDRAATW-LERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILML 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2095 DEPTTGMDPQARRMLWNVIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFRCMGT 2153
Cdd:PRK11300 178 DEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGT 237
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
942-1156 |
3.45e-20 |
|
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: 97.89 E-value: 3.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 942 GRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIET-SLDAVRQSLGMCPQHNILFHHlTV 1020
Cdd:TIGR01193 486 GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDiDRHTLRQFINYLPQEPYIFSG-SI 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1021 AEHMLFYAQlKGKSQEE--AQLEMEAMLEDT-----GLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTSGVD 1093
Cdd:TIGR01193 565 LENLLLGAK-ENVSQDEiwAACEIAEIKDDIenmplGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLD 643
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 105990541 1094 PYSRRSIWDLLLKYRSgRTIIMSTHHMDEADLLgDRIAIIAQGRLYCSGT--PLFLKNCFGTGLY 1156
Cdd:TIGR01193 644 TITEKKIVNNLLNLQD-KTIIFVAHRLSVAKQS-DKIIVLDHGKIIEQGShdELLDRNGFYASLI 706
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
929-1143 |
3.66e-20 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 91.91 E-value: 3.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 929 VCVKNLVKIFEPCGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDI-ETSLDAVRQSLGM 1007
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVrDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1008 CPQHNILFHHlTVAEHMLFYAqlKGKSQEEAQLEMEA-------MLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDA 1080
Cdd:cd03251 81 VSQDVFLFND-TVAENIAYGR--PGATREEVEEAARAanahefiMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 105990541 1081 KVVILDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHM---DEAdllgDRIAIIAQGRLYCSGT 1143
Cdd:cd03251 158 PILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLstiENA----DRIVVLEDGKIVERGT 219
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1962-2191 |
3.82e-20 |
|
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: 92.71 E-value: 3.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT------------NISEVHQNMGYCPQFDAIDELLTG 2029
Cdd:cd03294 47 VREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAmsrkelrelrrkKISMVFQSFALLPHRTVLENVAFG 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2030 REhlylyarLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRML 2109
Cdd:cd03294 127 LE-------VQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREM 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2110 WNVIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFRCMGTIQHLkskfgdgyivtmkIKSPKDDLlpdlnpVEQF 2188
Cdd:cd03294 200 QDELLRLQAElQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEI-------------LTNPANDY------VREF 260
|
...
gi 105990541 2189 FQG 2191
Cdd:cd03294 261 FRG 263
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1938-2146 |
4.21e-20 |
|
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: 91.86 E-value: 4.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1938 LRLHELTKIYPGtSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-----------N 2006
Cdd:cd03256 1 IEVENLSKTYPN-GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKlkgkalrqlrrQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2007 ISEVHQNMGYCPQFDAIDELLTGR--EHLYLYARLRGVPAEEIEKvANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIA 2084
Cdd:cd03256 80 IGMIFQQFNLIERLSVLENVLSGRlgRRSTWRSLFGLFPKEEKQR-ALAALERVGLLDKAYQRADQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 105990541 2085 LIGCPPLVLLDEPTTGMDPQARRMLWNVIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKG 2146
Cdd:cd03256 159 LMQQPKLILADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDLAREYADRIVGLKDG 221
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
960-1142 |
5.51e-20 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 91.18 E-value: 5.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 960 AFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDiETSLDAVRQSLGMCPQHNILFHHLTVAEHMLF--YAQLKGKSQEE 1037
Cdd:PRK10771 29 AILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD-HTTTPPSRRPVSMLFQENNLFSHLTVAQNIGLglNPGLKLNAAQR 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1038 AQLemEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTSGVDPYSRRSIWDLLLKYRSGR--TIIM 1115
Cdd:PRK10771 108 EKL--HAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQERqlTLLM 185
|
170 180
....*....|....*....|....*..
gi 105990541 1116 STHHMDEADLLGDRIAIIAQGRLYCSG 1142
Cdd:PRK10771 186 VSHSLEDAARIAPRSLVVADGRIAWDG 212
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1940-2128 |
6.31e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 95.90 E-value: 6.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1940 LHELTKIYPGTssPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKsilTNISEVHQNMGYCPQ 2019
Cdd:COG0488 1 LENLSKSFGGR--PLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG---LRIGYLPQEPPLDDD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2020 FDAIDELLTGREHLY-LYARLR------GVPAEEIEKVAN----------WSIKS--------LGLT-VYADCLAGTYSG 2073
Cdd:COG0488 76 LTVLDTVLDGDAELRaLEAELEeleaklAEPDEDLERLAElqeefealggWEAEAraeeilsgLGFPeEDLDRPVSELSG 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 105990541 2074 GNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSiiREGrAVVLTSH 2128
Cdd:COG0488 156 GWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKN--YPG-TVLVVSH 207
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
945-1144 |
7.03e-20 |
|
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: 96.02 E-value: 7.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGT--VLVGGRDIETSLDA------VRQSLGMCPQHNILFH 1016
Cdd:TIGR03269 299 AVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEvnVRVGDEWVDMTKPGpdgrgrAKRYIGILHQEYDLYP 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1017 HLTVAEHMLFYAQLKgKSQEEAQLEMEAMLEDTGLHHKRNEEAQD-----LSGGMQRKLSVAIAFVGDAKVVILDEPTSG 1091
Cdd:TIGR03269 379 HRTVLDNLTEAIGLE-LPDELARMKAVITLKMVGFDEEKAEEILDkypdeLSEGERHRVALAQVLIKEPRIVILDEPTGT 457
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 105990541 1092 VDPYSRRSIWDLLLKYRS--GRTIIMSTHHMDEADLLGDRIAIIAQGRLYCSGTP 1144
Cdd:TIGR03269 458 MDPITKVDVTHSILKAREemEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDP 512
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
949-1143 |
7.91e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 91.65 E-value: 7.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLP------PTSGTVLVGGRDIeTSLDAV--RQSLGMCPQHNILFHHLTV 1020
Cdd:PRK14246 29 ITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDI-FQIDAIklRKEVGMVFQQPNPFPHLSI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1021 AEHMLFYAQLKG-KSQEEAQLEMEAMLEDTGL----HHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTSGVDPY 1095
Cdd:PRK14246 108 YDNIAYPLKSHGiKEKREIKKIVEECLRKVGLwkevYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIV 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 105990541 1096 SRRSIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIIAQGRLYCSGT 1143
Cdd:PRK14246 188 NSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGS 235
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1956-2128 |
8.82e-20 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 89.86 E-value: 8.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1956 DRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISEVHQNMGYCPQFDAIDELLTGREHLYL 2035
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLLYLGHQPGIKTELTALENLRF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2036 YARLRGVPAEEiekvANWSI-KSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIV 2114
Cdd:PRK13538 98 YQRLHGPGDDE----ALWEAlAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALLA 173
|
170
....*....|....
gi 105990541 2115 SIIREGRAVVLTSH 2128
Cdd:PRK13538 174 QHAEQGGMVILTTH 187
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1962-2148 |
1.05e-19 |
|
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: 88.64 E-value: 1.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI-LTNISEVHQN-MGYCPQfDAIDELLtgrehlylyarl 2039
Cdd:cd03215 23 VRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVtRRSPRDAIRAgIAYVPE-DRKREGL------------ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2040 rgvpaeeiekVANWSIKS-LGLTVYadclagtYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSIIR 2118
Cdd:cd03215 90 ----------VLDLSVAEnIALSSL-------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELAD 152
|
170 180 190
....*....|....*....|....*....|
gi 105990541 2119 EGRAVVLTSHSMEECEALCTRLAIMVKGAF 2148
Cdd:cd03215 153 AGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
931-1168 |
1.07e-19 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 91.23 E-value: 1.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 931 VKNLVKIFEPcgRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLP----PTSGTVLVG---------GRDIETS 997
Cdd:PRK09984 7 VEKLAKTFNQ--HQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdksAGSHIELLGrtvqregrlARDIRKS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 998 ldavRQSLGMCPQHNILFHHLTVAEHMLFYAQ---------LKGKSQEEAQLEMEAmLEDTGLHHKRNEEAQDLSGGMQR 1068
Cdd:PRK09984 85 ----RANTGYIFQQFNLVNRLSVLENVLIGALgstpfwrtcFSWFTREQKQRALQA-LTRVGMVHFAHQRVSTLSGGQQQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1069 KLSVAIAFVGDAKVVILDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIIAQGRLYCSGTPLF 1146
Cdd:PRK09984 160 RVAIARALMQQAKVILADEPIASLDPESARIVMDTLrdINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQ 239
|
250 260
....*....|....*....|..
gi 105990541 1147 LKNCFGTGLYLTLVRKMKNIQS 1168
Cdd:PRK09984 240 FDNERFDHLYRSINRVEENAKA 261
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
891-1138 |
1.49e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 94.75 E-value: 1.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 891 ERALEKTEPlteetEDPEHPEG-IHDSFFEREHPGWVPgVCVKNLVKIFEpcGRPAVDRLNITFYENQITAFLGHNGAGK 969
Cdd:COG0488 283 IKALEKLER-----EEPPRRDKtVEIRFPPPERLGKKV-LELEGLSKSYG--DKTLLDDLSLRIDRGDRIGLIGPNGAGK 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 970 TTTLSILTGLLPPTSGTVLVGgrdietsldaVRQSLGMCPQHNILFH-HLTVAEHMLFYAQlKGKSQEEAQLeMEAML-- 1046
Cdd:COG0488 355 STLLKLLAGELEPDSGTVKLG----------ETVKIGYFDQHQEELDpDKTVLDELRDGAP-GGTEQEVRGY-LGRFLfs 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1047 -EDtglHHKRneeAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTSGVDPYSRRSIWDLLLKYrSGrTIIMSTHHMDEADL 1125
Cdd:COG0488 423 gDD---AFKP---VGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDF-PG-TVLLVSHDRYFLDR 494
|
250
....*....|...
gi 105990541 1126 LGDRIAIIAQGRL 1138
Cdd:COG0488 495 VATRILEFEDGGV 507
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
931-1138 |
3.80e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 93.54 E-value: 3.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 931 VKNLvkifepCGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGR--DIETSLDAVRQSLGMC 1008
Cdd:COG1129 259 VEGL------SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKpvRIRSPRDAIRAGIAYV 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1009 P---QHNILFHHLTVAEHMLFyAQLKGKS-------QEEAQLeMEAMLEDtgLHHK---RNEEAQDLSGGMQRKlsVAIA 1075
Cdd:COG1129 333 PedrKGEGLVLDLSIRENITL-ASLDRLSrgglldrRRERAL-AEEYIKR--LRIKtpsPEQPVGNLSGGNQQK--VVLA 406
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 105990541 1076 --FVGDAKVVILDEPTSGVDPYSRRSIWDLLLKY-RSGRTIIMSTHHMDEadLLG--DRIAIIAQGRL 1138
Cdd:COG1129 407 kwLATDPKVLILDEPTRGIDVGAKAEIYRLIRELaAEGKAVIVISSELPE--LLGlsDRILVMREGRI 472
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
946-1138 |
4.13e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 89.20 E-value: 4.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 946 VDRLNITFYENQITAFLGHNGAGKTTTLSILTGLL-----PPTSGTVLVGGRDI-ETSLDAVRQSLGMCPQHNILFHHLT 1019
Cdd:PRK14247 19 LDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIelypeARVSGEVYLDGQDIfKMDVIELRRRVQMVFQIPNPIPNLS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1020 VAEHMLFYAQLK--GKSQEEAQLEMEAMLEDTGL----HHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTSGVD 1093
Cdd:PRK14247 99 IFENVALGLKLNrlVKSKKELQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLD 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 105990541 1094 PYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIIAQGRL 1138
Cdd:PRK14247 179 PENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFLYKGQI 223
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1962-2160 |
4.17e-19 |
|
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: 88.55 E-value: 4.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIlTNISEVHQNMGYCPQFDAIDELLTGREHLYLYARLRG 2041
Cdd:cd03299 22 VERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDI-TNLPPEKRDISYVPQNYALFPHMTVYKNIAYGLKKRK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2042 VPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSIIREGR 2121
Cdd:cd03299 101 VDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEFG 180
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 105990541 2122 AVVL-TSHSMEECEALCTRLAIMVKGAFRCMGTIQHLKSK 2160
Cdd:cd03299 181 VTVLhVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1938-2146 |
4.98e-19 |
|
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: 87.22 E-value: 4.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1938 LRLHELTKIYPGTSSPAVDRLCVGV----RPGECFGLLGVNGAGKTTTFKMLTGDTTV--TSGDATVAGKSIltNISEVH 2011
Cdd:cd03213 4 LSFRNLTVTVKSSPSKSGKQLLKNVsgkaKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRPL--DKRSFR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2012 QNMGYCPQFDAIDELLTGREHLYLYARLRGVpaeeiekvanwsikslgltvyadclagtySGGNKRKLSTAIALIGCPPL 2091
Cdd:cd03213 82 KIIGYVPQDDILHPTLTVRETLMFAAKLRGL-----------------------------SGGERKRVSIALELVSNPSL 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 105990541 2092 VLLDEPTTGMDP-QARRmlwnvIVSIIR----EGRAVVLTSHSM-EECEALCTRLAIMVKG 2146
Cdd:cd03213 133 LFLDEPTSGLDSsSALQ-----VMSLLRrladTGRTIICSIHQPsSEIFELFDKLLLLSQG 188
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
1947-2132 |
5.82e-19 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 86.90 E-value: 5.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1947 YPGTssPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILtnisevhqnmGYCPQFDAIDEL 2026
Cdd:NF040873 2 YGGR--PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARV----------AYVPQRSEVPDS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2027 L--TGRE--------HLYLYARLRGVPAEEIEKvanwSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDE 2096
Cdd:NF040873 70 LplTVRDlvamgrwaRRGLWRRLTRDDRAAVDD----ALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDE 145
|
170 180 190
....*....|....*....|....*....|....*.
gi 105990541 2097 PTTGMDPQARRMLWNVIVSIIREGRAVVLTSHSMEE 2132
Cdd:NF040873 146 PTTGLDAESRERIIALLAEEHARGATVVVVTHDLEL 181
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
957-1119 |
8.30e-19 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 86.78 E-value: 8.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 957 QITaflGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIETSLDAVRQSLgmcpqhniLF--HH------LTVAEHMLFYA 1028
Cdd:PRK13538 31 QIE---GPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDL--------LYlgHQpgikteLTALENLRFYQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1029 QLKGKSQEEAqleMEAMLEDTGLHhkRNEE--AQDLSGGMQRKlsVAIA--FVGDAKVVILDEPTSGVDPYSRRSIWDLL 1104
Cdd:PRK13538 100 RLHGPGDDEA---LWEALAQVGLA--GFEDvpVRQLSAGQQRR--VALArlWLTRAPLWILDEPFTAIDKQGVARLEALL 172
|
170
....*....|....*.
gi 105990541 1105 LKY-RSGRTIIMSTHH 1119
Cdd:PRK13538 173 AQHaEQGGMVILTTHQ 188
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
942-1119 |
9.75e-19 |
|
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: 86.78 E-value: 9.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 942 GRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIETSLDAVRQSLGMCPQHNILFHHLTVA 1021
Cdd:cd03231 12 GRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1022 EHMLFYAQLKGKSQ-EEAqlemeamLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTSGVDPYSRRSI 1100
Cdd:cd03231 92 ENLRFWHADHSDEQvEEA-------LARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARF 164
|
170 180
....*....|....*....|
gi 105990541 1101 WDLLLKY-RSGRTIIMSTHH 1119
Cdd:cd03231 165 AEAMAGHcARGGMVVLTTHQ 184
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1935-2159 |
1.09e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 87.86 E-value: 1.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1935 TDILRLHELTKIYPGTssPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSiLTNISEvHQ-- 2012
Cdd:COG4674 8 GPILYVEDLTVSFDGF--KALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTD-LTGLDE-HEia 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2013 NMGYCPQFD--AIDELLTGREHL------------YLYARLRGVPAEEIEKVAnwsiKSLGLTVYADCLAGTYSGGNKRK 2078
Cdd:COG4674 84 RLGIGRKFQkpTVFEELTVFENLelalkgdrgvfaSLFARLTAEERDRIEEVL----ETIGLTDKADRLAGLLSHGQKQW 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2079 LSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSiIREGRAVVLTSHSMEECEALCTRLAIMVKGAFRCMGTIQHLK 2158
Cdd:COG4674 160 LEIGMLLAQDPKLLLLDEPVAGMTDAETERTAELLKS-LAGKHSVVVVEHDMEFVRQIARKVTVLHQGSVLAEGSLDEVQ 238
|
.
gi 105990541 2159 S 2159
Cdd:COG4674 239 A 239
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
1912-2162 |
1.12e-18 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 92.97 E-value: 1.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1912 EPIVDEDDDVAEERQRIITGGNKTDIlRLHELTKIYPGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTV 1991
Cdd:COG2274 449 DDILDLPPEREEGRSKLSLPRLKGDI-ELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEP 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1992 TSGDATVAGKSILT-NISEVHQNMGYCPQfDaiDELLTG--REHLYLYArlRGVPAEEIEKVANWS-----IKSL--GL- 2060
Cdd:COG2274 528 TSGRILIDGIDLRQiDPASLRRQIGVVLQ-D--VFLFSGtiRENITLGD--PDATDEEIIEAARLAglhdfIEALpmGYd 602
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2061 TVYADcLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSIIReGRAVVLTSHSMeECEALCTRL 2140
Cdd:COG2274 603 TVVGE-GGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK-GRTVIIIAHRL-STIRLADRI 679
|
250 260
....*....|....*....|..
gi 105990541 2141 AIMVKGAFRCMGTIQHLKSKFG 2162
Cdd:COG2274 680 IVLDKGRIVEDGTHEELLARKG 701
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1933-2157 |
1.14e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 88.53 E-value: 1.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1933 NKTDILRLHELTKIYPGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKS--------IL 2004
Cdd:PRK13635 1 MKEEIIRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVlseetvwdVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2005 TNISEVHQNmgycP--QF---DAIDELLTGREHlylyarlRGVPAEE-IEKVaNWSIKSLGLTVYADCLAGTYSGGNKRK 2078
Cdd:PRK13635 81 RQVGMVFQN----PdnQFvgaTVQDDVAFGLEN-------IGVPREEmVERV-DQALRQVGMEDFLNREPHRLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2079 LSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSIIREGRAVVLT-SHSMEECeALCTRLAIMVKGAFRCMGTIQHL 2157
Cdd:PRK13635 149 VAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSiTHDLDEA-AQADRVIVMNKGEILEEGTPEEI 227
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
929-1152 |
1.15e-18 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 90.16 E-value: 1.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 929 VCVKNLVKIFepcGRPAV-DRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIETSldAVRQ-SLG 1006
Cdd:PRK11432 7 VVLKNITKRF---GSNTViDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHR--SIQQrDIC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1007 MCPQHNILFHHLTVAEHMLFYAQLKGKSQEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILD 1086
Cdd:PRK11432 82 MVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 105990541 1087 EPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIIAQGRLYCSGTP---------LFLKNCFG 1152
Cdd:PRK11432 162 EPLSNLDANLRRSMREKIreLQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPqelyrqpasRFMASFMG 238
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
942-1124 |
1.36e-18 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 86.38 E-value: 1.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 942 GRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPP---TSGTVLVGGRDIeTSLDAVRQSLGMCPQHNILFHHL 1018
Cdd:COG4136 13 GRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRL-TALPAEQRRIGILFQDDLLFPHL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1019 TVAEHMLFyAQLKGKSQEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTSGVDPYSRR 1098
Cdd:COG4136 92 SVGENLAF-ALPPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRA 170
|
170 180
....*....|....*....|....*...
gi 105990541 1099 SIWDLLLKYRSGRTI--IMSTHhmDEAD 1124
Cdd:COG4136 171 QFREFVFEQIRQRGIpaLLVTH--DEED 196
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
927-1142 |
1.46e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 91.65 E-value: 1.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 927 PGVCVKNLVKIFEpcGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIETSLDAVRQSLG 1006
Cdd:PRK15439 10 PLLCARSISKQYS--GVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1007 --MCPQHNILFHHLTVAEHMLFYAQLKGKSQEeaqlEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVI 1084
Cdd:PRK15439 88 iyLVPQEPLLFPNLSVKENILFGLPKRQASMQ----KMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILI 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 105990541 1085 LDEPTSGVDPYSRRSIWDLLLKYRS-GRTIIMSTHHMDEADLLGDRIAIIAQGRLYCSG 1142
Cdd:PRK15439 164 LDEPTASLTPAETERLFSRIRELLAqGVGIVFISHKLPEIRQLADRISVMRDGTIALSG 222
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1938-2146 |
1.54e-18 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 85.13 E-value: 1.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1938 LRLHELTKIYPGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISEVHQNMGY 2016
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDlDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2017 CPQfdaidelltgreHLYLYARlrgvpaeeiekvanwSIKSLGLtvyadclagtySGGNKRKLSTAIALIGCPPLVLLDE 2096
Cdd:cd03228 81 VPQ------------DPFLFSG---------------TIRENIL-----------SGGQRQRIAIARALLRDPPILILDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 105990541 2097 PTTGMDPQARRMLWNVIVSiIREGRAVVLTSHSMEECEaLCTRLAIMVKG 2146
Cdd:cd03228 123 ATSALDPETEALILEALRA-LAKGKTVIVIAHRLSTIR-DADRIIVLDDG 170
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
931-1123 |
1.89e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 88.60 E-value: 1.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 931 VKNLVKIFEPcGRP----AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIETS--------- 997
Cdd:PRK13651 5 VKNIVKIFNK-KLPtelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKkktkekekv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 998 ----------------LDAVRQSLGMCPQ--HNILFHHlTVAEHMLFYAQLKGKSQEEAQLEMEAMLEDTGLHHKRNEEA 1059
Cdd:PRK13651 84 leklviqktrfkkikkIKEIRRRVGVVFQfaEYQLFEQ-TIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDESYLQRS 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 105990541 1060 Q-DLSGGMQRKLSVAIAFVGDAKVVILDEPTSGVDPYSRRSIWDLLLK-YRSGRTIIMSTHHMDEA 1123
Cdd:PRK13651 163 PfELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNlNKQGKTIILVTHDLDNV 228
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1962-2146 |
1.96e-18 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 92.86 E-value: 1.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTT---VTSGDATVAGKSILTNISevhQNMGYCPQFDAIDELLTGREHLYLYAR 2038
Cdd:TIGR00956 786 VKPGTLTALMGASGAGKTTLLNVLAERVTtgvITGGDRLVNGRPLDSSFQ---RSIGYVQQQDLHLPTSTVRESLRFSAY 862
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2039 LR---GVPAEE----IEKVanwsIKSLGLTVYADCLAGTYSGG----NKRKLSTAIALIGCPPLVL-LDEPTTGMDPQAR 2106
Cdd:TIGR00956 863 LRqpkSVSKSEkmeyVEEV----IKLLEMESYADAVVGVPGEGlnveQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTA 938
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 105990541 2107 rmlWnVIVSIIRE----GRAVVLTSHS-----MEECEalctRLAIMVKG 2146
Cdd:TIGR00956 939 ---W-SICKLMRKladhGQAILCTIHQpsailFEEFD----RLLLLQKG 979
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1933-2155 |
2.00e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 91.38 E-value: 2.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1933 NKTDILRLHELTKIYPGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI--LTN---- 2006
Cdd:PRK09700 1 MATPYISMAGIGKSFGPVH--ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYnkLDHklaa 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2007 ---ISEVHQnmgycpQFDAIDELlTGREHLY----LYARLRGVPA---EEIEKVANWSIKSLGLTVYADCLAGTYSGGNK 2076
Cdd:PRK09700 79 qlgIGIIYQ------ELSVIDEL-TVLENLYigrhLTKKVCGVNIidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHK 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 105990541 2077 RKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFRCMGTIQ 2155
Cdd:PRK09700 152 QMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVS 230
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
958-1144 |
2.33e-18 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 87.33 E-value: 2.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 958 ITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDI--------------ETSLDAVRQSLGMCPQHNILFHHLTVAEH 1023
Cdd:PRK10619 33 VISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlvrdkdgqlkvadKNQLRLLRTRLTMVFQHFNLWSHMTVLEN 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1024 -MLFYAQLKGKSQEEAQLEMEAMLEDTGLHHK-RNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTSGVDPYSRRSIW 1101
Cdd:PRK10619 113 vMEAPIQVLGLSKQEARERAVKYLAKVGIDERaQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVL 192
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 105990541 1102 DLLLKY-RSGRTIIMSTHHMDEADLLGDRIAIIAQGRLYCSGTP 1144
Cdd:PRK10619 193 RIMQQLaEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAP 236
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1941-2146 |
2.83e-18 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 90.85 E-value: 2.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1941 HELTKIYPGTSSPA------VDRLCVG---------VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI-L 2004
Cdd:COG1129 239 RELEDLFPKRAAAPgevvleVEGLSVGgvvrdvsfsVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVrI 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2005 TNISE-VHQNMGYCPQfdaiDELLTG-------REHLYL-----YARLRGVPAEEIEKVANWSIKSLGL-TVYADCLAGT 2070
Cdd:COG1129 319 RSPRDaIRAGIAYVPE----DRKGEGlvldlsiRENITLasldrLSRGGLLDRRRERALAEEYIKRLRIkTPSPEQPVGN 394
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 105990541 2071 YSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
Cdd:COG1129 395 LSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREG 470
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1882-2148 |
2.96e-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: 90.63 E-value: 2.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1882 MVVEGVVYFLLTLLVQRHFflSQWIAEPTKEPIVDEDDDVAE------------------ERQRIITGGNktDILRLHEL 1943
Cdd:TIGR03269 210 ALEEAVKASGISMVLTSHW--PEVIEDLSDKAIWLENGEIKEegtpdevvavfmegvsevEKECEVEVGE--PIIKVRNV 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1944 TKIYPGTSS---PAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSG-----------DAT---VAGKSILTN 2006
Cdd:TIGR03269 286 SKRYISVDRgvvKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGevnvrvgdewvDMTkpgPDGRGRAKR 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2007 -ISEVHQNMGYCPQFDAIDELL--TGREHLYLYARLRGVpaeeiekvanWSIKSLGLT-VYA----DCLAGTYSGGNKRK 2078
Cdd:TIGR03269 366 yIGILHQEYDLYPHRTVLDNLTeaIGLELPDELARMKAV----------ITLKMVGFDeEKAeeilDKYPDELSEGERHR 435
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 105990541 2079 LSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAF 2148
Cdd:TIGR03269 436 VALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEmEQTFIIVSHDMDFVLDVCDRAALMRDGKI 506
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
949-1138 |
3.18e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 86.82 E-value: 3.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLL-----PPTSGTVLVGGRDI-ETSLDA--VRQSLGMCPQHNILFHHLTV 1020
Cdd:PRK14267 23 VDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLelneeARVEGEVRLFGRNIySPDVDPieVRREVGMVFQYPNPFPHLTI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1021 AEHMLFYAQLKG--KSQEEAQLEMEAMLEDTGL----HHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTSGVDP 1094
Cdd:PRK14267 103 YDNVAIGVKLNGlvKSKKELDERVEWALKKAALwdevKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDP 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 105990541 1095 YSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIIAQGRL 1138
Cdd:PRK14267 183 VGTAKIEELLFELKKEYTIVLVTHSPAQAARVSDYVAFLYLGKL 226
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
927-1144 |
3.22e-18 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 89.52 E-value: 3.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 927 PGVCVKNLVKIFEpcGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIE-TSLDAVRQSL 1005
Cdd:PRK09536 2 PMIDVSDLSVEFG--DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEaLSARAASRRV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1006 GMCPQHNIL---FHHLTVAE-----HMLFYAQLkgKSQEEAQLEmEAMlEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFV 1077
Cdd:PRK09536 80 ASVPQDTSLsfeFDVRQVVEmgrtpHRSRFDTW--TETDRAAVE-RAM-ERTGVAQFADRPVTSLSGGERQRVLLARALA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1078 GDAKVVILDEPTSGVDpySRRSIWDLLLKYR---SGRTIIMSTHHMDEADLLGDRIAIIAQGRLYCSGTP 1144
Cdd:PRK09536 156 QATPVLLLDEPTASLD--INHQVRTLELVRRlvdDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPP 223
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
944-1138 |
3.47e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 90.36 E-value: 3.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 944 PAVDRL-NITF--YENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGR-----DIETSLDA----VRQSLGMCPQh 1011
Cdd:PRK11288 15 PGVKALdDISFdcRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQemrfaSTTAALAAgvaiIYQELHLVPE- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1012 nilfhhLTVAEHmLFYAQLKGKS----QEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDE 1087
Cdd:PRK11288 94 ------MTVAEN-LYLGQLPHKGgivnRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 105990541 1088 PTSGVdpySRRSIWDLLLKYRS----GRTIIMSTHHMDEADLLGDRIAIIAQGRL 1138
Cdd:PRK11288 167 PTSSL---SAREIEQLFRVIRElraeGRVILYVSHRMEEIFALCDAITVFKDGRY 218
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1935-2143 |
4.26e-18 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 85.56 E-value: 4.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1935 TDILRLHELTKIYP-----GTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATV--AGKSI-LTN 2006
Cdd:COG4778 2 TTLLEVENLSKTFTlhlqgGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWVdLAQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2007 ISEVH------QNMGYCPQF----------DAIDELLtgrehlylyaRLRGVPAEE-IEKVANWsIKSLGL-----TVYA 2064
Cdd:COG4778 82 ASPREilalrrRTIGYVSQFlrviprvsalDVVAEPL----------LERGVDREEaRARAREL-LARLNLperlwDLPP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2065 dclaGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRmlwnVIVSIIRE----GRAVVLTSHSMEECEALCTRL 2140
Cdd:COG4778 151 ----ATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRA----VVVELIEEakarGTAIIGIFHDEEVREAVADRV 222
|
...
gi 105990541 2141 AIM 2143
Cdd:COG4778 223 VDV 225
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
1963-2164 |
4.94e-18 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 90.49 E-value: 4.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1963 RPGECFGLLGVNGAGKTT-----TFKMLTGdtTVTSGDATVAGKSIltNISEVHQNMGYCPQFDAIDELLTGREHLYLYA 2037
Cdd:TIGR00955 49 KPGELLAVMGSSGAGKTTlmnalAFRSPKG--VKGSGSVLLNGMPI--DAKEMRAISAYVQQDDLFIPTLTVREHLMFQA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2038 RLR---GVPAEE-IEKVANwSIKSLGLTVYADCLAGT------YSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARR 2107
Cdd:TIGR00955 125 HLRmprRVTKKEkRERVDE-VLQALGLRKCANTRIGVpgrvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAY 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 105990541 2108 MLWNVIVSIIREGRAVVLTSH--SMEECEaLCTRLAIMVKGAFRCMGTIQHLKSKFGDG 2164
Cdd:TIGR00955 204 SVVQVLKGLAQKGKTIICTIHqpSSELFE-LFDKIILMAEGRVAYLGSPDQAVPFFSDL 261
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1938-2147 |
6.45e-18 |
|
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: 83.42 E-value: 6.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1938 LRLHELTKIYPGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI-LTNISEVHQNMGY 2016
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADIsQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2017 CPQfDaiDELLTgrehlylyarlrGVPAEEIekvanwsikslgltvyadclagtYSGGNKRKLSTAIALIGCPPLVLLDE 2096
Cdd:cd03246 81 LPQ-D--DELFS------------GSIAENI-----------------------LSGGQRQRLGLARALYGNPRILVLDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 105990541 2097 PTTGMDPQARRMLWNVIVSIIREGRAVVLTSHSMEECEAlCTRLAIMVKGA 2147
Cdd:cd03246 123 PNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLAS-ADRILVLEDGR 172
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
945-1138 |
6.65e-18 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 85.32 E-value: 6.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIETSLDA--VRQSLGMCPQHNILFHHLTVAE 1022
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAkiMREAVAIVPEGRRVFSRMTVEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1023 HMLFYAQLKGKSQEEAQLEMEAMLEDTgLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTSGVDPYSRRSIWD 1102
Cdd:PRK11614 100 NLAMGGFFAERDQFQERIKWVYELFPR-LHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFD 178
|
170 180 190
....*....|....*....|....*....|....*..
gi 105990541 1103 LLLKYRS-GRTIIMSTHHMDEADLLGDRIAIIAQGRL 1138
Cdd:PRK11614 179 TIEQLREqGMTIFLVEQNANQALKLADRGYVLENGHV 215
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
949-1144 |
9.44e-18 |
|
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: 87.47 E-value: 9.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIETS-----LDAVRQSLGMCPQHNILFHHLTVAEH 1023
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSrkgifLPPEKRRIGYVFQEARLFPHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1024 MLFyaQLKGKSQEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTSGVDPYSRRSIWDL 1103
Cdd:TIGR02142 96 LRY--GMKRARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPY 173
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 105990541 1104 L--LKYRSGRTIIMSTHHMDEADLLGDRIAIIAQGRLYCSGTP 1144
Cdd:TIGR02142 174 LerLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPI 216
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1938-2128 |
1.10e-17 |
|
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: 82.75 E-value: 1.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1938 LRLHELTKIYPGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISEVHQNMGYC 2017
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2018 PQfdaidelltgREHLYlyarlrgvpaeeiekvaNWSIKS-LGLtvyadclagTYSGGNKRKLSTAIALIGCPPLVLLDE 2096
Cdd:cd03247 81 NQ----------RPYLF-----------------DTTLRNnLGR---------RFSGGERQRLALARILLQDAPIVLLDE 124
|
170 180 190
....*....|....*....|....*....|..
gi 105990541 2097 PTTGMDPQARRMLWNVIVSIIREGRAVVLTSH 2128
Cdd:cd03247 125 PTVGLDPITERQLLSLIFEVLKDKTLIWITHH 156
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1965-2128 |
1.33e-17 |
|
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: 83.31 E-value: 1.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1965 GECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISEVHQNMGYCPQFDAIDELLTGREHLYLYARLRGvpA 2044
Cdd:cd03231 26 GEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENLRFWHADHS--D 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2045 EEIEKvanwSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSIIREGRAVV 2124
Cdd:cd03231 104 EQVEE----ALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGHCARGGMVV 179
|
....
gi 105990541 2125 LTSH 2128
Cdd:cd03231 180 LTTH 183
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
940-1138 |
1.47e-17 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 89.40 E-value: 1.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 940 PCGRPAVDRL---NITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIET-SLDAV----RQSLGMCPQH 1011
Cdd:PRK10535 15 PSGEEQVEVLkgiSLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATlDADALaqlrREHFGFIFQR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1012 NILFHHLTVAEHMLFYAQLKGKSQEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTSG 1091
Cdd:PRK10535 95 YHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGA 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 105990541 1092 VDPYSRRSIWDLLLKYRS-GRTIIMSTHHMDEADlLGDRIAIIAQGRL 1138
Cdd:PRK10535 175 LDSHSGEEVMAILHQLRDrGHTVIIVTHDPQVAA-QAERVIEIRDGEI 221
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1943-2154 |
1.52e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 85.48 E-value: 1.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1943 LTKIY-PGT--SSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIL---TNISEVHQNMG- 2015
Cdd:PRK13637 8 LTHIYmEGTpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkkVKLSDIRKKVGl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2016 ---YcPQFDAIDEllTGREHLYLYARLRGVPAEEIEKVANWSIKSLGLT--VYADCLAGTYSGGNKRKLSTAIALIGCPP 2090
Cdd:PRK13637 88 vfqY-PEYQLFEE--TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPK 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 105990541 2091 LVLLDEPTTGMDPQARRMLWNVIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFRCMGTI 2154
Cdd:PRK13637 165 ILILDEPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTP 229
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1942-2131 |
1.90e-17 |
|
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: 83.23 E-value: 1.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1942 ELTKIYPGTSsPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIL----TNISEVHQNMGYC 2017
Cdd:cd03292 5 NVTKTYPNGT-AALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSdlrgRAIPYLRRKIGVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2018 PQFDAIDELLTGREHLYLYARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEP 2097
Cdd:cd03292 84 FQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEP 163
|
170 180 190
....*....|....*....|....*....|....
gi 105990541 2098 TTGMDPQARRMLWNVIVSIIREGRAVVLTSHSME 2131
Cdd:cd03292 164 TGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKE 197
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
926-1131 |
2.13e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 84.32 E-value: 2.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 926 VPGVCVKNLVKIFEPcgRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTgLLPPTSGTVLVGGR---------DIET 996
Cdd:PRK14258 5 IPAIKVNNLSFYYDT--QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLN-RMNELESEVRVEGRveffnqniyERRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 997 SLDAVRQSLGMC-PQHNILfhHLTVAEHMLFYAQLKG-KSQEEAQLEMEAMLEDTGL----HHKRNEEAQDLSGGMQRKL 1070
Cdd:PRK14258 82 NLNRLRRQVSMVhPKPNLF--PMSVYDNVAYGVKIVGwRPKLEIDDIVESALKDADLwdeiKHKIHKSALDLSGGQQQRL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 105990541 1071 SVAIAFVGDAKVVILDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIA 1131
Cdd:PRK14258 160 CIARALAVKPKVLLMDEPCFGLDPIASMKVESLIqsLRLRSELTMVIVSHNLHQVSRLSDFTA 222
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
957-1118 |
2.99e-17 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 83.29 E-value: 2.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 957 QITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDI----ETSLDAVR-QSLGMCPQHNILFHHLTVAEHMLFYAQLK 1031
Cdd:PRK10584 37 ETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLhqmdEEARAKLRaKHVGFVFQSFMLIPTLNALENVELPALLR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1032 GKSQEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTSGVDPYSRRSIWDLL--LKYRS 1109
Cdd:PRK10584 117 GESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLfsLNREH 196
|
....*....
gi 105990541 1110 GRTIIMSTH 1118
Cdd:PRK10584 197 GTTLILVTH 205
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
938-1162 |
3.19e-17 |
|
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: 83.30 E-value: 3.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 938 FEPCGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIET-SLDAVRQSLGMCPQHNILFH 1016
Cdd:cd03252 10 YKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALaDPAWLRRQVGVVLQENVLFN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1017 HlTVAEHMlfyaQLKGKSQEEAQLEMEAMLEDT---------GLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDE 1087
Cdd:cd03252 90 R-SIRDNI----ALADPGMSMERVIEAAKLAGAhdfiselpeGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDE 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 105990541 1088 PTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMdEADLLGDRIAIIAQGRLYCSGT--PLFLKNcfgtGLYLTLVRK 1162
Cdd:cd03252 165 ATSALDYESEHAIMRNMHDICAGRTVIIIAHRL-STVKNADRIIVMEKGRIVEQGShdELLAEN----GLYAYLYQL 236
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
1912-2160 |
3.29e-17 |
|
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: 87.89 E-value: 3.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1912 EPIVDEDDDVAEERQRIITGGNKTDIlRLHELTKIYPGtSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTV 1991
Cdd:COG4988 312 FALLDAPEPAAPAGTAPLPAAGPPSI-ELEDVSFSYPG-GRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPP 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1992 TSGDATVAGKSiLTNISE--VHQNMGYCPQFDAideLLTG--REHLYLYARlrGVPAEEIEKVAnwsiKSLGLTVYADCL 2067
Cdd:COG4988 390 YSGSILINGVD-LSDLDPasWRRQIAWVPQNPY---LFAGtiRENLRLGRP--DASDEELEAAL----EAAGLDEFVAAL 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2068 AGTY-----------SGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSiIREGRAVVLTSHSMEECeAL 2136
Cdd:COG4988 460 PDGLdtplgeggrglSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRR-LAKGRTVILITHRLALL-AQ 537
|
250 260
....*....|....*....|....
gi 105990541 2137 CTRLAIMVKGAFRCMGTIQHLKSK 2160
Cdd:COG4988 538 ADRILVLDDGRIVEQGTHEELLAK 561
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1951-2146 |
3.96e-17 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 83.22 E-value: 3.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1951 SSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIL---TNISEVHQNMGYC-------PQF 2020
Cdd:PRK09493 13 PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpkVDERLIRQEAGMVfqqfylfPHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2021 DAIDELLTGRehlylyARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTG 2100
Cdd:PRK09493 93 TALENVMFGP------LRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 105990541 2101 MDPQARRMLWNVIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
Cdd:PRK09493 167 LDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKG 212
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1937-2146 |
5.56e-17 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 86.62 E-value: 5.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1937 ILRLHELTKIYPGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGK---------SILTNI 2007
Cdd:COG3845 5 ALELRGITKRFGGVV--ANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKpvrirsprdAIALGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2008 SEVHQNMGYCPQFDAIDELLTGREHLYLYARLRGVPAEEIEKVAnwsiKSLGLTVYADCLAGTYSGGNKRKLSTAIALIG 2087
Cdd:COG3845 83 GMVHQHFMLVPNLTVAENIVLGLEPTKGGRLDRKAARARIRELS----ERYGLDVDPDAKVEDLSVGEQQRVEILKALYR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 105990541 2088 CPPLVLLDEPTTGMDPQARRMLWNVIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
Cdd:COG3845 159 GARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRG 217
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
931-1144 |
6.28e-17 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 84.75 E-value: 6.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 931 VKNLVKIFepcGRPAV-DRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIeTSLDAVRQSLGMCP 1009
Cdd:PRK10851 5 IANIKKSF---GRTQVlNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDV-SRLHARDRKVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1010 QHNILFHHLTVAEHMLF----YAQLKGKSQEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVIL 1085
Cdd:PRK10851 81 QHYALFRHMTVFDNIAFgltvLPRRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 105990541 1086 DEPTSGVDPYSRRSIWDLL------LKYRSgrtiIMSTHHMDEADLLGDRIAIIAQGRLYCSGTP 1144
Cdd:PRK10851 161 DEPFGALDAQVRKELRRWLrqlheeLKFTS----VFVTHDQEEAMEVADRVVVMSQGNIEQAGTP 221
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1949-2153 |
6.64e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 83.21 E-value: 6.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1949 GTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAG--KSILTNISEVHQNMGYCPQ------F 2020
Cdd:PRK13633 20 STEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldTSDEENLWDIRNKAGMVFQnpdnqiV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2021 DAIDE--LLTGREHLylyarlrGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPT 2098
Cdd:PRK13633 100 ATIVEedVAFGPENL-------GIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 105990541 2099 TGMDPQARRMLWNVIVSIIRE-GRAVVLTSHSMEECeALCTRLAIMVKGAFRCMGT 2153
Cdd:PRK13633 173 AMLDPSGRREVVNTIKELNKKyGITIILITHYMEEA-VEADRIIVMDSGKVVMEGT 227
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1937-2177 |
7.16e-17 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 82.83 E-value: 7.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1937 ILRLHELTKIYPGTssPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISE---VHQN 2013
Cdd:PRK11248 1 MLQISHLYADYGGK--PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAErgvVFQN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2014 MGYCPQFDAIDELLTGREhlylyarLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVL 2093
Cdd:PRK11248 79 EGLLPWRNVQDNVAFGLQ-------LAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2094 LDEPTTGMDPQARRMLWNVIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFRCMgtiQHLKSKFGDGYIVTMKIK 2172
Cdd:PRK11248 152 LDEPFGALDAFTREQMQTLLLKLWQEtGKQVLLITHDIEEAVFMATELVLLSPGPGRVV---ERLPLNFARRFVAGESSR 228
|
....*
gi 105990541 2173 SPKDD 2177
Cdd:PRK11248 229 SIKSD 233
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
943-1138 |
1.13e-16 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 82.05 E-value: 1.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 943 RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPP----TSGTVL----------VGGRDIETSLDAVRQSLGmc 1008
Cdd:PRK10418 16 QPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLldgkpvapcaLRGRKIATIMQNPRSAFN-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1009 PQHnilfhhlTVAEHMLFYAQLKGKSQEEAQleMEAMLEDTGLhhkrnEEAQ--------DLSGGMQRKLSVAIAFVGDA 1080
Cdd:PRK10418 94 PLH-------TMHTHARETCLALGKPADDAT--LTAALEAVGL-----ENAArvlklypfEMSGGMLQRMMIALALLCEA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1081 KVVILDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIIAQGRL 1138
Cdd:PRK10418 160 PFIIADEPTTDLDVVAQARILDLLesIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRI 219
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1935-2166 |
1.49e-16 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 84.12 E-value: 1.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1935 TDILRLHELTKIYPGtsSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSiLTNISEVHQNM 2014
Cdd:PRK11607 17 TPLLEIRNLTKSFDG--QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVD-LSHVPPYQRPI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2015 GYCPQFDAIDELLTGREHLYLYARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLL 2094
Cdd:PRK11607 94 NMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLL 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 105990541 2095 DEPTTGMDPQAR-RMLWNVIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFRCMGT----IQHLKSKFGDGYI 2166
Cdd:PRK11607 174 DEPMGALDKKLRdRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEpeeiYEHPTTRYSAEFI 250
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
931-1139 |
1.82e-16 |
|
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: 1.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 931 VKNLVKIFEpcGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRdietsldaVRqsLGMCPQ 1010
Cdd:COG0488 1 LENLSKSFG--GRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG--------LR--IGYLPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1011 HNILFHHLTVAEHML-----FYAQLKGKSQEEAQLEM--EAMLEDTGLHHKRNE------EAQ----------------- 1060
Cdd:COG0488 69 EPPLDDDLTVLDTVLdgdaeLRALEAELEELEAKLAEpdEDLERLAELQEEFEAlggweaEARaeeilsglgfpeedldr 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1061 ---DLSGGMQRKLSVAIAFVGDAKVVILDEPTSGVDPYSRRsiW--DLLLKYRSgrTIIMSTH--H-MDEadlLGDRIAI 1132
Cdd:COG0488 149 pvsELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIE--WleEFLKNYPG--TVLVVSHdrYfLDR---VATRILE 221
|
....*..
gi 105990541 1133 IAQGRLY 1139
Cdd:COG0488 222 LDRGKLT 228
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
928-1152 |
1.93e-16 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 83.25 E-value: 1.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 928 GVCVKNLVKIFEPCgrPAVDRLNITFYENQITAFLGHNGAgktttlSILTGLLPPTSGTVLVGGRDIE-----TSLDAVR 1002
Cdd:NF000106 13 AVEVRGLVKHFGEV--KAVDGVDLDVREGTVLGVLGP*GA------A**RGALPAHV*GPDAGRRPWRf*twcANRRALR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1003 QSLGMC-PQHNILFHHLTVAEHMLFYAQLKGKSQEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAK 1081
Cdd:NF000106 85 RTIG*HrPVR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 105990541 1082 VVILDEPTSGVDPYSRRSIWDLLLKY-RSGRTIIMSTHHMDEADLLGDRIAIIAQGRLYCSGTPLFLKNCFG 1152
Cdd:NF000106 165 VLYLDEPTTGLDPRTRNEVWDEVRSMvRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVG 236
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
950-1151 |
2.04e-16 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 81.21 E-value: 2.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 950 NITFY--ENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGR--DIETSLDA-----VRQSLGMCPQHNILFHHLTV 1020
Cdd:COG4161 20 DINLEcpSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfDFSQKPSEkairlLRQKVGMVFQQYNLWPHLTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1021 AEHmLFYAQLK--GKSQEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTSGVDPYSRR 1098
Cdd:COG4161 100 MEN-LIEAPCKvlGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 105990541 1099 SIWDLLLKY-RSGRTIIMSTHHMDEADLLGDRIAIIAQGRLYCSGTplflKNCF 1151
Cdd:COG4161 179 QVVEIIRELsQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGD----ASHF 228
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
927-1142 |
2.05e-16 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 81.42 E-value: 2.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 927 PGVCVKNLVKIFEpcGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRD-----IETSLDAV 1001
Cdd:TIGR02323 2 PLLQVSGLSKSYG--GGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSgaeleLYQLSEAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1002 RQSL-----GMCPQHNILFHHLTVA-------EHMLFYAQLKGKSQEEAQLEMEAMLEDTGlhhKRNEEAQDLSGGMQRK 1069
Cdd:TIGR02323 80 RRRLmrtewGFVHQNPRDGLRMRVSaganigeRLMAIGARHYGNIRATAQDWLEEVEIDPT---RIDDLPRAFSGGMQQR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 105990541 1070 LSVAIAFVGDAKVVILDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIIAQGRLYCSG 1142
Cdd:TIGR02323 157 LQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLrgLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESG 231
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
927-1142 |
2.77e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 81.68 E-value: 2.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 927 PGVCVKNLVKIFepCGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSG-----TVLVGGRDIETSLDAV 1001
Cdd:PRK14271 20 PAMAAVNLTLGF--AGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRDVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1002 --RQSLGMCPQHNILFHhLTVAEHMLFYAQL-KGKSQEEAQLEMEAMLEDTGLHHKRNEEAQD----LSGGMQRKLSVAI 1074
Cdd:PRK14271 98 efRRRVGMLFQRPNPFP-MSIMDNVLAGVRAhKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDspfrLSGGQQQLLCLAR 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 105990541 1075 AFVGDAKVVILDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIIAQGRLYCSG 1142
Cdd:PRK14271 177 TLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEG 244
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
950-1138 |
3.03e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 84.45 E-value: 3.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 950 NITFY--ENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIETS--LDAVRQSLGMCPQH---NILFHHLTVAE 1022
Cdd:PRK09700 281 DISFSvcRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRspLDAVKKGMAYITESrrdNGFFPNFSIAQ 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1023 HMLFYAQLK-GK---------SQEEAQLEmEAMLEDTGLH-HKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTSG 1091
Cdd:PRK09700 361 NMAISRSLKdGGykgamglfhEVDEQRTA-ENQRELLALKcHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRG 439
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 105990541 1092 VDPYSRRSIWDLLLKY-RSGRTIIMSTHHMDEADLLGDRIAIIAQGRL 1138
Cdd:PRK09700 440 IDVGAKAEIYKVMRQLaDDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
1937-2140 |
3.24e-16 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 79.89 E-value: 3.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1937 ILRLHELTkiYPGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTniSEVHQNMGY 2016
Cdd:PRK13543 11 LLAAHALA--FSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATR--GDRSRFMAY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2017 CPQFDAIDELLTGREHLYLYARLRGVPAEEIEKVAnwsIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDE 2096
Cdd:PRK13543 87 LGHLPGLKADLSTLENLHFLCGLHGRRAKQMPGSA---LAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDE 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 105990541 2097 PTTGMDPQARRMLWNVIVSIIREGRAVVLTSHSMEECEALCTRL 2140
Cdd:PRK13543 164 PYANLDLEGITLVNRMISAHLRGGGAALVTTHGAYAAPPVRTRM 207
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1962-2130 |
3.87e-16 |
|
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: 79.50 E-value: 3.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIL---TNISEVHQNMGYCPQfdaidelltgreHLYLYAR 2038
Cdd:cd03262 23 VKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTddkKNINELRQKVGMVFQ------------QFNLFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2039 L-------------RGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQA 2105
Cdd:cd03262 91 LtvlenitlapikvKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPEL 170
|
170 180
....*....|....*....|....*
gi 105990541 2106 RRMLWNVIVSIIREGRAVVLTSHSM 2130
Cdd:cd03262 171 VGEVLDVMKDLAEEGMTMVVVTHEM 195
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1938-2143 |
4.54e-16 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 80.29 E-value: 4.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1938 LRLHELTKIYPGTSS--PAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISE---VHQ 2012
Cdd:COG4525 4 LTVRHVSVRYPGGGQpqPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADrgvVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2013 NMGYCPQFDAIDELLTGrehlylyARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLV 2092
Cdd:COG4525 84 KDALLPWLNVLDNVAFG-------LRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 105990541 2093 LLDEPTTGMDPQAR-RM------LWNvivsiiREGRAVVLTSHSMEECEALCTRLAIM 2143
Cdd:COG4525 157 LMDEPFGALDALTReQMqellldVWQ------RTGKGVFLITHSVEEALFLATRLVVM 208
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1938-2131 |
4.87e-16 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 83.88 E-value: 4.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1938 LRLHELTKIYPGTSsPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSiLTNISEVH--QNMG 2015
Cdd:TIGR02857 322 LEFSGVSVAYPGRR-PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVP-LADADADSwrDQIA 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2016 YCPQ----FDAidellTGREHLYLYArlRGVPAEEIEKV-----ANWSIKSLGL---TVYADCLAGtYSGGNKRKLSTAI 2083
Cdd:TIGR02857 400 WVPQhpflFAG-----TIAENIRLAR--PDASDAEIREAleragLDEFVAALPQgldTPIGEGGAG-LSGGQAQRLALAR 471
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 105990541 2084 ALIGCPPLVLLDEPTTGMDPQARrmlwNVIVSIIRE---GRAVVLTSHSME 2131
Cdd:TIGR02857 472 AFLRDAPLLLLDEPTAHLDAETE----AEVLEALRAlaqGRTVLLVTHRLA 518
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
1938-2129 |
4.98e-16 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 83.95 E-value: 4.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1938 LRLHELTKIYPGtSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISEVHQNMGY 2016
Cdd:TIGR02868 335 LELRDLSAGYPG-APPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSlDQDEVRRRVSV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2017 CPQ----FDAidellTGREHLYLyARlRGVPAEEIEKV------ANWsIKSL--GLTVYADCLAGTYSGGNKRKLSTAIA 2084
Cdd:TIGR02868 414 CAQdahlFDT-----TVRENLRL-AR-PDATDEELWAAlervglADW-LRALpdGLDTVLGEGGARLSGGERQRLALARA 485
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 105990541 2085 LIGCPPLVLLDEPTTGMDPQAR----RMLWNVIvsiirEGRAVVLTSHS 2129
Cdd:TIGR02868 486 LLADAPILLLDEPTEHLDAETAdellEDLLAAL-----SGRTVVLITHH 529
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1952-2168 |
7.11e-16 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 82.39 E-value: 7.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1952 SPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT------------NISEVHQNMGYCPQ 2019
Cdd:PRK10070 41 SLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKisdaelrevrrkKIAMVFQSFALMPH 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2020 FDAIDELLTGREhlylyarLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTT 2099
Cdd:PRK10070 121 MTVLDNTAFGME-------LAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFS 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2100 GMDPQARRMLWNVIVSI-IREGRAVVLTSHSMEECEALCTRLAIMVKGAFRCMGTIQHLKSKFGDGYIVT 2168
Cdd:PRK10070 194 ALDPLIRTEMQDELVKLqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRT 263
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1938-2142 |
8.20e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 83.04 E-value: 8.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1938 LRLHELTKIYPGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGK---------SILTNIS 2008
Cdd:PRK11288 5 LSFDGIGKTFPGVK--ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQemrfasttaALAAGVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2009 EVHQNMGYCPQFDAIDELLTGRehlyLYARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGC 2088
Cdd:PRK11288 83 IIYQELHLVPEMTVAENLYLGQ----LPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARN 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 105990541 2089 PPLVLLDEPTTGMDPQARRMLWNVIVSIIREGRAVVLTSHSMEECEALCTRLAI 2142
Cdd:PRK11288 159 ARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITV 212
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
950-1118 |
8.42e-16 |
|
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: 78.05 E-value: 8.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 950 NITFY--ENQITAFLGHNGAGKTTTLSIL-----TGLlppTSGTVLVGGRDIETSLdavRQSLGMCPQHNILFHHLTVAE 1022
Cdd:cd03232 25 NISGYvkPGTLTALMGESGAGKTTLLDVLagrktAGV---ITGEILINGRPLDKNF---QRSTGYVEQQDVHSPNLTVRE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1023 HMLFYAQLKGKSQEEaqlemeamledtglhhkrneeaqdlsggmQRKLSVAIAFVGDAKVVILDEPTSGVDPYSRRSIWD 1102
Cdd:cd03232 99 ALRFSALLRGLSVEQ-----------------------------RKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVR 149
|
170
....*....|....*..
gi 105990541 1103 LLLKY-RSGRTIIMSTH 1118
Cdd:cd03232 150 FLKKLaDSGQAILCTIH 166
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
930-1144 |
9.76e-16 |
|
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: 77.95 E-value: 9.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 930 CVKNL-VKIfepCGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLlP---PTSGTVLVGGRDIeTSL---DAVR 1002
Cdd:cd03217 2 EIKDLhVSV---GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGH-PkyeVTEGEILFKGEDI-TDLppeERAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1003 QSLGMCPQHNILFHHLTVAEhmlfyaqlkgksqeeaqlemeaMLEDTglhhkrNEeaqDLSGGMQRKLSVAIAFVGDAKV 1082
Cdd:cd03217 77 LGIFLAFQYPPEIPGVKNAD----------------------FLRYV------NE---GFSGGEKKRNEILQLLLLEPDL 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 105990541 1083 VILDEPTSGVDPYSRRSIWDLLLKYRS-GRTIIMSTHHMDEADLL-GDRIAIIAQGRLYCSGTP 1144
Cdd:cd03217 126 AILDEPDSGLDIDALRLVAEVINKLREeGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGDK 189
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1937-2153 |
1.29e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 79.35 E-value: 1.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1937 ILRLHELTKIYP-GTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNIS---EVHQ 2012
Cdd:PRK13639 1 ILETRDLKYSYPdGTE--ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKsllEVRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2013 NMGYCPQfDAIDELL--TGREHLYLYARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPP 2090
Cdd:PRK13639 79 TVGIVFQ-NPDDQLFapTVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 105990541 2091 LVLLDEPTTGMDPQARRMLWNVIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFRCMGT 2153
Cdd:PRK13639 158 IIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGT 220
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
938-1122 |
1.35e-15 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 78.22 E-value: 1.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 938 FEPCGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIET-SLDAVRQSLGMCPQHNILFH 1016
Cdd:PRK10247 15 YLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTlKPEIYRQQVSYCAQTPTLFG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1017 HlTVAEHMLFYAQLKGKSQEEAQLEMEAM---LEDTGLHHKRNEeaqdLSGGMQRKLSVA--IAFVgdAKVVILDEPTSG 1091
Cdd:PRK10247 95 D-TVYDNLIFPWQIRNQQPDPAIFLDDLErfaLPDTILTKNIAE----LSGGEKQRISLIrnLQFM--PKVLLLDEITSA 167
|
170 180 190
....*....|....*....|....*....|...
gi 105990541 1092 VDPYSRRSIWDLLLKYRSGRTI--IMSTHHMDE 1122
Cdd:PRK10247 168 LDESNKHNVNEIIHRYVREQNIavLWVTHDKDE 200
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1936-2140 |
1.48e-15 |
|
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: 1.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1936 DILRLHELTKIYPGTssPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVaGKSIltnisevhqNMG 2015
Cdd:COG0488 314 KVLELEGLSKSYGDK--TLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV---------KIG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2016 YCPQ-FDAIDELLTGREHLYLYAR------LRGV------PAEEIEKvanwSIKSLgltvyadclagtySGGNKRKLSTA 2082
Cdd:COG0488 382 YFDQhQEELDPDKTVLDELRDGAPggteqeVRGYlgrflfSGDDAFK----PVGVL-------------SGGEKARLALA 444
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 105990541 2083 IALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSIirEGrAVVLTSHSMEECEALCTRL 2140
Cdd:COG0488 445 KLLLSPPNVLLLDEPTNHLDIETLEALEEALDDF--PG-TVLLVSHDRYFLDRVATRI 499
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
945-1131 |
1.83e-15 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 78.67 E-value: 1.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSI---LTGLLPP--TSGTVLVGGRDIETS-LD--AVRQSLGMCPQHNILFH 1016
Cdd:PRK14243 25 AVKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrLNDLIPGfrVEGKVTFHGKNLYAPdVDpvEVRRRIGMVFQKPNPFP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1017 HlTVAEHMLFYAQL---KGKSQE--EAQLEMEAMLEDtgLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTSG 1091
Cdd:PRK14243 105 K-SIYDNIAYGARIngyKGDMDElvERSLRQAALWDE--VKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSA 181
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 105990541 1092 VDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIA 1131
Cdd:PRK14243 182 LDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTA 221
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1938-2146 |
1.90e-15 |
|
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: 77.99 E-value: 1.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1938 LRLHELTKiYPGTSSpAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTG-----DTTVTSGDATVAGKSILT---NISE 2009
Cdd:cd03260 1 IELRDLNV-YYGDKH-ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLDGKDIYDldvDVLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2010 VHQNMGYCPQ----FDAidellTGREHLYLYARLRGV-PAEEIEKVANWSIKSLGLT--VYADCLAGTYSGGNKRKLSTA 2082
Cdd:cd03260 79 LRRRVGMVFQkpnpFPG-----SIYDNVAYGLRLHGIkLKEELDERVEEALRKAALWdeVKDRLHALGLSGGQQQRLCLA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 105990541 2083 IALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSIIREgRAVVLTSHSMEECEALCTRLAIMVKG 2146
Cdd:cd03260 154 RALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNG 216
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
942-1138 |
2.40e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 81.61 E-value: 2.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 942 GRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIeTSLD-AVRQSLGMC-----PQHNILF 1015
Cdd:COG3845 270 GVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDI-TGLSpRERRRLGVAyipedRLGRGLV 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1016 HHLTVAEHMLFYAQLKGK-------SQEEAQLEMEAMLED-----TGLHHKrneeAQDLSGGMQRKLSVAIAFVGDAKVV 1083
Cdd:COG3845 349 PDMSVAENLILGRYRRPPfsrggflDRKAIRAFAEELIEEfdvrtPGPDTP----ARSLSGGNQQKVILARELSRDPKLL 424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 105990541 1084 ILDEPTSGVDPYSRRSIWDLLLKYR-SGRTIIMSTHHMDEADLLGDRIAIIAQGRL 1138
Cdd:COG3845 425 IAAQPTRGLDVGAIEFIHQRLLELRdAGAAVLLISEDLDEILALSDRIAVMYEGRI 480
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
1962-2154 |
2.51e-15 |
|
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: 77.51 E-value: 2.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISE---VHQNMGYCPqfdaideLLTGREHLYLYAR 2038
Cdd:TIGR01184 8 IQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDrmvVFQNYSLLP-------WLTVRENIALAVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2039 --LRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSI 2116
Cdd:TIGR01184 81 rvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQI 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 105990541 2117 IREGR-AVVLTSHSMEECEALCTRLAIMVKGAFRCMGTI 2154
Cdd:TIGR01184 161 WEEHRvTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQI 199
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
929-1118 |
2.86e-15 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 74.79 E-value: 2.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 929 VCVKNLVKIFEpcGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGgrdietsldavrqslgmc 1008
Cdd:cd03221 1 IELENLSKTYG--GKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG------------------ 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1009 pqhnilfHHLTVAehmlFYAQlkgksqeeaqlemeamledtglhhkrneeaqdLSGGMQRKLSVAIAFVGDAKVVILDEP 1088
Cdd:cd03221 61 -------STVKIG----YFEQ--------------------------------LSGGEKMRLALAKLLLENPNLLLLDEP 97
|
170 180 190
....*....|....*....|....*....|
gi 105990541 1089 TSGVDPYSRRSIWDLLLKYRsgRTIIMSTH 1118
Cdd:cd03221 98 TNHLDLESIEALEEALKEYP--GTVILVSH 125
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1915-2147 |
3.57e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 81.11 E-value: 3.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1915 VDEDDDVAE-ERQRIIT---GGNKTDI------------LRLHELTKiyPGTSSPAvdrlCVGVRPGECFGLLGVNGAGK 1978
Cdd:PRK11288 219 VATFDDMAQvDRDQLVQamvGREIGDIygyrprplgevrLRLDGLKG--PGLREPI----SFSVRAGEIVGLFGLVGAGR 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1979 TTTFKMLTGDTTVTSGDATVAGKSILTN--ISEVHQNMGYCPQ---FDAIDELLTGREHLYLYARLRGVPAEEI------ 2047
Cdd:PRK11288 293 SELMKLLYGATRRTAGQVYLDGKPIDIRspRDAIRAGIMLCPEdrkAEGIIPVHSVADNINISARRHHLRAGCLinnrwe 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2048 EKVANWSIKSLGL-TVYADCLAGTYSGGNKRK------LSTAIALIgcpplvLLDEPTTGMDPQARRMLWNVIVSIIREG 2120
Cdd:PRK11288 373 AENADRFIRSLNIkTPSREQLIMNLSGGNQQKailgrwLSEDMKVI------LLDEPTRGIDVGAKHEIYNVIYELAAQG 446
|
250 260
....*....|....*....|....*..
gi 105990541 2121 RAVVLTSHSMEECEALCTRLAIMVKGA 2147
Cdd:PRK11288 447 VAVLFVSSDLPEVLGVADRIVVMREGR 473
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
931-1138 |
3.62e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 80.82 E-value: 3.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 931 VKNLvkifepCGrPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIETSldavrqslgmCPQ 1010
Cdd:PRK10762 260 VDNL------SG-PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTR----------SPQ 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1011 HNI---------------LFHHLTVAEHMLFYAqLKGKSQEEAQL----EMEAMLEDTGLHH----KRNEEAQDLSGGMQ 1067
Cdd:PRK10762 323 DGLangivyisedrkrdgLVLGMSVKENMSLTA-LRYFSRAGGSLkhadEQQAVSDFIRLFNiktpSMEQAIGLLSGGNQ 401
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 105990541 1068 RKLSVAIAFVGDAKVVILDEPTSGVDPYSRRSIWDLLLKYRS-GRTIIMSTHHMDEadLLG--DRIAIIAQGRL 1138
Cdd:PRK10762 402 QKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAeGLSIILVSSEMPE--VLGmsDRILVMHEGRI 473
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
943-1138 |
3.92e-15 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 76.74 E-value: 3.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 943 RPAVDRL-NITF--YENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIETS----LDAVRQSLGMCP------ 1009
Cdd:cd03248 24 RPDTLVLqDVSFtlHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYehkyLHSKVSLVGQEPvlfars 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1010 -QHNILFHHLTVAEHMLFYAQLKGKSQEEAQLEMEAMLEDTGlhhkrnEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEP 1088
Cdd:cd03248 104 lQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVG------EKGSQLSGGQKQRVAIARALIRNPQVLILDEA 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 105990541 1089 TSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADlLGDRIAIIAQGRL 1138
Cdd:cd03248 178 TSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVE-RADQILVLDGGRI 226
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
929-1143 |
4.08e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 81.04 E-value: 4.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 929 VCVKNLVkIFEPCGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTsGTVLVGGRDI-ETSLDAVRQSLGM 1007
Cdd:PRK11174 350 IEAEDLE-ILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GSLKINGIELrELDPESWRKHLSW 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1008 CPQHNILFHHlTVAEHMLFyaqlkGKSQ-EEAQLEmeAMLEDT-----------GLHHKRNEEAQDLSGGMQRKLSVAIA 1075
Cdd:PRK11174 428 VGQNPQLPHG-TLRDNVLL-----GNPDaSDEQLQ--QALENAwvseflpllpqGLDTPIGDQAAGLSVGQAQRLALARA 499
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 105990541 1076 FVGDAKVVILDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDeaDLLG-DRIAIIAQGRLYCSGT 1143
Cdd:PRK11174 500 LLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLE--DLAQwDQIWVMQDGQIVQQGD 566
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1962-2153 |
4.99e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 77.85 E-value: 4.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1962 VRPGECFGLLGVNGAGKTTTFKMLTG-----DTTVTSGDATVAGKSILTNISEVHQNMGYCPQF--------DAIDELLT 2028
Cdd:PRK13643 29 VKKGSYTALIGHTGSGKSTLLQHLNGllqptEGKVTVGDIVVSSTSKQKEIKPVRKKVGVVFQFpesqlfeeTVLKDVAF 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2029 GREHLylyarlrGVPAEEIEKVANWSIKSLGLTV-YADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARR 2107
Cdd:PRK13643 109 GPQNF-------GIPKEKAEKIAAEKLEMVGLADeFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARI 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 105990541 2108 MLWNVIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFRCMGT 2153
Cdd:PRK13643 182 EMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGT 227
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1937-2159 |
5.10e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 77.72 E-value: 5.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1937 ILRLHELTKIYPgTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI--LTNISEVHQNM 2014
Cdd:PRK13644 1 MIRLENVSYSYP-DGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTgdFSKLQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2015 GYC---PQFDAI-----DELLTGREHLYLyarlrgvPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALI 2086
Cdd:PRK13644 80 GIVfqnPETQFVgrtveEDLAFGPENLCL-------PPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILT 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 105990541 2087 GCPPLVLLDEPTTGMDPQARRMLWNVIVSIIREGRAVVLTSHSMEECEAlCTRLAIMVKGAFRCMGTIQHLKS 2159
Cdd:PRK13644 153 MEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGEPENVLS 224
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1943-2153 |
6.38e-15 |
|
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: 76.61 E-value: 6.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1943 LTKIYPgtSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIlTNISEVHQNMGYCPQFDA 2022
Cdd:cd03296 8 VSKRFG--DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDA-TDVPVQERNVGFVFQHYA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2023 IDELLTGREH----LYLYARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPT 2098
Cdd:cd03296 85 LFRHMTVFDNvafgLRVKPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPF 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 105990541 2099 TGMDPQARRML--WnvivsiIRE-----GRAVVLTSHSMEECEALCTRLAIMVKGAFRCMGT 2153
Cdd:cd03296 165 GALDAKVRKELrrW------LRRlhdelHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGT 220
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1970-2157 |
6.61e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 77.54 E-value: 6.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1970 LLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIL-TNISEVHQNMGYCPQfDAIDELL--TGREHLYLYARLRGVPAEE 2046
Cdd:PRK13652 35 VIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITkENIREVRKFVGLVFQ-NPDDQIFspTVEQDIAFGPINLGLDEET 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2047 IEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSIIRE-GRAVVL 2125
Cdd:PRK13652 114 VAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIF 193
|
170 180 190
....*....|....*....|....*....|..
gi 105990541 2126 TSHSMEECEALCTRLAIMVKGAFRCMGTIQHL 2157
Cdd:PRK13652 194 STHQLDLVPEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
931-1144 |
1.10e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 76.67 E-value: 1.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 931 VKNLVKIFEPcgRPAVDRLN---ITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGG-RDIETSLDAVRQSLG 1006
Cdd:PRK13642 7 VENLVFKYEK--ESDVNQLNgvsFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGeLLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1007 MCPQH-NILFHHLTVAEHMLFYAQLKGKSQEEAQLEM-EAMLEDTGLHHKRNEEAQdLSGGMQRKLSVAIAFVGDAKVVI 1084
Cdd:PRK13642 85 MVFQNpDNQFVGATVEDDVAFGMENQGIPREEMIKRVdEALLAVNMLDFKTREPAR-LSGGQKQRVAVAGIIALRPEIII 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 105990541 1085 LDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEAdLLGDRIAIIAQGRLYCSGTP 1144
Cdd:PRK13642 164 LDESTSMLDPTGRQEIMRVIheIKEKYQLTVLSITHDLDEA-ASSDRILVMKAGEIIKEAAP 224
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
943-1143 |
1.26e-14 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 79.62 E-value: 1.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 943 RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIET-SLDAVRQSLGMCPQHNILFHHlTVA 1021
Cdd:PRK13657 348 RQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTvTRASLRRNIAVVFQDAGLFNR-SIE 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1022 EHMLFyaqlkGK---SQEEAQLEMEA-------MLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTSG 1091
Cdd:PRK13657 427 DNIRV-----GRpdaTDEEMRAAAERaqahdfiERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSA 501
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 105990541 1092 VDPYSRRSIWDLLLKYRSGRTIIMSTHHMD---EAdllgDRIAIIAQGRLYCSGT 1143
Cdd:PRK13657 502 LDVETEAKVKAALDELMKGRTTFIIAHRLStvrNA----DRILVFDNGRVVESGS 552
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
949-1151 |
1.47e-14 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 75.44 E-value: 1.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGR--DIETSLDA-----VRQSLGMCPQHNILFHHLTVA 1021
Cdd:PRK11124 21 ITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfDFSKTPSDkaireLRRNVGMVFQQYNLWPHLTVQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1022 EHmLFYAQLK--GKSQEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTSGVDPYSRRS 1099
Cdd:PRK11124 101 QN-LIEAPCRvlGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQ 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 105990541 1100 IWDLLLKYR-SGRTIIMSTHHMDEADLLGDRIAIIAQGRLYCSGTplflKNCF 1151
Cdd:PRK11124 180 IVSIIRELAeTGITQVIVTHEVEVARKTASRVVYMENGHIVEQGD----ASCF 228
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1937-2148 |
1.70e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 78.89 E-value: 1.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1937 ILRLHELTKIYPGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTN---------I 2007
Cdd:PRK10762 4 LLQLKGIDKAFPGVK--ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNgpkssqeagI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2008 SEVHQNMGYCPQFDAIDELLTGREhlyLYARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIG 2087
Cdd:PRK10762 82 GIIHQELNLIPQLTIAENIFLGRE---FVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSF 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 105990541 2088 CPPLVLLDEPTTGMDPQARRMLWNVIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAF 2148
Cdd:PRK10762 159 ESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQF 219
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
931-1138 |
1.71e-14 |
|
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: 76.00 E-value: 1.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 931 VKNLVKIFEPCG-------RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIeTSLD---- 999
Cdd:TIGR02769 5 VRDVTHTYRTGGlfgakqrAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDL-YQLDrkqr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1000 -AVRQSLGMC---------PQHNIlfhHLTVAEHMLFYAQLKGKSQEEAQLEMeamLEDTGLhhkRNEEAQ----DLSGG 1065
Cdd:TIGR02769 84 rAFRRDVQLVfqdspsavnPRMTV---RQIIGEPLRHLTSLDESEQKARIAEL---LDMVGL---RSEDADklprQLSGG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 105990541 1066 MQRKLSVAIAFVGDAKVVILDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIIAQGRL 1138
Cdd:TIGR02769 155 QLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLrkLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1958-2129 |
2.03e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 74.14 E-value: 2.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1958 LCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIltNISEVHQNMGYCPQFDAIDELLTGREHLYLYA 2037
Cdd:PRK13539 21 LSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI--DDPDVAEACHYLGHRNAMKPALTVAENLEFWA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2038 RLRGVPAEEIEKvanwSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSII 2117
Cdd:PRK13539 99 AFLGGEELDIAA----ALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELIRAHL 174
|
170
....*....|..
gi 105990541 2118 REGRAVVLTSHS 2129
Cdd:PRK13539 175 AQGGIVIAATHI 186
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
944-1137 |
2.08e-14 |
|
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: 74.04 E-value: 2.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 944 PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGrdietsldavrqSLGMCPQ----------HNI 1013
Cdd:cd03250 19 FTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG------------SIAYVSQepwiqngtirENI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1014 LFHHLtvaehmlFYAQLKGKSQEEAQLE--MEAMledtglhhkrneEAQD----------LSGGMQRKLSVAIAFVGDAK 1081
Cdd:cd03250 87 LFGKP-------FDEERYEKVIKACALEpdLEIL------------PDGDlteigekginLSGGQKQRISLARAVYSDAD 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1082 VVILDEPTSGVDPYSRRSIWDLLL--KYRSGRTIIMSTHHMdeaDLLG--DRIAIIAQGR 1137
Cdd:cd03250 148 IYLLDDPLSAVDAHVGRHIFENCIlgLLLNNKTRILVTHQL---QLLPhaDQIVVLDNGR 204
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1951-2186 |
2.23e-14 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 77.57 E-value: 2.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1951 SSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI-LTNISEVHQNMGYCPQFDAIDELLTG 2029
Cdd:PRK09536 15 DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVeALSARAASRRVASVPQDTSLSFEFDV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2030 RE--------HLYLYARLrgvpAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGM 2101
Cdd:PRK09536 95 RQvvemgrtpHRSRFDTW----TETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2102 D-PQARRMLwNVIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFRCMG------TIQHLKSKFGDGYIVTMK--IK 2172
Cdd:PRK09536 171 DiNHQVRTL-ELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGppadvlTADTLRAAFDARTAVGTDpaTG 249
|
250
....*....|....
gi 105990541 2173 SPKDDLLPDLNPVE 2186
Cdd:PRK09536 250 APTVTPLPDPDRTE 263
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1937-2153 |
2.85e-14 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 75.05 E-value: 2.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1937 ILRLHELTKIYPGTssPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIlTNIS--EVHQNM 2014
Cdd:PRK11231 2 TLRTENLTVGYGTK--RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPI-SMLSsrQLARRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2015 GYCPQFDAIDELLTGRE--------HLYLYARLrgvpAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALI 2086
Cdd:PRK11231 79 ALLPQHHLTPEGITVRElvaygrspWLSLWGRL----SAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 105990541 2087 GCPPLVLLDEPTTGMDPQARRMLWNVIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFRCMGT 2153
Cdd:PRK11231 155 QDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGT 221
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
942-1137 |
3.22e-14 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 77.85 E-value: 3.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 942 GRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIE--TSLDAVRQSLGMCPQHNILFHHLT 1019
Cdd:PRK10982 10 GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfkSSKEALENGISMVHQELNLVLQRS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1020 VAEHM-LFYAQLKGKSQEEAQL--EMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTSGVDPYS 1096
Cdd:PRK10982 90 VMDNMwLGRYPTKGMFVDQDKMyrDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKE 169
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 105990541 1097 RRSIWDLLLKYR-SGRTIIMSTHHMDEADLLGDRIAIIAQGR 1137
Cdd:PRK10982 170 VNHLFTIIRKLKeRGCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1937-2143 |
3.29e-14 |
|
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: 75.86 E-value: 3.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1937 ILRLHELTKIYPGTSSP--AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTG---DTTVTSGDATVAGKSILT------ 2005
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVvkAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGllpPPGITSGEILFDGEDLLKlsekel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2006 ------NISEVHQN-MGYC-PQF---DAIDELLtgREHlylyarlRGVPAEEIEKVANWSIKSLGLTVYADcLAGTY--- 2071
Cdd:COG0444 81 rkirgrEIQMIFQDpMTSLnPVMtvgDQIAEPL--RIH-------GGLSKAEARERAIELLERVGLPDPER-RLDRYphe 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 105990541 2072 -SGGNKRKLSTAIALIGCPPLVLLDEPTTGMDP--QARRMlwNVIVSIIRE-GRAVVLTSHSMEECEALCTRLAIM 2143
Cdd:COG0444 151 lSGGMRQRVMIARALALEPKLLIADEPTTALDVtiQAQIL--NLLKDLQRElGLAILFITHDLGVVAEIADRVAVM 224
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1938-2153 |
3.30e-14 |
|
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: 78.25 E-value: 3.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1938 LRLHELTKIYPGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISEVHQNMGY 2016
Cdd:COG4618 331 LSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQwDREELGRHIGY 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2017 CPQfdaiD-ELLTG--REHLylyARLRGVPAEEIEKVAnwsiKSLGL------------TVYADclAGTY-SGGNKRKLS 2080
Cdd:COG4618 411 LPQ----DvELFDGtiAENI---ARFGDADPEKVVAAA----KLAGVhemilrlpdgydTRIGE--GGARlSGGQRQRIG 477
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 105990541 2081 TAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSIIREGRAVVLTSHSMeecEAL--CTRLAIMVKGAFRCMGT 2153
Cdd:COG4618 478 LARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRP---SLLaaVDKLLVLRDGRVQAFGP 549
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
949-1144 |
4.23e-14 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 74.64 E-value: 4.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIET-SLDAVRQSLGMCPQHNILFHHLTVAE----- 1022
Cdd:PRK10253 26 LTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHyASKEVARRIGLLAQNATTPGDITVQElvarg 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1023 ---HMLFYAQLKGKSQEEAQLEMEAmledTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTSGVDPYSRRS 1099
Cdd:PRK10253 106 rypHQPLFTRWRKEDEEAVTKAMQA----TGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQID 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 105990541 1100 IWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIIAQGRLYCSGTP 1144
Cdd:PRK10253 182 LLELLseLNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAP 228
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1969-2134 |
4.62e-14 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 78.24 E-value: 4.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1969 GLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILtniSEVHQN-----MGYCPQfdaidEL-------LTGREHLYLY 2036
Cdd:NF033858 31 GLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMA---DARHRRavcprIAYMPQ-----GLgknlyptLSVFENLDFF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2037 ARLRGVPAEEIEkvanWSIKSL----GLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNV 2112
Cdd:NF033858 103 GRLFGQDAAERR----RRIDELlratGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRRQFWEL 178
|
170 180
....*....|....*....|....*.
gi 105990541 2113 IVSiIREGRA----VVLTSHsMEECE 2134
Cdd:NF033858 179 IDR-IRAERPgmsvLVATAY-MEEAE 202
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
957-1138 |
5.19e-14 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 74.33 E-value: 5.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 957 QITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGgrdiETSLDAVRQSLGMCPQHNILFHHLTVAEHMLFyaQLKGKSQE 1036
Cdd:PRK11247 39 QFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAG----TAPLAEAREDTRLMFQDARLLPWKKVIDNVGL--GLKGQWRD 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1037 EAQlemEAmLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTSGVDPYSRRSIWDLL--LKYRSGRTII 1114
Cdd:PRK11247 113 AAL---QA-LAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIesLWQQHGFTVL 188
|
170 180
....*....|....*....|....
gi 105990541 1115 MSTHHMDEADLLGDRIAIIAQGRL 1138
Cdd:PRK11247 189 LVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
907-1138 |
5.37e-14 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 77.17 E-value: 5.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 907 PEHPEGIHDSFFEREHpgwvpgvcvknlVKIFEPCG--RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPT- 983
Cdd:TIGR02633 247 PHEPHEIGDVILEARN------------LTCWDVINphRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKf 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 984 SGTVLVGGR--DIETSLDAVRQSLGMCPQ----HNIL-----FHHLTVAEHMLFyaqlKGKSQEEAQLEMEAMLEDTGLH 1052
Cdd:TIGR02633 315 EGNVFINGKpvDIRNPAQAIRAGIAMVPEdrkrHGIVpilgvGKNITLSVLKSF----CFKMRIDAAAELQIIGSAIQRL 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1053 HKRNEEA----QDLSGGMQRKLSVAIAFVGDAKVVILDEPTSGVDPYSRRSIWDLLLKY-RSGRTIIMSTHHMDEADLLG 1127
Cdd:TIGR02633 391 KVKTASPflpiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLaQEGVAIIVVSSELAEVLGLS 470
|
250
....*....|.
gi 105990541 1128 DRIAIIAQGRL 1138
Cdd:TIGR02633 471 DRVLVIGEGKL 481
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1937-2146 |
5.55e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 74.35 E-value: 5.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1937 ILRLHELTKI-YPGTSS--PAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIlTN------- 2006
Cdd:COG1101 1 MLELKNLSKTfNPGTVNekRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDV-TKlpeykra 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2007 --ISEVHQN--MGYCPQfdaidelLTGREHLYL-YAR-----LR-GVPAEEIEKVANW-SIKSLGLTVYADCLAGTYSGG 2074
Cdd:COG1101 80 kyIGRVFQDpmMGTAPS-------MTIEENLALaYRRgkrrgLRrGLTKKRRELFRELlATLGLGLENRLDTKVGLLSGG 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 105990541 2075 NKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSIIREGRavvLTS----HSMEECEALCTRLAIMVKG 2146
Cdd:COG1101 153 QRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENN---LTTlmvtHNMEQALDYGNRLIMMHEG 225
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1951-2146 |
5.65e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 76.97 E-value: 5.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1951 SSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTN------------ISE--------- 2009
Cdd:PRK10762 264 SGPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRspqdglangivyISEdrkrdglvl 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2010 ---VHQNMGYCpqfdAIDELLtgrehlYLYARLRGvpAEEIEKVANW----SIKslglTVYADCLAGTYSGGNKRKLSTA 2082
Cdd:PRK10762 344 gmsVKENMSLT----ALRYFS------RAGGSLKH--ADEQQAVSDFirlfNIK----TPSMEQAIGLLSGGNQQKVAIA 407
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 105990541 2083 IALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
Cdd:PRK10762 408 RGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEG 471
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1937-2180 |
6.33e-14 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 76.79 E-value: 6.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1937 ILRLHELTKIYPGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTG--DTTVTSGDATVAGKSILTN-------- 2006
Cdd:TIGR02633 1 LLEMKGIVKTFGGVK--ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGvyPHGTWDGEIYWSGSPLKASnirdtera 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2007 -ISEVHQNMGYCPQFDAIDELLTGREhLYLYARLRGVP-----AEEIEKVANWSIKSLGLTVyadclaGTYSGGNKRKLS 2080
Cdd:TIGR02633 79 gIVIIHQELTLVPELSVAENIFLGNE-ITLPGGRMAYNamylrAKNLLRELQLDADNVTRPV------GDYGGGQQQLVE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2081 TAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGafrcmgtiQHLKSK 2160
Cdd:TIGR02633 152 IAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDG--------QHVATK 223
|
250 260
....*....|....*....|....
gi 105990541 2161 FGDGY----IVTMKIKSPKDDLLP 2180
Cdd:TIGR02633 224 DMSTMseddIITMMVGREITSLYP 247
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1939-2146 |
6.46e-14 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 75.61 E-value: 6.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1939 RLHELTKIYPGTSSP--AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSiLTNISE-----VH 2011
Cdd:PRK11153 3 ELKNISKVFPQGGRTihALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQD-LTALSEkelrkAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2012 QNMGYCPQ-FDaideLLTGR---EHLYLYARLRGVPAEEIEKVANWSIKSLGLTVYADclagTY----SGGNKRKLSTAI 2083
Cdd:PRK11153 82 RQIGMIFQhFN----LLSSRtvfDNVALPLELAGTPKAEIKARVTELLELVGLSDKAD----RYpaqlSGGQKQRVAIAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 105990541 2084 ALiGCPPLVLL-DEPTTGMDPQARRMLWNVIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKG 2146
Cdd:PRK11153 154 AL-ASNPKVLLcDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVIDAG 217
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1934-2134 |
6.74e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 74.45 E-value: 6.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1934 KTDILRLHELTKIYPGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTG--------DTTVTSGDATVAGKSILt 2005
Cdd:PRK13640 2 KDNIVEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGlllpddnpNSKITVDGITLTAKTVW- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2006 NISE----VHQNmgycP--QFDAI---DELLTGREHlylyarlRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNK 2076
Cdd:PRK13640 81 DIREkvgiVFQN----PdnQFVGAtvgDDVAFGLEN-------RAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQK 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 105990541 2077 RKLSTAIALIGCPPLVLLDEPTTGMDPQARrmlwNVIVSIIRE-----GRAVVLTSHSMEECE 2134
Cdd:PRK13640 150 QRVAIAGILAVEPKIIILDESTSMLDPAGK----EQILKLIRKlkkknNLTVISITHDIDEAN 208
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
938-1147 |
1.18e-13 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 73.28 E-value: 1.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 938 FEPCGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIET-SLDAVRQSLGMCPQHNILFH 1016
Cdd:PRK10575 19 FRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESwSSKAFARKVAYLPQQLPAAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1017 HLTVAEHML-----FYAQLkGKSQEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTSG 1091
Cdd:PRK10575 99 GMTVRELVAigrypWHGAL-GRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSA 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 105990541 1092 VDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIIAQGRLYCSGTPLFL 1147
Cdd:PRK10575 178 LDIAHQVDVLALVhrLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1962-2146 |
1.51e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 75.86 E-value: 1.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI--LTNISEVHQNMGYCPQfdaiDELLTGrehLYLYARL 2039
Cdd:PRK15439 286 VRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEInaLSTAQRLARGLVYLPE----DRQSSG---LYLDAPL 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2040 R-----------GV---PAEEIEKVANWSiKSLGLTV-YADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQ 2104
Cdd:PRK15439 359 AwnvcalthnrrGFwikPARENAVLERYR-RALNIKFnHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVS 437
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 105990541 2105 ARRMLWNVIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
Cdd:PRK15439 438 ARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQG 479
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1964-2146 |
2.04e-13 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 71.56 E-value: 2.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1964 PGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAG-------KSIltNISEVHQNMGYCPQFDAIDELLTGREHLyLY 2036
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfdsrKKI--NLPPQQRKIGLVFQQYALFPHLNVRENL-AF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2037 ArLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSI 2116
Cdd:cd03297 99 G-LKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQI 177
|
170 180 190
....*....|....*....|....*....|.
gi 105990541 2117 IRE-GRAVVLTSHSMEECEALCTRLAIMVKG 2146
Cdd:cd03297 178 KKNlNIPVIFVTHDLSEAEYLADRIVVMEDG 208
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1937-2160 |
3.92e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 72.19 E-value: 3.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1937 ILRLHELTKIYP-GTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI---LTNISEVHQ 2012
Cdd:PRK13636 5 ILKVEELNYNYSdGTH--ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdysRKGLMKLRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2013 NMGYCPQfDAIDELLTGR--EHLYLYARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPP 2090
Cdd:PRK13636 83 SVGMVFQ-DPDNQLFSASvyQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPK 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 105990541 2091 LVLLDEPTTGMDPQARRMLWNVIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFRCMGTIQHLKSK 2160
Cdd:PRK13636 162 VLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAE 232
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
957-1126 |
4.57e-13 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 75.15 E-value: 4.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 957 QITAFLGHNGAGKTTTLSIL-----TGLLppTSGTVLVGGRDIETSLdavRQSLGMCPQHNILFHHLTVAEHMLFYAQL- 1030
Cdd:TIGR00956 790 TLTALMGASGAGKTTLLNVLaervtTGVI--TGGDRLVNGRPLDSSF---QRSIGYVQQQDLHLPTSTVRESLRFSAYLr 864
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1031 --KGKSQEEAQ---------LEMEAMLE------DTGLhhkrNEEaqdlsggmQRK-LSVAIAFVGDAKVVI-LDEPTSG 1091
Cdd:TIGR00956 865 qpKSVSKSEKMeyveeviklLEMESYADavvgvpGEGL----NVE--------QRKrLTIGVELVAKPKLLLfLDEPTSG 932
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 105990541 1092 VDPYSRRSIWDLLLKY-RSGRTIIMSTHH-----MDEADLL 1126
Cdd:TIGR00956 933 LDSQTAWSICKLMRKLaDHGQAILCTIHQpsailFEEFDRL 973
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
943-1138 |
4.83e-13 |
|
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: 74.34 E-value: 4.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 943 RPAVDRLNITFYENQITAFLGHNGAGKT-TTLSILtGLLPP----TSGTVLVGGRDI----ETSLDAVR-QSLGMC---- 1008
Cdd:COG4172 23 VEAVKGVSFDIAAGETLALVGESGSGKSvTALSIL-RLLPDpaahPSGSILFDGQDLlglsERELRRIRgNRIAMIfqep 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1009 -----PQHNI-------LFHHltvaehmlfyaqlKGKSQEEAQLEMEAMLEDTGLhhkRNEEAQ------DLSGGMQRKL 1070
Cdd:COG4172 102 mtslnPLHTIgkqiaevLRLH-------------RGLSGAAARARALELLERVGI---PDPERRldayphQLSGGQRQRV 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 105990541 1071 SVAIAFVGDAKVVILDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHhmdeaDL-----LGDRIAIIAQGRL 1138
Cdd:COG4172 166 MIAMALANEPDLLIADEPTTALDVTVQAQILDLLkdLQRELGMALLLITH-----DLgvvrrFADRVAVMRQGEI 235
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1937-2146 |
5.17e-13 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 71.50 E-value: 5.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1937 ILRLHELTKIYpgtsspAVDRLCVGV----RPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKS----ILTNIS 2008
Cdd:PRK11701 6 LLSVRGLTKLY------GPRKGCRDVsfdlYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDgqlrDLYALS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2009 E-------------VHQN--MGYCPQFDA---IDELL--TGREHlylYARLRGVPAEEIEKVanwSIKSLGLtvyaDCLA 2068
Cdd:PRK11701 80 EaerrrllrtewgfVHQHprDGLRMQVSAggnIGERLmaVGARH---YGDIRATAGDWLERV---EIDAARI----DDLP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2069 GTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMD--PQARrmLWNVIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVK 2145
Cdd:PRK11701 150 TTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDvsVQAR--LLDLLRGLVRElGLAVVIVTHDLAVARLLAHRLLVMKQ 227
|
.
gi 105990541 2146 G 2146
Cdd:PRK11701 228 G 228
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
932-1093 |
5.90e-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: 69.98 E-value: 5.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 932 KNLVKIFEPCGRPAVDRL-NITFY--ENQITAFLGHNGAGKTTTLSILTGLLPPT---SGTVLVGGRDIETSLDAVRQSL 1005
Cdd:cd03233 6 WRNISFTTGKGRSKIPILkDFSGVvkPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPGEI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1006 GMCPQHNILFHHLTVAEHMLFYAQLKGksqeeaqlemeamledtglhhkrNEEAQDLSGGMQRKLSVAIAFVGDAKVVIL 1085
Cdd:cd03233 86 IYVSEEDVHFPTLTVRETLDFALRCKG-----------------------NEFVRGISGGERKRVSIAEALVSRASVLCW 142
|
....*...
gi 105990541 1086 DEPTSGVD 1093
Cdd:cd03233 143 DNSTRGLD 150
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1934-2153 |
5.92e-13 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 73.06 E-value: 5.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1934 KTDILRLHELTKIYPGTssPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIlTNISEVHQN 2013
Cdd:PRK09452 11 LSPLVELRGISKSFDGK--EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDI-THVPAENRH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2014 MGYCPQFDAIDELLTGREHLYLYARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVL 2093
Cdd:PRK09452 88 VNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 105990541 2094 LDEPTTGMDPQARRMLWNVIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFRCMGT 2153
Cdd:PRK09452 168 LDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGT 228
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1935-2163 |
7.00e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 71.30 E-value: 7.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1935 TDILRLHELT-KIYPGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGK--------SILT 2005
Cdd:PRK13650 2 SNIIEVKNLTfKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDllteenvwDIRH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2006 NISEVHQNmgycP--QFDAI---DELLTGREHlylyarlRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLS 2080
Cdd:PRK13650 82 KIGMVFQN----PdnQFVGAtveDDVAFGLEN-------KGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2081 TAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSIIRE-GRAVVLTSHSMEECeALCTRLAIMVKGAFRCMGTIQHLKS 2159
Cdd:PRK13650 151 IAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDEV-ALSDRVLVMKNGQVESTSTPRELFS 229
|
....
gi 105990541 2160 KFGD 2163
Cdd:PRK13650 230 RGND 233
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
957-1119 |
9.27e-13 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 73.76 E-value: 9.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 957 QITAFLGHNGAGKTTTLSILTGLLPPTS--GTVLVGGRDIETSldaVRQSLGMCPQHNILFHHLTVAEHMLFYAQL---K 1031
Cdd:PLN03211 95 EILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTKQ---ILKRTGFVTQDDILYPHLTVRETLVFCSLLrlpK 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1032 GKSQEEAQLEMEAMLEDTGLHHKRNEEA-----QDLSGGMQRKLSVAIAFVGDAKVVILDEPTSGVDPYSR-RSIWDLLL 1105
Cdd:PLN03211 172 SLTKQEKILVAESVISELGLTKCENTIIgnsfiRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAyRLVLTLGS 251
|
170
....*....|....
gi 105990541 1106 KYRSGRTIIMSTHH 1119
Cdd:PLN03211 252 LAQKGKTIVTSMHQ 265
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1937-2131 |
1.01e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 70.92 E-value: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1937 ILRLHELTKIYP-GTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI-LTNISEVHQNM 2014
Cdd:PRK13647 4 IIEVEDLHFRYKdGTK--ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVnAENEKWVRSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2015 GYCPQfDAIDELLTGR--EHLYLYARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLV 2092
Cdd:PRK13647 82 GLVFQ-DPDDQVFSSTvwDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVI 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 105990541 2093 LLDEPTTGMDPQARRMLWNVIVSIIREGRAVVLTSHSME 2131
Cdd:PRK13647 161 VLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVD 199
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
950-1138 |
1.13e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 73.16 E-value: 1.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 950 NITF--YENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDI--ETSLDAVRQSLGMCP---QHNILF------- 1015
Cdd:PRK15439 281 NISLevRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEInaLSTAQRLARGLVYLPedrQSSGLYldaplaw 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1016 --HHLTVAEhMLFYAQLKgksQEEAQLEMEAMLEDTGLHHKrNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTSGVD 1093
Cdd:PRK15439 361 nvCALTHNR-RGFWIKPA---RENAVLERYRRALNIKFNHA-EQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVD 435
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 105990541 1094 PYSRRSIWDLLlkyRS----GRTIIMSTHHMDEADLLGDRIAIIAQGRL 1138
Cdd:PRK15439 436 VSARNDIYQLI---RSiaaqNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
943-1160 |
1.19e-12 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 73.60 E-value: 1.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 943 RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIE--------TSLDAVRQS---LGMCPQH 1011
Cdd:TIGR00958 494 VPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVqydhhylhRQVALVGQEpvlFSGSVRE 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1012 NILFhHLTVAEHMLFYAQLKGKSQEEAQLEMEamledTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTSG 1091
Cdd:TIGR00958 574 NIAY-GLTDTPDEEIMAAAKAANAHDFIMEFP-----NGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSA 647
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 105990541 1092 VDPYSRRSIWDllLKYRSGRTIIMSTHHMDEADlLGDRIAIIAQGRLYCSGTPLFLKNcfGTGLYLTLV 1160
Cdd:TIGR00958 648 LDAECEQLLQE--SRSRASRTVLLIAHRLSTVE-RADQILVLKKGSVVEMGTHKQLME--DQGCYKHLV 711
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1965-2146 |
1.23e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 70.68 E-value: 1.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1965 GECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSilTNiSEVHQNM-GYCPQFDAID---------ELLTGRehlY 2034
Cdd:PRK15056 33 GSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQP--TR-QALQKNLvAYVPQSEEVDwsfpvlvedVVMMGR---Y 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2035 LYARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRK--LSTAIALIGcpPLVLLDEPTTGMDPQ--ARrmlw 2110
Cdd:PRK15056 107 GHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRvfLARAIAQQG--QVILLDEPFTGVDVKteAR---- 180
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 105990541 2111 nvIVSIIR----EGRAVVLTSHSMEECEALCTrLAIMVKG 2146
Cdd:PRK15056 181 --IISLLRelrdEGKTMLVSTHNLGSVTEFCD-YTVMVKG 217
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
944-1138 |
1.96e-12 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 72.36 E-value: 1.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 944 PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDI-ETSLDAVRQSLGMCPQHNILFHHlTVAE 1022
Cdd:PRK11176 357 PALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLrDYTLASLRNQVALVSQNVHLFND-TIAN 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1023 HMLfYAQLKGKSQE--EAQLEMEAMLE-----DTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTSGVDPY 1095
Cdd:PRK11176 436 NIA-YARTEQYSREqiEEAARMAYAMDfinkmDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTE 514
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 105990541 1096 SRRSIWDLLLKYRSGRTIIMSTHHMDEADlLGDRIAIIAQGRL 1138
Cdd:PRK11176 515 SERAIQAALDELQKNRTSLVIAHRLSTIE-KADEILVVEDGEI 556
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
942-1136 |
2.67e-12 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 72.06 E-value: 2.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 942 GRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIET-SLDAVRQSLGMCPQHNILfhhltV 1020
Cdd:PRK10790 353 DNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSlSHSVLRQGVAMVQQDPVV-----L 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1021 AEHMLFYAQLkGKSQEEAQ----LEMEAMLE-----DTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTSG 1091
Cdd:PRK10790 428 ADTFLANVTL-GRDISEEQvwqaLETVQLAElarslPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATAN 506
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 105990541 1092 VDPYSRRSIWDLLLKYRSGRTIIMSTHHMD---EAD--LLGDRIAIIAQG 1136
Cdd:PRK10790 507 IDSGTEQAIQQALAAVREHTTLVVIAHRLStivEADtiLVLHRGQAVEQG 556
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
931-1137 |
3.24e-12 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 68.23 E-value: 3.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 931 VKNLVKIFEPCGR-----PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVggRDIETSLD------ 999
Cdd:COG4778 7 VENLSKTFTLHLQggkrlPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILV--RHDGGWVDlaqasp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1000 ----AVRQS-LGMCPQHnilfhhL----------TVAEHMLfyaqLKGKSQEEAQLEMEAMLEDTGLHhkrnEEAQDL-- 1062
Cdd:COG4778 85 reilALRRRtIGYVSQF------LrviprvsaldVVAEPLL----ERGVDREEARARARELLARLNLP----ERLWDLpp 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 105990541 1063 ---SGGMQRKLSVAIAFVGDAKVVILDEPTSGVDPYSRRSIWDLLLKY-RSGRTIIMSTHHMDEADLLGDRIAIIAQGR 1137
Cdd:COG4778 151 atfSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAkARGTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
949-1144 |
4.17e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 68.42 E-value: 4.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLpPTSGTVLVGGRDIET----SLDAVRQSLgmCPQHNILF-----HHLT 1019
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAwsaaELARHRAYL--SQQQTPPFampvfQYLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1020 vaehmLFYAQLKGKSQEEAQLEMEA---MLEDtglhhKRNEEAQDLSGG-MQR-KLSVAIAFVG-----DAKVVILDEPT 1089
Cdd:PRK03695 92 -----LHQPDKTRTEAVASALNEVAealGLDD-----KLGRSVNQLSGGeWQRvRLAAVVLQVWpdinpAGQLLLLDEPM 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 105990541 1090 SGVDpYSRRSIWDLLLKY--RSGRTIIMSTHHMDEADLLGDRIAIIAQGRLYCSGTP 1144
Cdd:PRK03695 162 NSLD-VAQQAALDRLLSElcQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRR 217
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
957-1138 |
4.71e-12 |
|
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: 71.32 E-value: 4.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 957 QITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIET-SLDAVRQSLGMCPQHNILFHHlTVAEHMlfyAQLKGKSQ 1035
Cdd:COG4618 359 EVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQwDREELGRHIGYLPQDVELFDG-TIAENI---ARFGDADP 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1036 EE----AQL----EM--------EAMLEDTGLHhkrneeaqdLSGG-MQRkLSVAIAFVGDAKVVILDEPTSGVDPYSRR 1098
Cdd:COG4618 435 EKvvaaAKLagvhEMilrlpdgyDTRIGEGGAR---------LSGGqRQR-IGLARALYGDPRLVVLDEPNSNLDDEGEA 504
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 105990541 1099 SIWDLL--LKYRsGRTIIMSTHHMdeaDLLG--DRIAIIAQGRL 1138
Cdd:COG4618 505 ALAAAIraLKAR-GATVVVITHRP---SLLAavDKLLVLRDGRV 544
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
958-1142 |
6.01e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 68.37 E-value: 6.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 958 ITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIETSLdavRQSL-GMCPQHN-------ILFHHLTVAE---HMLF 1026
Cdd:PRK15056 35 IAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQAL---QKNLvAYVPQSEevdwsfpVLVEDVVMMGrygHMGW 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1027 YAQLKGKSQEEaqleMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTSGVDPYSRRSIWDLLLK 1106
Cdd:PRK15056 112 LRRAKKRDRQI----VTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRE 187
|
170 180 190
....*....|....*....|....*....|....*..
gi 105990541 1107 YRS-GRTIIMSTHHMDEADLLGDRIAIIaQGRLYCSG 1142
Cdd:PRK15056 188 LRDeGKTMLVSTHNLGSVTEFCDYTVMV-KGTVLASG 223
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
922-1143 |
6.26e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 71.55 E-value: 6.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 922 HPGwVPGVCVKNLVKIFE-PCGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPtsgtvlvggrdIETSLDA 1000
Cdd:PLN03232 609 QPG-APAISIKNGYFSWDsKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSH-----------AETSSVV 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1001 VRQSLGMCPQHNILFHhLTVAEHMLFYAQLKGKSQEEAqLEMEAMLEDTGLHHKRN-----EEAQDLSGGMQRKLSVAIA 1075
Cdd:PLN03232 677 IRGSVAYVPQVSWIFN-ATVRENILFGSDFESERYWRA-IDVTALQHDLDLLPGRDlteigERGVNISGGQKQRVSMARA 754
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 105990541 1076 FVGDAKVVILDEPTSGVDPYSRRSIWDLLLKYR-SGRTIIMSTHHMDEADLLgDRIAIIAQGRLYCSGT 1143
Cdd:PLN03232 755 VYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDElKGKTRVLVTNQLHFLPLM-DRIILVSEGMIKEEGT 822
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
932-1137 |
6.80e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 70.34 E-value: 6.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 932 KNLVKIFEpcGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLP--PTSGTVLVGGRDIETS--LDAVRQSLGM 1007
Cdd:PRK13549 9 KNITKTFG--GVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPhgTYEGEIIFEGEELQASniRDTERAGIAI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1008 CPQHNILFHHLTVAEHMLFYAQL-KGK--SQEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVI 1084
Cdd:PRK13549 87 IHQELALVKELSVLENIFLGNEItPGGimDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 105990541 1085 LDEPTSGVDPYSRRSIWDLL--LKyRSGRTIIMSTHHMDEADLLGDRIAIIAQGR 1137
Cdd:PRK13549 167 LDEPTASLTESETAVLLDIIrdLK-AHGIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
945-1137 |
7.79e-12 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 68.98 E-value: 7.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPP---TSGTVLVGGRDI----ETSLDAVR-QSLGMCPQHNI--L 1014
Cdd:PRK09473 31 AVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREIlnlpEKELNKLRaEQISMIFQDPMtsL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1015 FHHLTVAEHMLFYAQL-KGKSQEEAQLEMEAMLEDTGL--HHKR-NEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTS 1090
Cdd:PRK09473 111 NPYMRVGEQLMEVLMLhKGMSKAEAFEESVRMLDAVKMpeARKRmKMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTT 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 105990541 1091 GVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIIAQGR 1137
Cdd:PRK09473 191 ALDVTVQAQIMTLLneLKREFNTAIIMITHDLGVVAGICDKVLVMYAGR 239
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1933-2174 |
9.85e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 67.71 E-value: 9.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1933 NKTDILRLHELTKIYPGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI-LTNISEVH 2011
Cdd:PRK13632 3 NKSVMIKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITIsKENLKEIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2012 QNMGYC---P--QFDAI---DELLTGREHlylyarlRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAI 2083
Cdd:PRK13632 83 KKIGIIfqnPdnQFIGAtveDDIAFGLEN-------KKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIAS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2084 ALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSIIREGRAVVLT-SHSMEECeALCTRLAIMVKGAFRCMGTIQH-LKSKf 2161
Cdd:PRK13632 156 VLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISiTHDMDEA-ILADKVIVFSEGKLIAQGKPKEiLNNK- 233
|
250
....*....|...
gi 105990541 2162 gdGYIVTMKIKSP 2174
Cdd:PRK13632 234 --EILEKAKIDSP 244
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1962-2149 |
1.12e-11 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 66.73 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSiLTNISEVH------QNMGYCPQFDAIDELLTGREHLYL 2035
Cdd:PRK10584 33 VKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQP-LHQMDEEAraklraKHVGFVFQSFMLIPTLNALENVEL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2036 YARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVS 2115
Cdd:PRK10584 112 PALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFS 191
|
170 180 190
....*....|....*....|....*....|....*
gi 105990541 2116 IIRE-GRAVVLTSHSmEECEALCTRLAIMVKGAFR 2149
Cdd:PRK10584 192 LNREhGTTLILVTHD-LQLAARCDRRLRLVNGQLQ 225
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
1963-2146 |
1.36e-11 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 70.65 E-value: 1.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1963 RPGECFGLLGVNGAGKTTTFKMLTGDTT--VTSGDATVAG----KSILTNISevhqnmGYCPQFDAIDELLTGREHLYLY 2036
Cdd:PLN03140 904 RPGVLTALMGVSGAGKTTLMDVLAGRKTggYIEGDIRISGfpkkQETFARIS------GYCEQNDIHSPQVTVRESLIYS 977
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2037 ARLR---GVPAEEIEKVANWSIKSLGLTVYADCLAGT-----YSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRM 2108
Cdd:PLN03140 978 AFLRlpkEVSKEEKMMFVDEVMELVELDNLKDAIVGLpgvtgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAI 1057
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 105990541 2109 LWNVIVSIIREGRAVVLTSH--SMEECEALcTRLAIMVKG 2146
Cdd:PLN03140 1058 VMRTVRNTVDTGRTVVCTIHqpSIDIFEAF-DELLLMKRG 1096
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1937-2146 |
1.64e-11 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 68.18 E-value: 1.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1937 ILRLHELTKIYPGTSSP--AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIlTNISE----- 2009
Cdd:COG1135 1 MIELENLSKTFPTKGGPvtALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDL-TALSErelra 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2010 VHQNMGYCPQfdaidelltgreHLYLYAR----------LR--GVPAEEIEKVANWSIKSLGLTVYADclagTY----SG 2073
Cdd:COG1135 80 ARRKIGMIFQ------------HFNLLSSrtvaenvalpLEiaGVPKAEIRKRVAELLELVGLSDKAD----AYpsqlSG 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 105990541 2074 GNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKG 2146
Cdd:COG1135 144 GQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHEMDVVRRICDRVAVLENG 217
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
931-1137 |
1.67e-11 |
|
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: 69.08 E-value: 1.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 931 VKNLVKIFEpcGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLP--PTSGTVLVGGRDIETS--LDAVRQSLG 1006
Cdd:TIGR02633 4 MKGIVKTFG--GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSPLKASniRDTERAGIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1007 MCPQHNILFHHLTVAEHMLFYAQLKGKSQEEAQLEM----EAMLEDTGLHHKRN-EEAQDLSGGMQRKLSVAIAFVGDAK 1081
Cdd:TIGR02633 82 IIHQELTLVPELSVAENIFLGNEITLPGGRMAYNAMylraKNLLRELQLDADNVtRPVGDYGGGQQQLVEIAKALNKQAR 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 105990541 1082 VVILDEPTSGVDPYSRRSIWDLL--LKyRSGRTIIMSTHHMDEADLLGDRIAIIAQGR 1137
Cdd:TIGR02633 162 LLILDEPSSSLTEKETEILLDIIrdLK-AHGVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
1969-2159 |
1.88e-11 |
|
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: 68.21 E-value: 1.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1969 GLLGVNGAGKTTTFKMLTGDTTVTSGDATVAG-------KSILTNIsevHQN-MGYCPQFDAIDELLTGREHLyLYARLR 2040
Cdd:TIGR02142 27 AIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlfdsrKGIFLPP---EKRrIGYVFQEARLFPHLSVRGNL-RYGMKR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2041 GVPAEeieKVANWS--IKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSIIR 2118
Cdd:TIGR02142 103 ARPSE---RRISFErvIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLERLHA 179
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 105990541 2119 E-GRAVVLTSHSMEECEALCTRLAIMVKGAFRCMGTIQHLKS 2159
Cdd:TIGR02142 180 EfGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWA 221
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
957-1138 |
1.95e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 69.17 E-value: 1.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 957 QITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGR--DIETSLDAVRQSLGMCP----QHNILFHHlTVAE-------- 1022
Cdd:PRK11288 280 EIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKpiDIRSPRDAIRAGIMLCPedrkAEGIIPVH-SVADninisarr 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1023 HMLFYAQL--KGKSQEEAQLEMEAMLEDTglhhkRNEEaQD---LSGGMQRKLSVAIAFVGDAKVVILDEPTSGVDPYSR 1097
Cdd:PRK11288 359 HHLRAGCLinNRWEAENADRFIRSLNIKT-----PSRE-QLimnLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAK 432
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 105990541 1098 RSIWDLLLKY-RSGRTIIMSTHHMDEADLLGDRIAIIAQGRL 1138
Cdd:PRK11288 433 HEIYNVIYELaAQGVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
942-1138 |
2.28e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 68.80 E-value: 2.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 942 GRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLP-PTSGTVLVGGR--DIETSLDAVRQSLGMCP----QHNIL 1014
Cdd:PRK13549 274 HIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKpvKIRNPQQAIAQGIAMVPedrkRDGIV 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1015 F-----HHLTVAEhmlfYAQLKGKSQEEAQLEMEAMLEDTG-LHHKRNEEAQ---DLSGGMQRKLSVAIAFVGDAKVVIL 1085
Cdd:PRK13549 354 PvmgvgKNITLAA----LDRFTGGSRIDDAAELKTILESIQrLKVKTASPELaiaRLSGGNQQKAVLAKCLLLNPKILIL 429
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 105990541 1086 DEPTSGVDPYSRRSIWDLLLKY-RSGRTIIMSTHHMDEADLLGDRIAIIAQGRL 1138
Cdd:PRK13549 430 DEPTRGIDVGAKYEIYKLINQLvQQGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1965-2156 |
2.53e-11 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 66.19 E-value: 2.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1965 GECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAG-----------KSILT---NISEVHQNMGYCPQFDAIDELLTGR 2030
Cdd:PRK11124 28 GETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsktpsdKAIRElrrNVGMVFQQYNLWPHLTVQQNLIEAP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2031 ehlylyARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQarrmLW 2110
Cdd:PRK11124 108 ------CRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPE----IT 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 105990541 2111 NVIVSIIRE----GRAVVLTSHSMEECEALCTRLAIMVKGAFRCMGTIQH 2156
Cdd:PRK11124 178 AQIVSIIRElaetGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASC 227
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1937-2137 |
2.60e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 68.80 E-value: 2.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1937 ILRLHELTKIYPGTssPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGdttVT-----SGDATVAGKSI-LTNISE- 2009
Cdd:PRK13549 5 LLEMKNITKTFGGV--KALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG---VYphgtyEGEIIFEGEELqASNIRDt 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2010 -------VHQNMGYCPQFDAIDELLTGREHLY--------LYARlrgvpAEEIekvanwsIKSLGLTVYADCLAGTYSGG 2074
Cdd:PRK13549 80 eragiaiIHQELALVKELSVLENIFLGNEITPggimdydaMYLR-----AQKL-------LAQLKLDINPATPVGNLGLG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 105990541 2075 NKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSIIREGRAVVLTSHSMEECEALC 2137
Cdd:PRK13549 148 QQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAIS 210
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
949-1138 |
2.66e-11 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 68.67 E-value: 2.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 949 LNITFYENQITaFL-GHNGAGKTTTLSILTGLLPPTSGTVLVGGRDI-ETSLDAVRQslgmcpqhniLF------HHLtv 1020
Cdd:COG4615 351 IDLTIRRGELV-FIvGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVtADNREAYRQ----------LFsavfsdFHL-- 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1021 aehmlfYAQLKGKSQEEAQLEMEAMLEDTGLHHKRNEEAQ-----DLSGGmQRK-LSVAIAFVGDAKVVILDEPTSGVDP 1094
Cdd:COG4615 418 ------FDRLLGLDGEADPARARELLERLELDHKVSVEDGrfsttDLSQG-QRKrLALLVALLEDRPILVFDEWAADQDP 490
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 105990541 1095 YSRRSIW-DLL--LKyRSGRTIIMSTHhmDEA--DlLGDRIAIIAQGRL 1138
Cdd:COG4615 491 EFRRVFYtELLpeLK-ARGKTVIAISH--DDRyfD-LADRVLKMDYGKL 535
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
1964-2128 |
2.75e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 69.14 E-value: 2.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1964 PGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATvagksILTN----ISEVHQNMGYCPQFDAIDELLTGREHLYLYARL 2039
Cdd:PLN03211 93 PGEILAVLGPSGSGKSTLLNALAGRIQGNNFTGT-----ILANnrkpTKQILKRTGFVTQDDILYPHLTVRETLVFCSLL 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2040 R---GVPAEEIEKVANWSIKSLGLTVYADCLAGT-----YSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWN 2111
Cdd:PLN03211 168 RlpkSLTKQEKILVAESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVL 247
|
170
....*....|....*..
gi 105990541 2112 VIVSIIREGRAVVLTSH 2128
Cdd:PLN03211 248 TLGSLAQKGKTIVTSMH 264
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1953-2146 |
3.38e-11 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 68.13 E-value: 3.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1953 PAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIlTN-------------ISEVHQNMGYCPQ 2019
Cdd:COG3845 272 PALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDI-TGlsprerrrlgvayIPEDRLGRGLVPD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2020 FDAIDELLTGREHLYLYAR---LRGVPAEEI--EKVANWSIKSLGltvyADCLAGTYSGGNKRKLSTAIALIGCPPLVLL 2094
Cdd:COG3845 351 MSVAENLILGRYRRPPFSRggfLDRKAIRAFaeELIEEFDVRTPG----PDTPARSLSGGNQQKVILARELSRDPKLLIA 426
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 105990541 2095 DEPTTGMDPQARRMLWNVIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
Cdd:COG3845 427 AQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEG 478
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
931-1142 |
3.42e-11 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 66.10 E-value: 3.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 931 VKNLVKIFEPcgRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGR-----DIETSLDAVRQSL 1005
Cdd:PRK11701 9 VRGLTKLYGP--RKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrDLYALSEAERRRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1006 -----GMCPQH-------------NILFHHLTV-AEHmlfYAQLKGKSQEeaqlemeaMLEDTGLHHKRNEEA-QDLSGG 1065
Cdd:PRK11701 87 lrtewGFVHQHprdglrmqvsaggNIGERLMAVgARH---YGDIRATAGD--------WLERVEIDAARIDDLpTTFSGG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 105990541 1066 MQRKLSVAIAFVGDAKVVILDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIIAQGRLYCSG 1142
Cdd:PRK11701 156 MQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLrgLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESG 234
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1933-2131 |
4.39e-11 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 65.22 E-value: 4.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1933 NKTDILRLHELTKIY-PGTSSPAVDR-LCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSiLTNISEV 2010
Cdd:PRK11629 1 MNKILLQCDNLCKRYqEGSVQTDVLHnVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQP-MSKLSSA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2011 ------HQNMGYCPQFDAIDELLTGREHLYLYARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIA 2084
Cdd:PRK11629 80 akaelrNQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 105990541 2085 LIGCPPLVLLDEPTTGMDPQARRMLWNVIVSI-IREGRAVVLTSHSME 2131
Cdd:PRK11629 160 LVNNPRLVLADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDLQ 207
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1962-2146 |
5.05e-11 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 65.16 E-value: 5.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISE----------------VHQNMGYCPQFDAIDE 2025
Cdd:PRK11264 26 VKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLsqqkglirqlrqhvgfVFQNFNLFPHRTVLEN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2026 LLTGRehlylyARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQA 2105
Cdd:PRK11264 106 IIEGP------VIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPEL 179
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 105990541 2106 RRMLWNVIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
Cdd:PRK11264 180 VGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQG 220
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1957-2146 |
6.46e-11 |
|
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: 64.05 E-value: 6.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1957 RLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTN------ISEVHQNMGYCPQFDAIDELLTGR 2030
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAppadrpVSMLFQENNLFAHLTVEQNVGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2031 EHlylYARLRGVPAEEIEKVAnwsiKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLW 2110
Cdd:cd03298 96 SP---GLKLTAEDRQAIEVAL----ARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEML 168
|
170 180 190
....*....|....*....|....*....|....*..
gi 105990541 2111 NVIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKG 2146
Cdd:cd03298 169 DLVLDLHAEtKMTVLMVTHQPEDAKRLAQRVVFLDNG 205
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
932-1137 |
7.68e-11 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 67.12 E-value: 7.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 932 KNLVKIFePcGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTS--GTVLVGG-----RDIETSLDA---- 1000
Cdd:NF040905 5 RGITKTF-P-GVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGevcrfKDIRDSEALgivi 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1001 VRQSLGMCPQhnilfhhLTVAEHM-LFYAQLKGK--SQEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFV 1077
Cdd:NF040905 83 IHQELALIPY-------LSIAENIfLGNERAKRGviDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALS 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 105990541 1078 GDAKVVILDEPTSGVDPYSRRSIWDLLLKYRS-GRTIIMSTHHMDEADLLGDRIAIIAQGR 1137
Cdd:NF040905 156 KDVKLLILDEPTAALNEEDSAALLDLLLELKAqGITSIIISHKLNEIRRVADSITVLRDGR 216
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1937-2157 |
8.46e-11 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 65.03 E-value: 8.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1937 ILRLHELTKIYpgTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFK----MLTGDTTVTS-----GDATVAGKSILTNI 2007
Cdd:PRK09984 4 IIRVEKLAKTF--NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRhlsgLITGDKSAGShiellGRTVQREGRLARDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2008 SEVHQNMGYC-PQFDAIDELlTGREHLYLYArLRGVP---------AEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKR 2077
Cdd:PRK09984 82 RKSRANTGYIfQQFNLVNRL-SVLENVLIGA-LGSTPfwrtcfswfTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2078 KLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSIIR-EGRAVVLTSHSMEECEALCTRLAIMVKGAFRCMGTIQH 2156
Cdd:PRK09984 160 RVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQnDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQ 239
|
.
gi 105990541 2157 L 2157
Cdd:PRK09984 240 F 240
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1960-2160 |
9.02e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 65.04 E-value: 9.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1960 VGVRPGECFGLLGVNGAGKTTTFKMLTG-----DTTVTSGDATVAGKSILTNISEVHQNMGYCPQFDaidelltgrEH-L 2033
Cdd:PRK13634 28 VSIPSGSYVAIIGHTGSGKSTLLQHLNGllqptSGTVTIGERVITAGKKNKKLKPLRKKVGIVFQFP---------EHqL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2034 YLYARLR---------GVPAEEIEKVANWSIKSLGLTvyADCLAGT---YSGGNKRKLSTAIALIGCPPLVLLDEPTTGM 2101
Cdd:PRK13634 99 FEETVEKdicfgpmnfGVSEEDAKQKAREMIELVGLP--EELLARSpfeLSGGQMRRVAIAGVLAMEPEVLVLDEPTAGL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2102 DPQARRMLWNVIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFRCMGTIQHLKSK 2160
Cdd:PRK13634 177 DPKGRKEMMEMFYKLHKEkGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFAD 236
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1954-2194 |
9.63e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 65.19 E-value: 9.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1954 AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTG-----DTTVTSGDATVAGKSILTNISEVHQNMGYCPQF-------D 2021
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINAllkptTGTVTVDDITITHKTKDKYIRPVRKRIGMVFQFpesqlfeD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2022 AID-ELLTGREHLylyarlrGVPAEEIEKVANWSIKSLGLTvyADCLAGT---YSGGNKRKLSTAIALIGCPPLVLLDEP 2097
Cdd:PRK13646 102 TVErEIIFGPKNF-------KMNLDEVKNYAHRLLMDLGFS--RDVMSQSpfqMSGGQMRKIAIVSILAMNPDIIVLDEP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2098 TTGMDPQARRMLWNVIVSI-IREGRAVVLTSHSMEECEALCTRLAIMVKGAFRCMGTIQHLkskFGDG-YIVTMKIKSPk 2175
Cdd:PRK13646 173 TAGLDPQSKRQVMRLLKSLqTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKEL---FKDKkKLADWHIGLP- 248
|
250
....*....|....*....
gi 105990541 2176 dDLLPDLNPVEQFFQGNFP 2194
Cdd:PRK13646 249 -EIVQLQYDFEQKYQTKLK 266
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1938-2162 |
1.19e-10 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 66.77 E-value: 1.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1938 LRLHELTKIYPGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIlTNISE--VHQNMG 2015
Cdd:PRK11160 339 LTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPI-ADYSEaaLRQAIS 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2016 YCPQ----FDAidellTGREHLYLYA------RLRGVpaeeIEKVanwsikslGLTVYADCLAG----------TYSGGN 2075
Cdd:PRK11160 418 VVSQrvhlFSA-----TLRDNLLLAApnasdeALIEV----LQQV--------GLEKLLEDDKGlnawlgeggrQLSGGE 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2076 KRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMlwnvIVSIIRE---GRAVVLTSH---SMEECEALCtrlaIMVKGAFR 2149
Cdd:PRK11160 481 QRRLGIARALLHDAPLLLLDEPTEGLDAETERQ----ILELLAEhaqNKTVLMITHrltGLEQFDRIC----VMDNGQII 552
|
250
....*....|...
gi 105990541 2150 CMGTIQHLKSKFG 2162
Cdd:PRK11160 553 EQGTHQELLAQQG 565
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1970-2146 |
1.39e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 64.38 E-value: 1.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1970 LLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-----NISEVHQNMGYCPQF--------DAIDELLTGREHLyly 2036
Cdd:PRK13649 38 FIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITStsknkDIKQIRKKVGLVFQFpesqlfeeTVLKDVAFGPQNF--- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2037 arlrGVPAEEIEKVANwsiKSLGLTVYADCLAGT----YSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNV 2112
Cdd:PRK13649 115 ----GVSQEEAEALAR---EKLALVGISESLFEKnpfeLSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTL 187
|
170 180 190
....*....|....*....|....*....|....
gi 105990541 2113 IVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
Cdd:PRK13649 188 FKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKG 221
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1938-2128 |
1.40e-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: 61.31 E-value: 1.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1938 LRLHELTKIYPGtsSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKsiltnisevhQNMGYC 2017
Cdd:cd03221 1 IELENLSKTYGG--KLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST----------VKIGYF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2018 PQFdaidelltgrehlylyarlrgvpaeeiekvanwsikslgltvyadclagtySGGNKRKLSTAIALIGCPPLVLLDEP 2097
Cdd:cd03221 69 EQL---------------------------------------------------SGGEKMRLALAKLLLENPNLLLLDEP 97
|
170 180 190
....*....|....*....|....*....|.
gi 105990541 2098 TTGMDPQARRMLwnvIVSIIREGRAVVLTSH 2128
Cdd:cd03221 98 TNHLDLESIEAL---EEALKEYPGTVILVSH 125
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1946-2132 |
1.68e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 64.47 E-value: 1.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1946 IY-PGTS--SPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNIS-----EVHQNMGYC 2017
Cdd:PRK13641 11 IYsPGTPmeKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGnknlkKLRKKVSLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2018 PQFDAIdELL--TGREHLYLYARLRGVPAEEIEKVANWSIKSLGL-TVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLL 2094
Cdd:PRK13641 91 FQFPEA-QLFenTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCL 169
|
170 180 190
....*....|....*....|....*....|....*...
gi 105990541 2095 DEPTTGMDPQARRMLWNVIVSIIREGRAVVLTSHSMEE 2132
Cdd:PRK13641 170 DEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDD 207
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
931-1144 |
1.85e-10 |
|
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: 62.81 E-value: 1.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 931 VKNLVKIFEPCGRPAVDrlNITFY--ENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIET-SLDAVRQSLGM 1007
Cdd:cd03369 9 VENLSVRYAPDLPPVLK--NVSFKvkAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTiPLEDLRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1008 CPQHNILFHHlTVAEHMLFYAQlkgksQEEAQLeMEAMledtglhhKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDE 1087
Cdd:cd03369 87 IPQDPTLFSG-TIRSNLDPFDE-----YSDEEI-YGAL--------RVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDE 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 105990541 1088 PTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDE-ADLlgDRIAIIAQGRLYCSGTP 1144
Cdd:cd03369 152 ATASIDYATDALIQKTIREEFTNSTILTIAHRLRTiIDY--DKILVMDAGEVKEYDHP 207
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1964-2159 |
2.07e-10 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 63.49 E-value: 2.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1964 PGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI-------LTNISEVHQNMGYC-------PQFDAIDELLTG 2029
Cdd:COG4161 27 SGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsqkpsEKAIRLLRQKVGMVfqqynlwPHLTVMENLIEA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2030 RehlylyARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQarrmL 2109
Cdd:COG4161 107 P------CKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPE----I 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 105990541 2110 WNVIVSIIRE----GRAVVLTSHSMEECEALCTRLAIMVKGAFRCMGTIQHLKS 2159
Cdd:COG4161 177 TAQVVEIIRElsqtGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDASHFTQ 230
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
945-1138 |
2.16e-10 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 63.68 E-value: 2.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVlvgGRDIETSLDAVRQSLGmcpqhnilfHHLTVAEHM 1024
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV---DRNGEVSVIAISAGLS---------GQLTGIENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1025 LFYAQLKGKSQEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTSGVDPYSRRSIWDLL 1104
Cdd:PRK13546 107 EFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKI 186
|
170 180 190
....*....|....*....|....*....|....*
gi 105990541 1105 LKYR-SGRTIIMSTHHMDEADLLGDRIAIIAQGRL 1138
Cdd:PRK13546 187 YEFKeQNKTIFFVSHNLGQVRQFCTKIAWIEGGKL 221
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
943-1138 |
2.39e-10 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 65.89 E-value: 2.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 943 RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIET-SLDAVRQSLGMCPQHNILFHHlTVA 1021
Cdd:PRK10789 328 HPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKlQLDSWRSRLAVVSQTPFLFSD-TVA 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1022 EHMlfyaQLKGKSQEEAQLEMEAML----EDT-----GLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTSGV 1092
Cdd:PRK10789 407 NNI----ALGRPDATQQEIEHVARLasvhDDIlrlpqGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAV 482
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 105990541 1093 DPYSRRSIWDLLLKYRSGRTIIMSTHHMD---EAdllgDRIAIIAQGRL 1138
Cdd:PRK10789 483 DGRTEHQILHNLRQWGEGRTVIISAHRLSaltEA----SEILVMQHGHI 527
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1943-2146 |
2.41e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 65.52 E-value: 2.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1943 LTKIYPGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI--------LTN-ISEVHQN 2013
Cdd:PRK10982 4 ISKSFPGVK--ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfksskeaLENgISMVHQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2014 MGYCPQFDAIDELLTGR--------EHLYLYARLRGVPAE-EI-----EKVANWSIKSLGLTVyadcLAGTYSGGNKrkl 2079
Cdd:PRK10982 82 LNLVLQRSVMDNMWLGRyptkgmfvDQDKMYRDTKAIFDElDIdidprAKVATLSVSQMQMIE----IAKAFSYNAK--- 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 105990541 2080 staialigcppLVLLDEPTTGMDPQARRMLWNVIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
Cdd:PRK10982 155 -----------IVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDG 210
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1952-2131 |
2.51e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 63.49 E-value: 2.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1952 SPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGK----------SILTNISEVHQNMGYCPQFD 2021
Cdd:PRK13638 14 EPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKpldyskrgllALRQQVATVFQDPEQQIFYT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2022 AIDElltgreHLYLYARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGM 2101
Cdd:PRK13638 94 DIDS------DIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGL 167
|
170 180 190
....*....|....*....|....*....|
gi 105990541 2102 DPQARRMLWNVIVSIIREGRAVVLTSHSME 2131
Cdd:PRK13638 168 DPAGRTQMIAIIRRIVAQGNHVIISSHDID 197
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1962-2128 |
2.53e-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: 62.16 E-value: 2.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1962 VRPGECFGLLGVNGAGKTTTFKMLTG--DTTVTSGDATVAGKSIlTNISevhqnmgycpqfdaIDEllTGREHLYLY--- 2036
Cdd:cd03217 23 IKKGEVHALMGPNGSGKSTLAKTIMGhpKYEVTEGEILFKGEDI-TDLP--------------PEE--RARLGIFLAfqy 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2037 -ARLRGVpaeeieKVANWsIKSLGLTvyadclagtYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVS 2115
Cdd:cd03217 86 pPEIPGV------KNADF-LRYVNEG---------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINK 149
|
170
....*....|...
gi 105990541 2116 IIREGRAVVLTSH 2128
Cdd:cd03217 150 LREEGKSVLIITH 162
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
949-1118 |
3.31e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 61.81 E-value: 3.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIETSLDAVRQSLGmcpqHNI-LFHHLTVAEHMLFY 1027
Cdd:PRK13541 19 LSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYCTYIG----HNLgLKLEMTVFENLKFW 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1028 AQLKGKSQeeaqlEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTSGVDPYSRRSIWDLL-LK 1106
Cdd:PRK13541 95 SEIYNSAE-----TLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIvMK 169
|
170
....*....|..
gi 105990541 1107 YRSGRTIIMSTH 1118
Cdd:PRK13541 170 ANSGGIVLLSSH 181
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
920-1143 |
3.57e-10 |
|
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: 63.34 E-value: 3.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 920 REHPGWVPGVCVKNlvkiFEPCGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRdietsld 999
Cdd:cd03291 31 RKHSSDDNNLFFSN----LCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR------- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1000 avrqsLGMCPQHNILFHHlTVAEHMLF---YAQLKGKSQEEA-QLEmeamlED-TGLHHKRN----EEAQDLSGGMQRKL 1070
Cdd:cd03291 100 -----ISFSSQFSWIMPG-TIKENIIFgvsYDEYRYKSVVKAcQLE-----EDiTKFPEKDNtvlgEGGITLSGGQRARI 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 105990541 1071 SVAIAFVGDAKVVILDEPTSGVDPYSRRSIWD-LLLKYRSGRTIIMSTHHMDEADlLGDRIAIIAQGRLYCSGT 1143
Cdd:cd03291 169 SLARAVYKDADLYLLDSPFGYLDVFTEKEIFEsCVCKLMANKTRILVTSKMEHLK-KADKILILHEGSSYFYGT 241
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
943-1144 |
3.87e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 62.82 E-value: 3.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 943 RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLvggRDIETSLDAVRQSLGMCPQHNilfhhLTVAE 1022
Cdd:PRK09544 17 RRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK---RNGKLRIGYVPQKLYLDTTLP-----LTVNR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1023 HMlfyaQLKGKSQEEAQLemeAMLEDTGLHHKRNEEAQDLSGG-MQRKLsVAIAFVGDAKVVILDEPTSGVDPYSRRSIW 1101
Cdd:PRK09544 89 FL----RLRPGTKKEDIL---PALKRVQAGHLIDAPMQKLSGGeTQRVL-LARALLNRPQLLVLDEPTQGVDVNGQVALY 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 105990541 1102 DLLLKYRS--GRTIIMSTHHM-------DEADLLGDRIAiiaqgrlyCSGTP 1144
Cdd:PRK09544 161 DLIDQLRRelDCAVLMVSHDLhlvmaktDEVLCLNHHIC--------CSGTP 204
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
943-1137 |
5.05e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 64.73 E-value: 5.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 943 RPAVDRLNITFYENQITAFLGHNGAGKT-TTLSILtGLLPP-----TSGTVLVGGRDI----ETSLDAVR-QSLGMC--- 1008
Cdd:PRK15134 22 RTVVNDVSLQIEAGETLALVGESGSGKSvTALSIL-RLLPSppvvyPSGDIRFHGESLlhasEQTLRGVRgNKIAMIfqe 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1009 ------PQHNI---LFHHLTVaeHmlfyaqlKGKSQEEAQLEMEAMLEDTGLHH--KR-NEEAQDLSGGMQRKLSVAIAF 1076
Cdd:PRK15134 101 pmvslnPLHTLekqLYEVLSL--H-------RGMRREAARGEILNCLDRVGIRQaaKRlTDYPHQLSGGERQRVMIAMAL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 105990541 1077 VGDAKVVILDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIIAQGR 1137
Cdd:PRK15134 172 LTRPELLIADEPTTALDVSVQAQILQLLreLQQELNMGLLFITHNLSIVRKLADRVAVMQNGR 234
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
931-1167 |
6.42e-10 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 64.05 E-value: 6.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 931 VKNLVKIFEpcGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGL--LPPTSGTVL-------------------- 988
Cdd:TIGR03269 3 VKNLTKKFD--GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIyhvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 989 ----VGGRDIETSLD----------AVRQSLGMCPQHNI-LFHHLTVAEHMLFYAQLKGKSQEEAQLEMEAMLEDTGLHH 1053
Cdd:TIGR03269 81 pcpvCGGTLEPEEVDfwnlsdklrrRIRKRIAIMLQRTFaLYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1054 KRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTSGVDPYSRRSIWDLLLK--YRSGRTIIMSTHHMDEADLLGDRIA 1131
Cdd:TIGR03269 161 RITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEavKASGISMVLTSHWPEVIEDLSDKAI 240
|
250 260 270
....*....|....*....|....*....|....*.
gi 105990541 1132 IIAQGRLYCSGTPLFLKNCFGTGlyLTLVRKMKNIQ 1167
Cdd:TIGR03269 241 WLENGEIKEEGTPDEVVAVFMEG--VSEVEKECEVE 274
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
945-1139 |
7.39e-10 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 64.22 E-value: 7.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDI-ETSLDAVRQslgmcpqhniLFHHLTVAEH 1023
Cdd:PRK10522 338 SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVtAEQPEDYRK----------LFSAVFTDFH 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1024 mLFYAQLKGKSQEEAQLEMEAMLEDTGLHHKRNEEAQ-----DLSGGMQRKLSVAIAFVGDAKVVILDEPTSGVDPYSRR 1098
Cdd:PRK10522 408 -LFDQLLGPEGKPANPALVEKWLERLKMAHKLELEDGrisnlKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRR 486
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 105990541 1099 SIWDLLLKY--RSGRTIIMSTHHmDEADLLGDRIAIIAQGRLY 1139
Cdd:PRK10522 487 EFYQVLLPLlqEMGKTIFAISHD-DHYFIHADRLLEMRNGQLS 528
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
963-1121 |
7.91e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 60.73 E-value: 7.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 963 GHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIETSLDAVRQSLGMCPQHNILFHHLTVAEHMLFYAQLkgksqEEAQLEM 1042
Cdd:PRK13540 34 GSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGHRSGINPYLTLRENCLYDIHF-----SPGAVGI 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 105990541 1043 EAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMD 1121
Cdd:PRK13540 109 TELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSHQD 187
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1933-2155 |
8.43e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 62.08 E-value: 8.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1933 NKTDILRLHELTKIYPGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISEVH 2011
Cdd:PRK13648 3 DKNSIIVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDdNFEKLR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2012 QNMGYCpqFDAIDELLTGREHLYLYA---RLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGC 2088
Cdd:PRK13648 83 KHIGIV--FQNPDNQFVGSIVKYDVAfglENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALN 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 105990541 2089 PPLVLLDEPTTGMDPQARRMLWNvIVSIIREGRAVVLTSHSMEECEAL-CTRLAIMVKGAFRCMGTIQ 2155
Cdd:PRK13648 161 PSVIILDEATSMLDPDARQNLLD-LVRKVKSEHNITIISITHDLSEAMeADHVIVMNKGTVYKEGTPT 227
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
931-1136 |
8.92e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 63.87 E-value: 8.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 931 VKNLVKIFePcGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRdiETSLDAVRQS----LG 1006
Cdd:PRK10762 7 LKGIDKAF-P-GVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGK--EVTFNGPKSSqeagIG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1007 MCPQHNILFHHLTVAEHML----FYAQLKGKSQEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKV 1082
Cdd:PRK10762 83 IIHQELNLIPQLTIAENIFlgreFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 105990541 1083 VILDEPTSGVDPYSRRSIWDLLLKYRS-GRTIIMSTHHMDEADLLGDRIAIIAQG 1136
Cdd:PRK10762 163 IIMDEPTDALTDTETESLFRVIRELKSqGRGIVYISHRLKEIFEICDDVTVFRDG 217
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
1937-2146 |
9.74e-10 |
|
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: 61.74 E-value: 9.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1937 ILRLHELTKIYPGTS-------SPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAG--------- 2000
Cdd:TIGR02769 2 LLEVRDVTHTYRTGGlfgakqrAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGqdlyqldrk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2001 --KSILTNISEVHQNmgyCPqfDAIDELLTGR----EHLYLYARLRgvPAEEIEKVANWsIKSLGL-TVYADCLAGTYSG 2073
Cdd:TIGR02769 82 qrRAFRRDVQLVFQD---SP--SAVNPRMTVRqiigEPLRHLTSLD--ESEQKARIAEL-LDMVGLrSEDADKLPRQLSG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 105990541 2074 GNKRKLSTAIALIGCPPLVLLDEPTTGMDpqarRMLWNVIVSIIRE-----GRAVVLTSHSMEECEALCTRLAIMVKG 2146
Cdd:TIGR02769 154 GQLQRINIARALAVKPKLIVLDEAVSNLD----MVLQAVILELLRKlqqafGTAYLFITHDLRLVQSFCQRVAVMDKG 227
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
1887-2128 |
1.10e-09 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 63.44 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1887 VVYF--LLTLLVQR-----HFFLSQWIAEPTKEPIVDEDDDVA--EERQRIITGGNKTDILRLHELTKIYPGtSSPAVDR 1957
Cdd:PRK13657 275 VVAFvgFATLLIGRldqvvAFINQVFMAAPKLEEFFEVEDAVPdvRDPPGAIDLGRVKGAVEFDDVSFSYDN-SRQGVED 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1958 LCVGVRPGECFGLLGVNGAGKTTTFKML-------TGDTTVTSGD-ATVAGKSILTNISEVHQNMGYcpqFD-AI-DELL 2027
Cdd:PRK13657 354 VSFEAKPGQTVAIVGPTGAGKSTLINLLqrvfdpqSGRILIDGTDiRTVTRASLRRNIAVVFQDAGL---FNrSIeDNIR 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2028 TGR-----EHLYLYARlRGVPAEEIEKvanwsiKSLGLtvyaDCLAG----TYSGGNKRKLSTAIALIGCPPLVLLDEPT 2098
Cdd:PRK13657 431 VGRpdatdEEMRAAAE-RAQAHDFIER------KPDGY----DTVVGergrQLSGGERQRLAIARALLKDPPILILDEAT 499
|
250 260 270
....*....|....*....|....*....|
gi 105990541 2099 TGMDPQARRMLwNVIVSIIREGRAVVLTSH 2128
Cdd:PRK13657 500 SALDVETEAKV-KAALDELMKGRTTFIIAH 528
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1954-2146 |
1.11e-09 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 61.05 E-value: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1954 AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIL--TNISEVHQNMGYCPQFDAIDELLTGRE 2031
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITdwQTAKIMREAVAIVPEGRRVFSRMTVEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2032 HLYL--YARLRGVPAEEIEKVANWSIKSLGLTVYAdclAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRML 2109
Cdd:PRK11614 100 NLAMggFFAERDQFQERIKWVYELFPRLHERRIQR---AGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQI 176
|
170 180 190
....*....|....*....|....*....|....*..
gi 105990541 2110 WNVIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
Cdd:PRK11614 177 FDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENG 213
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
927-1148 |
1.33e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 63.99 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 927 PGVCVKNLVKIFEPCG-RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVggrdietsldaVRQSL 1005
Cdd:PLN03130 613 PAISIKNGYFSWDSKAeRPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVV-----------IRGTV 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1006 GMCPQHNILFHhLTVAEHMLFYAQLKGKSQEEAqlemeamLEDTGLHHKRN-----------EEAQDLSGGMQRKLSVAI 1074
Cdd:PLN03130 682 AYVPQVSWIFN-ATVRDNILFGSPFDPERYERA-------IDVTALQHDLDllpggdlteigERGVNISGGQKQRVSMAR 753
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1075 AFVGDAKVVILDEPTSGVDPYSRRSIWDLLLKYR-SGRTIIMST---HHMDEAdllgDRIAIIAQGRLYCSGT------- 1143
Cdd:PLN03130 754 AVYSNSDVYIFDDPLSALDAHVGRQVFDKCIKDElRGKTRVLVTnqlHFLSQV----DRIILVHEGMIKEEGTyeelsnn 829
|
....*.
gi 105990541 1144 -PLFLK 1148
Cdd:PLN03130 830 gPLFQK 835
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1962-2155 |
1.50e-09 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 60.94 E-value: 1.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSiLTNIS--EVHQNMGYCPQ-------FDAIDELLTGREH 2032
Cdd:PRK13548 25 LRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRP-LADWSpaELARRRAVLPQhsslsfpFTVEEVVAMGRAP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2033 LYL-YARLRGVPAEEIEKVanwsikslGLTVYADCLAGTYSGGNKRKLSTAIALI------GCPPLVLLDEPTTGMDPQ- 2104
Cdd:PRK13548 104 HGLsRAEDDALVAAALAQV--------DLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSALDLAh 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 105990541 2105 -------ARRMlwnvivsIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFRCMGTIQ 2155
Cdd:PRK13548 176 qhhvlrlARQL-------AHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPA 226
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1962-2147 |
1.71e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 62.76 E-value: 1.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSiLTNISEVH-QNMG-Y-CPQFDAIDELLTGREHLylyar 2038
Cdd:PRK15439 34 LHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNP-CARLTPAKaHQLGiYlVPQEPLLFPNLSVKENI----- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2039 LRGVPAEE--IEKVANWsIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSI 2116
Cdd:PRK15439 108 LFGLPKRQasMQKMKQL-LAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPAETERLFSRIREL 186
|
170 180 190
....*....|....*....|....*....|.
gi 105990541 2117 IREGRAVVLTSHSMEECEALCTRLAIMVKGA 2147
Cdd:PRK15439 187 LAQGVGIVFISHKLPEIRQLADRISVMRDGT 217
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1970-2128 |
1.94e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 59.58 E-value: 1.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1970 LLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISEVHQNMGYCPQFDAIDELLTGREHLYLYARLRGVPAEEIEK 2049
Cdd:PRK13540 32 LKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGHRSGINPYLTLRENCLYDIHFSPGAVGITEL 111
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 105990541 2050 VANWSIKSlgltvYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSIIREGRAVVLTSH 2128
Cdd:PRK13540 112 CRLFSLEH-----LIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSH 185
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1962-2147 |
2.30e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 62.49 E-value: 2.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI------------LTNISEVHQNMGYCPQFD-----AID 2024
Cdd:PRK09700 286 VCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIsprspldavkkgMAYITESRRDNGFFPNFSiaqnmAIS 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2025 ELL-TGRehlylYARLRGVPAEEIE-KVANWSIKSLGLTVYA-DCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGM 2101
Cdd:PRK09700 366 RSLkDGG-----YKGAMGLFHEVDEqRTAENQRELLALKCHSvNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGI 440
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 105990541 2102 DPQARRMLWNVIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGA 2147
Cdd:PRK09700 441 DVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGR 486
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
932-1145 |
2.76e-09 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 61.40 E-value: 2.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 932 KNLVKIFePCGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIeTSLDAVRQSLGMCPQH 1011
Cdd:PRK11650 7 QAVRKSY-DGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVV-NELEPADRDIAMVFQN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1012 NILFHHLTVAEHMLfYAqLK----GKSQ-----EEAQ--LEMEAMLEdtglhHKRNEeaqdLSGGmQRKlSVAI--AFVG 1078
Cdd:PRK11650 85 YALYPHMSVRENMA-YG-LKirgmPKAEieervAEAAriLELEPLLD-----RKPRE----LSGG-QRQ-RVAMgrAIVR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 105990541 1079 DAKVVILDEPTSGVDPYSR--------RsiwdllLKYRSGRTIIMSTHHMDEADLLGDRIAIIAQGRLYCSGTPL 1145
Cdd:PRK11650 152 EPAVFLFDEPLSNLDAKLRvqmrleiqR------LHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPV 220
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
906-1138 |
3.11e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 62.18 E-value: 3.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 906 DPEHPEGIHDSFFEREhpgwvPGVCVKNLVK-------IFEPCGRP--AVDRLNITFYENQITAFLGHNGAGKTTTLSIL 976
Cdd:PRK10261 296 AKQEPPIEQDTVVDGE-----PILQVRNLVTrfplrsgLLNRVTREvhAVEKVSFDLWPGETLSLVGESGSGKSTTGRAL 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 977 TGLLPPTSGTVLVGGRDIET----SLDAVRQSL---------GMCPQHNILFhhlTVAEHMLFYAQLKGksqEEAQLEME 1043
Cdd:PRK10261 371 LRLVESQGGEIIFNGQRIDTlspgKLQALRRDIqfifqdpyaSLDPRQTVGD---SIMEPLRVHGLLPG---KAAAARVA 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1044 AMLEDTGLhhkRNEEA----QDLSGGMQRKLSVAIAFVGDAKVVILDEPTSGVDPYSRRSIWDLLLKYRS--GRTIIMST 1117
Cdd:PRK10261 445 WLLERVGL---LPEHAwrypHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRdfGIAYLFIS 521
|
250 260
....*....|....*....|.
gi 105990541 1118 HHMDEADLLGDRIAIIAQGRL 1138
Cdd:PRK10261 522 HDMAVVERISHRVAVMYLGQI 542
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1947-2162 |
3.16e-09 |
|
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: 59.81 E-value: 3.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1947 YPGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISE-VHQNMGYCPQfdaiDE 2025
Cdd:cd03252 10 YKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAwLRRQVGVVLQ----EN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2026 LL---TGREHLYLYArlRGVPAEEIEKVANWS-----IKSLGL---TVYADCLAGtYSGGNKRKLSTAIALIGCPPLVLL 2094
Cdd:cd03252 86 VLfnrSIRDNIALAD--PGMSMERVIEAAKLAgahdfISELPEgydTIVGEQGAG-LSGGQRQRIAIARALIHNPRILIF 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 105990541 2095 DEPTTGMDPQARRMLWNVIVSIIrEGRAVVLTSHSMEECEAlCTRLAIMVKGAFRCMGTIQHLKSKFG 2162
Cdd:cd03252 163 DEATSALDYESEHAIMRNMHDIC-AGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLAENG 228
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
952-1130 |
3.28e-09 |
|
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: 59.73 E-value: 3.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 952 TFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGtvlvggrDIETSLDAVRQSlgmcPQHNILFHHLTVaEHML------ 1025
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEG-------DIEIELDTVSYK----PQYIKADYEGTV-RDLLssitkd 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1026 FYAQLKGKSQEEAQLEMEAMLEdtglhhkrnEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTSGVDPYSR----RSIW 1101
Cdd:cd03237 89 FYTHPYFKTEIAKPLQIEQILD---------REVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRlmasKVIR 159
|
170 180
....*....|....*....|....*....
gi 105990541 1102 DLLLKYRSgrTIIMSTHHMDEADLLGDRI 1130
Cdd:cd03237 160 RFAENNEK--TAFVVEHDIIMIDYLADRL 186
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1947-2128 |
3.38e-09 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 62.10 E-value: 3.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1947 YPGtSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISEVHQNMGYCPQfDAIde 2025
Cdd:COG1132 349 YPG-DRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDlTLESLRRQIGVVPQ-DTF-- 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2026 LLTG--REHLyLYARLrGVPAEEIEKVANWS-----IKSL--GL-TVYADclAGTY-SGGNKRKLSTAIALIGCPPLVLL 2094
Cdd:COG1132 425 LFSGtiRENI-RYGRP-DATDEEVEEAAKAAqahefIEALpdGYdTVVGE--RGVNlSGGQRQRIAIARALLKDPPILIL 500
|
170 180 190
....*....|....*....|....*....|....
gi 105990541 2095 DEPTTGMDPQARRMLWNVIVSiIREGRAVVLTSH 2128
Cdd:COG1132 501 DEATSALDTETEALIQEALER-LMKGRTTIVIAH 533
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1947-2109 |
4.08e-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: 59.17 E-value: 4.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1947 YPGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISEVHQNMGYCPQfdaiDE 2025
Cdd:cd03251 10 YPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDyTLASLRRQIGLVSQ----DV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2026 LL---TGREHLyLYARlRGVPAEEIEKVANWS-----IKSL--GL-TVYADcLAGTYSGGNKRKLSTAIALIGCPPLVLL 2094
Cdd:cd03251 86 FLfndTVAENI-AYGR-PGATREEVEEAARAAnahefIMELpeGYdTVIGE-RGVKLSGGQRQRIAIARALLKDPPILIL 162
|
170
....*....|....*
gi 105990541 2095 DEPTTGMDPQARRML 2109
Cdd:cd03251 163 DEATSALDTESERLV 177
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1934-2146 |
4.43e-09 |
|
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: 61.38 E-value: 4.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1934 KTDILRLHELTKIYP-GTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGD-TTVTSGDATVAGKSILTN----- 2006
Cdd:TIGR02633 254 GDVILEARNLTCWDViNPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPVDIRnpaqa 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2007 -------ISEVHQNMGYCPQFdAIDELLTgREHLYLYARLRGVPAEEIEKVANWSIKSLGL-TVYADCLAGTYSGGNKRK 2078
Cdd:TIGR02633 334 iragiamVPEDRKRHGIVPIL-GVGKNIT-LSVLKSFCFKMRIDAAAELQIIGSAIQRLKVkTASPFLPIGRLSGGNQQK 411
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 105990541 2079 LSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
Cdd:TIGR02633 412 AVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEG 479
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1962-2128 |
4.46e-09 |
|
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: 59.16 E-value: 4.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISEVHQNMGYCPQfdaiDELL---TGREHLyLYA 2037
Cdd:cd03254 26 IKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDiSRKSLRSMIGVVLQ----DTFLfsgTIMENI-RLG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2038 RLRgVPAEEIEKV-----ANWSIKSL--GLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLW 2110
Cdd:cd03254 101 RPN-ATDEEVIEAakeagAHDFIMKLpnGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQ 179
|
170
....*....|....*...
gi 105990541 2111 NVIVSiIREGRAVVLTSH 2128
Cdd:cd03254 180 EALEK-LMKGRTSIIIAH 196
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
946-1138 |
4.51e-09 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 59.70 E-value: 4.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 946 VDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIeTSLD-----AVRQSLGMC---------PQH 1011
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPL-AKLNraqrkAFRRDIQMVfqdsisavnPRK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1012 NIlfhHLTVAEHMLFYAQLKGKSQEEAQLEM-EAMLEDTGLHHKRneeAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTS 1090
Cdd:PRK10419 107 TV---REIIREPLRHLLSLDKAERLARASEMlRAVDLDDSVLDKR---PPQLSGGQLQRVCLARALAVEPKLLILDEAVS 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 105990541 1091 GVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIIAQGRL 1138
Cdd:PRK10419 181 NLDLVLQAGVIRLLkkLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
2041-2153 |
4.94e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 60.25 E-value: 4.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2041 GVPAEEIEKVANWSIKSLGL-TVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSIIRE 2119
Cdd:PRK13631 146 GVKKSEAKKLAKFYLNKMGLdDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN 225
|
90 100 110
....*....|....*....|....*....|....
gi 105990541 2120 GRAVVLTSHSMEECEALCTRLAIMVKGAFRCMGT 2153
Cdd:PRK13631 226 NKTVFVITHTMEHVLEVADEVIVMDKGKILKTGT 259
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1938-2131 |
5.46e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 60.10 E-value: 5.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1938 LRLHELTKIY-PGTSS--PAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSG-------------------- 1994
Cdd:PRK13651 3 IKVKNIVKIFnKKLPTelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGtiewifkdeknkkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1995 --DATVAGKSI---LTNISEVHQNMGYCPQFdAIDELL--TGREHLYLYARLRGVPAEEIEKVANWSIKSLGLTV-YADC 2066
Cdd:PRK13651 83 vlEKLVIQKTRfkkIKKIKEIRRRVGVVFQF-AEYQLFeqTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDEsYLQR 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 105990541 2067 LAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSIIREGRAVVLTSHSME 2131
Cdd:PRK13651 162 SPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLD 226
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1969-2157 |
6.00e-09 |
|
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: 60.50 E-value: 6.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1969 GLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKsILTNISE-----VHQ-NMGYCPQfDAidEL---LTGREHLyLYARL 2039
Cdd:COG4148 29 ALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGE-VLQDSARgiflpPHRrRIGYVFQ-EA--RLfphLSVRGNL-LYGRK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2040 RGVPAE---EIEKVANWsiksLGLtvyADCLA---GTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVI 2113
Cdd:COG4148 104 RAPRAErriSFDEVVEL----LGI---GHLLDrrpATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILPYL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 105990541 2114 VSIIREGR-AVVLTSHSMEECEALCTRLAIMVKGAFRCMGTIQHL 2157
Cdd:COG4148 177 ERLRDELDiPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEV 221
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1962-2102 |
7.18e-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: 7.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVT---SGDATVAGKSILTNISEVHQNMGYCPQFDAIDELLTGREHLYLYAR 2038
Cdd:cd03233 30 VKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPGEIIYVSEEDVHFPTLTVRETLDFALR 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 105990541 2039 LRGvpaeeiekvaNWSIKSLgltvyadclagtySGGNKRKLSTAIALIGCPPLVLLDEPTTGMD 2102
Cdd:cd03233 110 CKG----------NEFVRGI-------------SGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
955-1133 |
1.09e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 60.21 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 955 ENQITAFLGHNGAGKTTTLSILTGLLPPTsgtvlVGGRDIETSLDAV-RQSLGmcpqhNILFHH--------LTVAeHML 1025
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGELIPN-----LGDYEEEPSWDEVlKRFRG-----TELQNYfkklyngeIKVV-HKP 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1026 FY-----AQLKGKSQEEaqLE-------MEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTSGVD 1093
Cdd:PRK13409 167 QYvdlipKVFKGKVREL--LKkvdergkLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD 244
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 105990541 1094 PYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIAII 1133
Cdd:PRK13409 245 IRQRLNVARLIRELAEGKYVLVVEHDLAVLDYLADNVHIA 284
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
923-1120 |
1.16e-08 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 60.73 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 923 PGWVPGVCVKNLVKIFEPCGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGrdietsldavr 1002
Cdd:TIGR00957 631 PGEGNSITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG----------- 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1003 qSLGMCPQHNILfHHLTVAEHMLFYAQLKGKsQEEAQLEMEAMLED-----TGLHHKRNEEAQDLSGGMQRKLSVAIAFV 1077
Cdd:TIGR00957 700 -SVAYVPQQAWI-QNDSLRENILFGKALNEK-YYQQVLEACALLPDleilpSGDRTEIGEKGVNLSGGQKQRVSLARAVY 776
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 105990541 1078 GDAKVVILDEPTSGVDPYSRRSIWDLLLKYR---SGRTIIMSTHHM 1120
Cdd:TIGR00957 777 SNADIYLFDDPLSAVDAHVGKHIFEHVIGPEgvlKNKTRILVTHGI 822
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
945-1093 |
1.18e-08 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 59.33 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDI----ETSLDAVRQSLGMCPQHNI--LFHHL 1018
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLlgmkDDEWRAVRSDIQMIFQDPLasLNPRM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1019 TVAEHM-----LFYAQLkgkSQEEAQLEMEAMLEDTGL-HHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTSGV 1092
Cdd:PRK15079 116 TIGEIIaeplrTYHPKL---SRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSAL 192
|
.
gi 105990541 1093 D 1093
Cdd:PRK15079 193 D 193
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
955-1133 |
1.37e-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: 60.18 E-value: 1.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 955 ENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGrDIETSLDAVRQSlgmcpqhnILFHHLT-VAEHMLFYA----- 1028
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELKPNLGDYDEEP-SWDEVLKRFRGT--------ELQDYFKkLANGEIKVAhkpqy 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1029 ------QLKG-------KSQEEAQLEMEAmlEDTGLHHKRNEEAQDLSGG-MQRkLSVAIAFVGDAKVVILDEPTSGVDP 1094
Cdd:COG1245 169 vdlipkVFKGtvrelleKVDERGKLDELA--EKLGLENILDRDISELSGGeLQR-VAIAAALLRDADFYFFDEPSSYLDI 245
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 105990541 1095 YSR----RSIWDLLlkyRSGRTIIMSTHHMDEADLLGDRIAII 1133
Cdd:COG1245 246 YQRlnvaRLIRELA---EEGKYVLVVEHDLAILDYLADYVHIL 285
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
1954-2163 |
1.39e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 59.90 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1954 AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISEvhqnmgycpqfdAIDELLTGREHL 2033
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISS------------GLNGQLTGIENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2034 YLYARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVI 2113
Cdd:PRK13545 107 ELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKM 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 105990541 2114 VSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFRCMGTIQHLKSKFGD 2163
Cdd:PRK13545 187 NEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDHYDE 236
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
938-1143 |
1.69e-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: 60.31 E-value: 1.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 938 FEPCGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRdietsldavrqsLGMCPQHNILFHH 1017
Cdd:TIGR01271 434 FSLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR------------ISFSPQTSWIMPG 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1018 lTVAEHMLF---YAQLKGKSQEEA-QLEmeamlEDTGLHHKRN-----EEAQDLSGGMQRKLSVAIAFVGDAKVVILDEP 1088
Cdd:TIGR01271 502 -TIKDNIIFglsYDEYRYTSVIKAcQLE-----EDIALFPEKDktvlgEGGITLSGGQRARISLARAVYKDADLYLLDSP 575
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 105990541 1089 TSGVDPYSRRSIWD-LLLKYRSGRTIIMST---HHMDEAdllgDRIAIIAQGRLYCSGT 1143
Cdd:TIGR01271 576 FTHLDVVTEKEIFEsCLCKLMSNKTRILVTsklEHLKKA----DKILLLHEGVCYFYGT 630
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1962-2146 |
1.77e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 58.18 E-value: 1.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISEVHQNMGYCpqFDAIDELLTG---REHLYLYA 2037
Cdd:PRK13642 30 ITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAeNVWNLRRKIGMV--FQNPDNQFVGatvEDDVAFGM 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2038 RLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSII 2117
Cdd:PRK13642 108 ENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIK 187
|
170 180 190
....*....|....*....|....*....|
gi 105990541 2118 REGRAVVLT-SHSMEECeALCTRLAIMVKG 2146
Cdd:PRK13642 188 EKYQLTVLSiTHDLDEA-ASSDRILVMKAG 216
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
943-1140 |
1.83e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 59.26 E-value: 1.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 943 RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPP--TSGTVLVGGR--------DIETSLDAVRQSLGM----- 1007
Cdd:PRK10938 273 RPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPQgySNDLTLFGRRrgsgetiwDIKKHIGYVSSSLHLdyrvs 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1008 CPQHNIL----FHHLTVaehmlfYAQLKGKSQEEAQ-----LEMEAMLEDTGLHhkrneeaqDLSGGMQRKLSVAIAFVG 1078
Cdd:PRK10938 353 TSVRNVIlsgfFDSIGI------YQAVSDRQQKLAQqwldiLGIDKRTADAPFH--------SLSWGQQRLALIVRALVK 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 105990541 1079 DAKVVILDEPTSGVDPYSR---RSIWDLLLkyRSGRT--IIMSTHHMDEADLLGDRIAIIAQGRLYC 1140
Cdd:PRK10938 419 HPTLLILDEPLQGLDPLNRqlvRRFVDVLI--SEGETqlLFVSHHAEDAPACITHRLEFVPDGDIYR 483
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
903-1142 |
1.85e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 60.18 E-value: 1.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 903 ETEDPEHPEGIHDSFFEREhpgwvPGVCVKNLvkifepcgrpavdrlNITFYENQITAFLGHNGAGKTTTLSILTGLLPP 982
Cdd:PTZ00243 653 SERSAKTPKMKTDDFFELE-----PKVLLRDV---------------SVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEI 712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 983 TSGTVLVggrdiETSLDAVRQslgmcpQHNILfhHLTVAEHMLFYAQLKGKSQEEA----QLEMEAMLEDTGLHHKRNEE 1058
Cdd:PTZ00243 713 SEGRVWA-----ERSIAYVPQ------QAWIM--NATVRGNILFFDEEDAARLADAvrvsQLEADLAQLGGGLETEIGEK 779
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1059 AQDLSGGMQRKLSVAIAFVGDAKVVILDEPTSGVDPY-SRRSIWDLLLKYRSGRTIIMSTHHMDEADlLGDRIAIIAQGR 1137
Cdd:PTZ00243 780 GVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHvGERVVEECFLGALAGKTRVLATHQVHVVP-RADYVVALGDGR 858
|
....*
gi 105990541 1138 LYCSG 1142
Cdd:PTZ00243 859 VEFSG 863
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1954-2152 |
1.90e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 59.48 E-value: 1.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1954 AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT----NISEVHQNMGYCPQ--FDAIDELL 2027
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTlspgKLQALRRDIQFIFQdpYASLDPRQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2028 TGREHLYLYARLRGV-PAEEIEKVANWSIKSLGLTV-YADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQA 2105
Cdd:PRK10261 419 TVGDSIMEPLRVHGLlPGKAAAARVAWLLERVGLLPeHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSI 498
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 105990541 2106 RRMLWNVIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFRCMG 2152
Cdd:PRK10261 499 RGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIVEIG 546
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
931-1093 |
2.11e-08 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 58.20 E-value: 2.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 931 VKNLVKIFE----PCGRP-----AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDI----ETS 997
Cdd:COG4608 10 VRDLKKHFPvrggLFGRTvgvvkAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDItglsGRE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 998 LDAVRQSLGMC---------PQHNIlfhHLTVAEHMLFYAQLKGKSQEEaqlEMEAMLEDTGLhhkrNEEAQD-----LS 1063
Cdd:COG4608 90 LRPLRRRMQMVfqdpyaslnPRMTV---GDIIAEPLRIHGLASKAERRE---RVAELLELVGL----RPEHADrypheFS 159
|
170 180 190
....*....|....*....|....*....|.
gi 105990541 1064 GGmQR-KLSVAIAFVGDAKVVILDEPTSGVD 1093
Cdd:COG4608 160 GG-QRqRIGIARALALNPKLIVCDEPVSALD 189
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
1954-2176 |
2.53e-08 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 57.52 E-value: 2.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1954 AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGksiltNISEVHQNMGYCPQfdaidelLTGREHL 2033
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG-----EVSVIAISAGLSGQ-------LTGIENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2034 YLYARLRGVPAEEIEKVANWSIK--SLGLTVYADclAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWN 2111
Cdd:PRK13546 107 EFKMLCMGFKRKEIKAMTPKIIEfsELGEFIYQP--VKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLD 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 105990541 2112 VIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFRCMGTIQHLKSKFgDGYIVTMKIKSPKD 2176
Cdd:PRK13546 185 KIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPKY-EAFLNDFKKKSKAE 248
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1967-2154 |
2.79e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 57.16 E-value: 2.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1967 CFGLLGVNGAGKTT---TFKMLT--GDTTVTSGDATVAGKSILT---NISEVHQNMGYCPQFDAIDELLTGREHLYLYAR 2038
Cdd:PRK14267 32 VFALMGPSGCGKSTllrTFNRLLelNEEARVEGEVRLFGRNIYSpdvDPIEVRREVGMVFQYPNPFPHLTIYDNVAIGVK 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2039 LRGV--PAEEIEKVANWSIKSLGL-TVYADCL---AGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNV 2112
Cdd:PRK14267 112 LNGLvkSKKELDERVEWALKKAALwDEVKDRLndyPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEEL 191
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 105990541 2113 IVSiIREGRAVVLTSHSmeecEALCTRLAIMVkgAFRCMGTI 2154
Cdd:PRK14267 192 LFE-LKKEYTIVLVTHS----PAQAARVSDYV--AFLYLGKL 226
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1955-2159 |
3.43e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 57.41 E-value: 3.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1955 VDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTG-DTTVT----SGDATVAGKSILT--NISEVHQNMGYCPQ------FD 2021
Cdd:PRK14271 37 LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRmNDKVSgyrySGDVLLGGRSIFNyrDVLEFRRRVGMLFQrpnpfpMS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2022 AIDELLTG-REHlylyarlRGVPAEEIEKVANWSIKSLGL-TVYADCLAGT---YSGGNKRKLSTAIALIGCPPLVLLDE 2096
Cdd:PRK14271 117 IMDNVLAGvRAH-------KLVPRKEFRGVAQARLTEVGLwDAVKDRLSDSpfrLSGGQQQLLCLARTLAVNPEVLLLDE 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 105990541 2097 PTTGMDPQARRMLWNVIVSIIrEGRAVVLTSHSMEECEALCTRLAIMVKGAFRCMGTIQHLKS 2159
Cdd:PRK14271 190 PTSALDPTTTEKIEEFIRSLA-DRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFS 251
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
931-1121 |
3.55e-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: 59.15 E-value: 3.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 931 VKNLVKIFEPCGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPpTSGTVLVGGRDIET-SLDAVRQSLGMCP 1009
Cdd:TIGR01271 1220 VQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSvTLQTWRKAFGVIP 1298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1010 QHNILFHHlTVAEHMLFYAQLkgkSQEE-----AQLEMEAMLEDtgLHHKRNEEAQD----LSGGMQRKLSVAIAFVGDA 1080
Cdd:TIGR01271 1299 QKVFIFSG-TFRKNLDPYEQW---SDEEiwkvaEEVGLKSVIEQ--FPDKLDFVLVDggyvLSNGHKQLMCLARSILSKA 1372
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 105990541 1081 KVVILDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMD 1121
Cdd:TIGR01271 1373 KILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVE 1413
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1936-2146 |
3.88e-08 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 56.63 E-value: 3.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1936 DILRLHELTkIYpgTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTT----FKMLTGDTTVTSGDATVAGKSILTN----- 2006
Cdd:PRK10418 3 QQIELRNIA-LQ--AAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTcaaaLGILPAGVRQTAGRVLLDGKPVAPCalrgr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2007 -ISEVHQNmgycPQfDAIDELLTGREHLYLYARLRGVPAEEIEKVAnwSIKSLGLTvYADCLAGTY----SGGNKRKLST 2081
Cdd:PRK10418 80 kIATIMQN----PR-SAFNPLHTMHTHARETCLALGKPADDATLTA--ALEAVGLE-NAARVLKLYpfemSGGMLQRMMI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 105990541 2082 AIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKG 2146
Cdd:PRK10418 152 ALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKrALGMLLVTHDMGVVARLADDVAVMSHG 217
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
931-1143 |
3.95e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 58.71 E-value: 3.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 931 VKNLVKIFEPCGR--PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGG----RDIETSLDAVRQS 1004
Cdd:PRK10261 15 VENLNIAFMQEQQkiAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrRRSRQVIELSEQS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1005 -----------LGMCPQH-----NILFhhlTVAEHMLFYAQL-KGKSQEEAQLEMEAMLEDTglhhkRNEEAQ------- 1060
Cdd:PRK10261 95 aaqmrhvrgadMAMIFQEpmtslNPVF---TVGEQIAESIRLhQGASREEAMVEAKRMLDQV-----RIPEAQtilsryp 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1061 -DLSGGMQRKLSVAIAFVGDAKVVILDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIIAQGR 1137
Cdd:PRK10261 167 hQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIkvLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGE 246
|
....*.
gi 105990541 1138 LYCSGT 1143
Cdd:PRK10261 247 AVETGS 252
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
655-856 |
5.07e-08 |
|
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: 57.40 E-value: 5.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 655 FPIFMVLAWIYSVSMTVKSIVLEKELRLKETLKNQGVSNAVIWCTWFLdSFSIMSMSIFLLTIFIMHGRILHYSDPFILF 734
Cdd:pfam12698 164 VGLILMIIILIGAAIIAVSIVEEKESRIKERLLVSGVSPLQYWLGKIL-GDFLVGLLQLLIILLLLFGIGIPFGNLGLLL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 735 LFLLAFSTATIMLCFLLSTFFSKASLAAACSGVIYFTLYLPHILCFAWQDrMTAELKKAVSLLSPVAFGFGteylvrFEE 814
Cdd:pfam12698 243 LLFLLYGLAYIALGYLLGSLFKNSEDAQSIIGIVILLLSGFFGGLFPLED-PPSFLQWIFSIIPFFSPIDG------LLR 315
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 105990541 815 QGLGLQWSNIgnsptegdefsfLLSMQMMLLDAAVYGLLAWY 856
Cdd:pfam12698 316 LIYGDSLWEI------------APSLIILLLFAVVLLLLALL 345
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1955-2126 |
5.13e-08 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 56.76 E-value: 5.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1955 VDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTT--VTSGDATVAGKSILT-------NISEVHQNMGYCPQ------ 2019
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTggGAPRGARVTGDVTLNgeplaaiDAPRLARLRAVLPQaaqpaf 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2020 -FDAIDELLTGRehlYLYARLRGVPAEEIEKVANWSIKSLGltvyADCLAG----TYSGGNKRKLSTAIAL--------- 2085
Cdd:PRK13547 97 aFSAREIVLLGR---YPHARRAGALTHRDGEIAWQALALAG----ATALVGrdvtTLSGGELARVQFARVLaqlwpphda 169
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 105990541 2086 IGCPPLVLLDEPTTGMDPQARRMLWNVIVSIIREGRAVVLT 2126
Cdd:PRK13547 170 AQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLA 210
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
931-1138 |
5.46e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 57.82 E-value: 5.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 931 VKNLVKIfepcGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIE--TSLDAV------- 1001
Cdd:PRK10982 253 VRNLTSL----RQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINnhNANEAInhgfalv 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1002 ---RQSLGMCPQHNILFHHL--TVAEHMLFYAQLK-GKSQEEAQLEMEAMLEDTGLHHKrneEAQDLSGGMQRKLSVAIA 1075
Cdd:PRK10982 329 teeRRSTGIYAYLDIGFNSLisNIRNYKNKVGLLDnSRMKSDTQWVIDSMRVKTPGHRT---QIGSLSGGNQQKVIIGRW 405
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 105990541 1076 FVGDAKVVILDEPTSGVDPYSRRSIWDLLLKY-RSGRTIIMSTHHMDEadLLG--DRIAIIAQGRL 1138
Cdd:PRK10982 406 LLTQPEILMLDEPTRGIDVGAKFEIYQLIAELaKKDKGIIIISSEMPE--LLGitDRILVMSNGLV 469
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
955-1144 |
5.99e-08 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 56.22 E-value: 5.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 955 ENQITAFLGHNGAGKTTTLSILTGLLPPTSG---------TVL--VGGRDIETSLDAVRQ---SLGMCPQHNILFHhltv 1020
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLKPNLGkfddppdwdEILdeFRGSELQNYFTKLLEgdvKVIVKPQYVDLIP---- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1021 aehmlfyAQLKGKSQE--EAQLE---MEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTSGVDPY 1095
Cdd:cd03236 101 -------KAVKGKVGEllKKKDErgkLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIK 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 105990541 1096 SR----RSIWDLLlkyRSGRTIIMSTHHMDEADLLGDRIAIiaqgrLYcsGTP 1144
Cdd:cd03236 174 QRlnaaRLIRELA---EDDNYVLVVEHDLAVLDYLSDYIHC-----LY--GEP 216
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
956-1139 |
5.99e-08 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 53.92 E-value: 5.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 956 NQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGgrDIETSLDAVRQSLgmcpqhnilfhhltvaehmlfyaqlkgksq 1035
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYI--DGEDILEEVLDQL------------------------------ 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1036 eeaqlemeamledtgLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTSGVDPYSRRSIWDLL-------LKYR 1108
Cdd:smart00382 50 ---------------LLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEelrllllLKSE 114
|
170 180 190
....*....|....*....|....*....|.
gi 105990541 1109 SGRTIIMSTHhmDEADLLGDRIAIIAQGRLY 1139
Cdd:smart00382 115 KNLTVILTTN--DEKDLGPALLRRRFDRRIV 143
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1962-2162 |
6.51e-08 |
|
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: 55.62 E-value: 6.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISEVHQNMGYCPQ----FDAidellTGREHLyLY 2036
Cdd:cd03249 26 IPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDlNLRWLRSQIGLVSQepvlFDG-----TIAENI-RY 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2037 ARLRGVPAEEIE--KVANWS--IKSL--GLtvyaDCLAGTY----SGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQAR 2106
Cdd:cd03249 100 GKPDATDEEVEEaaKKANIHdfIMSLpdGY----DTLVGERgsqlSGGQKQRIAIARALLRNPKILLLDEATSALDAESE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 105990541 2107 RMLWNVIVSiIREGRAVVLTSHSmeeceaLCT-----RLAIMVKGAFRCMGTIQHLKSKFG 2162
Cdd:cd03249 176 KLVQEALDR-AMKGRTTIVIAHR------LSTirnadLIAVLQNGQVVEQGTHDELMAQKG 229
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1962-2125 |
7.04e-08 |
|
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: 55.88 E-value: 7.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIltnisevhqnmGYCPQFDAIDELLTGREHLYLYARLRG 2041
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV-----------SYKPQYIKADYEGTVRDLLSSITKDFY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2042 VPAEEIEKVanwsIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSIIREGR 2121
Cdd:cd03237 91 THPYFKTEI----AKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENNE 166
|
....
gi 105990541 2122 AVVL 2125
Cdd:cd03237 167 KTAF 170
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1962-2125 |
1.16e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 57.13 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKsiltnISevhqnmgYCPQFDAIDELLTgrehlyLYARLRG 2041
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELK-----IS-------YKPQYIKPDYDGT------VEDLLRS 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2042 VPA--------EEIekvanwsIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVI 2113
Cdd:PRK13409 424 ITDdlgssyykSEI-------IKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAI 496
|
170
....*....|..
gi 105990541 2114 VSIIREGRAVVL 2125
Cdd:PRK13409 497 RRIAEEREATAL 508
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
1947-2162 |
1.23e-07 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 57.04 E-value: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1947 YPGTSS-PAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISEVHQNMGYCPQfdaiD 2024
Cdd:TIGR00958 488 YPNRPDvPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQyDHHYLHRQVALVGQ----E 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2025 ELLTGR--EHLYLYArLRGVPAEEIEKVANWS-----IKSLGLTVYADC-LAGTY-SGGNKRKLSTAIALIGCPPLVLLD 2095
Cdd:TIGR00958 564 PVLFSGsvRENIAYG-LTDTPDEEIMAAAKAAnahdfIMEFPNGYDTEVgEKGSQlSGGQKQRIAIARALVRKPRVLILD 642
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 105990541 2096 EPTTGMDPQARRMLWNvivSIIREGRAVVLTSHSMEECEAlCTRLAIMVKGAFRCMGTIQHLKSKFG 2162
Cdd:TIGR00958 643 EATSALDAECEQLLQE---SRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQG 705
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
943-1136 |
1.29e-07 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 54.58 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 943 RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLP--PTSGTVLVGGRDIETSldavrqslgmcpqhnilfhhLTV 1020
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVPDNQFGRE--------------------ASL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1021 AEHMLfyaqLKGKSQEEAQLEMEAMLEDTGLHHKRNEEaqdLSGGMQRKLSVAIAFVGDAKVVILDEPTSGVDP-YSRR- 1098
Cdd:COG2401 103 IDAIG----RKGDFKDAVELLNAVGLSDAVLWLRRFKE---LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRqTAKRv 175
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 105990541 1099 -SIWDLLLKyRSGRTIIMSTHHMD-EADLLGDRIAIIAQG 1136
Cdd:COG2401 176 aRNLQKLAR-RAGITLVVATHHYDvIDDLQPDLLIFVGYG 214
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
1949-2102 |
2.05e-07 |
|
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: 56.29 E-value: 2.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1949 GTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIlTNIS--EVHQNMGYCPQFDAIdel 2026
Cdd:TIGR01193 484 GYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSL-KDIDrhTLRQFINYLPQEPYI--- 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2027 LTGR--EHLYLYARlRGVPAEEIEKVANWS-IK------SLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEP 2097
Cdd:TIGR01193 560 FSGSilENLLLGAK-ENVSQDEIWAACEIAeIKddienmPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDES 638
|
....*
gi 105990541 2098 TTGMD 2102
Cdd:TIGR01193 639 TSNLD 643
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
945-1136 |
2.19e-07 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 54.80 E-value: 2.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIETSLDAVR-QSLGMCPQ--HNILFHHLTVA 1021
Cdd:PRK15112 28 AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRsQRIRMIFQdpSTSLNPRQRIS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1022 EHMLFYAQLKGK-SQEEAQLEMEAMLEDTGLhhkRNEEA----QDLSGGMQRKLSVAIAFVGDAKVVILDEPTSGVDPYS 1096
Cdd:PRK15112 108 QILDFPLRLNTDlEPEQREKQIIETLRQVGL---LPDHAsyypHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSM 184
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 105990541 1097 RRSIWDLLLKY--RSGRTIIMSTHHMDEADLLGDRIAIIAQG 1136
Cdd:PRK15112 185 RSQLINLMLELqeKQGISYIYVTQHLGMMKHISDQVLVMHQG 226
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1955-2148 |
2.29e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 55.95 E-value: 2.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1955 VDRLCVGVRPGECFGLLGVNGAGKTTtFKM-LTGDT--TVTSGDATVAGKSIltNISEVHqnmgycpqfDAIDELLT--- 2028
Cdd:NF040905 276 VDDVSLNVRRGEIVGIAGLMGAGRTE-LAMsVFGRSygRNISGTVFKDGKEV--DVSTVS---------DAIDAGLAyvt 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2029 -GREHLYL-----------YARLRGV-------PAEEIeKVANWSIKSLGL---TVYAdcLAGTYSGGNKRKLSTAIALI 2086
Cdd:NF040905 344 eDRKGYGLnliddikrnitLANLGKVsrrgvidENEEI-KVAEEYRKKMNIktpSVFQ--KVGNLSGGNQQKVVLSKWLF 420
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 105990541 2087 GCPPLVLLDEPTTGMDPQARRMLWNVIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAF 2148
Cdd:NF040905 421 TDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMNEGRI 482
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1937-2102 |
2.31e-07 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 53.98 E-value: 2.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1937 ILRLHELTKIYPGTSSP--AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSiLTNISE----- 2009
Cdd:COG4181 8 IIELRGLTKTVGTGAGEltILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQD-LFALDEdarar 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2010 -VHQNMGYCPQ-FDAIDELlTGREHLYLYARLRGVP------AEEIEKVanwsikslGLTVYADCLAGTYSGGNKRKLST 2081
Cdd:COG4181 87 lRARHVGFVFQsFQLLPTL-TALENVMLPLELAGRRdararaRALLERV--------GLGHRLDHYPAQLSGGEQQRVAL 157
|
170 180
....*....|....*....|.
gi 105990541 2082 AIALIGCPPLVLLDEPTTGMD 2102
Cdd:COG4181 158 ARAFATEPAILFADEPTGNLD 178
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
943-1137 |
2.54e-07 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 53.38 E-value: 2.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 943 RPAVDRLNITFYENqITAFLGHNGAGKTTTLS----ILTGLLPPTSgTVLVGGRDI--ETSLDA-VRQSLGMCPQHNILF 1015
Cdd:cd03240 10 RSFHERSEIEFFSP-LTLIVGQNGAGKTTIIEalkyALTGELPPNS-KGGAHDPKLirEGEVRAqVKLAFENANGKKYTI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1016 HH-LTVAEHMLFYaqlkgkSQEEAQLEMEAMLEdtglhhkrneeaqDLSGGMQRKLSVAI------AFVGDAKVVILDEP 1088
Cdd:cd03240 88 TRsLAILENVIFC------HQGESNWPLLDMRG-------------RCSGGEKVLASLIIrlalaeTFGSNCGILALDEP 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 105990541 1089 TSGVDPYSRR-SIWDLLLKYRS--GRTIIMSTHHMDEADLLGDRIAIIAQGR 1137
Cdd:cd03240 149 TTNLDEENIEeSLAEIIEERKSqkNFQLIVITHDEELVDAADHIYRVEKDGR 200
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
929-1119 |
2.57e-07 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 52.54 E-value: 2.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 929 VCVKNLvKIFEPCGRPAVDRLNITFYENQ---ITaflGHNGAGKTTTLSILTGLLPPTSGTVlvggrdietsldavrqsl 1005
Cdd:cd03223 1 IELENL-SLATPDGRVLLKDLSFEIKPGDrllIT---GPSGTGKSSLFRALAGLWPWGSGRI------------------ 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1006 GMCPQHNILFhhltVAEHMLFYA-QLKgksqeeaqlemEAML---EDTglhhkrneeaqdLSGGMQRKLSVAIAFVGDAK 1081
Cdd:cd03223 59 GMPEGEDLLF----LPQRPYLPLgTLR-----------EQLIypwDDV------------LSGGEQQRLAFARLLLHKPK 111
|
170 180 190
....*....|....*....|....*....|....*...
gi 105990541 1082 VVILDEPTSGVDPYSRRSIWDLLLKYrsGRTIIMSTHH 1119
Cdd:cd03223 112 FVFLDEATSALDEESEDRLYQLLKEL--GITVISVGHR 147
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1938-2102 |
2.90e-07 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 54.22 E-value: 2.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1938 LRLHELTKIYpGTSSPAVDrLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNIS-EVHQNMGY 2016
Cdd:PRK10253 8 LRGEQLTLGY-GKYTVAEN-LTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASkEVARRIGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2017 CPQFDA------IDELLT-GR-EHLYLYARLRgvpaEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGC 2088
Cdd:PRK10253 86 LAQNATtpgditVQELVArGRyPHQPLFTRWR----KEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQE 161
|
170
....*....|....
gi 105990541 2089 PPLVLLDEPTTGMD 2102
Cdd:PRK10253 162 TAIMLLDEPTTWLD 175
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1938-2135 |
2.99e-07 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 53.25 E-value: 2.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1938 LRLHELTKIYPGTssPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTT---VTSGDATVAGKSILTniSEVHQ-N 2013
Cdd:COG4136 2 LSLENLTITLGGR--PLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSpafSASGEVLLNGRRLTA--LPAEQrR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2014 MGYCPQfdaiDELLTgrEHLYLYARL-----RGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGC 2088
Cdd:COG4136 78 IGILFQ----DDLLF--PHLSVGENLafalpPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAE 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 105990541 2089 PPLVLLDEPTTGMDP----QARRMLWNvivSIIREGRAVVLTSHSMEECEA 2135
Cdd:COG4136 152 PRALLLDEPFSKLDAalraQFREFVFE---QIRQRGIPALLVTHDEEDAPA 199
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1965-2139 |
3.11e-07 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 53.91 E-value: 3.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1965 GECFGLLGVNGAGKTTTFKMLTGDTTVTSGDaTVAGKSILTNISE----VHQNMGYCPQFDAIDELLTGrehlylyarLR 2040
Cdd:PRK11247 38 GQFVAVVGRSGCGKSTLLRLLAGLETPSAGE-LLAGTAPLAEAREdtrlMFQDARLLPWKKVIDNVGLG---------LK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2041 GvpaeeiekvaNW------SIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIV 2114
Cdd:PRK11247 108 G----------QWrdaalqALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIE 177
|
170 180
....*....|....*....|....*.
gi 105990541 2115 SIIRE-GRAVVLTSHSMEECEALCTR 2139
Cdd:PRK11247 178 SLWQQhGFTVLLVTHDVSEAVAMADR 203
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
949-1120 |
3.17e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 56.19 E-value: 3.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGG----RDIetSLDAVRQSLGMCPQHNILF--------- 1015
Cdd:PTZ00265 404 LNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDshnlKDI--NLKWWRSKIGVVSQDPLLFsnsiknnik 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1016 ---HHLTVAEHMLFYAQLKGKSQEEAQ---------------LEMEAMLEDTGLHHKRNEE------------------- 1058
Cdd:PTZ00265 482 yslYSLKDLEALSNYYNEDGNDSQENKnkrnscrakcagdlnDMSNTTDSNELIEMRKNYQtikdsevvdvskkvlihdf 561
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 105990541 1059 ---------------AQDLSGGMQRKLSVAIAFVGDAKVVILDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHM 1120
Cdd:PTZ00265 562 vsalpdkyetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTInnLKGNENRITIIIAHRL 640
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
945-1137 |
3.92e-07 |
|
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: 55.08 E-value: 3.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 945 AVDRLNITFYENQITAFLGHNGAGKTTT-LSILtGLLPpTSGTVLVGGRDIET----SLDAVRQSLGMC---------PQ 1010
Cdd:COG4172 301 AVDGVSLTLRRGETLGLVGESGSGKSTLgLALL-RLIP-SEGEIRFDGQDLDGlsrrALRPLRRRMQVVfqdpfgslsPR 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1011 HNILfhhLTVAEHMLFYA-QLKGKSQEEAqleMEAMLEDTGLhhkrNEEAQD-----LSGGmQR-KLSVAIAFVGDAKVV 1083
Cdd:COG4172 379 MTVG---QIIAEGLRVHGpGLSAAERRAR---VAEALEEVGL----DPAARHrypheFSGG-QRqRIAIARALILEPKLL 447
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 105990541 1084 ILDEPTSGVDpysrRS----IWDLL--LKYRSGRTIIMSTHhmdeaDL-----LGDRIAIIAQGR 1137
Cdd:COG4172 448 VLDEPTSALD----VSvqaqILDLLrdLQREHGLAYLFISH-----DLavvraLAHRVMVMKDGK 503
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1962-2130 |
3.92e-07 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 53.58 E-value: 3.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGdatvagksilTNISEVHQNMGYCPQ---FDAIDELLTGRehlylYAR 2038
Cdd:PRK09544 27 LKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEG----------VIKRNGKLRIGYVPQklyLDTTLPLTVNR-----FLR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2039 LR-GVPAEEIEKVanwsIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSII 2117
Cdd:PRK09544 92 LRpGTKKEDILPA----LKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLR 167
|
170
....*....|....
gi 105990541 2118 RE-GRAVVLTSHSM 2130
Cdd:PRK09544 168 RElDCAVLMVSHDL 181
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
947-1118 |
4.91e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 55.62 E-value: 4.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 947 DRLNI------TFYENQITAFLGHNGAGKTTTLSILTGllpPTSGTVLVGgrDIETSLDAVRQSL-----GMCPQHNILF 1015
Cdd:PLN03140 891 DRLQLlrevtgAFRPGVLTALMGVSGAGKTTLMDVLAG---RKTGGYIEG--DIRISGFPKKQETfarisGYCEQNDIHS 965
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1016 HHLTVAEHMLFYAQL---KGKSQEEAQLEMEAMLEDTGLHHKRNE-----EAQDLSGGMQRKLSVAIAFVGDAKVVILDE 1087
Cdd:PLN03140 966 PQVTVRESLIYSAFLrlpKEVSKEEKMMFVDEVMELVELDNLKDAivglpGVTGLSTEQRKRLTIAVELVANPSIIFMDE 1045
|
170 180 190
....*....|....*....|....*....|....*
gi 105990541 1088 PTSGVDPysrRSIWDLLLKYR----SGRTIIMSTH 1118
Cdd:PLN03140 1046 PTSGLDA---RAAAIVMRTVRntvdTGRTVVCTIH 1077
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
963-1094 |
5.20e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 52.54 E-value: 5.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 963 GHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIETSlDAVR--QSLGMCPQhniLFHHLTVAEHMLFYAQLKGKsqeEAQL 1040
Cdd:PRK13543 44 GDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRG-DRSRfmAYLGHLPG---LKADLSTLENLHFLCGLHGR---RAKQ 116
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 105990541 1041 EMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTSGVDP 1094
Cdd:PRK13543 117 MPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1948-2146 |
5.59e-07 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 52.47 E-value: 5.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1948 PGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKsiltnisevhqnMGYCPQFDAIdelL 2027
Cdd:cd03250 14 EQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------IAYVSQEPWI---Q 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2028 TG--REHLylyarLRGVP--AEEIEKVanwsIKSLGLTVYADCLAG-----------TYSGGNKRKLSTAIALIGCPPLV 2092
Cdd:cd03250 79 NGtiRENI-----LFGKPfdEERYEKV----IKACALEPDLEILPDgdlteigekgiNLSGGQKQRISLARAVYSDADIY 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 105990541 2093 LLDEPTTGMDPQARRMLW-NVIVSIIREGRAVVLTSHSMEECEAlCTRLAIMVKG 2146
Cdd:cd03250 150 LLDDPLSAVDAHVGRHIFeNCILGLLLNNKTRILVTHQLQLLPH-ADQIVVLDNG 203
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1938-2146 |
9.05e-07 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 52.28 E-value: 9.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1938 LRLHELTKIYPGTSSpavdRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGK------------SIL- 2004
Cdd:PRK10771 2 LKLTDITWLYHHLPM----RFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQdhtttppsrrpvSMLf 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2005 --TNISE---VHQNMGYcpqfdAIDELLtgrehlylyaRLRGVPAEEIEKVAnwsiKSLGLTVYADCLAGTYSGGNKRKL 2079
Cdd:PRK10771 78 qeNNLFShltVAQNIGL-----GLNPGL----------KLNAAQREKLHAIA----RQMGIEDLLARLPGQLSGGQRQRV 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 105990541 2080 STAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSIIREGRAVVL-TSHSMEECEALCTRLAIMVKG 2146
Cdd:PRK10771 139 ALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQERQLTLLmVSHSLEDAARIAPRSLVVADG 206
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1955-2149 |
9.13e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 54.16 E-value: 9.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1955 VDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGD-TTVTSGDATVAGKSILTNISE--VHQNMGYCPQ---FDAIDELLT 2028
Cdd:PRK13549 278 VDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAyPGRWEGEIFIDGKPVKIRNPQqaIAQGIAMVPEdrkRDGIVPVMG 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2029 GREHLYL-----YARLRGVPAEEIEKVANWSIKSLGLTVYADCLA-GTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMD 2102
Cdd:PRK13549 358 VGKNITLaaldrFTGGSRIDDAAELKTILESIQRLKVKTASPELAiARLSGGNQQKAVLAKCLLLNPKILILDEPTRGID 437
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 105990541 2103 PQARRMLWNVIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFR 2149
Cdd:PRK13549 438 VGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKLK 484
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1965-2131 |
1.05e-06 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 52.28 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1965 GECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKsiltNISEVHQNMGYCPQFDAID-ELLTGR-----EHLYLYAR 2038
Cdd:PRK10619 31 GDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQ----TINLVRDKDGQLKVADKNQlRLLRTRltmvfQHFNLWSH 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2039 LrgvpaEEIEKVANWSIKSLGLT---------VYADCLA------GTY----SGGNKRKLSTAIALIGCPPLVLLDEPTT 2099
Cdd:PRK10619 107 M-----TVLENVMEAPIQVLGLSkqeareravKYLAKVGideraqGKYpvhlSGGQQQRVSIARALAMEPEVLLFDEPTS 181
|
170 180 190
....*....|....*....|....*....|..
gi 105990541 2100 GMDPQARRMLWNVIVSIIREGRAVVLTSHSME 2131
Cdd:PRK10619 182 ALDPELVGEVLRIMQQLAEEGKTMVVVTHEMG 213
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
891-1119 |
1.08e-06 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 54.04 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 891 ERALEKTEPLTEETEDPEHPEGihdsfferehpgwvPGVCVKNLvKIFEPCGRPAVDRLNITFYENQ---ITaflGHNGA 967
Cdd:COG4178 339 EEALEAADALPEAASRIETSED--------------GALALEDL-TLRTPDGRPLLEDLSLSLKPGErllIT---GPSGS 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 968 GKTTTLSILTGLLPPTSGTVLvggrdietsldavrqslgmCPQHnilfhhltvaEHMLFYAQ--------LK------GK 1033
Cdd:COG4178 401 GKSTLLRAIAGLWPYGSGRIA-------------------RPAG----------ARVLFLPQrpylplgtLReallypAT 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1034 SQEEAQLEMEAMLEDTGLHH--KRNEEAQD----LSGGMQRKLSVAIAFVGDAKVVILDEPTSGVDPYSRRSIWDLLLKY 1107
Cdd:COG4178 452 AEAFSDAELREALEAVGLGHlaERLDEEADwdqvLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREE 531
|
250
....*....|..
gi 105990541 1108 RSGRTIIMSTHH 1119
Cdd:COG4178 532 LPGTTVISVGHR 543
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1965-2155 |
1.08e-06 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 53.16 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1965 GECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKsiltNISEVH---QNMGYCPQFDAIDELLTGREH----LYLYA 2037
Cdd:PRK10851 28 GQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGT----DVSRLHardRKVGFVFQHYALFRHMTVFDNiafgLTVLP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2038 RLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSII 2117
Cdd:PRK10851 104 RRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLH 183
|
170 180 190
....*....|....*....|....*....|....*....
gi 105990541 2118 REGR-AVVLTSHSMEECEALCTRLAIMVKGAFRCMGTIQ 2155
Cdd:PRK10851 184 EELKfTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPD 222
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1964-2102 |
1.13e-06 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 52.48 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1964 PGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISEVH-QNMGYCPQFDAIDELLTGREHLYL-----YA 2037
Cdd:PRK10575 36 AGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFaRKVAYLPQQLPAAEGMTVRELVAIgrypwHG 115
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 105990541 2038 RLRGVPAEEIEKVANwSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMD 2102
Cdd:PRK10575 116 ALGRFGAADREKVEE-AISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALD 179
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1962-2125 |
1.69e-06 |
|
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: 53.25 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKsiltnISevhqnmgYCPQFDAIDELLTGREHlylyarLRG 2041
Cdd:COG1245 363 IREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLK-----IS-------YKPQYISPDYDGTVEEF------LRS 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2042 VPAEEIEkvANWS----IKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSII 2117
Cdd:COG1245 425 ANTDDFG--SSYYkteiIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFA 502
|
....*...
gi 105990541 2118 REGRAVVL 2125
Cdd:COG1245 503 ENRGKTAM 510
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
942-1120 |
1.75e-06 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 51.18 E-value: 1.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 942 GRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTV-----LVGGRDIETSLDAVRQSLGMCPQHNILFH 1016
Cdd:cd03290 13 GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnkNESEPSFEATRSRNRYSVAYAAQKPWLLN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1017 hLTVAEHMLF---YAQLKGKSQEEA-QLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTSGV 1092
Cdd:cd03290 93 -ATVEENITFgspFNKQRYKAVTDAcSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSAL 171
|
170 180 190
....*....|....*....|....*....|.
gi 105990541 1093 DPY-SRRSIWDLLLKY--RSGRTIIMSTHHM 1120
Cdd:cd03290 172 DIHlSDHLMQEGILKFlqDDKRTLVLVTHKL 202
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1970-2188 |
1.83e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 51.93 E-value: 1.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1970 LLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISEVHQ------NMGYCPQF-------DAID-ELLTGREHLyl 2035
Cdd:PRK13645 42 VIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKIKEvkrlrkEIGLVFQFpeyqlfqETIEkDIAFGPVNL-- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2036 yarlrGVPAEEIEKVANWSIKSLGLTV-YADCLAGTYSGGNKRKLSTA--IALIGcpPLVLLDEPTTGMDPQARRMLWNV 2112
Cdd:PRK13645 120 -----GENKQEAYKKVPELLKLVQLPEdYVKRSPFELSGGQKRRVALAgiIAMDG--NTLVLDEPTGGLDPKGEEDFINL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2113 IVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFRCMGTI------QHLKSKFG----DGYIVTMKIKSPKDDLL-P 2180
Cdd:PRK13645 193 FERLNKEyKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPfeifsnQELLTKIEidppKLYQLMYKLKNKGIDLLnK 272
|
....*...
gi 105990541 2181 DLNPVEQF 2188
Cdd:PRK13645 273 NIRTIEEF 280
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
907-1093 |
2.00e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 53.59 E-value: 2.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 907 PEHPEGIHDSffeREHPGWvP---GVCVKNLVKIFEPCGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPT 983
Cdd:PLN03130 1217 SEAPLVIENN---RPPPGW-PssgSIKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELE 1292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 984 SGTVLVGGRDIET-SLDAVRQSLGMCPQHNILFHHlTVAEHMLFYAQLKGKSQEEAqLEmEAMLEDT------GLHHKRN 1056
Cdd:PLN03130 1293 RGRILIDGCDISKfGLMDLRKVLGIIPQAPVLFSG-TVRFNLDPFNEHNDADLWES-LE-RAHLKDVirrnslGLDAEVS 1369
|
170 180 190
....*....|....*....|....*....|....*..
gi 105990541 1057 EEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTSGVD 1093
Cdd:PLN03130 1370 EAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVD 1406
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1947-2113 |
2.00e-06 |
|
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: 50.96 E-value: 2.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1947 YPGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTT----FKMLTgdttVTSGDATVAGKSILT-NISEVHQNMGYCPQfD 2021
Cdd:cd03244 12 YRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLllalFRLVE----LSSGSILIDGVDISKiGLHDLRSRISIIPQ-D 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2022 AIdeLLTG--REHL-----YLYARLRGVpaeeIEKVANWS-IKSLGLTVYADCLAG--TYSGGNKRKLSTAIALIGCPPL 2091
Cdd:cd03244 87 PV--LFSGtiRSNLdpfgeYSDEELWQA----LERVGLKEfVESLPGGLDTVVEEGgeNLSVGQRQLLCLARALLRKSKI 160
|
170 180
....*....|....*....|..
gi 105990541 2092 VLLDEPTTGMDPQARRMLWNVI 2113
Cdd:cd03244 161 LVLDEATASVDPETDALIQKTI 182
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
931-1134 |
2.02e-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: 53.02 E-value: 2.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 931 VKNLVKIFEpcGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGgrdiET-SLDAVRQSL-GMC 1008
Cdd:TIGR03719 325 AENLTKAFG--DKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIG----ETvKLAYVDQSRdALD 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1009 PQHNIL------FHHLTVAEHML--------FyaQLKGKSQEeaqlemeamledtglhhKRneeAQDLSGGMQRKLSVAI 1074
Cdd:TIGR03719 399 PNKTVWeeisggLDIIKLGKREIpsrayvgrF--NFKGSDQQ-----------------KK---VGQLSGGERNRVHLAK 456
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 105990541 1075 AFVGDAKVVILDEPTSGVDPYSRRSIWDLLLKYrSGRTIIMStHhmDEADLlgDRIA--IIA 1134
Cdd:TIGR03719 457 TLKSGGNVLLLDEPTNDLDVETLRALEEALLNF-AGCAVVIS-H--DRWFL--DRIAthILA 512
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1934-2146 |
2.20e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 52.81 E-value: 2.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1934 KTDILRLHELTKIypgtSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISEVHQN 2013
Cdd:PRK10982 247 GEVILEVRNLTSL----RQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAIN 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2014 MGYCpqfdaideLLTG-REHLYLYARL------------------RGVPAEEIEKVANWSIKSLGL-TVYADCLAGTYSG 2073
Cdd:PRK10982 323 HGFA--------LVTEeRRSTGIYAYLdigfnslisnirnyknkvGLLDNSRMKSDTQWVIDSMRVkTPGHRTQIGSLSG 394
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 105990541 2074 GNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
Cdd:PRK10982 395 GNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNG 467
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
931-1138 |
2.81e-06 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 51.39 E-value: 2.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 931 VKNLVKIFEPCGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLpPTSGTVLVGGRDIET-SLDAVRQSLGMCP 1009
Cdd:cd03289 5 VKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLL-NTEGDIQIDGVSWNSvPLQKWRKAFGVIP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1010 QHNILFHHlTVAEHMLFYAQLKG----KSQEEAQL---------EMEAMLEDTGLHhkrneeaqdLSGGMQRKLSVAIAF 1076
Cdd:cd03289 84 QKVFIFSG-TFRKNLDPYGKWSDeeiwKVAEEVGLksvieqfpgQLDFVLVDGGCV---------LSHGHKQLMCLARSV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 105990541 1077 VGDAKVVILDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMdEADLLGDRIAIIAQGRL 1138
Cdd:cd03289 154 LSKAKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRI-EAMLECQRFLVIEENKV 214
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1934-2107 |
2.99e-06 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 51.64 E-value: 2.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1934 KTDILRLHELTKIYpGTSSpAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIlTNISEvhQN 2013
Cdd:PRK11432 3 QKNFVVLKNITKRF-GSNT-VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDV-THRSI--QQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2014 MGYCPQFDAIDELltgrEHLYLYA------RLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIG 2087
Cdd:PRK11432 78 RDICMVFQSYALF----PHMSLGEnvgyglKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALIL 153
|
170 180
....*....|....*....|
gi 105990541 2088 CPPLVLLDEPTTGMDPQARR 2107
Cdd:PRK11432 154 KPKVLLFDEPLSNLDANLRR 173
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
944-1093 |
3.51e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 52.26 E-value: 3.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 944 PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGG------------RDIE-TSLDAVRQSLGMCPQ 1010
Cdd:PRK11147 17 PLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQdlivarlqqdppRNVEgTVYDFVAEGIEEQAE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1011 HNILFHHLTV------AEHMLfyAQLkGKSQEEA------QLE--MEAMLEDTGLhhkrNEEAQ--DLSGGMQRKLSVAI 1074
Cdd:PRK11147 97 YLKRYHDISHlvetdpSEKNL--NEL-AKLQEQLdhhnlwQLEnrINEVLAQLGL----DPDAAlsSLSGGWLRKAALGR 169
|
170
....*....|....*....
gi 105990541 1075 AFVGDAKVVILDEPTSGVD 1093
Cdd:PRK11147 170 ALVSNPDVLLLDEPTNHLD 188
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1968-2167 |
5.57e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 50.43 E-value: 5.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1968 FGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIL-------TNISEVHQNMGYCPQFDAIDELLTGREHLYLYARLR 2040
Cdd:PRK14246 39 FGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYfgkdifqIDAIKLRKEVGMVFQQPNPFPHLSIYDNIAYPLKSH 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2041 GVPAE-EIEKVANWSIKSLGL--TVY--ADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVS 2115
Cdd:PRK14246 119 GIKEKrEIKKIVEECLRKVGLwkEVYdrLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITE 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 105990541 2116 IIREgRAVVLTSHSMEECEALCTRLAIMVKGAFRCMGTIQHL----KSKFGDGYIV 2167
Cdd:PRK14246 199 LKNE-IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIftspKNELTEKYVI 253
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1962-2105 |
9.37e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 50.94 E-value: 9.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILtniSEVHQNMgycPQFD--AIDELLTG-REHLYLYAR 2038
Cdd:PRK10636 24 INPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQL---AWVNQET---PALPqpALEYVIDGdREYRQLEAQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2039 LRGVPAE-----------EIEKVANWSIKSL------GLTVYADCL---AGTYSGGNKRKLSTAIALIGCPPLVLLDEPT 2098
Cdd:PRK10636 98 LHDANERndghaiatihgKLDAIDAWTIRSRaasllhGLGFSNEQLerpVSDFSGGWRMRLNLAQALICRSDLLLLDEPT 177
|
....*..
gi 105990541 2099 TGMDPQA 2105
Cdd:PRK10636 178 NHLDLDA 184
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1932-2128 |
1.09e-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: 50.70 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1932 GNKtdILRLHELTKIYpgTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVaGKSIltnisevh 2011
Cdd:TIGR03719 319 GDK--VIEAENLTKAF--GDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV-------- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2012 qNMGYCPQF-DAID-------ELLTGREHLylyarlrgvpaeeieKVANWSIKSlgltvYADC------------LAGTY 2071
Cdd:TIGR03719 386 -KLAYVDQSrDALDpnktvweEISGGLDII---------------KLGKREIPS-----RAYVgrfnfkgsdqqkKVGQL 444
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 105990541 2072 SGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSIirEGRAVVLtSH 2128
Cdd:TIGR03719 445 SGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNF--AGCAVVI-SH 498
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1938-2161 |
1.14e-05 |
|
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: 50.57 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1938 LRLHELTKIYPGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGdttvTSGDATVAGKSILtnisevhqNMGYC 2017
Cdd:TIGR03269 1 IEVKNLTKKFDGKE--VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRG----MDQYEPTSGRIIY--------HVALC 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2018 PQ---------------------------FDAIDELLTGR----------EHLYLYARLR------------GVPAEEIE 2048
Cdd:TIGR03269 67 EKcgyverpskvgepcpvcggtlepeevdFWNLSDKLRRRirkriaimlqRTFALYGDDTvldnvlealeeiGYEGKEAV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2049 KVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVS-IIREGRAVVLTS 2127
Cdd:TIGR03269 147 GRAVDLIEMVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEaVKASGISMVLTS 226
|
250 260 270
....*....|....*....|....*....|....
gi 105990541 2128 HSMEECEALCTRLAIMVKGAFRCMGTIQHLKSKF 2161
Cdd:TIGR03269 227 HWPEVIEDLSDKAIWLENGEIKEEGTPDEVVAVF 260
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
957-1093 |
1.14e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 50.88 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 957 QITAFLGHNGAGKTTTLSILT----GLLPPTSGTVLVGGRDIETSLDAVRQSLGMCPQHNILFHHLTVAEHMLFYAQLK- 1031
Cdd:TIGR00956 88 ELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGITPEEIKKHYRGDVVYNAETDVHFPHLTVGETLDFAARCKt 167
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 105990541 1032 ------GKSQEE-AQLEMEAMLEDTGLHHKRNEEAQD-----LSGGMQRKLSVAIAFVGDAKVVILDEPTSGVD 1093
Cdd:TIGR00956 168 pqnrpdGVSREEyAKHIADVYMATYGLSHTRNTKVGNdfvrgVSGGERKRVSIAEASLGGAKIQCWDNATRGLD 241
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
931-1118 |
1.40e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 50.28 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 931 VKNLVKIFEpcGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVlvggrdiETSLDAvrqSLGMCPQ 1010
Cdd:PRK15064 322 VENLTKGFD--NGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV-------KWSENA---NIGYYAQ 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1011 -HNILFHH-LTVAEHMLFYAQLKGKSQEeaqleMEAML-------EDTglhhkrNEEAQDLSGGMQRKLSVAIAFVGDAK 1081
Cdd:PRK15064 390 dHAYDFENdLTLFDWMSQWRQEGDDEQA-----VRGTLgrllfsqDDI------KKSVKVLSGGEKGRMLFGKLMMQKPN 458
|
170 180 190
....*....|....*....|....*....|....*..
gi 105990541 1082 VVILDEPTSGVDPYSRRSIWDLLLKYRSgrTIIMSTH 1118
Cdd:PRK15064 459 VLVMDEPTNHMDMESIESLNMALEKYEG--TLIFVSH 493
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1965-2132 |
1.98e-05 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 48.61 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1965 GECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI----LTNISEVHQNMGYCPQFDAIDELLTG--------REH 2032
Cdd:PRK11831 33 GKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamsRSRLYTVRKRMSMLFQSGALFTDMNVfdnvayplREH 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2033 LYLyarlrgvPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRK--LSTAIALIgcPPLVLLDEPTTGMDPqarrMLW 2110
Cdd:PRK11831 113 TQL-------PAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRaaLARAIALE--PDLIMFDEPFVGQDP----ITM 179
|
170 180
....*....|....*....|....*..
gi 105990541 2111 NVIVSIIRE-----GRAVVLTSHSMEE 2132
Cdd:PRK11831 180 GVLVKLISElnsalGVTCVVVSHDVPE 206
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
1947-2107 |
3.19e-05 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 49.25 E-value: 3.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1947 YPGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAG--------KSILTNISEVHQNMgycp 2018
Cdd:PRK11176 351 YPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGhdlrdytlASLRNQVALVSQNV---- 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2019 qfdaidelltgreHLY--------LYARLRGVPAEEIEKVANWS-----IKSL--GLtvyaDCLAG----TYSGGNKRKL 2079
Cdd:PRK11176 427 -------------HLFndtianniAYARTEQYSREQIEEAARMAyamdfINKMdnGL----DTVIGengvLLSGGQRQRI 489
|
170 180
....*....|....*....|....*...
gi 105990541 2080 STAIALIGCPPLVLLDEPTTGMDPQARR 2107
Cdd:PRK11176 490 AIARALLRDSPILILDEATSALDTESER 517
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
2072-2131 |
3.25e-05 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 48.15 E-value: 3.25e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 105990541 2072 SGGNKRKLSTAIALIGCPP---LVLLDEPTTGMDPQARRMLWNVIVSIIREGRAVVLTSHSME 2131
Cdd:pfam13304 238 SDGTKRLLALLAALLSALPkggLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTHSPL 300
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1965-2128 |
3.57e-05 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 48.81 E-value: 3.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1965 GECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI-LTNISEvhqnmgYCPQFDAI-------DELLTGrehlyly 2036
Cdd:PRK10522 349 GELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVtAEQPED------YRKLFSAVftdfhlfDQLLGP------- 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2037 arlRGVPAEEiEKVANWsIKSLG----LTVYADCLAGT-YSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWN 2111
Cdd:PRK10522 416 ---EGKPANP-ALVEKW-LERLKmahkLELEDGRISNLkLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQ 490
|
170
....*....|....*...
gi 105990541 2112 VIVSIIRE-GRAVVLTSH 2128
Cdd:PRK10522 491 VLLPLLQEmGKTIFAISH 508
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
947-1118 |
3.62e-05 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 46.20 E-value: 3.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 947 DRLNITFYENQITAFLGHNGAGKTTTL-SILtgllpptsgtVLVGGRdietSLDAVRQSLGMCPQhnilfhhltvaehml 1025
Cdd:cd03227 12 VPNDVTFGEGSLTIITGPNGSGKSTILdAIG----------LALGGA----QSATRRRSGVKAGC--------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1026 fyaqlkgksqEEAQLEMEAMLEDTGLhhkrneeaqdlSGGMQRKLSVAIAF----VGDAKVVILDEPTSGVDPYSRRSIW 1101
Cdd:cd03227 63 ----------IVAAVSAELIFTRLQL-----------SGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALA 121
|
170
....*....|....*...
gi 105990541 1102 DLLLKYR-SGRTIIMSTH 1118
Cdd:cd03227 122 EAILEHLvKGAQVIVITH 139
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
1980-2128 |
3.69e-05 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 46.20 E-value: 3.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1980 TTFKMLTGDTTvtsgdatvAGKSILtnisevhqnmgycpqFDAIdELLTGREHLYLYARLRGVPAEEIEKVanwsikSLG 2059
Cdd:cd03227 21 GSLTIITGPNG--------SGKSTI---------------LDAI-GLALGGAQSATRRRSGVKAGCIVAAV------SAE 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 105990541 2060 LTVYADCLagtySGGNKRKLSTAIALIGCP----PLVLLDEPTTGMDPQARRMLWNVIVSIIREGRAVVLTSH 2128
Cdd:cd03227 71 LIFTRLQL----SGGEKELSALALILALASlkprPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITH 139
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1935-2128 |
4.00e-05 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 48.95 E-value: 4.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1935 TDILRLHELTKIYP-GTSSPAV-DRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISEV-- 2010
Cdd:PRK10535 2 TALLELKDIRRSYPsGEEQVEVlKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADAla 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2011 ---HQNMGYCPQFDAIDELLTGREHLYLYARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIG 2087
Cdd:PRK10535 82 qlrREHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMN 161
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 105990541 2088 CPPLVLLDEPTTGMDPQARRMLWNVIVSIIREGRAVVLTSH 2128
Cdd:PRK10535 162 GGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTH 202
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
2068-2129 |
6.12e-05 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 45.78 E-value: 6.12e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 105990541 2068 AGTYSGGNKRKLSTAIALIGCPP--LVLLDEPTTGMDPQARRMLWNVIVSIIREGRAVVLTSHS 2129
Cdd:cd03238 85 LSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHN 148
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
943-1093 |
6.56e-05 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 48.40 E-value: 6.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 943 RPAVD----RLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDI-ETSLDAVRQSLGMCPQHNILFHH 1017
Cdd:TIGR00957 1295 REDLDlvlrHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIaKIGLHDLRFKITIIPQDPVLFSG 1374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1018 lTVAEHMLFYAQLkgkSQEEAQLEME-AMLED------TGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTS 1090
Cdd:TIGR00957 1375 -SLRMNLDPFSQY---SDEEVWWALElAHLKTfvsalpDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATA 1450
|
...
gi 105990541 1091 GVD 1093
Cdd:TIGR00957 1451 AVD 1453
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
960-1093 |
7.90e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 47.27 E-value: 7.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 960 AFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDI----ETSLDAVRQSLGMC---------PQHNILFhhlTVAEHMLF 1026
Cdd:PRK11308 45 AVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLlkadPEAQKLLRQKIQIVfqnpygslnPRKKVGQ---ILEEPLLI 121
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 105990541 1027 YAQLkgkSQEEAQLEMEAMLEDTGLhhkRNEEAQD----LSGGMQRKLSVAIAFVGDAKVVILDEPTSGVD 1093
Cdd:PRK11308 122 NTSL---SAAERREKALAMMAKVGL---RPEHYDRyphmFSGGQRQRIAIARALMLDPDVVVADEPVSALD 186
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
1972-2128 |
1.63e-04 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 44.91 E-value: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1972 GVNGAGKTTTF---KM-LTGDTTVTS----GDATVAGKSilTNISEVHQNMgycpqfdaidELLTGREHLYL--YARLRG 2041
Cdd:cd03240 29 GQNGAGKTTIIealKYaLTGELPPNSkggaHDPKLIREG--EVRAQVKLAF----------ENANGKKYTITrsLAILEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2042 V---PAEEIEKVANWSIKSLgltvyadclagtySGGNKRKLSTAIAL-------IGCPPLVLlDEPTTGMDPQARRmlwN 2111
Cdd:cd03240 97 VifcHQGESNWPLLDMRGRC-------------SGGEKVLASLIIRLalaetfgSNCGILAL-DEPTTNLDEENIE---E 159
|
170 180
....*....|....*....|..
gi 105990541 2112 VIVSIIRE-----GRAVVLTSH 2128
Cdd:cd03240 160 SLAEIIEErksqkNFQLIVITH 181
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1057-1138 |
1.79e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 46.71 E-value: 1.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1057 EEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTSGVD---PYSRRSIWDLLLKyrSGRTIIMSTHHMDEadLLG--DRIA 1131
Cdd:NF040905 400 QKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDvgaKYEIYTIINELAA--EGKGVIVISSELPE--LLGmcDRIY 475
|
....*..
gi 105990541 1132 IIAQGRL 1138
Cdd:NF040905 476 VMNEGRI 482
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1970-2105 |
1.89e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.78 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1970 LLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISEVHqnmgycpqFDAIDelLTGREHLYLYARLRGVPAEEIEK 2049
Cdd:PLN03073 540 MVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMAVFSQHH--------VDGLD--LSSNPLLYMMRCFPGVPEQKLRA 609
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 105990541 2050 vanwSIKSLGLT-------VYadclagTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQA 2105
Cdd:PLN03073 610 ----HLGSFGVTgnlalqpMY------TLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDA 662
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1937-2146 |
2.47e-04 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 45.15 E-value: 2.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1937 ILRLHELTKIYpgTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLT--GD---TTVTSGDATVAGKSIltnisevh 2011
Cdd:PRK14239 5 ILQVSDLSVYY--NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDlnpEVTITGSIVYNGHNI-------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2012 qnmgYCPQFDAID---EL-----------LTGREHLYLYARLRGVPAEEI-EKVANWSIKslGLTVY---ADCL---AGT 2070
Cdd:PRK14239 75 ----YSPRTDTVDlrkEIgmvfqqpnpfpMSIYENVVYGLRLKGIKDKQVlDEAVEKSLK--GASIWdevKDRLhdsALG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 105990541 2071 YSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSiIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
Cdd:PRK14239 149 LSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLG-LKDDYTMLLVTRSMQQASRISDRTGFFLDG 223
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1938-2102 |
2.58e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 46.04 E-value: 2.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1938 LRLHELTKIYPGTssPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSiltnisevhqNMGYC 2017
Cdd:PRK15064 320 LEVENLTKGFDNG--PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENA----------NIGYY 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2018 PQ-----FDaIDELLTgrEHLYLYAR-------LRGV------PAEEIEKvanwSIKSLgltvyadclagtySGGNKRKL 2079
Cdd:PRK15064 388 AQdhaydFE-NDLTLF--DWMSQWRQegddeqaVRGTlgrllfSQDDIKK----SVKVL-------------SGGEKGRM 447
|
170 180
....*....|....*....|...
gi 105990541 2080 STAIALIGCPPLVLLDEPTTGMD 2102
Cdd:PRK15064 448 LFGKLMMQKPNVLVMDEPTNHMD 470
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
984-1120 |
2.83e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 46.56 E-value: 2.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 984 SGTVLVGGRDI-ETSLDAVRQSLGMCPQHNILFHhLTVAEHMLFyaqlkgkSQEEAQLE----------MEAMLEDTGLH 1052
Cdd:PTZ00265 1276 SGKILLDGVDIcDYNLKDLRNLFSIVSQEPMLFN-MSIYENIKF-------GKEDATREdvkrackfaaIDEFIESLPNK 1347
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 105990541 1053 HKRN--EEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHM 1120
Cdd:PTZ00265 1348 YDTNvgPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIvdIKDKADKTIITIAHRI 1419
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2072-2132 |
3.37e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 44.64 E-value: 3.37e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 105990541 2072 SGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSI-IREGRAVVLTSHSMEE 2132
Cdd:PRK14258 152 SGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLrLRSELTMVIVSHNLHQ 213
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
931-1004 |
3.55e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 45.49 E-value: 3.55e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 105990541 931 VKNLVKIFEpcGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGgrdiET-SLDAVRQS 1004
Cdd:PRK11819 327 AENLSKSFG--DRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIG----ETvKLAYVDQS 395
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
950-1122 |
4.01e-04 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 45.65 E-value: 4.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 950 NITFY--ENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVlvggrDIETSLDAVRQSLGMCPQhnilfhhLTVAEHMLFY 1027
Cdd:PRK13545 42 NISFEvpEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV-----DIKGSAALIAISSGLNGQ-------LTGIENIELK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1028 AQLKGKSQEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTSGVDPYSRRSIWDLLLKY 1107
Cdd:PRK13545 110 GLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNEF 189
|
170
....*....|....*.
gi 105990541 1108 R-SGRTIIMSTHHMDE 1122
Cdd:PRK13545 190 KeQGKTIFFISHSLSQ 205
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1964-2102 |
4.04e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 45.49 E-value: 4.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1964 PGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVaGKSIltnisevhqNMGYCPQF-DAID-------ELLTGREHLyl 2035
Cdd:PRK11819 349 PGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV---------KLAYVDQSrDALDpnktvweEISGGLDII-- 416
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 105990541 2036 yarlrgvpaeeieKVANWSIKSlgltvYADC------------LAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMD 2102
Cdd:PRK11819 417 -------------KVGNREIPS-----RAYVgrfnfkggdqqkKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLD 477
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1943-2199 |
4.21e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 45.87 E-value: 4.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1943 LTKIYPGTSSPAVDRL--CVGV-RPGECFGLLGVNGAGKTTTFKMLTGDT--TVTSGDATVAGKSILTNISEVH--QNMG 2015
Cdd:TIGR00956 62 FRKLKKFRDTKTFDILkpMDGLiKPGELTVVLGRPGSGCSTLLKTIASNTdgFHIGVEGVITYDGITPEEIKKHyrGDVV 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2016 YCPQFDAIDELLTGREHLYLYARLR-------GVPAEE-IEKVANWSIKSLGLTVYADCLAGT-----YSGGNKRKLSTA 2082
Cdd:TIGR00956 142 YNAETDVHFPHLTVGETLDFAARCKtpqnrpdGVSREEyAKHIADVYMATYGLSHTRNTKVGNdfvrgVSGGERKRVSIA 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2083 IALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSIIREGRAVVLTS--HSMEECEALCTRLAIMVKGAFRCMGTIQHLKSk 2160
Cdd:TIGR00956 222 EASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVAiyQCSQDAYELFDKVIVLYEGYQIYFGPADKAKQ- 300
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 105990541 2161 fgdgYIVTMKIKSPKDDLLPDL-----NPVEQFFQGNFPGSVQR 2199
Cdd:TIGR00956 301 ----YFEKMGFKCPDRQTTADFltsltSPAERQIKPGYEKKVPR 340
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1962-2146 |
4.93e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 44.13 E-value: 4.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTV-----TSGDATVAGKSILT-NISEVHQNMGYCPQFDAIDELLTGREHLYL 2035
Cdd:PRK14247 26 IPDNTITALMGPSGSGKSTLLRVFNRLIELypearVSGEVYLDGQDIFKmDVIELRRRVQMVFQIPNPIPNLSIFENVAL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2036 YARL-RGVPAE-EIEKVANWSIKSLGL----TVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRML 2109
Cdd:PRK14247 106 GLKLnRLVKSKkELQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKI 185
|
170 180 190
....*....|....*....|....*....|....*..
gi 105990541 2110 WNVIVSIIREgRAVVLTSHSMEECEALCTRLAIMVKG 2146
Cdd:PRK14247 186 ESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKG 221
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
962-1120 |
8.56e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 44.39 E-value: 8.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 962 LGHNGAGKTTTLSILTGLLPPTSGTV-LVGGrdietsldavrQSLGMCPQHNILFhhLTVAEHMLfyaqlkgksQEEAQL 1040
Cdd:PRK10636 344 LGRNGAGKSTLIKLLAGELAPVSGEIgLAKG-----------IKLGYFAQHQLEF--LRADESPL---------QHLARL 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1041 ---EMEAMLEDT----GLH-HKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTSGVDPYSRRSIWDLLLKYRSGRT 1112
Cdd:PRK10636 402 apqELEQKLRDYlggfGFQgDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGALV 481
|
....*...
gi 105990541 1113 IIMSTHHM 1120
Cdd:PRK10636 482 VVSHDRHL 489
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
931-1140 |
9.86e-04 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 43.74 E-value: 9.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 931 VKNL-VKIFEPCGR-PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPP----TSGTVLVGGRDIetsldavrqs 1004
Cdd:COG4170 6 IRNLtIEIDTPQGRvKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGIDL---------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1005 LGMCPQ--HNILFHHLTvaehMLFyaqlkgksQE-----------EAQLeMEAMLEDTG------------------LH- 1052
Cdd:COG4170 76 LKLSPRerRKIIGREIA----MIF--------QEpsscldpsakiGDQL-IEAIPSWTFkgkwwqrfkwrkkraielLHr 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1053 -----HKR--NEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTSGVDPYSRRSIWDLLLKYR--SGRTIIMSTHHMDEA 1123
Cdd:COG4170 143 vgikdHKDimNSYPHELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNqlQGTSILLISHDLESI 222
|
250
....*....|....*..
gi 105990541 1124 DLLGDRIAIiaqgrLYC 1140
Cdd:COG4170 223 SQWADTITV-----LYC 234
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1061-1143 |
1.24e-03 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 43.25 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1061 DLSGGMQRKLSVAIAFVGDAKVVILDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIiaqgrL 1138
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLtrLNQNNNTTILLISHDLQMLSQWADKINV-----L 232
|
....*
gi 105990541 1139 YCSGT 1143
Cdd:PRK15093 233 YCGQT 237
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1942-2160 |
1.33e-03 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 42.92 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1942 ELTKIYPGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTF----KMLTgdttvTSGDATVAGKSILT-NISEVHQNMGY 2016
Cdd:cd03289 7 DLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLsaflRLLN-----TEGDIQIDGVSWNSvPLQKWRKAFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2017 CPQFDAIdelLTG--REHLYLYARLRGvpaEEIEKVANwsikSLGLTVYADCLAG-----------TYSGGNKRKLSTAI 2083
Cdd:cd03289 82 IPQKVFI---FSGtfRKNLDPYGKWSD---EEIWKVAE----EVGLKSVIEQFPGqldfvlvdggcVLSHGHKQLMCLAR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2084 ALIGCPPLVLLDEPTTGMDPqarrMLWNVIVSIIREGRA---VVLTSHSMeecEAL--CTRLAIMVKGAFRCMGTIQHLK 2158
Cdd:cd03289 152 SVLSKAKILLLDEPSAHLDP----ITYQVIRKTLKQAFAdctVILSEHRI---EAMleCQRFLVIEENKVRQYDSIQKLL 224
|
..
gi 105990541 2159 SK 2160
Cdd:cd03289 225 NE 226
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1938-2153 |
1.34e-03 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 43.29 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1938 LRLHELTKIYPGtSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT------NISEVH 2011
Cdd:PRK11650 4 LKLQAVRKSYDG-KTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNElepadrDIAMVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2012 QNMGYCPQfdaidelLTGREHLYlYA-RLRGVPAEEIEK-VANwSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCP 2089
Cdd:PRK11650 83 QNYALYPH-------MSVRENMA-YGlKIRGMPKAEIEErVAE-AARILELEPLLDRKPRELSGGQRQRVAMGRAIVREP 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 105990541 2090 PLVLLDEPTTGMDPQAR-RMLwnviVSIIREGRAVVLTS----HSMEECEALCTRLAIMVKGAFRCMGT 2153
Cdd:PRK11650 154 AVFLFDEPLSNLDAKLRvQMR----LEIQRLHRRLKTTSlyvtHDQVEAMTLADRVVVMNGGVAEQIGT 218
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
931-1164 |
1.81e-03 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 42.59 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 931 VKNLVKIFEPCGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDI-ETSLDAVRQSLGMCP 1009
Cdd:cd03288 22 IHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDIsKLPLHTLRSRLSIIL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1010 QHNILFH---------HLTVAEHMLFYAQlkgksqEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDA 1080
Cdd:cd03288 102 QDPILFSgsirfnldpECKCTDDRLWEAL------EIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKS 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1081 KVVILDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEAdLLGDRIAIIAQGRLYCSGTP--LFLKNcfgTGLYLT 1158
Cdd:cd03288 176 SILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTI-LDADLVLVLSRGILVECDTPenLLAQE---DGVFAS 251
|
....*.
gi 105990541 1159 LVRKMK 1164
Cdd:cd03288 252 LVRTDK 257
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
2071-2146 |
1.93e-03 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 43.16 E-value: 1.93e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 105990541 2071 YSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSIIREGR-AVVLTSHSMEECEALCTRLAIMVKG 2146
Cdd:PRK15134 426 FSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQlAYLFISHDLHVVRALCHQVIVLRQG 502
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1937-1987 |
2.02e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 43.24 E-value: 2.02e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 105990541 1937 ILRLHELTKIYPGTssPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTG 1987
Cdd:NF040905 1 ILEMRGITKTFPGV--KALDDVNLSVREGEIHALCGENGAGKSTLMKVLSG 49
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
1946-1995 |
3.27e-03 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 42.39 E-value: 3.27e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 105990541 1946 IYPGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGD 1995
Cdd:PRK10789 322 TYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGD 371
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1062-1143 |
3.67e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 42.04 E-value: 3.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1062 LSGGMQRKLSVAIAFVGDAKVVILDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIIAQGRLY 1139
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLleLQQKENMALVLITHDLALVAEAAHKIIVMYAGQVV 233
|
....
gi 105990541 1140 CSGT 1143
Cdd:PRK11022 234 ETGK 237
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
2089-2131 |
3.79e-03 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 41.91 E-value: 3.79e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 105990541 2089 PPLVLLDEPTTGMDPQARRMLWNVIVSIIREGRAVVLTSHSME 2131
Cdd:COG3593 188 NPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTHSPH 230
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
2070-2130 |
4.12e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.51 E-value: 4.12e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 105990541 2070 TYSGGNKRKLSTAIALIGC---PPLVLLDEPTTGMDPQARRMLWNVIVSIIREGRAVVLTSHSM 2130
Cdd:PRK00635 809 SLSGGEIQRLKLAYELLAPskkPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNM 872
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
1015-1150 |
4.91e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.51 E-value: 4.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1015 FHHLTVAEHMLFYAQLKGKSQ--EEAQLEME---AMLEDTGLHHKRNEEAQD-LSGGMQRKLSVAIAFVGDAKVV--ILD 1086
Cdd:PRK00635 424 FQQMSLQELFIFLSQLPSKSLsiEEVLQGLKsrlSILIDLGLPYLTPERALAtLSGGEQERTALAKHLGAELIGItyILD 503
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 105990541 1087 EPTSGVDPYSRRSIWDLLLKYR-SGRTIIMSTHhmDEADL-LGDRI------AIIAQGRLYCSGTPL-FLKNC 1150
Cdd:PRK00635 504 EPSIGLHPQDTHKLINVIKKLRdQGNTVLLVEH--DEQMIsLADRIidigpgAGIFGGEVLFNGSPReFLAKS 574
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1943-2134 |
9.53e-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: 41.43 E-value: 9.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 1943 LTKIYPGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTgDTTVTSGDATVAGKSILT-NISEVHQNMGYCPQFD 2021
Cdd:TIGR01271 1223 LTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALL-RLLSTEGEIQIDGVSWNSvTLQTWRKAFGVIPQKV 1301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990541 2022 AIdelLTG--REHLYLYARLRGvpaEEIEKVAN-WSIKSLgLTVYADCLA-----GTY--SGGNKRKLSTAIALIGCPPL 2091
Cdd:TIGR01271 1302 FI---FSGtfRKNLDPYEQWSD---EEIWKVAEeVGLKSV-IEQFPDKLDfvlvdGGYvlSNGHKQLMCLARSILSKAKI 1374
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 105990541 2092 VLLDEPTTGMDPqarrMLWNVIVSIIREGRA---VVLTSHSME---ECE 2134
Cdd:TIGR01271 1375 LLLDEPSAHLDP----VTLQIIRKTLKQSFSnctVILSEHRVEallECQ 1419
|
|
| |
