|
Name |
Accession |
Description |
Interval |
E-value |
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1-2271 |
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: 4943.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1 MGFLRQIQLLLWKNWTLRKRQKIRFVVELVWPLSLFLVLIWLRNANPLYSQHECHFPNKAMPSAGLLPWLQGIFCNMNNP 80
Cdd:TIGR01257 1 MGFLRQIQLLLWKNWTLRKRQKIRFVVELVWPLSLFLVLIWLRNANPLYSQHECHFPNKAMPSAGMLPWLQGIFCNVNNP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 81 CFQNPTPGESPGTVSNYNNSILARVYRDFQELFMDTPEVQHLGQVWAELRTLSQFMDTLRTHPERFAGRGLQIRDILKDE 160
Cdd:TIGR01257 81 CFQSPTPGESPGIVSNYNNSILARVYRDFQELLMDAPESQHLGQVWAELRTLSQFMDTLRTHPERIAGRGIRIRDILKDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 161 EALTLFLMRNIGLSDSVAHLLVNSQVRVEQFAYGVPDLELTDIACSEALLQRFIIFSQRRGAQTVRDALCPLSQVTLQWI 240
Cdd:TIGR01257 161 EALTLFLMKNIGLSDSVVYLLVNSQVRPEQFAYGVPDLELKDIACSEALLERFIIFSQRRGAQTVRDALCSLSQGTLQWI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 241 EDTLYADVDFFKLFHVLPTLLDSSSQGINLRFWGGILSDLSPRMQKFIHRPSVQDLLWVSRPLLQNGGPETFTQLMSILS 320
Cdd:TIGR01257 241 EDTLYANVDFFKLFHVLPTLLDSRSQGINLRSWGGILSDMSPRIQEFIHRPSVQDLLWVTRPLLQNGGPETFTQLMGILS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 321 DLLCGYPEGGGSRVFSFNWYEDNNYKAFLGIDSTRKDPAYSYDKRTTSFCNSLIQSLESNPLTKIAWRAAKPLLMGKILF 400
Cdd:TIGR01257 321 DLLCGYPEGGGSRVFSFNWYEDNNYKAFLGIDSTRKDPIYSYDKRTTSFCNALIQSLESNPLTKIAWRAAKPLLMGKILF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 401 TPDSPAARRIMKNANSTFEELDRVRKLVKAWEEVGPQIWYFFEKSTQMTVIRDTLQHPTVKDFINRQLGEEGITTEAVLN 480
Cdd:TIGR01257 401 TPDSPAARRILKNANSTFEELERVRKLVKAWEEVGPQIWYFFDKSTQMTMIRDTLQNPTVKDFINRQLGEEGITAEAVLN 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 481 FFSNGPQEKQADDMTSFDWRDIFNITDRFLRLANQYLECLVLDKFESYDDEVQLTQRALSLLEENRFWAGVVFPGMYPWA 560
Cdd:TIGR01257 481 FLYNGPREKQADDMTNFDWRDIFNITDRFLRLANQYLECLVLDKFESYDDEVQLTQRALSLLEENRFWAGVVFPDMYPWT 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 561 SSLPPHVKYKIRMDIDVVEKTNKIKDRYWDSGPRADPVEDFRYIWGGFAYLQDMVEQGIVKSQMQAEPPIGVYLQQMPYP 640
Cdd:TIGR01257 561 SSLPPHVKYKIRMDIDVVEKTNKIKDRYWDSGPRADPVEDFRYIWGGFAYLQDMVEQGITRSQMQAEPPVGIYLQQMPYP 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 641 CFVDDSFMIILNRCFPIFMVLAWIYSVSMTVKGIVLEKELRLKETLKNQGVSNAVIWCTWFLDSFSIMALSIFLLTLFIM 720
Cdd:TIGR01257 641 CFVDDSFMIILNRCFPIFMVLAWIYSVSMTVKSIVLEKELRLKETLKNQGVSNAVIWCTWFLDSFSIMSMSIFLLTIFIM 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 721 HGRILHYSDPFILFLFLLAFATATIMQSFLLSTLFSKASLAAACSGVIYFTLYLPHVLCFAWQDRMTADLKTTVSLLSSV 800
Cdd:TIGR01257 721 HGRILHYSDPFILFLFLLAFSTATIMQCFLLSTFFSKASLAAACSGVIYFTLYLPHILCFAWQDRMTADLKTAVSLLSPV 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 801 AFGFGTEYLVRFEEQGLGLQWSNIGKSPLEGDEFSFLLSMKMMLLDAALYGLLAWYLDQVFPGDYGTPLPWYFLLQESYW 880
Cdd:TIGR01257 801 AFGFGTEYLVRFEEQGLGLQWSNIGNSPLEGDEFSFLLSMKMMLLDAALYGLLAWYLDQVFPGDYGTPLPWYFLLQESYW 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 881 LGGEGCSTREERALEKTEPLTEEMEDPEHPEGMNDSFFERELPGLVPGVCVKNLVKVFEPSGRPAVDRLNITFYENQITA 960
Cdd:TIGR01257 881 LGGEGCSTREERALEKTEPLTEEMEDPEHPEGINDSFFERELPGLVPGVCVKNLVKIFEPSGRPAVDRLNITFYENQITA 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 961 FLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIETNLDVVRQSLGMCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQL 1040
Cdd:TIGR01257 961 FLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQL 1040
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1041 EMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHM 1120
Cdd:TIGR01257 1041 EMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHM 1120
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1121 DEADLLGDRIAIISQGRLYCSGTPLFLKNCFGTGFYLTLVRKMKNIQSQRGGCEGVCSCTSKGFSTRCPTRVDEITEEQV 1200
Cdd:TIGR01257 1121 DEADLLGDRIAIISQGRLYCSGTPLFLKNCFGTGFYLTLVRKMKNIQSQRGGCEGTCSCTSKGFSTRCPARVDEITPEQV 1200
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1201 LDGDVQELMDLVYHHVPEAKLVECIGQELIFLLPNKNFKQRAYASLFRELEETLADLGLSSFGISDTPLEEIFLKVTEDA 1280
Cdd:TIGR01257 1201 LDGDVNELMDLVYHHVPEAKLVECIGQELIFLLPNKNFKQRAYASLFRELEETLADLGLSSFGISDTPLEEIFLKVTEDA 1280
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1281 GAGSMFVGGAQQKREQAGLRHPCSAPTEKLRQYAQAPHTCSPGQ-VDPPKGQPSPEPEDPGVPFNTGARLILQHVQALLV 1359
Cdd:TIGR01257 1281 DSGSLFAGGAQQKRENANLRHPCSGPTEKAGQTPQASHTCSPGQpAAHPEGQPPPEPEDPGVPLNTGARLILQHVQALLV 1360
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1360 KRFHHTIRSRKDFVAQIVLPATFVFLALMLSIIVPPFGEFPALTLHPWMYGHQYTFFSMDEPNNEHLEVLADVLLNRPGF 1439
Cdd:TIGR01257 1361 KRFQHTIRSHKDFLAQIVLPATFVFLALMLSIIIPPFGEYPALTLHPWMYGQQYTFFSMDEPNSEHLEVLADVLLNKPGF 1440
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1440 GNRCLKEEWLPEYPCINATSWKTPSVSPNITHLFQKQKWTAAHPSPSCKCSTREKLTMLPECPEGAGGLPPPQRTQRSTE 1519
Cdd:TIGR01257 1441 GNRCLKEEWLPEYPCGNSTPWKTPSVSPNITHLFQKQKWTAAHPSPSCRCSTREKLTMLPECPEGAGGLPPPQRTQRSTE 1520
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1520 VLQDLTNRNISDYLVKTYPALIRSSLKSKFWVNEQRYGGISIGGKLPAIPISGEALVGFLSGLGQMMNVSGGPVTREASK 1599
Cdd:TIGR01257 1521 ILQDLTDRNISDFLVKTYPALIRSSLKSKFWVNEQRYGGISIGGKLPAIPITGEALVGFLSDLGQMMNVSGGPVTREASK 1600
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1600 EMLDFLKHLETTDNIKVWFNNKGWHALVSFLNVAHNAILRASLPRDRDPEEYGITVISQPLNLTKEQLSDITVLTTSVDA 1679
Cdd:TIGR01257 1601 EMPDFLKHLETEDNIKVWFNNKGWHALVSFLNVAHNAILRASLPKDRDPEEYGITVISQPLNLTKEQLSEITVLTTSVDA 1680
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1680 VVAICVIFAMSFVPASFVLYLIQERVTKAKHLQFISGVSPTTYWLTNFLWDIMNYAVSAGLVVGIFIGFQKKAYTSPDNL 1759
Cdd:TIGR01257 1681 VVAICVIFAMSFVPASFVLYLIQERVNKAKHLQFISGVSPTTYWLTNFLWDIMNYAVSAGLVVGIFIGFQKKAYTSPENL 1760
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1760 PALVSLLMLYGWAVIPMMYPASFLFEVPSTAYVALSCANLFIGINSSAITFVLELFENNRTLLRFNAMLRKLLIVFPHFC 1839
Cdd:TIGR01257 1761 PALVALLMLYGWAVIPMMYPASFLFDVPSTAYVALSCANLFIGINSSAITFVLELFENNRTLLRFNAMLRKLLIVFPHFC 1840
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1840 LGRGLIDLALSQAVTDVYAQFGEEYSANPFQWDLIGKNLVAMAIEGVVYFLLTLLIQHHFFLTRWIAEPAREPVFDEDDD 1919
Cdd:TIGR01257 1841 LGRGLIDLALSQAVTDVYAQFGEEHSANPFQWDLIGKNLVAMAVEGVVYFLLTLLIQHHFFLSRWIAEPAKEPIFDEDDD 1920
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1920 VAEERQRVMSGGNKTDILKLNELTKVYSGSSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAG 1999
Cdd:TIGR01257 1921 VAEERQRIISGGNKTDILRLNELTKVYSGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAG 2000
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2000 KSILTSISDVHQNMGYCPQFDAIDDLLTGREHLYLYARLRGVPSKEIEKVANWGIQSLGLSLYADRLAGTYSGGNKRKLS 2079
Cdd:TIGR01257 2001 KSILTNISDVHQNMGYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLS 2080
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2080 TAIALTGCPPLLLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGTFQCLGTIQHLKYK 2159
Cdd:TIGR01257 2081 TAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSK 2160
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2160 FGDGYIVTMKIKSPKDDLLPDLNPVEQFFQGNFPGSVQRERHHSMLQFQVPSSSLARIFQLLISHKDSLLIEEYSVTQTT 2239
Cdd:TIGR01257 2161 FGDGYIVTMKIKSPKDDLLPDLNPVEQFFQGNFPGSVQRERHYNMLQFQVSSSSLARIFQLLISHKDSLLIEEYSVTQTT 2240
|
2250 2260 2270
....*....|....*....|....*....|..
gi 6671495 2240 LDQVFVNFAKQQTETYDLPLHPRAAGASWQAK 2271
Cdd:TIGR01257 2241 LDQVFVNFAKQQTETYDLPLHPRAAGASRQAK 2272
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1937-2157 |
4.36e-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: 4.36e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1937 LKLNELTKVYSGSSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTSISDVHQNMGYC 2016
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2017 PQFDAIDDLLTGREHLYLYARLRGVPSKEIEKVANWGIQSLGLSLYADRLAGTYSGGNKRKLSTAIALTGCPPLLLLDEP 2096
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6671495 2097 TTGMDPQARRMLWNTIVSiIREGRAVVLTSHSMEECEALCTRLAIMVKGTFQCLGTIQHLK 2157
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 |
1.28e-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: 359.51 E-value: 1.28e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 929 VCVKNLVKVFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIETNLDVVRQSLGMC 1008
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1009 PQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEP 1088
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1089 TSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFLK 1148
Cdd:cd03263 161 TSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
931-1144 |
5.09e-84 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 275.40 E-value: 5.09e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 931 VKNLVKVFepSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIETNLDVVRQSLGMCPQ 1010
Cdd:COG1131 3 VRGLTKRY--GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1011 HNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTS 1090
Cdd:COG1131 81 EPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 6671495 1091 GVDPYSRRSIWDLLLKYRS-GRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
Cdd:COG1131 161 GLDPEARRELWELLRELAAeGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTP 215
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
1937-2157 |
9.99e-79 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 260.38 E-value: 9.99e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1937 LKLNELTKVYSGSssPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTSISDVHQNMGYC 2016
Cdd:COG1131 1 IEVRGLTKRYGDK--TALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2017 PQFDAIDDLLTGREHLYLYARLRGVPSKEIEKVANWGIQSLGLSLYADRLAGTYSGGNKRKLSTAIALTGCPPLLLLDEP 2096
Cdd:COG1131 79 PQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6671495 2097 TTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGTFQCLGTIQHLK 2157
Cdd:COG1131 159 TSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELK 219
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
931-1138 |
4.02e-66 |
|
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: 221.50 E-value: 4.02e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 931 VKNLVKVFepSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIETNLDVVRQSLGMCPQ 1010
Cdd:cd03230 3 VRNLSKRY--GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1011 HNILFHHLTVAEHIlfyaqlkgrsweeaqlemeamledtglhhkrneeaqDLSGGMQRKLSVAIAFVGDSKVVVLDEPTS 1090
Cdd:cd03230 81 EPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTS 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 6671495 1091 GVDPYSRRSIWDLLLKYRS-GRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
Cdd:cd03230 125 GLDPESRREFWELLRELKKeGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1941-2157 |
4.46e-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: 217.62 E-value: 4.46e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1941 ELTKVYSGSSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTSISDVHQNMGYCPQFD 2020
Cdd:cd03265 5 NLVKKYGDFE--AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIVFQDL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2021 AIDDLLTGREHLYLYARLRGVPSKEIEKVANWGIQSLGLSLYADRLAGTYSGGNKRKLSTAIALTGCPPLLLLDEPTTGM 2100
Cdd:cd03265 83 SVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 6671495 2101 DPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGTFQCLGTIQHLK 2157
Cdd:cd03265 163 DPQTRAHVWEYIEKLKEEfGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
944-1277 |
6.03e-64 |
|
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: 220.72 E-value: 6.03e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 944 PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIETNLDVVRQSLGMCPQHNILFHHLTVAEH 1023
Cdd:TIGR01188 7 KAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVRRSIGIVPQYASVDEDLTGREN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1024 ILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTSGVDPYSRRSIWDL 1103
Cdd:TIGR01188 87 LEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRAIWDY 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1104 LLKYR-SGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFLKNCFGTGFYLTLVRKMKNIQSQRGgcEGVCSCTSK 1182
Cdd:TIGR01188 167 IRALKeEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKRRLGKDTLESRPRDIQSLKVEVS--MLIAELGET 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1183 GFSTRCPTRVDEITEEQVLDGDVQelmdlvyhhVPEAklvecigqelifllpnknfkqrayaslFRELEETlaDLGLSSF 1262
Cdd:TIGR01188 245 GLGLLAVTVDSDRIKILVPDGDET---------VPEI---------------------------VEAAIRN--GIRIRSI 286
|
330
....*....|....*
gi 6671495 1263 GISDTPLEEIFLKVT 1277
Cdd:TIGR01188 287 STERPSLDDVFLKLT 301
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
931-1152 |
3.63e-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: 3.63e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 931 VKNLVKVFepSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIETNLDVVRQSLGMCPQ 1010
Cdd:COG4555 4 VENLSKKY--GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGVLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1011 HNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTS 1090
Cdd:COG4555 82 ERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6671495 1091 GVDPYSRRSIWDLLLKYR-SGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFLKNCFG 1152
Cdd:COG4555 162 GLDVMARRLLREILRALKkEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
931-1148 |
4.10e-58 |
|
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: 200.67 E-value: 4.10e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 931 VKNLVKVFepSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIETNLDVVRQSLGMCPQ 1010
Cdd:cd03265 3 VENLVKKY--GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1011 HNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTS 1090
Cdd:cd03265 81 DLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1091 GVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFLK 1148
Cdd:cd03265 161 GLDPQTRAHVWEYIekLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1937-2145 |
1.89e-57 |
|
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: 196.85 E-value: 1.89e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1937 LKLNELTKVYSgsSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTSISDVHQNMGYC 2016
Cdd:cd03230 1 IEVRNLSKRYG--KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2017 PQFDAIDDLLTGREHLYlyarlrgvpskeiekvanwgiqslglslyadrlagtYSGGNKRKLSTAIALTGCPPLLLLDEP 2096
Cdd:cd03230 79 PEEPSLYENLTVRENLK------------------------------------LSGGMKQRLALAQALLHDPELLILDEP 122
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 6671495 2097 TTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2145
Cdd:cd03230 123 TSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNG 171
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
931-1282 |
2.49e-57 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 201.49 E-value: 2.49e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 931 VKNLVKVFepSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIEtnlDVVRQSLGMCPQ 1010
Cdd:COG4152 4 LKGLTKRF--GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD---PEDRRRIGYLPE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1011 HNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTS 1090
Cdd:COG4152 79 ERGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1091 GVDPYSRRSIWDLLLKYR-SGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFLKNCFGTGFYltlvrkmkniqsq 1169
Cdd:COG4152 159 GLDPVNVELLKDVIRELAaKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQFGRNTL------------- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1170 rggcegvcsctskgfstrcptRVdeiteeqVLDGDVQELmdlvyHHVPEAKLVECIGQELIFLLPNKNFKQRayasLFRE 1249
Cdd:COG4152 226 ---------------------RL-------EADGDAGWL-----RALPGVTVVEEDGDGAELKLEDGADAQE----LLRA 268
|
330 340 350
....*....|....*....|....*....|...
gi 6671495 1250 LeetLADLGLSSFGISDTPLEEIFLKVTEDAGA 1282
Cdd:COG4152 269 L---LARGPVREFEEVRPSLNEIFIEVVGEKAE 298
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1937-2162 |
3.43e-56 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 195.85 E-value: 3.43e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1937 LKLNELTKVYSgsSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTSISDVHQNMGYC 2016
Cdd:COG4555 2 IEVENLSKKYG--KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2017 PQFDAIDDLLTGREHLYLYARLRGVPSKEIEKVANWGIQSLGLSLYADRLAGTYSGGNKRKLSTAIALTGCPPLLLLDEP 2096
Cdd:COG4555 80 PDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6671495 2097 TTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGTFQCLGTIQHLKYKFGD 2162
Cdd:COG4555 160 TNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGE 225
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
940-1144 |
6.10e-55 |
|
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: 191.78 E-value: 6.10e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 940 PSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDI-ETNLDVVRQSLGMCPQH--NILFh 1016
Cdd:COG1122 11 PGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDItKKNLRELRRKVGLVFQNpdDQLF- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1017 HLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTSGVDPYS 1096
Cdd:COG1122 90 APTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRG 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 6671495 1097 RRSIWDLLLKY-RSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
Cdd:COG1122 170 RRELLELLKRLnKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTP 218
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
931-1137 |
5.80e-52 |
|
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: 182.67 E-value: 5.80e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 931 VKNLVKVFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDI-ETNLDVVRQSLGMCP 1009
Cdd:cd03225 2 LKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLtKLSLKELRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1010 QH--NILFHHlTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDE 1087
Cdd:cd03225 82 QNpdDQFFGP-TVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 6671495 1088 PTSGVDPYSRRSIWDLLLKY-RSGRTIIMSTHHMDEADLLGDRIAIISQGR 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 |
1.22e-49 |
|
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: 175.84 E-value: 1.22e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 931 VKNLVKVFePSGRpAVDRLNITFyENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIETNLDVVRQSLGMCPQ 1010
Cdd:cd03264 3 LENLTKRY-GKKR-ALDGVSLTL-GPGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1011 HNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTS 1090
Cdd:cd03264 80 EFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 6671495 1091 GVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSG 1142
Cdd:cd03264 160 GLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1936-2145 |
8.17e-48 |
|
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: 171.01 E-value: 8.17e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1936 ILKLNELTKVYSGSSSP--AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTSISDVHQNM 2013
Cdd:cd03266 1 MITADALTKRFRDVKKTvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2014 GYCPQFDAIDDLLTGREHLYLYARLRGVPSKEIEKVANWGIQSLGLSLYADRLAGTYSGGNKRKLSTAIALTGCPPLLLL 2093
Cdd:cd03266 81 GFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 6671495 2094 DEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2145
Cdd:cd03266 161 DEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRG 212
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
931-1138 |
2.04e-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: 169.62 E-value: 2.04e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 931 VKNLVKVFEpsGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIeTNLDVVRQSLGMCPQ 1010
Cdd:cd03259 3 LKGLSKTYG--SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV-TGVPPERRNIGMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1011 HNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTS 1090
Cdd:cd03259 80 DYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 6671495 1091 GVDPYSRRSIWDLLLKY--RSGRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
Cdd:cd03259 160 ALDAKLREELREELKELqrELGITTIYVTHDQEEALALADRIAVMNEGRI 209
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
931-1137 |
2.67e-47 |
|
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: 169.00 E-value: 2.67e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 931 VKNLVKVFEPsgRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIEtnlDVVRQSLGMCPQ 1010
Cdd:cd03269 3 VENVTKRFGR--VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD---IAARNRIGYLPE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1011 HNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTS 1090
Cdd:cd03269 78 ERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFS 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 6671495 1091 GVDPYSRRSIWDLLLKY-RSGRTIIMSTHHMDEADLLGDRIAIISQGR 1137
Cdd:cd03269 158 GLDPVNVELLKDVIRELaRAGKTVILSTHQMELVEELCDRVLLLNKGR 205
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
1937-2146 |
3.81e-47 |
|
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: 168.55 E-value: 3.81e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1937 LKLNELTKVYSGSssPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTSISDVhQNMGYC 2016
Cdd:cd03268 1 LKTNDLTKTYGKK--RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEAL-RRIGAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2017 PQFDAIDDLLTGREHLYLYARLRGVPSKEIEKVanwgIQSLGLSLYADRLAGTYSGGNKRKLSTAIALTGCPPLLLLDEP 2096
Cdd:cd03268 78 IEAPGFYPNLTARENLRLLARLLGIRKKRIDEV----LDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 6671495 2097 TTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGT 2146
Cdd:cd03268 154 TNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGK 203
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
931-1134 |
4.99e-47 |
|
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: 168.80 E-value: 4.99e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 931 VKNLVKVFEPSGRP--AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIETnldvVRQSLGMC 1008
Cdd:cd03293 3 VRNVSKTYGGGGGAvtALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG----PGPDRGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1009 PQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEP 1088
Cdd:cd03293 79 FQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEP 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 6671495 1089 TSGVDPYSRRSIWDLLLK--YRSGRTIIMSTHHMDEADLLGDRIAIIS 1134
Cdd:cd03293 159 FSALDALTREQLQEELLDiwRETGKTVLLVTHDIDEAVFLADRVVVLS 206
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1934-2145 |
5.92e-47 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 171.91 E-value: 5.92e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1934 TDILKLNELTKVYSGSSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTSISDVHQNM 2013
Cdd:PRK13537 5 VAPIDFRNVEKRYGDKL--VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2014 GYCPQFDAIDDLLTGREHLYLYARLRGVPSKEIEKVANWGIQSLGLSLYADRLAGTYSGGNKRKLSTAIALTGCPPLLLL 2093
Cdd:PRK13537 83 GVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 6671495 2094 DEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2145
Cdd:PRK13537 163 DEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEG 214
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
931-1144 |
9.28e-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: 168.77 E-value: 9.28e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 931 VKNLVKVFepSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIeTNL---DVVRQSLGM 1007
Cdd:cd03219 3 VRGLTKRF--GGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDI-TGLpphEIARLGIGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1008 CPQHNILFHHLTVAEHILFYAQLKGRSW--------EEAQLEMEAM--LEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFV 1077
Cdd:cd03219 80 TFQIPRLFPELTVLENVMVAAQARTGSGlllararrEEREARERAEelLERVGLADLADRPAGELSYGQQRRLEIARALA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6671495 1078 GDSKVVVLDEPTSGVDPYSRRSIWDLLLKYR-SGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
Cdd:cd03219 160 TDPKLLLLDEPAAGLNPEETEELAELIRELReRGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTP 227
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
931-1144 |
1.78e-46 |
|
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: 168.68 E-value: 1.78e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 931 VKNLVKVFepSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIeTNL---DVVRQSLGM 1007
Cdd:COG0411 7 VRGLTKRF--GGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDI-TGLpphRIARLGIAR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1008 CPQHNILFHHLTVAEHILFYAQLKGRSW-------------EEAQLEMEAM--LEDTGLHHKRNEEAQDLSGGMQRKLSV 1072
Cdd:COG0411 84 TFQNPRLFPELTVLENVLVAAHARLGRGllaallrlprarrEEREARERAEelLERVGLADRADEPAGNLSYGQQRRLEI 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6671495 1073 AIAFVGDSKVVVLDEPTSGVDPYSRRSIWDLLLKYR--SGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
Cdd:COG0411 164 ARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRdeRGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTP 237
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1901-2145 |
4.59e-46 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 170.40 E-value: 4.59e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1901 LTRWIAEPAR----EPVFDEDDDVAEERQRVMSGGNKTDILKLNELTKVYSGSssPAVDRLCVGVRPGECFGLLGVNGAG 1976
Cdd:PRK13536 2 LTRAVAEEAPrrleLSPIERKHQGISEAKASIPGSMSTVAIDLAGVSKSYGDK--AVVNGLSFTVASGECFGLLGPNGAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1977 KTTTFKMLTGDTTVTSGDATVAGKSILTSISDVHQNMGYCPQFDAIDDLLTGREHLYLYARLRGVPSKEIEKVANWGIQS 2056
Cdd:PRK13536 80 KSTIARMILGMTSPDAGKITVLGVPVPARARLARARIGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2057 LGLSLYADRLAGTYSGGNKRKLSTAIALTGCPPLLLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALC 2136
Cdd:PRK13536 160 ARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLC 239
|
....*....
gi 6671495 2137 TRLAIMVKG 2145
Cdd:PRK13536 240 DRLCVLEAG 248
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
931-1130 |
1.18e-45 |
|
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: 164.19 E-value: 1.18e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 931 VKNLVKVFEpsGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIETNLDVVRQSLGMCPQ 1010
Cdd:COG4133 5 AENLSCRRG--ERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYLGH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1011 HNILFHHLTVAEHILFYAQLKGRSWEEAQLemEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTS 1090
Cdd:COG4133 83 ADGLKPELTVRENLRFWAALYGLRADREAI--DEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFT 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 6671495 1091 GVDPYSRRSIWDLLLKYR-SGRTIIMSTHhmDEADLLGDRI 1130
Cdd:COG4133 161 ALDAAGVALLAELIAAHLaRGGAVLLTTH--QPLELAAARV 199
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
931-1138 |
2.47e-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: 2.47e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 931 VKNLVKVFepSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIETNLDVVRQsLGMCPQ 1010
Cdd:cd03268 3 TNDLTKTY--GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRR-IGALIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1011 HNILFHHLTVAEHILFYAQLKGRSWEEAqlemEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTS 1090
Cdd:cd03268 80 APGFYPNLTARENLRLLARLLGIRKKRI----DEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTN 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 6671495 1091 GVDPYSRRSIWDLLLKYR-SGRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
Cdd:cd03268 156 GLDPDGIKELRELILSLRdQGITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
932-1144 |
3.06e-45 |
|
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: 164.40 E-value: 3.06e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 932 KNLVKVFePSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIeTNLDVV--RQSLGMCP 1009
Cdd:cd03295 4 ENVTKRY-GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDI-REQDPVelRRKIGYVI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1010 QHNILFHHLTVAEHILFYAQLKGrsWEEAQLEMEA--MLEDTGL--HHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVL 1085
Cdd:cd03295 82 QQIGLFPHMTVEENIALVPKLLK--WPKEKIRERAdeLLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLLM 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6671495 1086 DEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
Cdd:cd03295 160 DEPFGALDPITRDQLQEEFkrLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTP 220
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
927-1136 |
8.01e-45 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 163.72 E-value: 8.01e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 927 PGVCVKNLVKVFEPSG--RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIETnldvVRQS 1004
Cdd:COG1116 6 PALELRGVSKRFPTGGggVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG----PGPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1005 LGMCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVV 1084
Cdd:COG1116 82 RGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 6671495 1085 LDEPTSGVDPYSRRSIWDLLLKY--RSGRTIIMSTHHMDEADLLGDRIAIISQG 1136
Cdd:COG1116 162 MDEPFGALDALTRERLQDELLRLwqETGKTVLFVTHDVDEAVFLADRVVVLSAR 215
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
931-1144 |
2.24e-44 |
|
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: 161.52 E-value: 2.24e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 931 VKNLVKVFEpsGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDI----ETNLDVVRQSLG 1006
Cdd:cd03261 3 LRGLTKSFG--GRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDIsglsEAELYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1007 MCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAM-LEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVL 1085
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFPLREHTRLSEEEIREIVLEkLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLY 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6671495 1086 DEPTSGVDPYSRRSIWDLLLKYR--SGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
Cdd:cd03261 161 DEPTAGLDPIASGVIDDLIRSLKkeLGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTP 221
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
931-1144 |
4.36e-44 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 160.92 E-value: 4.36e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 931 VKNLVKVFEpsGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDI----ETNLDVVRQSLG 1006
Cdd:COG1127 8 VRNLTKSFG--DRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDItglsEKELYELRRRIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1007 MCPQHNILFHHLTVAEHILFY-AQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVL 1085
Cdd:COG1127 86 MLFQGGALFDSLTVFENVAFPlREHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILLY 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6671495 1086 DEPTSGVDPYSRRSIWDLLLKYRS--GRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
Cdd:COG1127 166 DEPTAGLDPITSAVIDELIRELRDelGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTP 226
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
931-1138 |
1.06e-43 |
|
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: 159.19 E-value: 1.06e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 931 VKNLVKVFEPSGR--PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDI----ETNLDVVR-Q 1003
Cdd:cd03255 3 LKNLSKTYGGGGEkvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDIsklsEKELAAFRrR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1004 SLGMCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVV 1083
Cdd:cd03255 83 HIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPKII 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 6671495 1084 VLDEPTSGVDPYSRRSIWDLLLKYR--SGRTIIMSTHHMDEADlLGDRIAIISQGRL 1138
Cdd:cd03255 163 LADEPTGNLDSETGKEVMELLRELNkeAGTTIVVVTHDPELAE-YADRIIELRDGKI 218
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
931-1142 |
1.41e-43 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 158.69 E-value: 1.41e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 931 VKNLVKVFEPSGRP--AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIETNLDVVRQSLGMC 1008
Cdd:cd03266 4 ADALTKRFRDVKKTvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLGFV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1009 PQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEP 1088
Cdd:cd03266 84 SDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 6671495 1089 TSGVDPYSRRSIWDLLLKYRS-GRTIIMSTHHMDEADLLGDRIAIISQGRLYCSG 1142
Cdd:cd03266 164 TTGLDVMATRALREFIRQLRAlGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
927-1144 |
1.78e-43 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 163.35 E-value: 1.78e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 927 PGVCVKNLVKVFepSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIeTNLDVVRQSLG 1006
Cdd:COG3842 4 PALELENVSKRY--GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDV-TGLPPEKRNVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1007 MCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGG-MQRklsVAIA--FVGDSKVV 1083
Cdd:COG3842 81 MVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGqQQR---VALAraLAPEPRVL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6671495 1084 VLDEPTSGVDPYSRRSIWDLLLKY--RSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
Cdd:COG3842 158 LLDEPLSALDAKLREEMREELRRLqrELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTP 220
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
942-1144 |
8.05e-43 |
|
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: 157.90 E-value: 8.05e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 942 GRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIET--NLDVVRQsLGMCPQHNILFHHLT 1019
Cdd:COG1120 13 GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASlsRRELARR-IAYVPQEPPAPFGLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1020 VAE--------HILFYAQLKGRSWEEAqlemEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTSG 1091
Cdd:COG1120 92 VRElvalgrypHLGLFGRPSAEDREAV----EEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSH 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 6671495 1092 VDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
Cdd:COG1120 168 LDLAHQLEVLELLrrLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPP 222
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
931-1138 |
1.23e-41 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 153.66 E-value: 1.23e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 931 VKNLVKVFePSG---RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDI----ETNLDVVR- 1002
Cdd:COG1136 7 LRNLTKSY-GTGegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDIsslsERELARLRr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1003 QSLGMCPQ-HNiLFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGG-MQRklsVAIA--FVG 1078
Cdd:COG1136 86 RHIGFVFQfFN-LLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGqQQR---VAIAraLVN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6671495 1079 DSKVVVLDEPTSGVDPYSRRSIWDLLLKY--RSGRTIIMSTHHMDEADlLGDRIAIISQGRL 1138
Cdd:COG1136 162 RPKLILADEPTGNLDSKTGEEVLELLRELnrELGTTIVMVTHDPELAA-RADRVIRLRDGRI 222
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
930-1137 |
1.36e-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: 150.86 E-value: 1.36e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 930 CVKNLVKVFEpsGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIETNLDV-VRQSLGMC 1008
Cdd:cd00267 1 EIENLSFRYG--GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEeLRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1009 PQhnilfhhltvaehilfyaqlkgrsweeaqlemeamledtglhhkrneeaqdLSGGMQRKLSVAIAFVGDSKVVVLDEP 1088
Cdd:cd00267 79 PQ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEP 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 6671495 1089 TSGVDPYSRRSIWDLLLKY-RSGRTIIMSTHHMDEADLLGDRIAIISQGR 1137
Cdd:cd00267 108 TSGLDPASRERLLELLRELaEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1936-2253 |
1.99e-41 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 155.27 E-value: 1.99e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1936 ILKLNELTKVYSgsSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIltsISDVHQNMGY 2015
Cdd:COG4152 1 MLELKGLTKRFG--DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPL---DPEDRRRIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2016 CP-------QFDAIDDLltgrehLYLyARLRGVPSKEIEKVANWGIQSLGLSLYADRLAGTYSGGNKRKLSTAIALTGCP 2088
Cdd:COG4152 76 LPeerglypKMKVGEQL------VYL-ARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2089 PLLLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGT--FQclGTIQHLKYKFGdGYIV 2166
Cdd:COG4152 149 ELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRkvLS--GSVDEIRRQFG-RNTL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2167 TMKIKSPKDDLLpdlnpveqffqgNFPGSVQRERHHSMLQFQVPSSSLAR-IFQLLISHKDsllIEEYSVTQTTLDQVFV 2245
Cdd:COG4152 226 RLEADGDAGWLR------------ALPGVTVVEEDGDGAELKLEDGADAQeLLRALLARGP---VREFEEVRPSLNEIFI 290
|
....*...
gi 6671495 2246 NFAKQQTE 2253
Cdd:COG4152 291 EVVGEKAE 298
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1937-2127 |
2.46e-41 |
|
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: 151.86 E-value: 2.46e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1937 LKLNELTKVYSGSssPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTSISDVHQNMGYC 2016
Cdd:COG4133 3 LEAENLSCRRGER--LLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2017 PQFDAIDDLLTGREHLYLYARLRGVPSKEiEKVANWgIQSLGLSLYADRLAGTYSGGNKRKLSTAIALTGCPPLLLLDEP 2096
Cdd:COG4133 81 GHADGLKPELTVRENLRFWAALYGLRADR-EAIDEA-LEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEP 158
|
170 180 190
....*....|....*....|....*....|.
gi 6671495 2097 TTGMDPQARRMLWNTIVSIIREGRAVVLTSH 2127
Cdd:COG4133 159 FTALDAAGVALLAELIAAHLARGGAVLLTTH 189
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1937-2145 |
4.29e-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: 151.19 E-value: 4.29e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1937 LKLNELTKVYSGSSspAVD----RLCVGVrpgecFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTSISDVHQN 2012
Cdd:cd03264 1 LQLENLTKRYGKKR--ALDgvslTLGPGM-----YGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2013 MGYCPQFDAIDDLLTGREHLYLYARLRGVPSKEIEKVANWGIQSLGLSLYADRLAGTYSGGNKRKLSTAIALTGCPPLLL 2092
Cdd:cd03264 74 IGYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILI 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 6671495 2093 LDEPTTGMDPqARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2145
Cdd:cd03264 154 VDEPTAGLDP-EERIRFRNLLSELGEDRIVILSTHIVEDVESLCNQVAVLNKG 205
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
931-1137 |
8.50e-41 |
|
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: 149.26 E-value: 8.50e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 931 VKNLVKVFepSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIETNLDVV---RQSLGM 1007
Cdd:cd03229 3 LKNVSKRY--GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELpplRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1008 CPQHNILFHHLTVAEHILFyaqlkgrsweeaqlemeamledtglhhkrneeaqDLSGGMQRKLSVAIAFVGDSKVVVLDE 1087
Cdd:cd03229 81 VFQDFALFPHLTVLENIAL----------------------------------GLSGGQQQRVALARALAMDPDVLLLDE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 6671495 1088 PTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGR 1137
Cdd:cd03229 127 PTSALDPITRREVRALLksLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
922-1144 |
9.31e-41 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 153.81 E-value: 9.31e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 922 LPGLVPGVCVKNLVKVFepSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIETNLDVV 1001
Cdd:PRK13537 1 GPMSVAPIDFRNVEKRY--GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1002 RQSLGMCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSK 1081
Cdd:PRK13537 79 RQRVGVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6671495 1082 VVVLDEPTSGVDPYSRRSIWDLLlkyRS----GRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
Cdd:PRK13537 159 VLVLDEPTTGLDPQARHLMWERL---RSllarGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAP 222
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
944-1144 |
1.09e-40 |
|
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: 150.66 E-value: 1.09e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 944 PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIeTNL---DVVRQSLGMCPQHNILFHHLTV 1020
Cdd:cd03224 14 QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDI-TGLpphERARAGIGYVPEGRRIFPELTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1021 AEHILFYAQLKGRSWEEAQLE-MEAMLEDtgLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTSGVDPYSRRS 1099
Cdd:cd03224 93 EENLLLGAYARRRAKRKARLErVYELFPR--LKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEE 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 6671495 1100 IWDLLLKYR-SGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
Cdd:cd03224 171 IFEAIRELRdEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTA 216
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
929-1137 |
1.42e-40 |
|
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: 148.30 E-value: 1.42e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 929 VCVKNLVKVFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIET-NLDVVRQSLGM 1007
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDlDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1008 CPQHNILFhHLTVAEHIlfyaqlkgrsweeaqlemeamledtglhhkrneeaqdLSGGMQRKLSVAIAFVGDSKVVVLDE 1087
Cdd:cd03228 81 VPQDPFLF-SGTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 6671495 1088 PTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADlLGDRIAIISQGR 1137
Cdd:cd03228 123 ATSALDPETEALILEALRALAKGKTVIVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
946-1090 |
3.65e-40 |
|
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: 146.25 E-value: 3.65e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 946 VDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDI-ETNLDVVRQSLGMCPQHNILFHHLTVAEHI 1024
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLtDDERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1025 LFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQD----LSGGMQRKLSVAIAFVGDSKVVVLDEPTS 1090
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVGErpgtLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
931-1144 |
4.70e-40 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 157.37 E-value: 4.70e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 931 VKNLVKVFEPSGR---PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIET----NLDVVRQ 1003
Cdd:COG1123 263 VRNLSKRYPVRGKggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKlsrrSLRELRR 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1004 SLGMCPQH--NILFHHLTVAEHILF-YAQLKGRSWEEAQLEMEAMLEDTGLhhkrNEEAQD-----LSGGMQRKLSVAIA 1075
Cdd:COG1123 343 RVQMVFQDpySSLNPRMTVGDIIAEpLRLHGLLSRAERRERVAELLERVGL----PPDLADrypheLSGGQRQRVAIARA 418
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6671495 1076 FVGDSKVVVLDEPTSGVDPYSRRSIWDLLLKYR--SGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
Cdd:COG1123 419 LALEPKLLILDEPTSALDVSVQAQILNLLRDLQreLGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPT 489
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
931-1144 |
1.23e-39 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 148.25 E-value: 1.23e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 931 VKNLVKVFepSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIeTNLDV-VRQSLGM-- 1007
Cdd:COG1137 6 AENLVKSY--GKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDI-THLPMhKRARLGIgy 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1008 CPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDE 1087
Cdd:COG1137 83 LPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6671495 1088 PTSGVDPYSRRSIWDLL--LKYRsGRTIIMSTHHMDEAdlLG--DRIAIISQGRLYCSGTP 1144
Cdd:COG1137 163 PFAGVDPIAVADIQKIIrhLKER-GIGVLITDHNVRET--LGicDRAYIISEGKVLAEGTP 220
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1938-2146 |
1.25e-39 |
|
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: 147.23 E-value: 1.25e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1938 KLNELTKVYSGSSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIL-TSISDVHQNMGYC 2016
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTkLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2017 PQF--------DAIDDLLTGREHLylyarlrGVPSKEIEKVANWGIQSLGLSLYADRLAGTYSGGNKRKLSTAIALTGCP 2088
Cdd:cd03225 81 FQNpddqffgpTVEEEVAFGLENL-------GLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 6671495 2089 PLLLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGT 2146
Cdd:cd03225 154 DILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
931-1144 |
2.69e-39 |
|
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: 146.92 E-value: 2.69e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 931 VKNLVKVFepSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIeTNLDVVRQS-LGMC- 1008
Cdd:cd03218 3 AENLSKRY--GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDI-TKLPMHKRArLGIGy 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1009 -PQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDE 1087
Cdd:cd03218 80 lPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 6671495 1088 PTSGVDPYSRRSIWDLLLKYR-SGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
Cdd:cd03218 160 PFAGVDPIAVQDIQKIIKILKdRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTP 217
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
892-1144 |
3.49e-39 |
|
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: 156.08 E-value: 3.49e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 892 RALEKTEPLTEEMEDPEHPEGmndsfferelpglVPGVCVKNLVKVFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTT 971
Cdd:COG4987 310 NELLDAPPAVTEPAEPAPAPG-------------GPSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKST 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 972 TLSILTGLLPPTSGTVLIGGKDIET-NLDVVRQSLGMCPQHNILFHHlTVAEHILFyaqlkGRswEEA-QLEMEAMLEDT 1049
Cdd:COG4987 377 LLALLLRFLDPQSGSITLGGVDLRDlDEDDLRRRIAVVPQRPHLFDT-TLRENLRL-----AR--PDAtDEELWAALERV 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1050 GLHH----KRN-------EEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTH 1118
Cdd:COG4987 449 GLGDwlaaLPDgldtwlgEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITH 528
|
250 260
....*....|....*....|....*.
gi 6671495 1119 HMDEADlLGDRIAIISQGRLYCSGTP 1144
Cdd:COG4987 529 RLAGLE-RMDRILVLEDGRIVEQGTH 553
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
891-1144 |
3.85e-39 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 150.37 E-value: 3.85e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 891 ERALEKTEPLTEEMEDPEHPEGMNdsfferELPGLVPGVCVkNLVKVFEPSG-RPAVDRLNITFYENQITAFLGHNGAGK 969
Cdd:PRK13536 8 EEAPRRLELSPIERKHQGISEAKA------SIPGSMSTVAI-DLAGVSKSYGdKAVVNGLSFTVASGECFGLLGPNGAGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 970 TTTLSILTGLLPPTSGTVLIGGKDIETNLDVVRQSLGMCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDT 1049
Cdd:PRK13536 81 STIARMILGMTSPDAGKITVLGVPVPARARLARARIGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1050 GLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTSGVDPYSRRSIWDLLlkyRS----GRTIIMSTHHMDEADL 1125
Cdd:PRK13536 161 RLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERL---RSllarGKTILLTTHFMEEAER 237
|
250
....*....|....*....
gi 6671495 1126 LGDRIAIISQGRLYCSGTP 1144
Cdd:PRK13536 238 LCDRLCVLEAGRKIAEGRP 256
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
927-1144 |
1.05e-38 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 145.62 E-value: 1.05e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 927 PGVCVKNLVKVFEpsGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIETnldvVRQSLG 1006
Cdd:COG1121 5 PAIELENLTVSYG--GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR----ARRRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1007 MCPQHNILFHH--LTVAE--------HILFYAQLKGRSWEEAqlemEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAF 1076
Cdd:COG1121 79 YVPQRAEVDWDfpITVRDvvlmgrygRRGLFRRPSRADREAV----DEALERVGLEDLADRPIGELSGGQQQRVLLARAL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6671495 1077 VGDSKVVVLDEPTSGVDPYSRRSIWDLLLKYRS-GRTIIMSTHHMDEADLLGDRIAIISqGRLYCSGTP 1144
Cdd:COG1121 155 AQDPDLLLLDEPFAGVDAATEEALYELLRELRReGKTILVVTHDLGAVREYFDRVLLLN-RGLVAHGPP 222
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
931-1144 |
1.27e-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: 145.07 E-value: 1.27e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 931 VKNLVKVFepSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIeTNLDVVRQSLGMCPQ 1010
Cdd:cd03300 3 LENVSKFY--GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI-TNLPPHKRPVNTVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1011 HNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTS 1090
Cdd:cd03300 80 NYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLG 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 6671495 1091 GVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
Cdd:cd03300 160 ALDLKLRKDMQLELkrLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTP 215
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
931-1142 |
1.66e-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: 142.57 E-value: 1.66e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 931 VKNLVkvFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIETnldvvrqslgmcpq 1010
Cdd:cd03214 2 VENLS--VGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLAS-------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1011 hnilFHHLTVAEHILFYAQlkgrsweeaqlemeaMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTS 1090
Cdd:cd03214 66 ----LSPKELARKIAYVPQ---------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTS 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 6671495 1091 GVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSG 1142
Cdd:cd03214 127 HLDIAHQIELLELLrrLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1937-2145 |
2.06e-38 |
|
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: 143.58 E-value: 2.06e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1937 LKLNELTKVYSgsSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIltSISDVHQnMGYC 2016
Cdd:cd03269 1 LEVENVTKRFG--RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPL--DIAARNR-IGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2017 PQFDAIDDLLTGREHLYLYARLRGVPSKEIEKVANWGIQSLGLSLYADRLAGTYSGGNKRKLSTAIALTGCPPLLLLDEP 2096
Cdd:cd03269 76 PEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEP 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 6671495 2097 TTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2145
Cdd:cd03269 156 FSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKG 204
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
931-1138 |
2.28e-38 |
|
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: 144.25 E-value: 2.28e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 931 VKNLVKVFEpsGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLP-----PTSGTVLIGGKDI-ETNLDVV--R 1002
Cdd:cd03260 3 LRDLNVYYG--DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIyDLDVDVLelR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1003 QSLGMCPQHNILFHhLTVAEHILFYAQLKGRSW-EEAQLEMEAMLEDTGLHH--KRNEEAQDLSGGMQRKLSVAIAFVGD 1079
Cdd:cd03260 81 RRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIKLkEELDERVEEALRKAALWDevKDRLHALGLSGGQQQRLCLARALANE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 6671495 1080 SKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
Cdd:cd03260 160 PEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVADRTAFLLNGRL 218
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
931-1144 |
2.67e-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: 145.48 E-value: 2.67e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 931 VKNLVKVFEPSGRPAVDRL--------------------NITF--YENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVL 988
Cdd:cd03294 3 IKGLYKIFGKNPQKAFKLLakgkskeeilkktgqtvgvnDVSLdvREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 989 IGGKDIETN-----LDVVRQSLGMCPQHNILFHHLTVAEHILFYAQLKGRSWEE-AQLEMEAmLEDTGLHHKRNEEAQDL 1062
Cdd:cd03294 83 IDGQDIAAMsrkelRELRRKKISMVFQSFALLPHRTVLENVAFGLEVQGVPRAErEERAAEA-LELVGLEGWEHKYPDEL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1063 SGGMQRKLSVAIAFVGDSKVVVLDEPTSGVDPYSRRSIWDLLLKYRS--GRTIIMSTHHMDEADLLGDRIAIISQGRLYC 1140
Cdd:cd03294 162 SGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAelQKTIVFITHDLDEALRLGDRIAIMKDGRLVQ 241
|
....
gi 6671495 1141 SGTP 1144
Cdd:cd03294 242 VGTP 245
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
931-1143 |
2.72e-38 |
|
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: 144.26 E-value: 2.72e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 931 VKNLVKVFEPSGR--PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDI----ETNLDVVRQS 1004
Cdd:cd03258 4 LKNVSKVFGDTGGkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLtllsGKELRKARRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1005 LGMCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVV 1084
Cdd:cd03258 84 IGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6671495 1085 LDEPTSGVDPYSRRSIWDLLLKY--RSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGT 1143
Cdd:cd03258 164 CDEATSALDPETTQSILALLRDInrELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGT 224
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
929-1145 |
6.40e-38 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 146.76 E-value: 6.40e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 929 VCVKNLVKVFepSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIeTNLDVVRQSLGMC 1008
Cdd:COG3839 4 LELENVSKSY--GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDV-TDLPPKDRNIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1009 PQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGG-MQRklsVAI--AFVGDSKVVVL 1085
Cdd:COG3839 81 FQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGqRQR---VALgrALVREPKVFLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6671495 1086 DEPTSGVDPYSRRSIWDLLLKY--RSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPL 1145
Cdd:COG3839 158 DEPLSNLDAKLRVEMRAEIKRLhrRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPE 219
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
903-1144 |
7.16e-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: 151.83 E-value: 7.16e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 903 EMEDPEHPEGmndsffERELPGLVPG-VCVKNLVkVFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLP 981
Cdd:COG4988 316 DAPEPAAPAG------TAPLPAAGPPsIELEDVS-FSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLP 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 982 PTSGTVLIGGKDIET-NLDVVRQSLGMCPQHNILFHhLTVAEHILFY------AQLKgRSWEEAQL-EMEAMLEDtGLHH 1053
Cdd:COG4988 389 PYSGSILINGVDLSDlDPASWRRQIAWVPQNPYLFA-GTIRENLRLGrpdasdEELE-AALEAAGLdEFVAALPD-GLDT 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1054 KRNEEAQDLSGG-MQRkLSVAIAFVGDSKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADlLGDRIAI 1132
Cdd:COG4988 466 PLGEGGRGLSGGqAQR-LALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLA-QADRILV 543
|
250
....*....|..
gi 6671495 1133 ISQGRLYCSGTP 1144
Cdd:COG4988 544 LDDGRIVEQGTH 555
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
931-1144 |
1.11e-37 |
|
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: 142.41 E-value: 1.11e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 931 VKNLVKVFepSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIeTNLDV---VRQSLGM 1007
Cdd:TIGR04406 4 AENLIKSY--KKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDI-THLPMherARLGIGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1008 CPQHNILFHHLTVAEHILFYAQLKGR-SWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLD 1086
Cdd:TIGR04406 81 LPQEASIFRKLTVEENIMAVLEIRKDlDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 6671495 1087 EPTSGVDPYSRRSIWDLLLKYRS-GRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
Cdd:TIGR04406 161 EPFAGVDPIAVGDIKKIIKHLKErGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTP 219
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
927-1144 |
1.59e-36 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 146.97 E-value: 1.59e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 927 PGVCVKNLVKVFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPT---SGTVLIGGKDI-ETNLDVVR 1002
Cdd:COG1123 3 PLLEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLlELSEALRG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1003 QSLGMCPQH-NILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSK 1081
Cdd:COG1123 83 RRIGMVFQDpMTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6671495 1082 VVVLDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
Cdd:COG1123 163 LLIADEPTTALDVTTQAEILDLLreLQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPP 227
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1937-2152 |
1.61e-36 |
|
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: 139.00 E-value: 1.61e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1937 LKLNELTKVYSGSSsPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIL-TSISDVHQNMGY 2015
Cdd:COG1122 1 IELENLSFSYPGGT-PALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITkKNLRELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2016 CPQ------FDAI--DDLLTGREHLylyarlrGVPSKEIEKVANWGIQSLGLSLYADRLAGTYSGGNKRKLSTAIALTGC 2087
Cdd:COG1122 80 VFQnpddqlFAPTveEDVAFGPENL-------GLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAME 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6671495 2088 PPLLLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGTFQCLGT 2152
Cdd:COG1122 153 PEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGT 217
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
893-1144 |
2.07e-36 |
|
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: 149.60 E-value: 2.07e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 893 ALEKTEPLTEEmeDPEHPEGMNDsffeRELPGLVPGVCVKNLVKVFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTT 972
Cdd:COG2274 444 ALERLDDILDL--PPEREEGRSK----LSLPRLKGDIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTL 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 973 LSILTGLLPPTSGTVLIGGKDIET-NLDVVRQSLGMCPQHNILFHHlTVAEHILFYAQlkGRSWEEAQ--LEMEAMLEDT 1049
Cdd:COG2274 518 LKLLLGLYEPTSGRILIDGIDLRQiDPASLRRQIGVVLQDVFLFSG-TIRENITLGDP--DATDEEIIeaARLAGLHDFI 594
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1050 -----GLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEAD 1124
Cdd:COG2274 595 ealpmGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIR 674
|
250 260
....*....|....*....|
gi 6671495 1125 LLgDRIAIISQGRLYCSGTP 1144
Cdd:COG2274 675 LA-DRIIVLDKGRIVEDGTH 693
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
932-1138 |
2.37e-36 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 138.26 E-value: 2.37e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 932 KNLVKVFePSGRPAVDRLNITFYENQItAFL-GHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIET----NLDVVRQSLG 1006
Cdd:COG2884 5 ENVSKRY-PGGREALSDVSLEIEKGEF-VFLtGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRlkrrEIPYLRRRIG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1007 MCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLD 1086
Cdd:COG2884 83 VVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLAD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 6671495 1087 EPTSGVDPYSRRSIWDLLLKY-RSGRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
Cdd:COG2884 163 EPTGNLDPETSWEIMELLEEInRRGTTVLIATHDLELVDRMPKRVLELEDGRL 215
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
931-1144 |
3.41e-36 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 138.47 E-value: 3.41e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 931 VKNLVKVFePSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIET----NLDVVRQSLG 1006
Cdd:cd03256 3 VENLSKTY-PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKlkgkALRQLRRQIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1007 MCPQHNILFHHLTVAEHIL--------FYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVG 1078
Cdd:cd03256 82 MIFQQFNLIERLSVLENVLsgrlgrrsTWRSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6671495 1079 DSKVVVLDEPTSGVDPYSRRSIWDLLLKYRS--GRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
Cdd:cd03256 162 QPKLILADEPVASLDPASSRQVMDLLKRINReeGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPP 229
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
938-1138 |
4.19e-36 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 136.87 E-value: 4.19e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 938 FEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIET-NLDVVRQSLGMCPQHNILFH 1016
Cdd:COG4619 8 FRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAmPPPEWRRQVAYVPQEPALWG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1017 HlTVAEHILFYAQLKGRSWEEAqlEMEAMLEDTGLHHK-RNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTSGVDPY 1095
Cdd:COG4619 88 G-TVRDNLPFPFQLRERKFDRE--RALELLERLGLPPDiLDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPE 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 6671495 1096 SRRSIWDLLLKYR--SGRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
Cdd:COG4619 165 NTRRVEELLREYLaeEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
931-1138 |
5.71e-36 |
|
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: 137.25 E-value: 5.71e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 931 VKNLVKVFEPSGRP--AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIETNLD----VVRQS 1004
Cdd:cd03257 4 VKNLSVSFPTGGGSvkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRrlrkIRRKE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1005 LGMCPQH--NILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKR---NEEAQDLSGGMQRKLSVAIAFVGD 1079
Cdd:cd03257 84 IQMVFQDpmSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEevlNRYPHELSGGQRQRVAIARALALN 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6671495 1080 SKVVVLDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
Cdd:cd03257 164 PKLLIADEPTSALDVSVQAQILDLLkkLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
940-1148 |
3.71e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 137.07 E-value: 3.71e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 940 PSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDI-----ETNLDVVRQSLGMC---PQH 1011
Cdd:PRK13634 17 PFERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkkNKKLKPLRKKVGIVfqfPEH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1012 NiLFHHlTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQ-DLSGGMQRKlsVAIAFV--GDSKVVVLDEP 1088
Cdd:PRK13634 97 Q-LFEE-TVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEELLARSPfELSGGQMRR--VAIAGVlaMEPEVLVLDEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6671495 1089 TSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP--LFLK 1148
Cdd:PRK13634 173 TAGLDPKGRKEMMEMFykLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPreIFAD 236
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
931-1136 |
8.67e-35 |
|
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: 133.15 E-value: 8.67e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 931 VKNLVKVFEPSGRpAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIetNLDVVRQSLGMCPQ 1010
Cdd:cd03226 2 IENISFSYKKGTE-ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI--KAKERRKSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1011 HniLFHHL---TVAEHILFYAQLKGRSWEEAqlemEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDE 1087
Cdd:cd03226 79 D--VDYQLftdSVREELLLGLKELDAGNEQA----ETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 6671495 1088 PTSGVDPYSRRSIWDLLLK-YRSGRTIIMSTHHMDEADLLGDRIAIISQG 1136
Cdd:cd03226 153 PTSGLDYKNMERVGELIRElAAQGKAVIVITHDYEFLAKVCDRVLLLANG 202
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
941-1142 |
1.27e-34 |
|
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: 132.66 E-value: 1.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 941 SGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIETnldvVRQSLGMCPQH-NILFHH-L 1018
Cdd:cd03235 10 GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEK----ERKRIGYVPQRrSIDRDFpI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1019 TVAE--------HILFYAQLKGRSWEEAqlemEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTS 1090
Cdd:cd03235 86 SVRDvvlmglygHKGLFRRLSKADKAKV----DEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 6671495 1091 GVDPYSRRSIWDLLLKYRS-GRTIIMSTHHMDEADLLGDRIAIISqGRLYCSG 1142
Cdd:cd03235 162 GVDPKTQEDIYELLRELRReGMTILVVTHDLGLVLEYFDRVLLLN-RTVVASG 213
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
932-1138 |
2.05e-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: 2.05e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 932 KNLVKVFePSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDI----ETNLDVVRQSLGM 1007
Cdd:cd03292 4 INVTKTY-PNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVsdlrGRAIPYLRRKIGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1008 CPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDE 1087
Cdd:cd03292 83 VFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 6671495 1088 PTSGVDPYSRRSIWDLLLKY-RSGRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
Cdd:cd03292 163 PTGNLDPDTTWEIMNLLKKInKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
949-1140 |
2.30e-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: 132.39 E-value: 2.30e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPP---TSGTVLIGGKdiETNLDVVRQSLGMCPQHNILFHHLTVAEHIL 1025
Cdd:cd03234 26 VSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQ--PRKPDQFQKCVAYVRQDDILLPGLTVRETLT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1026 FYAQLK-GRSWEEAQLEMEA---MLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTSGVDPYSRRSIW 1101
Cdd:cd03234 104 YTAILRlPRKSSDAIRKKRVedvLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLV 183
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 6671495 1102 DLLLKY-RSGRTIIMSTHHmDEADL--LGDRIAIISQGRL-YC 1140
Cdd:cd03234 184 STLSQLaRRNRIVILTIHQ-PRSDLfrLFDRILLLSSGEIvYS 225
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
942-1168 |
3.03e-34 |
|
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: 136.52 E-value: 3.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 942 GRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIeTNLD------VVRQSLGMCPQHNILF 1015
Cdd:TIGR01186 5 GKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENI-MKQSpvelreVRRKKIGMVFQQFALF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1016 HHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTSGVDPY 1095
Cdd:TIGR01186 84 PHMTILQNTSLGPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSALDPL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6671495 1096 SRRSIWDLLLKYRS--GRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFLKNCFGTGFYLTLVRKMKNIQS 1168
Cdd:TIGR01186 164 IRDSMQDELKKLQAtlQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIGKVDLSQV 238
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1938-2146 |
1.43e-33 |
|
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: 127.75 E-value: 1.43e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1938 KLNELTKVYSGSssPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-SISDVHQNMGYC 2016
Cdd:cd00267 1 EIENLSFRYGGR--TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKlPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2017 PQFdaiddlltgrehlylyarlrgvpskeiekvanwgiqslglslyadrlagtySGGNKRKLSTAIALTGCPPLLLLDEP 2096
Cdd:cd00267 79 PQL---------------------------------------------------SGGQRQRVALARALLLNPDLLLLDEP 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 6671495 2097 TTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGT 2146
Cdd:cd00267 108 TSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
948-1142 |
1.46e-33 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 129.92 E-value: 1.46e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 948 RLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIeTNLDVVRQSLGMCPQHNILFHHLTVAEHILFY 1027
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDV-TAAPPADRPVSMLFQENNLFAHLTVEQNVGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1028 AQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTSGVDPYSRRSIWDLLLKY 1107
Cdd:cd03298 95 LSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDL 174
|
170 180 190
....*....|....*....|....*....|....*..
gi 6671495 1108 R--SGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSG 1142
Cdd:cd03298 175 HaeTKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1932-2155 |
2.03e-33 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 130.59 E-value: 2.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1932 NKTDILKLNELTKVYSGSssPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIltsiSDVHQ 2011
Cdd:COG1121 2 MMMPAIELENLTVSYGGR--PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP----RRARR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2012 NMGYCPQFDAIDDL--LTGRE--HLYLYAR---LRGVPSKEIEKVANWgIQSLGLSLYADRLAGTYSGGNKRKLSTAIAL 2084
Cdd:COG1121 76 RIGYVPQRAEVDWDfpITVRDvvLMGRYGRrglFRRPSRADREAVDEA-LERVGLEDLADRPIGELSGGQQQRVLLARAL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6671495 2085 TGCPPLLLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGTFqCLGTIQH 2155
Cdd:COG1121 155 AQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLV-AHGPPEE 224
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1937-2152 |
2.08e-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: 130.25 E-value: 2.08e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1937 LKLNELTKVYSGSSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT---------SIS 2007
Cdd:cd03219 1 LEVRGLTKRFGGLV--ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGlppheiarlGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2008 DVHQNMGYCPQFDAIDDLLTG----REHLYLYARLRGVPSKEIEKVANWgIQSLGLSLYADRLAGTYSGGNKRKLSTAIA 2083
Cdd:cd03219 79 RTFQIPRLFPELTVLENVMVAaqarTGSGLLLARARREEREARERAEEL-LERVGLADLADRPAGELSYGQQRRLEIARA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6671495 2084 LTGCPPLLLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGTFQCLGT 2152
Cdd:cd03219 158 LATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGT 226
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
902-1144 |
2.08e-33 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 138.37 E-value: 2.08e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 902 EEMEDPEHPegmndsffeRELPGLVPGVCVKNLVkvFE-PSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLL 980
Cdd:COG1132 322 PEIPDPPGA---------VPLPPVRGEIEFENVS--FSyPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFY 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 981 PPTSGTVLIGGKDI-ETNLDVVRQSLGMCPQHNILFhHLTVAEHILFyaqlkGRswEEAQLE--MEAM-----------L 1046
Cdd:COG1132 391 DPTSGRILIDGVDIrDLTLESLRRQIGVVPQDTFLF-SGTIRENIRY-----GR--PDATDEevEEAAkaaqahefieaL 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1047 EDtGLHHKRNEEAQDLSGGmQR-KLSVAIAFVGDSKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTH------H 1119
Cdd:COG1132 463 PD-GYDTVVGERGVNLSGG-QRqRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHrlstirN 540
|
250 260
....*....|....*....|....*
gi 6671495 1120 MdeadllgDRIAIISQGRLYCSGTP 1144
Cdd:COG1132 541 A-------DRILVLDDGRIVEQGTH 558
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1937-2145 |
3.34e-33 |
|
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: 128.79 E-value: 3.34e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1937 LKLNELTKVYSgsSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIlTSISDVHQNMGYC 2016
Cdd:cd03259 1 LELKGLSKTYG--SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV-TGVPPERRNIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2017 PQFDAIDDLLTGREHLYLYARLRGVPSKEIEKVANWGIQSLGLSLYADRLAGTYSGGNKRKLSTAIALTGCPPLLLLDEP 2096
Cdd:cd03259 78 FQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 6671495 2097 TTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKG 2145
Cdd:cd03259 158 LSALDAKLREELREELKELQRElGITTIYVTHDQEEALALADRIAVMNEG 207
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
945-1144 |
3.59e-33 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 140.64 E-value: 3.59e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGK-----DIETnldvvRQSLGMCPQHNILFHHLT 1019
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQpvdagDIAT-----RRRVGYMSQAFSLYGELT 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1020 VAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTSGVDPYSRRS 1099
Cdd:NF033858 356 VRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDM 435
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 6671495 1100 IWDLL--LKYRSGRTIIMSTHHMDEAdLLGDRIAIISQGRLYCSGTP 1144
Cdd:NF033858 436 FWRLLieLSREDGVTIFISTHFMNEA-ERCDRISLMHAGRVLASDTP 481
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
960-1144 |
5.96e-33 |
|
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: 128.99 E-value: 5.96e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 960 AFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIeTNLDVVRQSLGMCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQ 1039
Cdd:cd03299 29 VILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDI-TNLPPEKRDISYVPQNYALFPHMTVYKNIAYGLKKRKVDKKEIE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1040 LEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTSGVDPYSRRSIWDLLLKYR--SGRTIIMST 1117
Cdd:cd03299 108 RKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRkeFGVTVLHVT 187
|
170 180
....*....|....*....|....*..
gi 6671495 1118 HHMDEADLLGDRIAIISQGRLYCSGTP 1144
Cdd:cd03299 188 HDFEEAWALADKVAIMLNGKLIQVGKP 214
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
929-1138 |
6.57e-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: 127.76 E-value: 6.57e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 929 VCVKNLVKVFEpsGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIeTNLDVVRQSLGMC 1008
Cdd:cd03301 1 VELENVTKRFG--NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDV-TDLPPKDRDIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1009 PQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEP 1088
Cdd:cd03301 78 FQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 6671495 1089 TSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
Cdd:cd03301 158 LSNLDAKLRVQMRAELkrLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
931-1138 |
7.03e-33 |
|
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: 127.65 E-value: 7.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 931 VKNLVKVFepSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDI---ETNLDVVRQSLGM 1007
Cdd:cd03262 3 IKNLHKSF--GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtddKKNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1008 CPQHNILFHHLTVAEHI-LFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLD 1086
Cdd:cd03262 81 VFQQFNLFPHLTVLENItLAPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 6671495 1087 EPTSGVDPYSRRSIWDLLLKY-RSGRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
Cdd:cd03262 161 EPTSALDPELVGEVLDVMKDLaEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
944-1144 |
1.87e-32 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 127.41 E-value: 1.87e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 944 PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIeTNL---DVVRQSLGMCPQHNILFHHLTV 1020
Cdd:COG0410 17 HVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDI-TGLpphRIARLGIGYVPEGRRIFPSLTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1021 AEHILFyAQLKGRSWEEAQLEMEAMLE---DtgLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTSGVDPYSR 1097
Cdd:COG0410 96 EENLLL-GAYARRDRAEVRADLERVYElfpR--LKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIV 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 6671495 1098 RSIWDLL--LKyRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
Cdd:COG0410 173 EEIFEIIrrLN-REGVTILLVEQNARFALEIADRAYVLERGRIVLEGTA 220
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
931-1143 |
3.49e-32 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 129.81 E-value: 3.49e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 931 VKNLVKVFEPSGRP--AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIeTNLD-----VVRQ 1003
Cdd:COG1135 4 LENLSKTFPTKGGPvtALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDL-TALSerelrAARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1004 SLGMCPQH-NiLFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNE-EAQdLSGGM-QRklsVAIA--FVG 1078
Cdd:COG1135 83 KIGMIFQHfN-LLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAyPSQ-LSGGQkQR---VGIAraLAN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6671495 1079 DSKVVVLDEPTSGVDPYSRRSIWDLLLKYRS--GRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGT 1143
Cdd:COG1135 158 NPKVLLCDEATSALDPETTRSILDLLKDINRelGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGP 224
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
928-1144 |
6.84e-32 |
|
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: 125.91 E-value: 6.84e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 928 GVCVKNLVKVFEpsGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIeTNLDVVRQSLGM 1007
Cdd:cd03296 2 SIEVRNVSKRFG--DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDA-TDVPVQERNVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1008 CPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEA----MLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVV 1083
Cdd:cd03296 79 VFQHYALFRHMTVFDNVAFGLRVKPRSERPPEAEIRAkvheLLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6671495 1084 VLDEPTSGVDPYSRRSI--WDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
Cdd:cd03296 159 LLDEPFGALDAKVRKELrrWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTP 221
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
1603-1894 |
7.38e-32 |
|
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: 129.05 E-value: 7.38e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1603 DFLKHLET--TDNIKVWFNNKGWHALVSFLNVAHNAILRASLPRDRDPEEYGITVISQPLNLTKEQLSditvLTTSVDAV 1680
Cdd:pfam12698 88 GFSKDLLKgeSATVTVYINSSNLLVSKLILNALQSLLQQLNASALVLLLEALSTSAPIPVESTPLFNP----QSGYAYYL 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1681 VAICVIFAMSFVPASFVLYLIQERVTKAKHLQFISGVSPTTYWLTNFLWDIMNYAVSAGLVVGIFIGFqkkaYTSPDNLP 1760
Cdd:pfam12698 164 VGLILMIIILIGAAIIAVSIVEEKESRIKERLLVSGVSPLQYWLGKILGDFLVGLLQLLIILLLLFGI----GIPFGNLG 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1761 ALVSLLMLYGWAVIPMMYPASFLFEVPSTAYVALSCANLFIGInSSAITFVLELFENnrtllrfnaMLRKLLIVFPHFCL 1840
Cdd:pfam12698 240 LLLLLFLLYGLAYIALGYLLGSLFKNSEDAQSIIGIVILLLSG-FFGGLFPLEDPPS---------FLQWIFSIIPFFSP 309
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 6671495 1841 GRGLIDLALsqavTDVYAQfgeeysanpfqwdlIGKNLVAMAIEGVVYFLLTLL 1894
Cdd:pfam12698 310 IDGLLRLIY----GDSLWE--------------IAPSLIILLLFAVVLLLLALL 345
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
940-1138 |
9.58e-32 |
|
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: 123.82 E-value: 9.58e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 940 PSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPP--TSGTVLIGGKDIEtnLDVVRQSLGMCPQHNILFHH 1017
Cdd:cd03213 19 KSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRPLD--KRSFRKIIGYVPQDDILHPT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1018 LTVAEHILFYAQLKGrsweeaqlemeamledtglhhkrneeaqdLSGGMQRKLSVAIAFVGDSKVVVLDEPTSGVDPYSR 1097
Cdd:cd03213 97 LTVRETLMFAAKLRG-----------------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 6671495 1098 RSIWDLLLKYRS-GRTIIMSTHH-MDEADLLGDRIAIISQGRL 1138
Cdd:cd03213 148 LQVMSLLRRLADtGRTIICSIHQpSSEIFELFDKLLLLSQGRV 190
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
931-1145 |
3.07e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 125.10 E-value: 3.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 931 VKNLVKVFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIET-NLDVVRQSLGmcp 1009
Cdd:PRK13632 10 VENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKeNLKEIRKKIG--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1010 qhnILFHH-------LTVAEHILFyaqlkgrSWEEAQL---EMEAMLED----TGLHHKRNEEAQDLSGGM-QRklsVAI 1074
Cdd:PRK13632 87 ---IIFQNpdnqfigATVEDDIAF-------GLENKKVppkKMKDIIDDlakkVGMEDYLDKEPQNLSGGQkQR---VAI 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6671495 1075 AFV--GDSKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGR--TIIMSTHHMDEAdLLGDRIAIISQGRLYCSGTPL 1145
Cdd:PRK13632 154 ASVlaLNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkkTLISITHDMDEA-ILADKVIVFSEGKLIAQGKPK 227
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1961-2098 |
7.95e-31 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 119.67 E-value: 7.95e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1961 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIL-TSISDVHQNMGYCPQFDAIDDLLTGREHLYLYARLR 2039
Cdd:pfam00005 8 LNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTdDERKSLRKEIGYVFQDPQLFPRLTVRENLRLGLLLK 87
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6671495 2040 GVPSKEIEKVANWGIQSLGLSLYADRLAG----TYSGGNKRKLSTAIALTGCPPLLLLDEPTT 2098
Cdd:pfam00005 88 GLSKREKDARAEEALEKLGLGDLADRPVGerpgTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
931-1144 |
1.26e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 123.26 E-value: 1.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 931 VKNLVKVFePSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIETN---LDVVRQSLGM 1007
Cdd:PRK13639 4 TRDLKYSY-PDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDkksLLEVRKTVGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1008 CPQH--NILFHHlTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVL 1085
Cdd:PRK13639 83 VFQNpdDQLFAP-TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1086 DEPTSGVDPYSRRSIWDLLLKY-RSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
Cdd:PRK13639 162 DEPTSGLDPMGASQIMKLLYDLnKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTP 221
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1936-2146 |
1.67e-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: 122.45 E-value: 1.67e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1936 ILKLNELTKVYSGSssPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIlTSISdVH----- 2010
Cdd:COG0411 4 LLEVRGLTKRFGGL--VAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDI-TGLP-PHriarl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2011 ------QNMGYCPQFDAIDDLLTGREH------LYLYARLRGVPSKE---IEKVANWgIQSLGLSLYADRLAGTYSGGNK 2075
Cdd:COG0411 80 giartfQNPRLFPELTVLENVLVAAHArlgrglLAALLRLPRARREEreaRERAEEL-LERVGLADRADEPAGNLSYGQQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6671495 2076 RKLSTAIALTGCPPLLLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGT 2146
Cdd:COG0411 159 RRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErGITILLIEHDMDLVMGLADRIVVLDFGR 230
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
940-1144 |
2.20e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 123.03 E-value: 2.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 940 PSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIETN---LDVVRQSLGMCPQH--NIL 1014
Cdd:PRK13636 16 SDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSrkgLMKLRESVGMVFQDpdNQL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1015 FhHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTSGVDP 1094
Cdd:PRK13636 96 F-SASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDP 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 6671495 1095 YSRRSIWDLLLKYRS--GRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
Cdd:PRK13636 175 MGVSEIMKLLVEMQKelGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNP 226
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1938-2151 |
2.31e-30 |
|
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: 120.72 E-value: 2.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1938 KLNELTKVYSGSssPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIltsiSDVHQNMGYCP 2017
Cdd:cd03235 1 EVEDLTVSYGGH--PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPL----EKERKRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2018 QFDAID--------DL-LTGRehlYLYARLRGVPSKEIEKVANWGIQSLGLSLYADRLAGTYSGGNKRKLSTAIALTGCP 2088
Cdd:cd03235 75 QRRSIDrdfpisvrDVvLMGL---YGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDP 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6671495 2089 PLLLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRlAIMVKGTFQCLG 2151
Cdd:cd03235 152 DLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDR-VLLLNRTVVASG 213
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
893-1124 |
2.61e-30 |
|
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: 128.17 E-value: 2.61e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 893 ALEKTEPLTEEMEDPEHPEgmndsffeRELPGLVPGVCVKNLVKVFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTT 972
Cdd:TIGR02857 293 AAEALFAVLDAAPRPLAGK--------APVTAAPASSLEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTL 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 973 LSILTGLLPPTSGTVLIGGKDI-ETNLDVVRQSLGMCPQHNILFHHlTVAEHILFY------AQLKGRSWEEAQLEMEAM 1045
Cdd:TIGR02857 365 LNLLLGFVDPTEGSIAVNGVPLaDADADSWRDQIAWVPQHPFLFAG-TIAENIRLArpdasdAEIREALERAGLDEFVAA 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1046 LEDtGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTH---HMDE 1122
Cdd:TIGR02857 444 LPQ-GLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHrlaLAAL 522
|
..
gi 6671495 1123 AD 1124
Cdd:TIGR02857 523 AD 524
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1936-2152 |
7.64e-30 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 120.53 E-value: 7.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1936 ILKLNELTKVYSGSssPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-SISDVHQNMG 2014
Cdd:COG1120 1 MLEAENLSVGYGGR--PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASlSRRELARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2015 YCPQFDAIDDLLT-------GRehlYLYARLRGVPSKEIEKVANWGIQSLGLSLYADRLAGTYSGGNKRKLSTAIALTGC 2087
Cdd:COG1120 79 YVPQEPPAPFGLTvrelvalGR---YPHLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6671495 2088 PPLLLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGTFQCLGT 2152
Cdd:COG1120 156 PPLLLLDEPTSHLDLAHQLEVLELLRRLARErGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGP 221
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
931-1144 |
7.99e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 121.31 E-value: 7.99e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 931 VKNLVKVFEPsGRP----AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDI---ETNLDVVRQ 1003
Cdd:PRK13637 5 IENLTHIYME-GTPfekkALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdkKVKLSDIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1004 SLGMC---PQHNiLFHHlTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHK--RNEEAQDLSGGMQRKLSVAIAFVG 1078
Cdd:PRK13637 84 KVGLVfqyPEYQ-LFEE-TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDYEdyKDKSPFELSGGQKRRVAIAGVVAM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6671495 1079 DSKVVVLDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
Cdd:PRK13637 162 EPKILILDEPTAGLDPKGRDEILNKIkeLHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTP 229
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1937-2145 |
1.14e-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: 119.18 E-value: 1.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1937 LKLNELTKVYSgsSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIltSISDVHQ----N 2012
Cdd:cd03218 1 LRAENLSKRYG--KRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDI--TKLPMHKrarlG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2013 MGYCPQFDAIDDLLTGREHLYLYARLRGVPSKEIEKVANWGIQSLGLSLYADRLAGTYSGGNKRKLSTAIALTGCPPLLL 2092
Cdd:cd03218 77 IGYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 6671495 2093 LDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2145
Cdd:cd03218 157 LDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEG 209
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
940-1144 |
1.32e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 120.62 E-value: 1.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 940 PSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIET---NLDV--VRQSLGMCPQ--HN 1012
Cdd:PRK13649 17 PFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITStskNKDIkqIRKKVGLVFQfpES 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1013 ILFHHlTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHK-RNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTSG 1091
Cdd:PRK13649 97 QLFEE-TVLKDVAFGPQNFGVSQEEAEALAREKLALVGISESlFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 6671495 1092 VDPYSRRSIWDLLLK-YRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
Cdd:PRK13649 176 LDPKGRKELMTLFKKlHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKP 229
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
932-1144 |
1.48e-29 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 119.23 E-value: 1.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 932 KNLVKVFEpsGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIeTNLDV---VRQSLGMC 1008
Cdd:PRK10895 7 KNLAKAYK--GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDI-SLLPLharARRGIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1009 PQHNILFHHLTVAEHILFYAQL-KGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDE 1087
Cdd:PRK10895 84 PQEASIFRRLSVYDNLMAVLQIrDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 6671495 1088 PTSGVDPYSRRSIWDLLLKYR-SGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
Cdd:PRK10895 164 PFAGVDPISVIDIKRIIEHLRdSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTP 221
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
931-1138 |
1.53e-29 |
|
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: 119.52 E-value: 1.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 931 VKNLVKVFEPSGR--PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIETNLD-VVRQSLGM 1007
Cdd:COG1124 4 VRNLSVSYGQGGRrvPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRkAFRRRVQM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1008 CPQHNIL-FH-HLTVAEHILFYAQLKGRSWEEAQLEmeAMLEDTGLH----HKRNEEaqdLSGG-MQRklsVAI--AFVG 1078
Cdd:COG1124 84 VFQDPYAsLHpRHTVDRILAEPLRIHGLPDREERIA--ELLEQVGLPpsflDRYPHQ---LSGGqRQR---VAIarALIL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6671495 1079 DSKVVVLDEPTSGVDPYSRRSIWDLLLKYR--SGRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
Cdd:COG1124 156 EPELLLLDEPTSALDVSVQAEILNLLKDLReeRGLTYLFVSHDLAVVAHLCDRVAVMQNGRI 217
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
941-1149 |
1.63e-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: 118.87 E-value: 1.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 941 SGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIET-NLDVVRQSLGMCPQHNILFHHlT 1019
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDiSRKSLRSMIGVVLQDTFLFSG-T 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1020 VAEHILFyaqlkGRSWEEAQLEMEAM-----------LEDtGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEP 1088
Cdd:cd03254 93 IMENIRL-----GRPNATDEEVIEAAkeagahdfimkLPN-GYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6671495 1089 TSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMD---EAdllgDRIAIISQGRLYCSGTP--LFLKN 1149
Cdd:cd03254 167 TSNIDTETEKLIQEALEKLMKGRTSIIIAHRLStikNA----DKILVLDDGKIIEEGTHdeLLAKK 228
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
929-1138 |
4.33e-29 |
|
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: 115.22 E-value: 4.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 929 VCVKNLVKVFepSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIETN--LDVVRQSLG 1006
Cdd:cd03216 1 LELRGITKRF--GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFAspRDARRAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1007 MCPQhnilfhhltvaehilfyaqlkgrsweeaqlemeamledtglhhkrneeaqdLSGGMQRKLSVAIAFVGDSKVVVLD 1086
Cdd:cd03216 79 MVYQ---------------------------------------------------LSVGERQMVEIARALARNARLLILD 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 6671495 1087 EPTSGVDPYSRRSIWDLLLKYRS-GRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
Cdd:cd03216 108 EPTAALTPAEVERLFKVIRRLRAqGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
931-1138 |
4.76e-29 |
|
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: 116.92 E-value: 4.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 931 VKNLVKVFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIET-NLDVVRQSLGMCP 1009
Cdd:cd03245 5 FRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQlDPADLRRNIGYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1010 QHNILFHHlTVAEHILFyaqlkGRSWEEAQLEMEAMlEDTGLH-----HKR------NEEAQDLSGGMQRKLSVAIAFVG 1078
Cdd:cd03245 85 QDVTLFYG-TLRDNITL-----GAPLADDERILRAA-ELAGVTdfvnkHPNgldlqiGERGRGLSGGQRQAVALARALLN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1079 DSKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLgDRIAIISQGRL 1138
Cdd:cd03245 158 DPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLV-DRIIVMDSGRI 216
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
932-1138 |
6.79e-29 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 120.29 E-value: 6.79e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 932 KNLVKVFEPSGRP--AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIeTNLDV-----VRQS 1004
Cdd:PRK11153 5 KNISKVFPQGGRTihALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDL-TALSEkelrkARRQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1005 LGMCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGM-QRklsVAIA--FVGDSK 1081
Cdd:PRK11153 84 IGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQkQR---VAIAraLASNPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 6671495 1082 VVVLDEPTSGVDPYSRRSIWDLLLKY--RSGRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
Cdd:PRK11153 161 VLLCDEATSALDPATTRSILELLKDInrELGLTIVLITHEMDVVKRICDRVAVIDAGRL 219
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
931-1138 |
9.96e-29 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 122.82 E-value: 9.96e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 931 VKNLVKVFepSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIE--TNLDVVRQSLGMC 1008
Cdd:COG1129 7 MRGISKSF--GGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRfrSPRDAQAAGIAII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1009 PQHNILFHHLTVAEHILFYAQLKGR---SWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGmQRKLsVAI--AFVGDSKVV 1083
Cdd:COG1129 85 HQELNLVPNLSVAENIFLGREPRRGgliDWRAMRRRARELLARLGLDIDPDTPVGDLSVA-QQQL-VEIarALSRDARVL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 6671495 1084 VLDEPTSGVDPYSRRSIWDLLLKYRS-GRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
Cdd:COG1129 163 ILDEPTASLTEREVERLFRIIRRLKAqGVAIIYISHRLDEVFEIADRVTVLRDGRL 218
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1961-2145 |
1.21e-28 |
|
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: 115.99 E-value: 1.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1961 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI--LTSISDVHQNMGYCPQFDAIDDLLTGREHLYL--YA 2036
Cdd:cd03224 23 VPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDItgLPPHERARAGIGYVPEGRRIFPELTVEENLLLgaYA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2037 RLRGVPSKEIEKVanwgiqslgLSLY------ADRLAGTYSGGNKRKLSTAIALTGCPPLLLLDEPTTGMDPQARRMLWN 2110
Cdd:cd03224 103 RRRAKRKARLERV---------YELFprlkerRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIFE 173
|
170 180 190
....*....|....*....|....*....|....*
gi 6671495 2111 TIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2145
Cdd:cd03224 174 AIRELRDEGVTILLVEQNARFALEIADRAYVLERG 208
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
948-1139 |
1.23e-28 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 116.39 E-value: 1.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 948 RLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIeTNLDVVRQSLGMCPQHNILFHHLTVAEHILFY 1027
Cdd:COG3840 17 RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDL-TALPPAERPVSMLFQENNLFPHLTVAQNIGLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1028 AQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGG-MQRklsVAIA--FVGDSKVVVLDEPTSGVDPYSRRSIWDLL 1104
Cdd:COG3840 96 LRPGLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGqRQR---VALArcLVRKRPILLLDEPFSALDPALRQEMLDLV 172
|
170 180 190
....*....|....*....|....*....|....*..
gi 6671495 1105 --LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLY 1139
Cdd:COG3840 173 deLCRERGLTVLMVTHDPEDAARIADRVLLVADGRIA 209
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1934-2156 |
2.76e-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: 121.93 E-value: 2.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1934 TDILKLNELTKVYSGSSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTG---DTTVTSGDATVAGKSILT-SISDV 2009
Cdd:COG1123 2 TPLLEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGllpHGGRISGEVLLDGRDLLElSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2010 HQNMGYCPQ-FDAIDDLLTGREHLYLYARLRGVPSKEIEKVANWGIQSLGLSLYADRLAGTYSGGNKRKLSTAIALTGCP 2088
Cdd:COG1123 82 GRRIGMVFQdPMTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6671495 2089 PLLLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGTFQCLGTIQHL 2156
Cdd:COG1123 162 DLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1937-2189 |
4.96e-28 |
|
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: 114.71 E-value: 4.96e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1937 LKLNELTKVYsGSSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT--------SISD 2008
Cdd:cd03295 1 IEFENVTKRY-GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREqdpvelrrKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2009 VHQNMGYCPQFdaiddllTGREHLYLYARLRGVPSKEIEKVANWGIQSLGL--SLYADRLAGTYSGGNKRKLSTAIALTG 2086
Cdd:cd03295 80 VIQQIGLFPHM-------TVEENIALVPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2087 CPPLLLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGTFQCLGTIQHLkykfgdgyi 2165
Cdd:cd03295 153 DPPLLLMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEI--------- 223
|
250 260
....*....|....*....|....
gi 6671495 2166 vtmkIKSPKDDLlpdlnpVEQFFQ 2189
Cdd:cd03295 224 ----LRSPANDF------VAEFVG 237
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
944-1138 |
7.60e-28 |
|
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: 113.97 E-value: 7.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 944 PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIETNLDVVRQSLG-MCPQHNILFHHLTVAE 1022
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGvVFGQKTQLWWDLPVID 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1023 HILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTSGVDPYSRRSIWD 1102
Cdd:cd03267 115 SFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRN 194
|
170 180 190
....*....|....*....|....*....|....*...
gi 6671495 1103 LLLKYRSGR--TIIMSTHHMDEADLLGDRIAIISQGRL 1138
Cdd:cd03267 195 FLKEYNRERgtTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1937-2145 |
1.14e-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: 112.97 E-value: 1.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1937 LKLNELTKVYSGSS--SPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIlTSISDV----- 2009
Cdd:cd03255 1 IELKNLSKTYGGGGekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDI-SKLSEKelaaf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2010 -HQNMGYCPQFDAIDDLLTGREHLYLYARLRGVPSKEIEKVANWGIQSLGLSLYADRLAGTYSGGNKRKLSTAIALTGCP 2088
Cdd:cd03255 80 rRRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 6671495 2089 PLLLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEEcEALCTRLAIMVKG 2145
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHDPEL-AEYADRIIELRDG 216
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
927-1138 |
1.77e-27 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 119.36 E-value: 1.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 927 PGVCVKNLVKVFepsgrPAV---DRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGK--DIETNLDVV 1001
Cdd:COG3845 4 PALELRGITKRF-----GGVvanDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKpvRIRSPRDAI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1002 RQSLGMCPQHNILFHHLTVAEHI-LFYAQLKGR--SWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKlsVAI--AF 1076
Cdd:COG3845 79 ALGIGMVHQHFMLVPNLTVAENIvLGLEPTKGGrlDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQR--VEIlkAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6671495 1077 VGDSKVVVLDEPTSGVDPYSRRSIWDLLLKYRS-GRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
Cdd:COG3845 157 YRGARILILDEPTAVLTPQEADELFEILRRLAAeGKSIIFITHKLREVMAIADRVTVLRRGKV 219
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1936-2145 |
4.07e-27 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 112.04 E-value: 4.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1936 ILKLNELTKVYSGSssPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIlTSISdVHQ---- 2011
Cdd:COG1137 3 TLEAENLVKSYGKR--TVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDI-THLP-MHKrarl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2012 NMGYCPQFDAIDDLLTGREHLYLYARLRGVPSKEIEKVANWGIQSLGLSLYADRLAGTYSGGNKRKLSTAIALTGCPPLL 2091
Cdd:COG1137 79 GIGYLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFI 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6671495 2092 LLDEPTTGMDPQArrmlwntiVS----IIRE----GRAVVLTSHSMEECEALCTRLAIMVKG 2145
Cdd:COG1137 159 LLDEPFAGVDPIA--------VAdiqkIIRHlkerGIGVLITDHNVRETLGICDRAYIISEG 212
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1953-2142 |
4.63e-27 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 120.61 E-value: 4.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1953 AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTSISDVHQNMGYCPQ-FdaidDL---LTG 2028
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIATRRRVGYMSQaF----SLygeLTV 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2029 REHLYLYARLRGVPSKEIEKVANWGIQSLGLSLYADRLAGTYSGGNKRKLSTAIALTGCPPLLLLDEPTTGMDPQARRML 2108
Cdd:NF033858 357 RQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMF 436
|
170 180 190
....*....|....*....|....*....|....*
gi 6671495 2109 WNTIVSIIREGRAVVLTS-HSMEECEaLCTRLAIM 2142
Cdd:NF033858 437 WRLLIELSREDGVTIFIStHFMNEAE-RCDRISLM 470
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
942-1142 |
7.10e-27 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 111.71 E-value: 7.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 942 GRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSG-TVLIGGKDI-ETNLDVVRQSLGMC-PQ-HNILFHH 1017
Cdd:COG1119 15 GKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRgGEDVWELRKRIGLVsPAlQLRFPRD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1018 LTVAEHIL--FYAQLkGRsWEEAQLEMEA----MLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTSG 1091
Cdd:COG1119 95 ETVLDVVLsgFFDSI-GL-YREPTDEQRErareLLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAG 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 6671495 1092 VDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSG 1142
Cdd:COG1119 173 LDLGARELLLALLdkLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAG 225
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
931-1144 |
9.47e-27 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 112.42 E-value: 9.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 931 VKNLVKVFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGK--DIETNLDVVRQsLGMC 1008
Cdd:PRK13635 8 VEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMvlSEETVWDVRRQ-VGMV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1009 PQH-NILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGmqRKLSVAIAFV--GDSKVVVL 1085
Cdd:PRK13635 87 FQNpDNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGG--QKQRVAIAGVlaLQPDIIIL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6671495 1086 DEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEAdLLGDRIAIISQGRLYCSGTP 1144
Cdd:PRK13635 165 DEATSMLDPRGRREVLETVrqLKEQKGITVLSITHDLDEA-AQADRVIVMNKGEILEEGTP 224
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
942-1123 |
1.20e-26 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 109.25 E-value: 1.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 942 GRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDietnldvvrqSLGMCPQHNILFHHL--T 1019
Cdd:NF040873 4 GRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGA----------RVAYVPQRSEVPDSLplT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1020 VAEHI---LF-YAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGG-MQRKLsVAIAFVGDSKVVVLDEPTSGVDP 1094
Cdd:NF040873 74 VRDLVamgRWaRRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGqRQRAL-LAQGLAQEADLLLLDEPTTGLDA 152
|
170 180 190
....*....|....*....|....*....|
gi 6671495 1095 YSRRSIWDLLLKYRS-GRTIIMSTHHMDEA 1123
Cdd:NF040873 153 ESRERIIALLAEEHArGATVVVVTHDLELV 182
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
902-1119 |
1.29e-26 |
|
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: 117.08 E-value: 1.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 902 EEMEDPEHPEGmnDSFFERELPGLV--PGVCVKNLvKVFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGL 979
Cdd:TIGR02868 308 VEVLDAAGPVA--EGSAPAAGAVGLgkPTLELRDL-SAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGL 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 980 LPPTSGTVLIGGKDIET-NLDVVRQSLGMCPQHNILFHHlTVAEHILFyaqlkGRSwEEAQLEMEAMLE----------- 1047
Cdd:TIGR02868 385 LDPLQGEVTLDGVPVSSlDQDEVRRRVSVCAQDAHLFDT-TVRENLRL-----ARP-DATDEELWAALErvgladwlral 457
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6671495 1048 DTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHH 1119
Cdd:TIGR02868 458 PDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHH 529
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
942-1144 |
1.43e-26 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 111.02 E-value: 1.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 942 GRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIE-TNLDVVRQSLGMCPQHNILFHHLTV 1020
Cdd:PRK13548 14 GRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLAdWSPAELARRRAVLPQHSSLSFPFTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1021 AEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGG-MQRklsVAIAFV--------GDSKVVVLDEPTSG 1091
Cdd:PRK13548 94 EEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGeQQR---VQLARVlaqlwepdGPPRWLLLDEPTSA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 6671495 1092 VDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
Cdd:PRK13548 171 LDLAHQHHVLRLArqLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTP 225
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1937-2142 |
1.83e-26 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 109.48 E-value: 1.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1937 LKLNELTKVYSGSSSP--AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIltsiSDVHQNMG 2014
Cdd:cd03293 1 LEVRNVSKTYGGGGGAvtALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPV----TGPGPDRG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2015 YCPQFDAIDDLLTGREHLYLYARLRGVPSKEIEKVANWGIQSLGLSLYADRLAGTYSGGNKRKLSTAIALTGCPPLLLLD 2094
Cdd:cd03293 77 YVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLD 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 6671495 2095 EPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIM 2142
Cdd:cd03293 157 EPFSALDALTREQLQEELLDIWREtGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1953-2177 |
1.84e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 112.49 E-value: 1.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1953 AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAG-------KSILTSISDVhqnMGycpQ-----FD 2020
Cdd:COG4586 37 AVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGyvpfkrrKEFARRIGVV---FG---QrsqlwWD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2021 aiddlLTGREHLYLYARLRGVPSKEIEKVANWGIQSLGLSLYADRLAgtysggnkRKLS--------TAIALTGCPPLLL 2092
Cdd:COG4586 111 -----LPAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGELLDTPV--------RQLSlgqrmrceLAAALLHRPKILF 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2093 LDEPTTGMDPQARRMLWNTIVSIIREGRA-VVLTSHSMEECEALCTRLAIMVKGTFQCLGTIQHLKYKFGDGYIVTMKIK 2171
Cdd:COG4586 178 LDEPTIGLDVVSKEAIREFLKEYNRERGTtILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEELKERFGPYKTIVLELA 257
|
....*.
gi 6671495 2172 SPKDDL 2177
Cdd:COG4586 258 EPVPPL 263
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
931-1138 |
2.18e-26 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 110.72 E-value: 2.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 931 VKNLVKVFEPSG--RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIeTNLDVVRqslGMC 1008
Cdd:COG4525 6 VRHVSVRYPGGGqpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPV-TGPGADR---GVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1009 PQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEP 1088
Cdd:COG4525 82 FQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 6671495 1089 TSGVDPYSRRSIWDLLLKY--RSGRTIIMSTHHMDEADLLGDRIAIIS--QGRL 1138
Cdd:COG4525 162 FGALDALTREQMQELLLDVwqRTGKGVFLITHSVEEALFLATRLVVMSpgPGRI 215
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1937-2152 |
2.31e-26 |
|
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: 109.63 E-value: 2.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1937 LKLNELTKVYSGSssPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT------SISDVH 2010
Cdd:cd03300 1 IELENVSKFYGGF--VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNlpphkrPVNTVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2011 QNMGYCPQFDAIDDLLTGrehlylyARLRGVPSKEIEKVANWGIQSLGLSLYADRLAGTYSGGNKRKLSTAIALTGCPPL 2090
Cdd:cd03300 79 QNYALFPHLTVFENIAFG-------LRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6671495 2091 LLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGTFQCLGT 2152
Cdd:cd03300 152 LLLDEPLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGT 214
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1936-2156 |
2.56e-26 |
|
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: 109.59 E-value: 2.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1936 ILKLNELTKVYSGSSS--PAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIlTSIS-----D 2008
Cdd:cd03258 1 MIELKNVSKVFGDTGGkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDL-TLLSgkelrK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2009 VHQNMGYCPQ-FDaiddLLTGR---EHLYLYARLRGVPSKEIEKVANWGIQSLGLSLYADRLAGTYSGGNKRKLSTAIAL 2084
Cdd:cd03258 80 ARRRIGMIFQhFN----LLSSRtvfENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARAL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6671495 2085 TGCPPLLLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGTFQCLGTIQHL 2156
Cdd:cd03258 156 ANNPKVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEV 228
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
925-1144 |
3.01e-26 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 113.39 E-value: 3.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 925 LVPGVCVKNLVKVFEpsGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIeTNLDVVRQS 1004
Cdd:PRK11607 16 LTPLLEIRNLTKSFD--GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDL-SHVPPYQRP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1005 LGMCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVV 1084
Cdd:PRK11607 93 INMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6671495 1085 LDEPTSGVDPYSRR----SIWDLLlkYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
Cdd:PRK11607 173 LDEPMGALDKKLRDrmqlEVVDIL--ERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEP 234
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
943-1144 |
4.61e-26 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 109.72 E-value: 4.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 943 RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIETNLD-VVRQSLGMCPQHNILFHHLTVA 1021
Cdd:PRK11231 15 KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSrQLARRLALLPQHHLTPEGITVR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1022 EHILF----YAQLKGR-SWEEAQLEMEAMlEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTSGVDPYS 1096
Cdd:PRK11231 95 ELVAYgrspWLSLWGRlSAEDNARVNQAM-EQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINH 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 6671495 1097 RRSIWDLLLKYRS-GRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
Cdd:PRK11231 174 QVELMRLMRELNTqGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTP 222
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1936-2156 |
5.13e-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: 115.00 E-value: 5.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1936 ILKLNELTKVYSGSSS---PAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT----SISD 2008
Cdd:COG1123 260 LLEVRNLSKRYPVRGKggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKlsrrSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2009 VHQNMGYCPQ--FDAIDDLLTGREHLYLYARLRGV-PSKEIEKVANWGIQSLGLSL-YADRLAGTYSGGNKRKLSTAIAL 2084
Cdd:COG1123 340 LRRRVQMVFQdpYSSLNPRMTVGDIIAEPLRLHGLlSRAERRERVAELLERVGLPPdLADRYPHELSGGQRQRVAIARAL 419
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6671495 2085 TGCPPLLLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGTFQCLGTIQHL 2156
Cdd:COG1123 420 ALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEV 492
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
941-1170 |
7.64e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 109.51 E-value: 7.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 941 SGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDI-ETNLDVVRQSLGMCPQH--NILFHH 1017
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPItKENIREVRKFVGLVFQNpdDQIFSP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1018 lTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTSGVDPYSR 1097
Cdd:PRK13652 95 -TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGV 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6671495 1098 RSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP--LFLKNCFGTGFYLTLVRKMKNIQSQR 1170
Cdd:PRK13652 174 KELIDFLndLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVeeIFLQPDLLARVHLDLPSLPKLIRSLQ 250
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
931-1138 |
9.05e-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: 106.36 E-value: 9.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 931 VKNLvkvfepSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIE--TNLDVVRQSLGMC 1008
Cdd:cd03215 7 VRGL------SVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTrrSPRDAIRAGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1009 P---QHNILFHHLTVAEHILFyaqlkgrsweeaqlemeamledtglhhkrneeAQDLSGGMQRKLSVAIAFVGDSKVVVL 1085
Cdd:cd03215 81 PedrKREGLVLDLSVAENIAL--------------------------------SSLLSGGNQQKVVLARWLARDPRVLIL 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 6671495 1086 DEPTSGVDPYSRRSIWDLLLKYRS-GRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
Cdd:cd03215 129 DEPTRGVDVGAKAEIYRLIRELADaGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
939-1166 |
9.72e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 109.41 E-value: 9.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 939 EPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDI--ETNLDVVRQSLGMC---PQHNI 1013
Cdd:PRK13633 19 ESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTsdEENLWDIRNKAGMVfqnPDNQI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1014 LfhHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTSGVD 1093
Cdd:PRK13633 99 V--ATIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLD 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6671495 1094 PYSRRSIWDLL--LKYRSGRTIIMSTHHMDEAdLLGDRIAIISQGRLYCSGTPlflKNCFGTgfyltlVRKMKNI 1166
Cdd:PRK13633 177 PSGRREVVNTIkeLNKKYGITIILITHYMEEA-VEADRIIVMDSGKVVMEGTP---KEIFKE------VEMMKKI 241
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1961-2145 |
1.13e-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: 108.25 E-value: 1.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1961 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSG-DATVAGKSI-LTSISDVHQNMGYC-----PQFD----AIDDLLTGr 2029
Cdd:COG1119 26 VKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRgGEDVWELRKRIGLVspalqLRFPrdetVLDVVLSG- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2030 ehlyLYA---RLRGVPSKEIEKVANWgIQSLGLSLYADRLAGTYSGGNKRKLSTAIALTGCPPLLLLDEPTTGMDPQARR 2106
Cdd:COG1119 105 ----FFDsigLYREPTDEQRERAREL-LELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARE 179
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 6671495 2107 MLWNTIVSIIREG-RAVVLTSHSMEECEALCTRLAIMVKG 2145
Cdd:COG1119 180 LLLALLDKLAAEGaPTLVLVTHHVEEIPPGITHVLLLKDG 219
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
949-1138 |
1.14e-25 |
|
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: 107.00 E-value: 1.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 949 LNITF-YENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGK-----DIETNLDVVRQSLGMCPQHNILFHHLTVAE 1022
Cdd:cd03297 15 LKIDFdLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfdsRKKINLPPQQRKIGLVFQQYALFPHLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1023 HILFyaQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTSGVDPYSRRSIWD 1102
Cdd:cd03297 95 NLAF--GLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLP 172
|
170 180 190
....*....|....*....|....*....|....*...
gi 6671495 1103 LL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
Cdd:cd03297 173 ELkqIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRL 210
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
931-1138 |
1.68e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 109.79 E-value: 1.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 931 VKNLVKVF-----EPSGR--------------PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGG 991
Cdd:COG4586 4 VENLSKTYrvyekEPGLKgalkglfrreyrevEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 992 KD-----IE--TNLDVVrqsLGmcpQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSG 1064
Cdd:COG4586 84 YVpfkrrKEfaRRIGVV---FG---QRSQLWWDLPAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGELLDTPVRQLSL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6671495 1065 GmQR-KLSVAIAFVGDSKVVVLDEPTSGVDPYSRRSIWDLLLKY--RSGRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
Cdd:COG4586 158 G-QRmRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYnrERGTTILLTSHDMDDIEALCDRVIVIDHGRI 233
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
945-1144 |
2.16e-25 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 107.77 E-value: 2.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIE--TNLDVVRQSLGMCPQHNILFHHLTVAE 1022
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEglPGHQIARMGVVRTFQHVRLFREMTVIE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1023 HILFyAQ------------LKGRSWEEAqlEMEAM------LEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVV 1084
Cdd:PRK11300 100 NLLV-AQhqqlktglfsglLKTPAFRRA--ESEALdraatwLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILM 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6671495 1085 LDEPTSGVDPYSRRSIWDLLLKYRS--GRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
Cdd:PRK11300 177 LDEPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTP 238
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
932-1144 |
2.42e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 108.38 E-value: 2.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 932 KNLVKVFEPsGRP----AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDI--ET---NLDVVR 1002
Cdd:PRK13641 6 ENVDYIYSP-GTPmekkGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItpETgnkNLKKLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1003 QSLGMCPQ--HNILFHHlTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHK-RNEEAQDLSGGMQRKLSVAIAFVGD 1079
Cdd:PRK13641 85 KKVSLVFQfpEAQLFEN-TVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDlISKSPFELSGGQMRRVAIAGVMAYE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6671495 1080 SKVVVLDEPTSGVDPYSRRSIWDLLLKY-RSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
Cdd:PRK13641 164 PEILCLDEPAAGLDPEGRKEMMQLFKDYqKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASP 229
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
942-1144 |
2.47e-25 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 107.51 E-value: 2.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 942 GRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIE--TNLDVVRQsLGMCPQHNILFHHLT 1019
Cdd:COG4559 13 GRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAawSPWELARR-RAVLPQHSSLAFPFT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1020 VAEHILF--YAQLKGRSwEEAQLEMEAMlEDTGLHHKRNEEAQDLSGG-MQRklsVAIAFV---------GDSKVVVLDE 1087
Cdd:COG4559 92 VEEVVALgrAPHGSSAA-QDRQIVREAL-ALVGLAHLAGRSYQTLSGGeQQR---VQLARVlaqlwepvdGGPRWLFLDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 6671495 1088 PTSGVDPYSRRSIWDLLLKY-RSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
Cdd:COG4559 167 PTSALDLAHQHAVLRLARQLaRRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTP 224
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
1961-2147 |
2.73e-25 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 105.67 E-value: 2.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1961 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-SISDVHQNMGYCPQ----FDAiddllTGREHLYLY 2035
Cdd:COG4619 23 LEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAmPPPEWRRQVAYVPQepalWGG-----TVRDNLPFP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2036 ARLRGVPSKEiEKVANWgIQSLGLSL-YADRLAGTYSGGNKRKLSTAIALTGCPPLLLLDEPTTGMDPQARRMLWNTIVS 2114
Cdd:COG4619 98 FQLRERKFDR-ERALEL-LERLGLPPdILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENTRRVEELLRE 175
|
170 180 190
....*....|....*....|....*....|....
gi 6671495 2115 IIRE-GRAVVLTSHSMEECEALCTRLAIMVKGTF 2147
Cdd:COG4619 176 YLAEeGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
931-1142 |
3.47e-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: 104.32 E-value: 3.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 931 VKNLVKVFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIETNLDVVRQSLGMCPQ 1010
Cdd:cd03247 3 INNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVLNQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1011 HNILFhhltvaehilfyaqlkgrsweeaqlemeamleDTGLhhkRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTS 1090
Cdd:cd03247 83 RPYLF--------------------------------DTTL---RNNLGRRFSGGERQRLALARILLQDAPIVLLDEPTV 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 6671495 1091 GVDPYSRRSIWDLLLKYRSGRTIIMSTHHmdeadLLG----DRIAIISQGRLYCSG 1142
Cdd:cd03247 128 GLDPITERQLLSLIFEVLKDKTLIWITHH-----LTGiehmDKILFLENGKIIMQG 178
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1937-2157 |
3.68e-25 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 106.81 E-value: 3.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1937 LKLNELTKVY--SGSSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTSIS-DVHQNM 2013
Cdd:COG1124 2 LEVRNLSVSYgqGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRkAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2014 GYCPQ--FDAIDDLLTGREHLYLYARLRGVPSKEiEKVANWgIQSLGLSL-YADRLAGTYSGGNKRKLSTAIALTGCPPL 2090
Cdd:COG1124 82 QMVFQdpYASLHPRHTVDRILAEPLRIHGLPDRE-ERIAEL-LEQVGLPPsFLDRYPHQLSGGQRQRVAIARALILEPEL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2091 LLLDEPTTGMDP--QARrmLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGTFQCLGTIQHLK 2157
Cdd:COG1124 160 LLLDEPTSALDVsvQAE--ILNLLKDLREErGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLL 227
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
942-1118 |
3.90e-25 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 105.34 E-value: 3.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 942 GRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIEtNLDVVRQS--LGmcpQHNILFHHLT 1019
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDID-DPDVAEAChyLG---HRNAMKPALT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1020 VAEHILFYAQLKGRsweeAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTSGVDPYSRRS 1099
Cdd:PRK13539 90 VAENLEFWAAFLGG----EELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVAL 165
|
170 180
....*....|....*....|
gi 6671495 1100 IWDLLLKYR-SGRTIIMSTH 1118
Cdd:PRK13539 166 FAELIRAHLaQGGIVIAATH 185
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
940-1144 |
4.00e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 107.90 E-value: 4.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 940 PSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGgkDI-------ETNLDVVRQSLGMCPQ-- 1010
Cdd:PRK13643 16 PFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVG--DIvvsstskQKEIKPVRKKVGVVFQfp 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1011 HNILFHHlTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQ-DLSGGMQRKLSVAIAFVGDSKVVVLDEPT 1089
Cdd:PRK13643 94 ESQLFEE-TVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPfELSGGQMRRVAIAGILAMEPEVLVLDEPT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 6671495 1090 SGVDPYSRRSIWDLLLK-YRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
Cdd:PRK13643 173 AGLDPKARIEMMQLFESiHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTP 228
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
955-1144 |
4.03e-25 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 110.51 E-value: 4.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 955 ENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIETNLD-----VVRQSLGMCPQHNILFHHLTVAEHILFYAQ 1029
Cdd:PRK10070 53 EGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDaelreVRRKKIAMVFQSFALMPHMTVLDNTAFGME 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1030 LKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTSGVDPYSRRSIWDLLLKYRS 1109
Cdd:PRK10070 133 LAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQA 212
|
170 180 190
....*....|....*....|....*....|....*..
gi 6671495 1110 G--RTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
Cdd:PRK10070 213 KhqRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTP 249
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
931-1143 |
5.11e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 106.35 E-value: 5.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 931 VKNLVKVFepSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIeTNLD---VVRQSLGM 1007
Cdd:COG4674 13 VEDLTVSF--DGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDL-TGLDeheIARLGIGR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1008 CPQHNILFHHLTVAEHIL--------FYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGD 1079
Cdd:COG4674 90 KFQKPTVFEELTVFENLElalkgdrgVFASLFARLTAEERDRIEEVLETIGLTDKADRLAGLLSHGQKQWLEIGMLLAQD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6671495 1080 SKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGT 1143
Cdd:COG4674 170 PKLLLLDEPVAGMTDAETERTAELLKSLAGKHSVVVVEHDMEFVRQIARKVTVLHQGSVLAEGS 233
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1961-2145 |
1.03e-24 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 104.54 E-value: 1.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1961 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKsiLTSISDVhqNMGYCPQfdaiddlLTGREHLYLYARLRG 2040
Cdd:cd03220 45 VPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR--VSSLLGL--GGGFNPE-------LTGRENIYLNGRLLG 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2041 VPSKEIEKVANWGIQSLGLSLYADRLAGTYSGGNKRKLSTAIALTGCPPLLLLDEPTTGMDPQARRMLWNTIVSIIREGR 2120
Cdd:cd03220 114 LSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGK 193
|
170 180
....*....|....*....|....*
gi 6671495 2121 AVVLTSHSMEECEALCTRLAIMVKG 2145
Cdd:cd03220 194 TVILVSHDPSSIKRLCDRALVLEKG 218
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
945-1158 |
1.20e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 106.40 E-value: 1.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDI-----ETNLDVVRQSLGMCPQ--HNILFHH 1017
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktkDKYIRPVRKRIGMVFQfpESQLFED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1018 lTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLhhKRNEEAQD---LSGGMQRKLSVAIAFVGDSKVVVLDEPTSGVDP 1094
Cdd:PRK13646 102 -TVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGF--SRDVMSQSpfqMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDP 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6671495 1095 YSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPlflKNCFGTGFYLT 1158
Cdd:PRK13646 179 QSKRQVMRLLksLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSP---KELFKDKKKLA 241
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
945-1144 |
1.27e-24 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 112.91 E-value: 1.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIETnlDVVRQSLG-----McPQ---HNiLFH 1016
Cdd:NF033858 16 ALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMAD--ARHRRAVCpriayM-PQglgKN-LYP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1017 HLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTSGVDPYS 1096
Cdd:NF033858 92 TLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLS 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 6671495 1097 RRSIWDLLLKYRSGR---TIIMSTHHMDEADLLgDRIAIISQGRLYCSGTP 1144
Cdd:NF033858 172 RRQFWELIDRIRAERpgmSVLVATAYMEEAERF-DWLVAMDAGRVLATGTP 221
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1936-2145 |
1.50e-24 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 104.12 E-value: 1.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1936 ILKLNELTKVYS--GSSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTS----ISDV 2009
Cdd:cd03257 1 LLEVKNLSVSFPtgGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLsrrlRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2010 HQNMGYCPQ--FDAIDDLLTGREHLY--LYARLRGVPSKEIEKVANWGIQSLGLSL-YADRLAGTYSGGNKRKLSTAIAL 2084
Cdd:cd03257 81 RKEIQMVFQdpMSSLNPRMTIGEQIAepLRIHGKLSKKEARKEAVLLLLVGVGLPEeVLNRYPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6671495 2085 TGCPPLLLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKG 2145
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAG 222
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1936-2152 |
2.40e-24 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 107.11 E-value: 2.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1936 ILKLNELTKVYSGSssPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKsiltSISDV--HQ-N 2012
Cdd:COG3842 5 ALELENVSKRYGDV--TALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGR----DVTGLppEKrN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2013 MGYCPQFDAIDDLLTGREHLYLYARLRGVPSKEIEKVANWGIQSLGLSLYADRLAGTYSGGNK------RklstAIALTg 2086
Cdd:COG3842 79 VGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQqrvalaR----ALAPE- 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6671495 2087 cPPLLLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGTFQCLGT 2152
Cdd:COG3842 154 -PRVLLLDEPLSALDAKLREEMREELRRLQRElGITFIYVTHDQEEALALADRIAVMNDGRIEQVGT 219
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1934-2145 |
2.83e-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: 103.91 E-value: 2.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1934 TDILKLNELTKVYSGSssPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTSISD--VHQ 2011
Cdd:COG0410 1 MPMLEVENLHAGYGGI--HVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHriARL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2012 NMGYCPQFDAIDDLLTGREHLYLYARLRGVPSKE---IEKVanwgiqslgLSLY------ADRLAGTYSGGNKRKLSTAI 2082
Cdd:COG0410 79 GIGYVPEGRRIFPSLTVEENLLLGAYARRDRAEVradLERV---------YELFprlkerRRQRAGTLSGGEQQMLAIGR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6671495 2083 ALTGCPPLLLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2145
Cdd:COG0410 150 ALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERG 212
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
1936-2156 |
3.08e-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: 103.89 E-value: 3.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1936 ILKLNELTKVYSgsSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIltSISDVHQ---- 2011
Cdd:TIGR04406 1 TLVAENLIKSYK--KRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDI--THLPMHErarl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2012 NMGYCPQFDAIDDLLTGREHLYLYARLRG-VPSKEIEKVANWGIQSLGLSLYADRLAGTYSGGNKRKLSTAIALTGCPPL 2090
Cdd:TIGR04406 77 GIGYLPQEASIFRKLTVEENIMAVLEIRKdLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKF 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6671495 2091 LLLDEPTTGMDPQARRMLwNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGTFQCLGTIQHL 2156
Cdd:TIGR04406 157 ILLDEPFAGVDPIAVGDI-KKIIKHLKErGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEI 222
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1961-2153 |
3.48e-24 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 103.62 E-value: 3.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1961 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKsiLTSISDVhqNMGYCPQfdaiddlLTGREHLYLYARLRG 2040
Cdd:COG1134 49 VERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR--VSALLEL--GAGFHPE-------LTGRENIYLNGRLLG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2041 VPSKEIEKVANwGIQSL-GLSLYADRLAGTYSGGNKRKL--STAIALTgcPPLLLLDEPTTGMDP--QAR---RMLwnti 2112
Cdd:COG1134 118 LSRKEIDEKFD-EIVEFaELGDFIDQPVKTYSSGMRARLafAVATAVD--PDILLVDEVLAVGDAafQKKclaRIR---- 190
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 6671495 2113 vSIIREGRAVVLTSHSMEECEALCTRLAIMVKGTFQCLGTI 2153
Cdd:COG1134 191 -ELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDP 230
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
931-1137 |
5.34e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 103.63 E-value: 5.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 931 VKNLVKVFEPSG---RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIeTNLDV------- 1000
Cdd:COG1101 4 LKNLSKTFNPGTvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDV-TKLPEykrakyi 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1001 --VRQ--SLGMCPqhnilfhHLTVAEHILFyAQLKGRSW---------------EE-AQLEMeamledtGLHHKRNEEAQ 1060
Cdd:COG1101 83 grVFQdpMMGTAP-------SMTIEENLAL-AYRRGKRRglrrgltkkrrelfrELlATLGL-------GLENRLDTKVG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1061 DLSGGmQRK-LSVAIAFVGDSKVVVLDEPTSGVDPYSRRSIWDLLLKY--RSGRTIIMSTHHMDEADLLGDRIAIISQGR 1137
Cdd:COG1101 148 LLSGG-QRQaLSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIveENNLTTLMVTHNMEQALDYGNRLIMMHEGR 226
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
931-1144 |
5.40e-24 |
|
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: 102.57 E-value: 5.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 931 VKNLVKVFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIET-NLDVVRQSLGMCP 1009
Cdd:cd03244 5 FKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKiGLHDLRSRISIIP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1010 QHNILFHHlTVAEHILFYAQL-KGRSW---EEAQLEMEAMLEDTGLHHKRNEEAQDLSGGmQRKL-SVAIAFVGDSKVVV 1084
Cdd:cd03244 85 QDPVLFSG-TIRSNLDPFGEYsDEELWqalERVGLKEFVESLPGGLDTVVEEGGENLSVG-QRQLlCLARALLRKSKILV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6671495 1085 LDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDE-ADLlgDRIAIISQGRLYCSGTP 1144
Cdd:cd03244 163 LDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTiIDS--DRILVLDKGRVVEFDSP 221
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1961-2146 |
5.63e-24 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 102.73 E-value: 5.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1961 VRPGECFGLLGVNGAGKTTTFKMLTG---DTTVTSGDATVAGKSIltSISDVHQNMGYCPQFDAIDDLLTGREHLYLYAR 2037
Cdd:cd03234 30 VESGQVMAILGSSGSGKTTLLDAISGrveGGGTTSGQILFNGQPR--KPDQFQKCVAYVRQDDILLPGLTVRETLTYTAI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2038 LRG---VPSKEIEKVAnwgiQSLGLSLYAD-RLAGTY----SGGNKRKLSTAIALTGCPPLLLLDEPTTGMDPqarrMLW 2109
Cdd:cd03234 108 LRLprkSSDAIRKKRV----EDVLLRDLALtRIGGNLvkgiSGGERRRVSIAVQLLWDPKVLILDEPTSGLDS----FTA 179
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 6671495 2110 NTIVSII----REGRAVVLTSHS-MEECEALCTRLAIMVKGT 2146
Cdd:cd03234 180 LNLVSTLsqlaRRNRIVILTIHQpRSDLFRLFDRILLLSSGE 221
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1952-2146 |
1.05e-23 |
|
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: 102.03 E-value: 1.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1952 PAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAG-------KSILTSISDVhqnMGYCPQ--FDai 2022
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGlvpwkrrKKFLRRIGVV---FGQKTQlwWD-- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2023 ddlLTGREHLYLYARLRGVPSKEIEKVANWGIQSLGLSLYADRLAGTYSGGNKRKLSTAIALTGCPPLLLLDEPTTGMDP 2102
Cdd:cd03267 110 ---LPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDV 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 6671495 2103 QARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGT 2146
Cdd:cd03267 187 VAQENIRNFLKEYNRErGTTVLLTSHYMKDIEALARRVLVIDKGR 231
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1928-2142 |
1.12e-23 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 102.86 E-value: 1.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1928 MSGGnkTDILKLNELTKVYSGSSS--PAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIlts 2005
Cdd:COG1116 1 MSAA--APALELRGVSKRFPTGGGgvTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPV--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2006 iSDVHQNMGYCPQfdaiDDLL----TGREHLYLYARLRGVPSKEIEKVANWGIQSLGLSLYADRLAGTYSGGNKRKLSTA 2081
Cdd:COG1116 76 -TGPGPDRGVVFQ----EPALlpwlTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6671495 2082 IALTGCPPLLLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIM 2142
Cdd:COG1116 151 RALANDPEVLLMDEPFGALDALTRERLQDELLRLWQEtGKTVLFVTHDVDEAVFLADRVVVL 212
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
932-1144 |
1.16e-23 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 102.09 E-value: 1.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 932 KNLVKVFEPSgrPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGG---KDIETNLDVVRQSLGMC 1008
Cdd:PRK09493 5 KNVSKHFGPT--QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGlkvNDPKVDERLIRQEAGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1009 PQHNILFHHLTVAEHILFYA-QLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDE 1087
Cdd:PRK09493 83 FQQFYLFPHLTALENVMFGPlRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6671495 1088 PTSGVDPYSR----RSIWDLLlkyRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
Cdd:PRK09493 163 PTSALDPELRhevlKVMQDLA---EEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDP 220
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
927-1144 |
1.36e-23 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 105.41 E-value: 1.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 927 PGVCVKNLVKVFEpsGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIeTNLDVVRQSLG 1006
Cdd:PRK09452 13 PLVELRGISKSFD--GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDI-THVPAENRHVN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1007 MCPQHNILFHHLTVAEHILFYAQLKGRSWEE-AQLEMEAM----LEDTGlhhkrNEEAQDLSGGMQRKLSVAIAFVGDSK 1081
Cdd:PRK09452 90 TVFQSYALFPHMTVFENVAFGLRMQKTPAAEiTPRVMEALrmvqLEEFA-----QRKPHQLSGGQQQRVAIARAVVNKPK 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6671495 1082 VVVLDEPTSGVDpYSRRSIWDLLLKY---RSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
Cdd:PRK09452 165 VLLLDESLSALD-YKLRKQMQNELKAlqrKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTP 229
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
931-1149 |
1.40e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 102.89 E-value: 1.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 931 VKNLvKVFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDI-ETNLDVVRQSLGMCP 1009
Cdd:PRK13647 7 VEDL-HFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVnAENEKWVRSKVGLVF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1010 Q--HNILFhHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDE 1087
Cdd:PRK13647 86 QdpDDQVF-SSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6671495 1088 PTSGVDPYSRRSIWDLLLK-YRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFLKN 1149
Cdd:PRK13647 165 PMAYLDPRGQETLMEILDRlHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTD 227
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
2026-2161 |
1.79e-23 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 104.43 E-value: 1.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2026 LTGREHLYLYARLRGVPSKEIEKVANWGIQSLGLSLYADRLAGTYSGGNKRKLSTAIALTGCPPLLLLDEPTTGMDPQAR 2105
Cdd:NF000106 101 FSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTR 180
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 6671495 2106 RMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGTFQCLGTIQHLKYKFG 2161
Cdd:NF000106 181 NEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVG 236
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
927-1142 |
3.24e-23 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 106.41 E-value: 3.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 927 PGVCVKNLVKVFepSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIE--TNLDVVRQS 1004
Cdd:PRK09700 4 PYISMAGIGKSF--GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNklDHKLAAQLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1005 LGMCPQHNILFHHLTVAEHiLFYAQLKGRS--------WEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAF 1076
Cdd:PRK09700 82 IGIIYQELSVIDELTVLEN-LYIGRHLTKKvcgvniidWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6671495 1077 VGDSKVVVLDEPTSGVDPYSRRSIWDLLLKYRS-GRTIIMSTHHMDEADLLGDRIAIISQGRLYCSG 1142
Cdd:PRK09700 161 MLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKeGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1929-2190 |
3.58e-23 |
|
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: 101.57 E-value: 3.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1929 SGGNKTDILKlneltkvySGSSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT---- 2004
Cdd:cd03294 23 KGKSKEEILK--------KTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAmsrk 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2005 --------SISDVHQNMGYCPQFDAIDDLLTGREhlylyarLRGVPSKEIEKVANWGIQSLGLSLYADRLAGTYSGGNKR 2076
Cdd:cd03294 95 elrelrrkKISMVFQSFALLPHRTVLENVAFGLE-------VQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQ 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2077 KLSTAIALTGCPPLLLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGTFQCLGTIQH 2155
Cdd:cd03294 168 RVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAElQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEE 247
|
250 260 270
....*....|....*....|....*....|....*
gi 6671495 2156 LkykfgdgyivtmkIKSPKDDLlpdlnpVEQFFQG 2190
Cdd:cd03294 248 I-------------LTNPANDY------VREFFRG 263
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
942-1138 |
3.98e-23 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 100.88 E-value: 3.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 942 GRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGL--LPP---TSGTVLIGGKDI---ETNLDVVRQSLGMCPQHNI 1013
Cdd:COG1117 23 DKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndLIPgarVEGEILLDGEDIydpDVDVVELRRRVGMVFQKPN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1014 LFHHlTVAEHILFYAQLKG-RSWEEAQLEMEAMLEDTGL----HHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEP 1088
Cdd:COG1117 103 PFPK-SIYDNVAYGLRLHGiKSKSELDEIVEESLRKAALwdevKDRLKKSALGLSGGQQQRLCIARALAVEPEVLLMDEP 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 6671495 1089 TSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
Cdd:COG1117 182 TSALDPISTAKIEELILELKKDYTIVIVTHNMQQAARVSDYTAFFYLGEL 231
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1952-2151 |
4.13e-23 |
|
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: 98.66 E-value: 4.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1952 PAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-SISDVHQNMGYCPQfdAIDdlLTGRE 2030
Cdd:cd03214 13 TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASlSPKELARKIAYVPQ--ALE--LLGLA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2031 HLylyarlrgvpskeiekvanwgiqslglslyADRLAGTYSGGNKRKLSTAIALTGCPPLLLLDEPTTGMDP--QARRMl 2108
Cdd:cd03214 89 HL------------------------------ADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIahQIELL- 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 6671495 2109 wNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGTFQCLG 2151
Cdd:cd03214 138 -ELLRRLARErGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1937-2151 |
4.14e-23 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 99.64 E-value: 4.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1937 LKLNELTKVYSgsSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIlTSISDVHQNMGYC 2016
Cdd:cd03301 1 VELENVTKRFG--NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDV-TDLPPKDRDIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2017 PQFDAIDDLLTGREHLYLYARLRGVPSKEIEKVANWGIQSLGLSLYADRLAGTYSGGNKRKLSTAIALTGCPPLLLLDEP 2096
Cdd:cd03301 78 FQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 6671495 2097 TTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGTFQCLG 2151
Cdd:cd03301 158 LSNLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
946-1136 |
4.72e-23 |
|
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: 100.23 E-value: 4.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 946 VDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDI-ETNLD--VVRQSLGMCPQhnilfhhLTVAE 1022
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQItEPGPDrmVVFQNYSLLPW-------LTVRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1023 HILFY--AQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTSGVDPYSRRSI 1100
Cdd:TIGR01184 74 NIALAvdRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNL 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 6671495 1101 WDLLLKY--RSGRTIIMSTHHMDEADLLGDRIAIISQG 1136
Cdd:TIGR01184 154 QEELMQIweEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
929-1171 |
7.02e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 101.03 E-value: 7.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 929 VCVKNLVKVFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPP-----TSGTVLiGGKDIETNLDVVRQ 1003
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnpnSKITVD-GITLTAKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1004 SLGMCPQH-NILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKV 1082
Cdd:PRK13640 85 KVGIVFQNpDNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1083 VVLDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADlLGDRIAIISQGRLYCSGTPL-------FLKNcfgT 1153
Cdd:PRK13640 165 IILDESTSMLDPAGKEQILKLIrkLKKKNNLTVISITHDIDEAN-MADQVLVLDDGKLLAQGSPVeifskveMLKE---I 240
|
250
....*....|....*...
gi 6671495 1154 GFYLTLVRKMKNIQSQRG 1171
Cdd:PRK13640 241 GLDIPFVYKLKNKLKEKG 258
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
936-1142 |
7.74e-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: 7.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 936 KVFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKdietnldvVRQSLGMcpqhNILF 1015
Cdd:cd03220 28 RKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR--------VSSLLGL----GGGF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1016 H-HLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLhhkrnEEAQDL-----SGGMQRKL--SVAIAFVGDskVVVLDE 1087
Cdd:cd03220 96 NpELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSEL-----GDFIDLpvktySSGMKARLafAIATALEPD--ILLIDE 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 6671495 1088 PTSGVDPYSRRSIWDLLLKYRS-GRTIIMSTHHMDEADLLGDRIAIISQGRLYCSG 1142
Cdd:cd03220 169 VLAVGDAAFQEKCQRRLRELLKqGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
942-1147 |
7.83e-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: 7.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 942 GRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDI-ETNLDVVRQSLGMCPQHNILFHHlTV 1020
Cdd:cd03253 13 GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIrEVTLDSLRRAIGVVPQDTVLFND-TI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1021 AEHILFyaqlkGRsWEEAQLEMEAMLEDTGLHHK--RNEEAQD---------LSGGMQRKLSVAIAFVGDSKVVVLDEPT 1089
Cdd:cd03253 92 GYNIRY-----GR-PDATDEEVIEAAKAAQIHDKimRFPDGYDtivgerglkLSGGEKQRVAIARAILKNPPILLLDEAT 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 6671495 1090 SGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEAdLLGDRIAIISQGRLYCSGTPLFL 1147
Cdd:cd03253 166 SALDTHTEREIQAALRDVSKGRTTIVIAHRLSTI-VNADKIIVLKDGRIVERGTHEEL 222
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
931-1138 |
8.37e-23 |
|
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: 97.29 E-value: 8.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 931 VKNLVKVFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIET-NLDVVRQSLGMCP 1009
Cdd:cd03246 3 VENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQwDPNELGDHVGYLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1010 QHNILFHHlTVAEHIlfyaqlkgrsweeaqlemeamledtglhhkrneeaqdLSGGMQRKLSVAIAFVGDSKVVVLDEPT 1089
Cdd:cd03246 83 QDDELFSG-SIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPN 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 6671495 1090 SGVDPYSRRSIWDLLLKYRS-GRTIIMSTHHMdEADLLGDRIAIISQGRL 1138
Cdd:cd03246 125 SHLDVEGERALNQAIAALKAaGATRIVIAHRP-ETLASADRILVLEDGRV 173
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1961-2157 |
1.00e-22 |
|
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: 99.11 E-value: 1.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1961 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI--LTSISDVH--QNMGYCPQFDAIDDLLTGREH--LYL 2034
Cdd:cd03261 23 VRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDIsgLSEAELYRlrRRMGMLFQSGALFDSLTVFENvaFPL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2035 YARLRGvPSKEIEKVANWGIQSLGLSLYADRLAGTYSGGNKRKLSTAIALTGCPPLLLLDEPTTGMDPQARRMLWNTIVS 2114
Cdd:cd03261 103 REHTRL-SEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRS 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 6671495 2115 IIRE-GRAVVLTSHSMEECEALCTRLAIMVKGTFQCLGTIQHLK 2157
Cdd:cd03261 182 LKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELR 225
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
931-1138 |
1.91e-22 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 99.05 E-value: 1.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 931 VKNLVKVFEpsGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIETNLDV---------V 1001
Cdd:PRK11264 6 VKNLVKKFH--GQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLsqqkglirqL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1002 RQSLGMCPQHNILFHHLTVAEHIL-FYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDS 1080
Cdd:PRK11264 84 RQHVGFVFQNFNLFPHRTVLENIIeGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6671495 1081 KVVVLDEPTSGVDPysrRSIWDLLLKYRS----GRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
Cdd:PRK11264 164 EVILFDEPTSALDP---ELVGEVLNTIRQlaqeKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
931-1132 |
2.11e-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: 100.51 E-value: 2.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 931 VKNLVKVFEPSGRP--AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPP---TSGTVLIGGKDI----ETNLDVV 1001
Cdd:COG0444 4 VRNLKVYFPTRRGVvkAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLlklsEKELRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1002 R-QSLGMCPQH-----NILFhhlTVAEHIL-FYAQLKGRSWEEAQLEMEAMLEDTGLHHKrnEEAQD-----LSGGMQRK 1069
Cdd:COG0444 84 RgREIQMIFQDpmtslNPVM---TVGDQIAePLRIHGGLSKAEARERAIELLERVGLPDP--ERRLDrypheLSGGMRQR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6671495 1070 LSVAIAFVGDSKVVVLDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAI 1132
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDVTIQAQILNLLkdLQRELGLAILFITHDLGVVAEIADRVAV 223
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
942-1119 |
2.95e-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: 96.66 E-value: 2.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 942 GRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIETNLDVVRQSLGMCPQHNILFHHLTVA 1021
Cdd:TIGR01189 12 ERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPELSAL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1022 EHILFYAQLKGrsweEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTSGVDPYSRRSIW 1101
Cdd:TIGR01189 92 ENLHFWAAIHG----GAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLA 167
|
170
....*....|....*....
gi 6671495 1102 DLLLKY-RSGRTIIMSTHH 1119
Cdd:TIGR01189 168 GLLRAHlARGGIVLLTTHQ 186
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
940-1143 |
3.32e-22 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 98.00 E-value: 3.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 940 PSgRPAV---DRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIET-NLDVVRQSLGMCPQHNILF 1015
Cdd:cd03249 11 PS-RPDVpilKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDlNLRWLRSQIGLVSQEPVLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1016 hHLTVAEHILFyaqlkGRswEEAQLEME------AMLED--TGLHHKRNEEAQD----LSGGMQRKLSVAIAFVGDSKVV 1083
Cdd:cd03249 90 -DGTIAENIRY-----GK--PDATDEEVeeaakkANIHDfiMSLPDGYDTLVGErgsqLSGGQKQRIAIARALLRNPKIL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6671495 1084 VLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMD---EAdllgDRIAIISQGRLYCSGT 1143
Cdd:cd03249 162 LLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLStirNA----DLIAVLQNGQVVEQGT 220
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
945-1145 |
3.77e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 98.93 E-value: 3.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIETNLDVV------RQSLGMC---PQHNiLF 1015
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKIkevkrlRKEIGLVfqfPEYQ-LF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1016 HHlTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQ-DLSGGMQRKLSVAIAFVGDSKVVVLDEPTSGVDP 1094
Cdd:PRK13645 105 QE-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDYVKRSPfELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDP 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 6671495 1095 YSRRSIWDLLLKYRS--GRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPL 1145
Cdd:PRK13645 184 KGEEDFINLFERLNKeyKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPF 236
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
953-1144 |
4.99e-22 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 103.59 E-value: 4.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 953 FYENQITAFLGHNGAGKTTTLSILTGLLPP---TSGTVLIGGKDIetNLDVVRQSLGMCPQHNILFHHLTVAEHILFYAQ 1029
Cdd:TIGR00955 48 AKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPI--DAKEMRAISAYVQQDDLFIPTLTVREHLMFQAH 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1030 LK-GRSW--EEAQLEMEAMLEDTGLHHKRNEEAQD------LSGGMQRKLSVAIAFVGDSKVVVLDEPTSGVDPYSRRSI 1100
Cdd:TIGR00955 126 LRmPRRVtkKEKRERVDEVLQALGLRKCANTRIGVpgrvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSV 205
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 6671495 1101 WDLLLKY-RSGRTIIMSTHHmDEADL--LGDRIAIISQGRLYCSGTP 1144
Cdd:TIGR00955 206 VQVLKGLaQKGKTIICTIHQ-PSSELfeLFDKIILMAEGRVAYLGSP 251
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1961-2157 |
6.16e-22 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 96.97 E-value: 6.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1961 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTSISD----VHQNMGYCPQFDA-IDDL---------L 2026
Cdd:COG1127 28 VPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKelyeLRRRIGMLFQGGAlFDSLtvfenvafpL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2027 tgREHlylyarlRGVPSKEIEKVANWGIQSLGLSLYADRLAGTYSGGNKRK--LSTAIALTgcPPLLLLDEPTTGMDPQA 2104
Cdd:COG1127 108 --REH-------TDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRvaLARALALD--PEILLYDEPTAGLDPIT 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 6671495 2105 RRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGTFQCLGTIQHLK 2157
Cdd:COG1127 177 SAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELL 230
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1952-2127 |
6.31e-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: 6.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1952 PAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTSISDVHQNMGYCPQFDAIDDLLTGREH 2031
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPELSALEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2032 LYLYARLRGVPSKEIEKvanwGIQSLGLSLYADRLAGTYSGGNKRKLSTAIALTGCPPLLLLDEPTTGMDPQARRMLWNT 2111
Cdd:TIGR01189 94 LHFWAAIHGGAQRTIED----ALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGL 169
|
170
....*....|....*.
gi 6671495 2112 IVSIIREGRAVVLTSH 2127
Cdd:TIGR01189 170 LRAHLARGGIVLLTTH 185
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
942-1136 |
7.92e-22 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 97.08 E-value: 7.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 942 GRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIE---TNLDVVRQSLGMCPQHNILfhhl 1018
Cdd:PRK11248 13 GKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEgpgAERGVVFQNEGLLPWRNVQ---- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1019 tvaEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTSGVDPYSRR 1098
Cdd:PRK11248 89 ---DNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTRE 165
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 6671495 1099 SIWDLLLK--YRSGRTIIMSTHHMDEADLLGDRIAIISQG 1136
Cdd:PRK11248 166 QMQTLLLKlwQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
945-1144 |
8.78e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 97.51 E-value: 8.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIET-NLDVVRQSLGMCPQH-NILFHHLTVAE 1022
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDdNFEKLRKHIGIVFQNpDNQFVGSIVKY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1023 HILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTSGVDPYSRRSIWD 1102
Cdd:PRK13648 104 DVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLD 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 6671495 1103 LLLKYRSGR--TIIMSTHHMDEAdLLGDRIAIISQGRLYCSGTP 1144
Cdd:PRK13648 184 LVRKVKSEHniTIISITHDLSEA-MEADHVIVMNKGTVYKEGTP 226
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
931-1144 |
8.83e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 98.77 E-value: 8.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 931 VKNLVKVF---EPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIETNLDVVRQSLGM 1007
Cdd:PRK13631 24 VKNLYCVFdekQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHELITNP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1008 CPQHNILFHHL------------------TVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQ-DLSGGMQR 1068
Cdd:PRK13631 104 YSKKIKNFKELrrrvsmvfqfpeyqlfkdTIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDSYLERSPfGLSGGQKR 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6671495 1069 KLSVAIAFVGDSKVVVLDEPTSGVDPYSRRSIWDLLLKYR-SGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
Cdd:PRK13631 184 RVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKaNNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTP 260
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
1937-2156 |
1.21e-21 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 101.77 E-value: 1.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1937 LKLNELTKVYSGSSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-SISDVHQNMGY 2015
Cdd:COG4987 334 LELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDlDEDDLRRRIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2016 CPQ----FDAiddllTGREHLyLYAR-------LRGVpskeIEKV--ANWgIQSL--GLSLYADRLAGTYSGGNKRKLST 2080
Cdd:COG4987 414 VPQrphlFDT-----TLRENL-RLARpdatdeeLWAA----LERVglGDW-LAALpdGLDTWLGEGGRRLSGGERRRLAL 482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6671495 2081 AIALTGCPPLLLLDEPTTGMDPQARRMLWNTIVSiIREGRAVVLTSHSMEECEAlCTRLAIMVKGTFQCLGTIQHL 2156
Cdd:COG4987 483 ARALLRDAPILLLDEPTEGLDAATEQALLADLLE-ALAGRTVLLITHRLAGLER-MDRILVLEDGRIVEQGTHEEL 556
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1936-2152 |
1.34e-21 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 96.12 E-value: 1.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1936 ILKLNELTKVYSGSSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIltSISDVH----Q 2011
Cdd:PRK10895 3 TLTAKNLAKAYKGRR--VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDI--SLLPLHararR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2012 NMGYCPQFDAIDDLLTGREHLYLYARLRGVPSKEIEKV-ANWGIQSLGLSLYADRLAGTYSGGNKRKLSTAIALTGCPPL 2090
Cdd:PRK10895 79 GIGYLPQEASIFRRLSVYDNLMAVLQIRDDLSAEQREDrANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKF 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6671495 2091 LLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGTFQCLGT 2152
Cdd:PRK10895 159 ILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGT 220
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
931-1143 |
1.45e-21 |
|
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: 101.72 E-value: 1.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 931 VKNLVKVFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDI-ETNLDVVRQSLGMCP 1009
Cdd:TIGR02203 333 FRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLaDYTLASLRRQVALVS 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1010 QHNILFHHlTVAEHILfYAQLKGRSWE--EAQLEMEAMLE-----DTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKV 1082
Cdd:TIGR02203 413 QDVVLFND-TIANNIA-YGRTEQADRAeiERALAAAYAQDfvdklPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPI 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6671495 1083 VVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADlLGDRIAIISQGRLYCSGT 1143
Cdd:TIGR02203 491 LILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIE-KADRIVVMDDGRIVERGT 550
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
945-1138 |
1.91e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 96.00 E-value: 1.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILT--GLLPP---TSGTVLIGGKDIET-NLDVV--RQSLGMCPQHNILFH 1016
Cdd:PRK14239 20 ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDLNPevtITGSIVYNGHNIYSpRTDTVdlRKEIGMVFQQPNPFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1017 hLTVAEHILFYAQLKG------------RSWEEAQL--EMEAMLEDTGLhhkrneeaqDLSGGMQRKLSVAIAFVGDSKV 1082
Cdd:PRK14239 100 -MSIYENVVYGLRLKGikdkqvldeaveKSLKGASIwdEVKDRLHDSAL---------GLSGGQQQRVCIARVLATSPKI 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 6671495 1083 VVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
Cdd:PRK14239 170 ILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRISDRTGFFLDGDL 225
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
931-1146 |
2.74e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 96.34 E-value: 2.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 931 VKNL-VKVFEPSGRPAVDrlNITFYENQ--ITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDI-ETNLDVVRQSLG 1006
Cdd:PRK13650 7 VKNLtFKYKEDQEKYTLN--DVSFHVKQgeWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLtEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1007 MCPQH-NILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVL 1085
Cdd:PRK13650 85 MVFQNpDNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIIL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6671495 1086 DEPTSGVDPYSRRSIWDLLLKYRS--GRTIIMSTHHMDEAdLLGDRIAIISQGRLYCSGTP--LF 1146
Cdd:PRK13650 165 DEATSMLDPEGRLELIKTIKGIRDdyQMTVISITHDLDEV-ALSDRVLVMKNGQVESTSTPreLF 228
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
945-1144 |
2.88e-21 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 95.15 E-value: 2.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKdIETNLDVvrqSLGMCPQhnilfhhLTVAEHI 1024
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR-VSALLEL---GAGFHPE-------LTGRENI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1025 LFYAQLKGRSWEeaqlEMEAMLED----TGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTSGVDPY-SRRS 1099
Cdd:COG1134 110 YLNGRLLGLSRK----EIDEKFDEivefAELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAfQKKC 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 6671495 1100 IwDLLLKYR-SGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
Cdd:COG1134 186 L-ARIRELReSGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDP 230
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1953-2146 |
2.96e-21 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 95.44 E-value: 2.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1953 AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI--LTS-------ISDVHQNMGYCPQFDAID 2023
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIegLPGhqiarmgVVRTFQHVRLFREMTVIE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2024 DLLTGrEHLYLYARL----------RGVPSKEIEKVANWgIQSLGLSLYADRLAGTYSGGNKRKLSTAIALTGCPPLLLL 2093
Cdd:PRK11300 100 NLLVA-QHQQLKTGLfsgllktpafRRAESEALDRAATW-LERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILML 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 6671495 2094 DEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGT 2146
Cdd:PRK11300 178 DEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGT 231
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
942-1160 |
3.31e-21 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 101.35 E-value: 3.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 942 GRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIEtNLD--VVRQSLGMCPQHNILFHHlT 1019
Cdd:TIGR01193 486 GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLK-DIDrhTLRQFINYLPQEPYIFSG-S 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1020 VAEHILFYAQ--------LKGRSWEEAQLEMEAMleDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTSG 1091
Cdd:TIGR01193 564 ILENLLLGAKenvsqdeiWAACEIAEIKDDIENM--PLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSN 641
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6671495 1092 VDPYSRRSIWDLLLKYRSgRTIIMSTHHMDEADLLgDRIAIISQGRLYCSGT--PLFLKNcfgtGFYLTLV 1160
Cdd:TIGR01193 642 LDTITEKKIVNNLLNLQD-KTIIFVAHRLSVAKQS-DKIIVLDHGKIIEQGShdELLDRN----GFYASLI 706
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
1961-2127 |
3.78e-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: 93.46 E-value: 3.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1961 VRPGECFGLLGVNGAGKTTTFKMLTGDTT--VTSGDATVAGKSILTSISDVhqnMGYCPQFDAIDDLLTGREHLYLYARL 2038
Cdd:cd03232 30 VKPGTLTALMGESGAGKTTLLDVLAGRKTagVITGEILINGRPLDKNFQRS---TGYVEQQDVHSPNLTVREALRFSALL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2039 RGvpskeiekvanwgiqslgLSLYadrlagtysggNKRKLSTAIALTGCPPLLLLDEPTTGMDPQARRMLWNTIVSIIRE 2118
Cdd:cd03232 107 RG------------------LSVE-----------QRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADS 157
|
....*....
gi 6671495 2119 GRAVVLTSH 2127
Cdd:cd03232 158 GQAILCTIH 166
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
1961-2147 |
4.96e-21 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 93.48 E-value: 4.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1961 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI-----LTSISDVHQNMGYCPQFDaiddllTGREHLYLY 2035
Cdd:cd03226 23 LYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIkakerRKSIGYVMQDVDYQLFTD------SVREELLLG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2036 ARLRGVPSKEIEKVanwgIQSLGLSLYADRLAGTYSGGNKRKLSTAIALTGCPPLLLLDEPTTGMDPQARRMLWNTIVSI 2115
Cdd:cd03226 97 LKELDAGNEQAETV----LKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIREL 172
|
170 180 190
....*....|....*....|....*....|..
gi 6671495 2116 IREGRAVVLTSHSMEECEALCTRLAIMVKGTF 2147
Cdd:cd03226 173 AAQGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
940-1144 |
5.75e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 95.44 E-value: 5.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 940 PSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDI--ETNLDVVRQSLGMCPQH-NILFH 1016
Cdd:PRK13644 12 PDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTgdFSKLQGIRKLVGIVFQNpETQFV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1017 HLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTSGVDPYS 1096
Cdd:PRK13644 92 GRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDS 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 6671495 1097 RRSIWDLLLK-YRSGRTIIMSTHHMDEADlLGDRIAIISQGRLYCSGTP 1144
Cdd:PRK13644 172 GIAVLERIKKlHEKGKTIVYITHNLEELH-DADRIIVMDRGKIVLEGEP 219
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
942-1139 |
6.71e-21 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 93.79 E-value: 6.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 942 GRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDI----ETNLDVVRQSLGMCPQHNILFHH 1017
Cdd:PRK10908 14 GRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItrlkNREVPFLRRQIGMIFQDHHLLMD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1018 LTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTSGVDPYSR 1097
Cdd:PRK10908 94 RTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALS 173
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 6671495 1098 RSIWDLLLKY-RSGRTIIMSTHHMDEADLLGDRIAIISQGRLY 1139
Cdd:PRK10908 174 EGILRLFEEFnRVGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1936-2142 |
6.99e-21 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 98.94 E-value: 6.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1936 ILKLNELTKVYSGSssPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI-LTSISD------ 2008
Cdd:COG1129 4 LLEMRGISKSFGGV--KALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVrFRSPRDaqaagi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2009 --VHQNMGYCPQFDAIDDLLTGREhlylYARLRGVPSKEIEKVANWGIQSLGLSLYADRLAGTYSGGNKRKLSTAIALTG 2086
Cdd:COG1129 82 aiIHQELNLVPNLSVAENIFLGRE----PRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSR 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 6671495 2087 CPPLLLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIM 2142
Cdd:COG1129 158 DARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVL 213
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
929-1152 |
7.35e-21 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 96.71 E-value: 7.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 929 VCVKNLVKVFepsGRPAV-DRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIeTNLDVVRQSLGM 1007
Cdd:PRK11432 7 VVLKNITKRF---GSNTViDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDV-THRSIQQRDICM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1008 CPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDE 1087
Cdd:PRK11432 83 VFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6671495 1088 PTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP---------LFLKNCFG 1152
Cdd:PRK11432 163 PLSNLDANLRRSMREKIreLQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPqelyrqpasRFMASFMG 238
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1937-2146 |
1.05e-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: 91.48 E-value: 1.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1937 LKLNELTKVYSGSssPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILtsisdvhqnmgyc 2016
Cdd:cd03229 1 LELKNVSKRYGQK--TVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLT------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2017 pqfDAIDDLLTGREHL-YLYARLRGVPSKEIekvanwgIQSLGLSLyadrlagtySGGNKRKLSTAIALTGCPPLLLLDE 2095
Cdd:cd03229 66 ---DLEDELPPLRRRIgMVFQDFALFPHLTV-------LENIALGL---------SGGQQQRVALARALAMDPDVLLLDE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 6671495 2096 PTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGT 2146
Cdd:cd03229 127 PTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
960-1138 |
1.06e-20 |
|
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: 93.27 E-value: 1.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 960 AFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIeTNLD------VVRQSLGMCPQHnilFH---HLTVAEHILFYAQL 1030
Cdd:COG4181 42 AIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDL-FALDedararLRARHVGFVFQS---FQllpTLTALENVMLPLEL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1031 KGRSweEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTSGVDPYSRRSIWDLL--LKYR 1108
Cdd:COG4181 118 AGRR--DARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLfeLNRE 195
|
170 180 190
....*....|....*....|....*....|.
gi 6671495 1109 SGRTIIMSTHhmDEADLL-GDRIAIISQGRL 1138
Cdd:COG4181 196 RGTTLVLVTH--DPALAArCDRVLRLRAGRL 224
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1961-2147 |
1.46e-20 |
|
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: 91.34 E-value: 1.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1961 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI-LTSISDVHQN-MGYCPqfdaiDDlltgrehlylyaRL 2038
Cdd:cd03215 23 VRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVtRRSPRDAIRAgIAYVP-----ED------------RK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2039 R-GVpskeiekVANWGIQ---SLGLSLyadrlagtySGGNKRKLSTAIALTGCPPLLLLDEPTTGMDPQARRMLWNTIVS 2114
Cdd:cd03215 86 ReGL-------VLDLSVAeniALSSLL---------SGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRE 149
|
170 180 190
....*....|....*....|....*....|...
gi 6671495 2115 IIREGRAVVLTSHSMEECEALCTRLAIMVKGTF 2147
Cdd:cd03215 150 LADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1937-2146 |
2.01e-20 |
|
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: 90.18 E-value: 2.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1937 LKLNELTKVYSGSssPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIltsisdvhqnmgyc 2016
Cdd:cd03216 1 LELRGITKRFGGV--KALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEV-------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2017 pQFDAIDDlltgrehlylyARLRGvpskeIEKVAnwgiQslglslyadrlagtYSGGNKRKLSTAIALTGCPPLLLLDEP 2096
Cdd:cd03216 65 -SFASPRD-----------ARRAG-----IAMVY----Q--------------LSVGERQMVEIARALARNARLLILDEP 109
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 6671495 2097 TTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGT 2146
Cdd:cd03216 110 TAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGR 159
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
891-1138 |
3.32e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 97.06 E-value: 3.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 891 ERALEKTEplteeMEDPEHPEG-MNDSFFE-RELPGLVpgVCVKNLVKVFEpsGRPAVDRLNITFYENQITAFLGHNGAG 968
Cdd:COG0488 283 IKALEKLE-----REEPPRRDKtVEIRFPPpERLGKKV--LELEGLSKSYG--DKTLLDDLSLRIDRGDRIGLIGPNGAG 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 969 KTTTLSILTGLLPPTSGTVLIGgkdieTNLdvvrqSLGMCPQHNILFH-HLTVAEHIlfyaqlkgRSWEEAQLEMEA--M 1045
Cdd:COG0488 354 KSTLLKLLAGELEPDSGTVKLG-----ETV-----KIGYFDQHQEELDpDKTVLDEL--------RDGAPGGTEQEVrgY 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1046 LEDTGLhhkRNEEAQ----DLSGGMQRKLSVAIAFVGDSKVVVLDEPTSGVDPYSRRSIWDLLLKYrSGrTIIMSTHHMD 1121
Cdd:COG0488 416 LGRFLF---SGDDAFkpvgVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDF-PG-TVLLVSHDRY 490
|
250
....*....|....*..
gi 6671495 1122 EADLLGDRIAIISQGRL 1138
Cdd:COG0488 491 FLDRVATRILEFEDGGV 507
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
960-1142 |
3.55e-20 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 91.57 E-value: 3.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 960 AFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDiETNLDVVRQSLGMCPQHNILFHHLTVAEHI---------LFYAQl 1030
Cdd:PRK10771 29 AILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD-HTTTPPSRRPVSMLFQENNLFSHLTVAQNIglglnpglkLNAAQ- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1031 kgrsweeaQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTSGVDPYSRRSIWDLLLKYRSG 1110
Cdd:PRK10771 107 --------REKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQE 178
|
170 180 190
....*....|....*....|....*....|....
gi 6671495 1111 R--TIIMSTHHMDEADLLGDRIAIISQGRLYCSG 1142
Cdd:PRK10771 179 RqlTLLMVSHSLEDAARIAPRSLVVADGRIAWDG 212
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
928-1155 |
7.92e-20 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 93.94 E-value: 7.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 928 GVCVKNLVKVFepsGRPAVDR-LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGK---DIETNldvvRQ 1003
Cdd:PRK11000 3 SVTLRNVTKAY---GDVVISKdINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKrmnDVPPA----ER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1004 SLGMCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGmQRKlSVAIA--FVGDSK 1081
Cdd:PRK11000 76 GVGMVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGG-QRQ-RVAIGrtLVAEPS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1082 VVVLDEPTSGVDPYSR---RSIWDLLLKyRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFL----KNCFGTG 1154
Cdd:PRK11000 154 VFLLDEPLSNLDAALRvqmRIEISRLHK-RLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELyhypANRFVAG 232
|
.
gi 6671495 1155 F 1155
Cdd:PRK11000 233 F 233
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
931-1123 |
8.41e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 92.46 E-value: 8.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 931 VKNLVKVFE---PSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIETN---------- 997
Cdd:PRK13651 5 VKNIVKIFNkklPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKkktkekekvl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 998 LDVV---------------RQSLGMCPQ--HNILFHHlTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQ 1060
Cdd:PRK13651 85 EKLViqktrfkkikkikeiRRRVGVVFQfaEYQLFEQ-TIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDESYLQRSP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6671495 1061 -DLSGGMQRKLSVAIAFVGDSKVVVLDEPTSGVDPYSRRSIWDLLLK-YRSGRTIIMSTHHMDEA 1123
Cdd:PRK13651 164 fELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNlNKQGKTIILVTHDLDNV 228
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
933-1127 |
9.15e-20 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 90.65 E-value: 9.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 933 NLVKVFEpSGRPAVDRL-NITFY--ENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIET-----NLDVVRQS 1004
Cdd:PRK11629 10 NLCKRYQ-EGSVQTDVLhNVSFSigEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKlssaaKAELRNQK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1005 LGMCPQhnilFHHL----TVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDS 1080
Cdd:PRK11629 89 LGFIYQ----FHHLlpdfTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNP 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 6671495 1081 KVVVLDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLG 1127
Cdd:PRK11629 165 RLVLADEPTGNLDARNADSIFQLLgeLNRLQGTAFLVVTHDLQLAKRMS 213
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
929-1143 |
9.65e-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: 90.37 E-value: 9.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 929 VCVKNLVKVFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDI-ETNLDVVRQSLGM 1007
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVrDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1008 CPQHNILFHHlTVAEHILFyaqlkGRSwEEAQLEMEAMLEDTGLHH--KRNEEAQD---------LSGGMQRKLSVAIAF 1076
Cdd:cd03251 81 VSQDVFLFND-TVAENIAY-----GRP-GATREEVEEAARAANAHEfiMELPEGYDtvigergvkLSGGQRQRIAIARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1077 VGDSKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHM---DEAdllgDRIAIISQGRLYCSGT 1143
Cdd:cd03251 154 LKDPPILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLstiENA----DRIVVLEDGKIVERGT 219
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1955-2127 |
9.87e-20 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 89.48 E-value: 9.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1955 DRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTSISDVHQNMGYCPQFDAIDDLLTGREHLYL 2034
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLLYLGHQPGIKTELTALENLRF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2035 YARLRGVPSKEIEKVAnwgIQSLGLSLYADRLAGTYSGGNKRKLSTA-IALTGCpPLLLLDEPTTGMDPQARRMLWNTIV 2113
Cdd:PRK13538 98 YQRLHGPGDDEALWEA---LAQVGLAGFEDVPVRQLSAGQQRRVALArLWLTRA-PLWILDEPFTAIDKQGVARLEALLA 173
|
170
....*....|....
gi 6671495 2114 SIIREGRAVVLTSH 2127
Cdd:PRK13538 174 QHAEQGGMVILTTH 187
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
938-1143 |
9.87e-20 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 96.05 E-value: 9.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 938 FEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDI----ETNLdvvRQSLGMCPQHNI 1013
Cdd:PRK11160 348 YPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIadysEAAL---RQAISVVSQRVH 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1014 LFHHlTVAEHILFYAqlkgrswEEAQLE-MEAMLEDTGLH-HKRNEEAQD---------LSGGMQRKLSVAIAFVGDSKV 1082
Cdd:PRK11160 425 LFSA-TLRDNLLLAA-------PNASDEaLIEVLQQVGLEkLLEDDKGLNawlgeggrqLSGGEQRRLGIARALLHDAPL 496
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6671495 1083 VVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTH------HMdeadllgDRIAIISQGRLYCSGT 1143
Cdd:PRK11160 497 LLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHrltgleQF-------DRICVMDNGQIIEQGT 556
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
880-1144 |
1.02e-19 |
|
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: 95.64 E-value: 1.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 880 WLGgEGCSTREERALEKTEPLTEEMEDPEHpegmndsffERELPGLVPGVCVKNLVKVFEPSGR---PAVDRLNITFYEN 956
Cdd:TIGR03269 241 WLE-NGEIKEEGTPDEVVAVFMEGVSEVEK---------ECEVEVGEPIIKVRNVSKRYISVDRgvvKAVDNVSLEVKEG 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 957 QITAFLGHNGAGKTTTLSILTGLLPPTSGT--VLIGGKDIE-TNLDV-----VRQSLGMCPQHNILFHHLTVAEHILFYA 1028
Cdd:TIGR03269 311 EIFGIVGTSGAGKTTLSKIIAGVLEPTSGEvnVRVGDEWVDmTKPGPdgrgrAKRYIGILHQEYDLYPHRTVLDNLTEAI 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1029 QLKgRSWEEAQLEMEAMLEDTGLHHKRNEEAQD-----LSGGMQRKLSVAIAFVGDSKVVVLDEPTSGVDPYSRRSIWDL 1103
Cdd:TIGR03269 391 GLE-LPDELARMKAVITLKMVGFDEEKAEEILDkypdeLSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHS 469
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 6671495 1104 LLKYRS--GRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
Cdd:TIGR03269 470 ILKAREemEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDP 512
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
927-1142 |
1.05e-19 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 95.50 E-value: 1.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 927 PGVCVKNLVKVFepSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIeTNLDVVR-QSL 1005
Cdd:PRK15439 10 PLLCARSISKQY--SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPC-ARLTPAKaHQL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1006 G--MCPQHNILFHHLTVAEHILFyaQLKGRswEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVV 1083
Cdd:PRK15439 87 GiyLVPQEPLLFPNLSVKENILF--GLPKR--QASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRIL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1084 VLDEPTSGVDPYSRRSIWDLLLKYRS-GRTIIMSTHHMDEADLLGDRIAIISQGRLYCSG 1142
Cdd:PRK15439 163 ILDEPTASLTPAETERLFSRIRELLAqGVGIVFISHKLPEIRQLADRISVMRDGTIALSG 222
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
933-1149 |
1.18e-19 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 91.36 E-value: 1.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 933 NLVKV----FEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDI----ETNLDVVRQS 1004
Cdd:PRK11831 6 NLVDMrgvsFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamsRSRLYTVRKR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1005 LGMCPQHNILFHHLTVAEHILF----YAQLKgrsweEAQLEMEAM--LEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVG 1078
Cdd:PRK11831 86 MSMLFQSGALFTDMNVFDNVAYplreHTQLP-----APLLHSTVMmkLEAVGLRGAAKLMPSELSGGMARRAALARAIAL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6671495 1079 DSKVVVLDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFLKN 1149
Cdd:PRK11831 161 EPDLIMFDEPFVGQDPITMGVLVKLIseLNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQA 233
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1937-2142 |
1.27e-19 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 91.08 E-value: 1.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1937 LKLNELTKVYSGSSS--PAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTSISD---VHQ 2011
Cdd:COG4525 4 LTVRHVSVRYPGGGQpqPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADrgvVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2012 NMGYCPQFDAIDDLLTGrehlylyARLRGVPSKEIEKVANWGIQSLGLSLYADRLAGTYSGGNKRKLSTAIALTGCPPLL 2091
Cdd:COG4525 84 KDALLPWLNVLDNVAFG-------LRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 6671495 2092 LLDEPTTGMDPQAR-RM------LWNtivsiiREGRAVVLTSHSMEECEALCTRLAIM 2142
Cdd:COG4525 157 LMDEPFGALDALTReQMqellldVWQ------RTGKGVFLITHSVEEALFLATRLVVM 208
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
1950-2131 |
1.53e-19 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 88.83 E-value: 1.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1950 SSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILtsisdvhqnmGYCPQFDAIDDLL--T 2027
Cdd:NF040873 4 GRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARV----------AYVPQRSEVPDSLplT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2028 GRE--------HLYLYARLRGVPSKEIEKVanwgIQSLGLSLYADRLAGTYSGGNKRKLSTAIALTGCPPLLLLDEPTTG 2099
Cdd:NF040873 74 VRDlvamgrwaRRGLWRRLTRDDRAAVDDA----LERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTG 149
|
170 180 190
....*....|....*....|....*....|..
gi 6671495 2100 MDPQARRMLWNTIVSIIREGRAVVLTSHSMEE 2131
Cdd:NF040873 150 LDAESRERIIALLAEEHARGATVVVVTHDLEL 181
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1936-2130 |
1.87e-19 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 89.34 E-value: 1.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1936 ILKLNELTKVYSGSSsPAVDRLCVGVRPGE-CFgLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSiLTSISDVH---- 2010
Cdd:COG2884 1 MIRFENVSKRYPGGR-EALSDVSLEIEKGEfVF-LTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQD-LSRLKRREipyl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2011 -QNMGYCPQfdaidD--LLTGR---EHLYLYARLRGVPSKEIEK-VANWgIQSLGLSLYADRLAGTYSGGNKRKLSTAIA 2083
Cdd:COG2884 78 rRRIGVVFQ-----DfrLLPDRtvyENVALPLRVTGKSRKEIRRrVREV-LDLVGLSDKAKALPHELSGGEQQRVAIARA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 6671495 2084 LTGCPPLLLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSME 2130
Cdd:COG2884 152 LVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLE 198
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1959-2127 |
2.06e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 94.36 E-value: 2.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1959 VGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKsilTSISDVHQNMGYCPQFDAIDDLLTGREHLY-LYAR 2037
Cdd:COG0488 19 LSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG---LRIGYLPQEPPLDDDLTVLDTVLDGDAELRaLEAE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2038 LR------GVPSKEIEKVAN----------WGIQS--------LGLS-LYADRLAGTYSGGNKRKLSTAIALTGCPPLLL 2092
Cdd:COG0488 96 LEeleaklAEPDEDLERLAElqeefealggWEAEAraeeilsgLGFPeEDLDRPVSELSGGWRRRVALARALLSEPDLLL 175
|
170 180 190
....*....|....*....|....*....|....*
gi 6671495 2093 LDEPTTGMDPQARRMLWNTIVSiiREGrAVVLTSH 2127
Cdd:COG0488 176 LDEPTNHLDLESIEWLEEFLKN--YPG-TVLVVSH 207
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1946-2145 |
2.59e-19 |
|
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: 88.80 E-value: 2.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1946 YSGSSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI-LTSISDVHQNMGYCPQfdaiDD 2024
Cdd:cd03245 12 YPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIrQLDPADLRRNIGYVPQ----DV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2025 LL---TGREHLYLYARLrgVPSKEIEKVANWGiqslGLSLYADRLAGTY-----------SGGNKRKLSTAIALTGCPPL 2090
Cdd:cd03245 88 TLfygTLRDNITLGAPL--ADDERILRAAELA----GVTDFVNKHPNGLdlqigergrglSGGQRQAVALARALLNDPPI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 6671495 2091 LLLDEPTTGMDPQARRMLWNTIVSIIReGRAVVLTSH--SMEEceaLCTRLAIMVKG 2145
Cdd:cd03245 162 LLLDEPTSAMDMNSEERLKERLRQLLG-DKTLIIITHrpSLLD---LVDRIIVMDSG 214
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1934-2130 |
3.17e-19 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 88.95 E-value: 3.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1934 TDILKLNELTKVY-SGSSS-PAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIlTSISDV-- 2009
Cdd:COG1136 2 SPLLELRNLTKSYgTGEGEvTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDI-SSLSERel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2010 ----HQNMGYCPQFDAIDDLLTGREHLYLYARLRGVPSKEIEKVANWGIQSLGLSLYADRLAGTYSGGNKRKLSTAIALT 2085
Cdd:COG1136 81 arlrRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALV 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 6671495 2086 GCPPLLLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSME 2130
Cdd:COG1136 161 NRPKLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHDPE 206
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
938-1144 |
3.34e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 90.07 E-value: 3.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 938 FEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIETN---LDVVRQSLGMC---PQH 1011
Cdd:PRK13638 9 FRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSkrgLLALRQQVATVfqdPEQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1012 NILFhhLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTSG 1091
Cdd:PRK13638 89 QIFY--TDIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAG 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 6671495 1092 VDPYSRRSIWDLLLK-YRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
Cdd:PRK13638 167 LDPAGRTQMIAIIRRiVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAP 220
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1937-2145 |
3.75e-19 |
|
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: 89.16 E-value: 3.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1937 LKLNELTKVYsGSSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-----------S 2005
Cdd:cd03256 1 IEVENLSKTY-PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKlkgkalrqlrrQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2006 ISDVHQNMGYCPQFDAIDDLLTGR--EHLYLYARLRGVPSKEIEKvANWGIQSLGLSLYADRLAGTYSGGNKRKLSTAIA 2083
Cdd:cd03256 80 IGMIFQQFNLIERLSVLENVLSGRlgRRSTWRSLFGLFPKEEKQR-ALAALERVGLLDKAYQRADQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6671495 2084 LTGCPPLLLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKG 2145
Cdd:cd03256 159 LMQQPKLILADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDLAREYADRIVGLKDG 221
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1961-2154 |
4.63e-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: 4.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1961 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIlTSISDVHQNMGYCPQFDAIDDLLTGREHLYLYARLRG 2040
Cdd:cd03299 22 VERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDI-TNLPPEKRDISYVPQNYALFPHMTVYKNIAYGLKKRK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2041 VPSKEIEKVANWGIQSLGLSLYADRLAGTYSGGNKRKLSTAIALTGCPPLLLLDEPTTGMDPQARRMLWNTIVSIIREGR 2120
Cdd:cd03299 101 VDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEFG 180
|
170 180 190
....*....|....*....|....*....|....*
gi 6671495 2121 AVVL-TSHSMEECEALCTRLAIMVKGTFQCLGTIQ 2154
Cdd:cd03299 181 VTVLhVTHDFEEAWALADKVAIMLNGKLIQVGKPE 215
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
949-1143 |
5.45e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 88.95 E-value: 5.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLP------PTSGTVLIGGKDI-ETNLDVVRQSLGMCPQHNILFHHLTVA 1021
Cdd:PRK14246 29 ITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIfQIDAIKLRKEVGMVFQQPNPFPHLSIY 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1022 EHILFYAQLKG-RSWEEAQLEMEAMLEDTGL----HHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTSGVDPYS 1096
Cdd:PRK14246 109 DNIAYPLKSHGiKEKREIKKIVEECLRKVGLwkevYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVN 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 6671495 1097 RRSIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGT 1143
Cdd:PRK14246 189 SQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGS 235
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
925-1131 |
6.35e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 88.94 E-value: 6.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 925 LVPGVCVKNLVkvFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTS-----GTVLIGGKDI---ET 996
Cdd:PRK14258 4 LIPAIKVNNLS--FYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIyerRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 997 NLDVVRQSLGMC-PQHNILfhHLTVAEHILFYAQLKGrsWEeAQLEMEAMLEDT--------GLHHKRNEEAQDLSGGMQ 1067
Cdd:PRK14258 82 NLNRLRRQVSMVhPKPNLF--PMSVYDNVAYGVKIVG--WR-PKLEIDDIVESAlkdadlwdEIKHKIHKSALDLSGGQQ 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6671495 1068 RKLSVAIAFVGDSKVVVLDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIA 1131
Cdd:PRK14258 157 QRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIqsLRLRSELTMVIVSHNLHQVSRLSDFTA 222
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1961-2145 |
6.59e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 92.77 E-value: 6.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1961 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI-LTSISD-VHQNMGYCPQfdaiDDLLTG-------REH 2031
Cdd:COG1129 275 VRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVrIRSPRDaIRAGIAYVPE----DRKGEGlvldlsiREN 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2032 LYL-----YARLRGVPSKEIEKVANWGIQSLGL---SLyaDRLAGTYSGGNKRKLSTAIALTGCPPLLLLDEPTTGMDPQ 2103
Cdd:COG1129 351 ITLasldrLSRGGLLDRRRERALAEEYIKRLRIktpSP--EQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVG 428
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 6671495 2104 ARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2145
Cdd:COG1129 429 AKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREG 470
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1961-2146 |
7.43e-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: 86.84 E-value: 7.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1961 VRPGECFGLLGVNGAGKTTTFKMLTGDTTV--TSGDATVAGKSIltSISDVHQNMGYCPQFDAIDDLLTGREHLYLYARL 2038
Cdd:cd03213 32 AKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRPL--DKRSFRKIIGYVPQDDILHPTLTVRETLMFAAKL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2039 RGVpskeiekvanwgiqslglslyadrlagtySGGNKRKLSTAIALTGCPPLLLLDEPTTGMDP-QARRMLwNTIVSIIR 2117
Cdd:cd03213 110 RGL-----------------------------SGGERKRVSIALELVSNPSLLFLDEPTSGLDSsSALQVM-SLLRRLAD 159
|
170 180 190
....*....|....*....|....*....|
gi 6671495 2118 EGRAVVLTSHS-MEECEALCTRLAIMVKGT 2146
Cdd:cd03213 160 TGRTIICSIHQpSSEIFELFDKLLLLSQGR 189
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1932-2156 |
7.79e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 88.92 E-value: 7.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1932 NKTDILKLNELTKVYSGSSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKS--------IL 2003
Cdd:PRK13635 1 MKEEIIRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVlseetvwdVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2004 TSISDVHQNmgycP--QF---DAIDDLLTGREHlylyarlRGVPSKE-IEKVaNWGIQSLGLSLYADRLAGTYSGGNKRK 2077
Cdd:PRK13635 81 RQVGMVFQN----PdnQFvgaTVQDDVAFGLEN-------IGVPREEmVERV-DQALRQVGMEDFLNREPHRLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2078 LSTAIALTGCPPLLLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLT-SHSMEECeALCTRLAIMVKGTFQCLGTIQHL 2156
Cdd:PRK13635 149 VAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSiTHDLDEA-AQADRVIVMNKGEILEEGTPEEI 227
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1924-2151 |
8.81e-19 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 91.05 E-value: 8.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1924 RQRVMSGGNKTDILKLNELTKVYSGSssPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSiL 2003
Cdd:PRK11607 7 RPQAKTRKALTPLLEIRNLTKSFDGQ--HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVD-L 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2004 TSISDVHQNMGYCPQFDAIDDLLTGREHLYLYARLRGVPSKEIEKVANWGIQSLGLSLYADRLAGTYSGGNKRKLSTAIA 2083
Cdd:PRK11607 84 SHVPPYQRPINMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARS 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6671495 2084 LTGCPPLLLLDEPTTGMDPQARRMLWNTIVSII-REGRAVVLTSHSMEECEALCTRLAIMVKGTFQCLG 2151
Cdd:PRK11607 164 LAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILeRVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIG 232
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
931-1138 |
9.15e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 92.39 E-value: 9.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 931 VKNLvkvfepSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGK--DIETNLDVVRQSLGMC 1008
Cdd:COG1129 259 VEGL------SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKpvRIRSPRDAIRAGIAYV 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1009 P---QHNILFHHLTVAEHILFyAQLKGRSW-------EEAQLeMEAMLEDtgLHHK---RNEEAQDLSGGMQRKlsVAIA 1075
Cdd:COG1129 333 PedrKGEGLVLDLSIRENITL-ASLDRLSRgglldrrRERAL-AEEYIKR--LRIKtpsPEQPVGNLSGGNQQK--VVLA 406
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6671495 1076 --FVGDSKVVVLDEPTSGVDPYSRRSIWDLLLKY-RSGRTIIMSTHHMDEadLLG--DRIAIISQGRL 1138
Cdd:COG1129 407 kwLATDPKVLILDEPTRGIDVGAKAEIYRLIRELaAEGKAVIVISSELPE--LLGlsDRILVMREGRI 472
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
931-1138 |
1.59e-18 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 91.63 E-value: 1.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 931 VKNLVkVFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIeTNLDV-VRQSLGMC- 1008
Cdd:COG3845 260 VENLS-VRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDI-TGLSPrERRRLGVAy 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1009 ----PQHNILFHHLTVAEHILFYAQLKGR-------SWEEAQLEMEAMLED-----TGLHHKrneeAQDLSGGMQRKLSV 1072
Cdd:COG3845 338 ipedRLGRGLVPDMSVAENLILGRYRRPPfsrggflDRKAIRAFAEELIEEfdvrtPGPDTP----ARSLSGGNQQKVIL 413
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6671495 1073 AIAFVGDSKVVVLDEPTSGVDPYSRRSIWDLLLKYR-SGRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
Cdd:COG3845 414 ARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRdAGAAVLLISEDLDEILALSDRIAVMYEGRI 480
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
945-1144 |
2.29e-18 |
|
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: 86.27 E-value: 2.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPP----TSGTVLIGGKDIETNldVVRQ-SLGMCPQH-----NIL 1014
Cdd:TIGR02770 1 LVQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPgltqTSGEILLDGRPLLPL--SIRGrHIATIMQNprtafNPL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1015 FhhlTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKrnEEAQD-----LSGGMQRKLSVAIAFVGDSKVVVLDEPT 1089
Cdd:TIGR02770 79 F---TMGNHAIETLRSLGKLSKQARALILEALEAVGLPDP--EEVLKkypfqLSGGMLQRVMIALALLLEPPFLIADEPT 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 6671495 1090 SGVDPYSRRSIWDLLLKYRS--GRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
Cdd:TIGR02770 154 TDLDVVNQARVLKLLRELRQlfGTGILLITHDLGVVARIADEVAVMDDGRIVERGTV 210
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1961-2145 |
2.47e-18 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 92.48 E-value: 2.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1961 VRPGECFGLLGVNGAGKTTTFKMLTGDTT---VTSGDATVAGKSILTSISdvhQNMGYCPQFDAIDDLLTGREHLYLYAR 2037
Cdd:TIGR00956 786 VKPGTLTALMGASGAGKTTLLNVLAERVTtgvITGGDRLVNGRPLDSSFQ---RSIGYVQQQDLHLPTSTVRESLRFSAY 862
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2038 LR---GVPSKE----IEKVanwgIQSLGLSLYADRLAGTYSGG----NKRKLSTAIALTGCPPLLL-LDEPTTGMDPQAR 2105
Cdd:TIGR00956 863 LRqpkSVSKSEkmeyVEEV----IKLLEMESYADAVVGVPGEGlnveQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTA 938
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 6671495 2106 rmlWnTIVSIIRE----GRAVVLTSHS-----MEECEalctRLAIMVKG 2145
Cdd:TIGR00956 939 ---W-SICKLMRKladhGQAILCTIHQpsailFEEFD----RLLLLQKG 979
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1928-2157 |
3.06e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 86.71 E-value: 3.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1928 MSGGNKTD-ILKLNELTKVYSGSssPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTsi 2006
Cdd:COG4674 1 MSLDTMHGpILYVEDLTVSFDGF--KALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTG-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2007 SDVHQ--NMGYCPQFD--AIDDLLTGREHL------------YLYARLRGVPSKEIEKVAnwgiQSLGLSLYADRLAGTY 2070
Cdd:COG4674 77 LDEHEiaRLGIGRKFQkpTVFEELTVFENLelalkgdrgvfaSLFARLTAEERDRIEEVL----ETIGLTDKADRLAGLL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2071 SGGNKRKLSTAIALTGCPPLLLLDEPTTGMDPQARRMLWNTIVSiIREGRAVVLTSHSMEECEALCTRLAIMVKGTFQCL 2150
Cdd:COG4674 153 SHGQKQWLEIGMLLAQDPKLLLLDEPVAGMTDAETERTAELLKS-LAGKHSVVVVEHDMEFVRQIARKVTVLHQGSVLAE 231
|
....*..
gi 6671495 2151 GTIQHLK 2157
Cdd:COG4674 232 GSLDEVQ 238
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
931-1144 |
3.13e-18 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 88.99 E-value: 3.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 931 VKNLVKVFepsGRPAV-DRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIeTNLDVVRQSLGMCP 1009
Cdd:PRK10851 5 IANIKKSF---GRTQVlNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDV-SRLHARDRKVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1010 QHNILFHHLTVAEHILFYAQLKGR----SWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVL 1085
Cdd:PRK10851 81 QHYALFRHMTVFDNIAFGLTVLPRrerpNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6671495 1086 DEPTSGVDPYSRRSIWDLL------LKYRSgrtiIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
Cdd:PRK10851 161 DEPFGALDAQVRKELRRWLrqlheeLKFTS----VFVTHDQEEAMEVADRVVVMSQGNIEQAGTP 221
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
946-1138 |
3.25e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 86.51 E-value: 3.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 946 VDRLNITFYENQITAFLGHNGAGKTTTLSILTGLL-----PPTSGTVLIGGKDIeTNLDVV--RQSLGMCPQHNILFHHL 1018
Cdd:PRK14247 19 LDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIelypeARVSGEVYLDGQDI-FKMDVIelRRRVQMVFQIPNPIPNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1019 TVAEHILFYAQLK--GRSWEEAQLEMEAMLEDTGL----HHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTSGV 1092
Cdd:PRK14247 98 SIFENVALGLKLNrlVKSKKELQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANL 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 6671495 1093 DPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
Cdd:PRK14247 178 DPENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFLYKGQI 223
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
933-1138 |
4.14e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 90.36 E-value: 4.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 933 NLVKVFepsgrPAVDRL-NITF--YENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKD---------IETNLDV 1000
Cdd:PRK11288 9 GIGKTF-----PGVKALdDISFdcRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEmrfasttaaLAAGVAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1001 VRQSLGMCPQhnilfhhLTVAEHILFyAQL--KGRSWEEAQLEMEAM--LEDTGLHHKRNEEAQDLSGGMQRKLSVAIAF 1076
Cdd:PRK11288 84 IYQELHLVPE-------MTVAENLYL-GQLphKGGIVNRRLLNYEAReqLEHLGVDIDPDTPLKYLSIGQRQMVEIAKAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6671495 1077 VGDSKVVVLDEPTSGVdpySRRSIWDLLLKYRS----GRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
Cdd:PRK11288 156 ARNARVIAFDEPTSSL---SAREIEQLFRVIRElraeGRVILYVSHRMEEIFALCDAITVFKDGRY 218
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
942-1124 |
4.55e-18 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 84.84 E-value: 4.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 942 GRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPP---TSGTVLIGGKDIeTNLDVVRQSLGMCPQHNILFHHL 1018
Cdd:COG4136 13 GRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRL-TALPAEQRRIGILFQDDLLFPHL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1019 TVAEHILFyAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTSGVDPYSRR 1098
Cdd:COG4136 92 SVGENLAF-ALPPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRA 170
|
170 180
....*....|....*....|....*...
gi 6671495 1099 SIWDLLLKYRSGRTI--IMSTHhmDEAD 1124
Cdd:COG4136 171 QFREFVFEQIRQRGIpaLLVTH--DEED 196
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
958-1144 |
5.30e-18 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 86.18 E-value: 5.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 958 ITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDI--------------ETNLDVVRQSLGMCPQHNILFHHLTVAEH 1023
Cdd:PRK10619 33 VISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlvrdkdgqlkvadKNQLRLLRTRLTMVFQHFNLWSHMTVLEN 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1024 ILFY-AQLKGRSWEEAQLEMEAMLEDTGLHHK-RNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTSGVDPYSRRSIW 1101
Cdd:PRK10619 113 VMEApIQVLGLSKQEARERAVKYLAKVGIDERaQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVL 192
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 6671495 1102 DLLLKY-RSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
Cdd:PRK10619 193 RIMQQLaEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAP 236
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
938-1143 |
7.53e-18 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 85.23 E-value: 7.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 938 FEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIET-NLDVVRQSLGMCPQHNILFH 1016
Cdd:cd03252 10 YKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALaDPAWLRRQVGVVLQENVLFN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1017 HlTVAEHILFY--AQLKGRSWEEAQL--EMEAMLE-DTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTSG 1091
Cdd:cd03252 90 R-SIRDNIALAdpGMSMERVIEAAKLagAHDFISElPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 6671495 1092 VDPYSRRSIWDLLLKYRSGRTIIMSTHHMdEADLLGDRIAIISQGRLYCSGT 1143
Cdd:cd03252 169 LDYESEHAIMRNMHDICAGRTVIIIAHRL-STVKNADRIIVMEKGRIVEQGS 219
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
945-1138 |
7.95e-18 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 84.93 E-value: 7.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIE--TNLDVVRQSLGMCPQHNILFHHLTVAE 1022
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITdwQTAKIMREAVAIVPEGRRVFSRMTVEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1023 HIL---FYAqlkgrSWEEAQLEMEAMLE-DTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTSGVDPYSRR 1098
Cdd:PRK11614 100 NLAmggFFA-----ERDQFQERIKWVYElFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQ 174
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 6671495 1099 SIWDLLLKYRS-GRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
Cdd:PRK11614 175 QIFDTIEQLREqGMTIFLVEQNANQALKLADRGYVLENGHV 215
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1937-2153 |
9.10e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 86.25 E-value: 9.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1937 LKLNELTKVYSGSS---SPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIL---TSISDVH 2010
Cdd:PRK13637 3 IKIENLTHIYMEGTpfeKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkkVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2011 QNMGYCPQF-------DAID-DLLTGREHLylyarlrGVPSKEIEKVANWGIQSLGLSL--YADRLAGTYSGGNKRKLST 2080
Cdd:PRK13637 83 KKVGLVFQYpeyqlfeETIEkDIAFGPINL-------GLSEEEIENRVKRAMNIVGLDYedYKDKSPFELSGGQKRRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6671495 2081 AIALTGCPPLLLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGTFQCLGTI 2153
Cdd:PRK13637 156 AGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTP 229
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
1961-2153 |
1.33e-17 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 84.05 E-value: 1.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1961 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTSISD---VHQNMGYCPqfdaiddLLTGREHLYLYAR 2037
Cdd:TIGR01184 8 IQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDrmvVFQNYSLLP-------WLTVRENIALAVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2038 --LRGVPSKEIEKVANWGIQSLGLSLYADRLAGTYSGGNKRKLSTAIALTGCPPLLLLDEPTTGMDPQARRMLWNTIVSI 2115
Cdd:TIGR01184 81 rvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQI 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 6671495 2116 IREGR-AVVLTSHSMEECEALCTRLAIMVKGTFQCLGTI 2153
Cdd:TIGR01184 161 WEEHRvTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQI 199
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
949-1138 |
1.35e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 84.89 E-value: 1.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLL-----PPTSGTVLIGGKDI---ETNLDVVRQSLGMCPQHNILFHHLTV 1020
Cdd:PRK14267 23 VDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLelneeARVEGEVRLFGRNIyspDVDPIEVRREVGMVFQYPNPFPHLTI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1021 AEHILFYAQLKG--RSWEEAQLEMEAMLEDTGL----HHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTSGVDP 1094
Cdd:PRK14267 103 YDNVAIGVKLNGlvKSKKELDERVEWALKKAALwdevKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDP 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 6671495 1095 YSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
Cdd:PRK14267 183 VGTAKIEELLFELKKEYTIVLVTHSPAQAARVSDYVAFLYLGKL 226
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
931-1168 |
1.52e-17 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 85.06 E-value: 1.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 931 VKNLVKVFEPSgrPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLP----PTSGTVLIG---------GKDIETN 997
Cdd:PRK09984 7 VEKLAKTFNQH--QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdksAGSHIELLGrtvqregrlARDIRKS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 998 ldvvRQSLGMCPQHNILFHHLTVAEHILFYAQLKGRSW---------EEAQLEMEAmLEDTGLHHKRNEEAQDLSGGMQR 1068
Cdd:PRK09984 85 ----RANTGYIFQQFNLVNRLSVLENVLIGALGSTPFWrtcfswftrEQKQRALQA-LTRVGMVHFAHQRVSTLSGGQQQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1069 KLSVAIAFVGDSKVVVLDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLF 1146
Cdd:PRK09984 160 RVAIARALMQQAKVILADEPIASLDPESARIVMDTLrdINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQ 239
|
250 260
....*....|....*....|..
gi 6671495 1147 LKNCFGTGFYLTLVRKMKNIQS 1168
Cdd:PRK09984 240 FDNERFDHLYRSINRVEENAKA 261
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
1911-2127 |
2.65e-17 |
|
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: 88.74 E-value: 2.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1911 EPVFDEDDDVAEERQRVMSGGNKTDIlKLNELTKVYSGSSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTV 1990
Cdd:COG2274 449 DDILDLPPEREEGRSKLSLPRLKGDI-ELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEP 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1991 TSGDATVAGKSILT-SISDVHQNMGYCPQfDaiDDLLTG--REHLYLYArlRGVPSKEIEKVAnwgiQSLGLSLYADRLA 2067
Cdd:COG2274 528 TSGRILIDGIDLRQiDPASLRRQIGVVLQ-D--VFLFSGtiRENITLGD--PDATDEEIIEAA----RLAGLHDFIEALP 598
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6671495 2068 GTY-----------SGGNKRKLSTAIALTGCPPLLLLDEPTTGMDPQARRMLWNTIVSIIReGRAVVLTSH 2127
Cdd:COG2274 599 MGYdtvvgeggsnlSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK-GRTVIIIAH 668
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1932-2154 |
3.08e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 87.53 E-value: 3.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1932 NKTDILKLNELTKVYSGSSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI--LT----- 2004
Cdd:PRK09700 1 MATPYISMAGIGKSFGPVH--ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYnkLDhklaa 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2005 --SISDVHQNMGYCPQFDAIDDLLTGRehlYLYARLRGVPS---KEIEKVANWGIQSLGLSLYADRLAGTYSGGNKRKLS 2079
Cdd:PRK09700 79 qlGIGIIYQELSVIDELTVLENLYIGR---HLTKKVCGVNIidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLE 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6671495 2080 TAIALTGCPPLLLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGTFQCLGTIQ 2154
Cdd:PRK09700 156 IAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVS 230
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1950-2145 |
3.30e-17 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 83.22 E-value: 3.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1950 SSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTSISDVH----------QNMGYCPQF 2019
Cdd:PRK09493 13 PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERlirqeagmvfQQFYLFPHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2020 DAIDDLLTGRehlylyARLRGVPSKEIEKVANWGIQSLGLSLYADRLAGTYSGGNKRKLSTAIALTGCPPLLLLDEPTTG 2099
Cdd:PRK09493 93 TALENVMFGP------LRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 6671495 2100 MDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2145
Cdd:PRK09493 167 LDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKG 212
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
930-1144 |
3.49e-17 |
|
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: 82.19 E-value: 3.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 930 CVKNL-VKVfepSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGlLP---PTSGTVLIGGKDIeTNLDV---VR 1002
Cdd:cd03217 2 EIKDLhVSV---GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG-HPkyeVTEGEILFKGEDI-TDLPPeerAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1003 QSLGMCPQHNILFHHLTVAEHIlfyaqlkgRSWEEAqlemeamledtglhhkrneeaqdLSGGMQRKLSVAIAFVGDSKV 1082
Cdd:cd03217 77 LGIFLAFQYPPEIPGVKNADFL--------RYVNEG-----------------------FSGGEKKRNEILQLLLLEPDL 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6671495 1083 VVLDEPTSGVDPYSRRSIWDLLLKYRS-GRTIIMSTHHMDEADLL-GDRIAIISQGRLYCSGTP 1144
Cdd:cd03217 126 AILDEPDSGLDIDALRLVAEVINKLREeGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGDK 189
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1877-2147 |
3.68e-17 |
|
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: 87.55 E-value: 3.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1877 NLVAMAI-EGVVYFLLTLLIQHHFflTRWIAEPAREPVFDEDDDVAE------------------ERQRVMSGGNktDIL 1937
Cdd:TIGR03269 205 KLVHNALeEAVKASGISMVLTSHW--PEVIEDLSDKAIWLENGEIKEegtpdevvavfmegvsevEKECEVEVGE--PII 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1938 KLNELTKVYSGSSS---PAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSG-----------DAT---VAGK 2000
Cdd:TIGR03269 281 KVRNVSKRYISVDRgvvKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGevnvrvgdewvDMTkpgPDGR 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2001 SILTS-ISDVHQNMGYCPQFDAIDDLL--TGREHLYLYARLRGVpskeiekvanWGIQSLGLS-LYA----DRLAGTYSG 2072
Cdd:TIGR03269 361 GRAKRyIGILHQEYDLYPHRTVLDNLTeaIGLELPDELARMKAV----------ITLKMVGFDeEKAeeilDKYPDELSE 430
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6671495 2073 GNKRKLSTAIALTGCPPLLLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGTF 2147
Cdd:TIGR03269 431 GERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEmEQTFIIVSHDMDFVLDVCDRAALMRDGKI 506
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1936-2176 |
3.84e-17 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 83.60 E-value: 3.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1936 ILKLNELTKVYSGSssPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTSISD---VHQN 2012
Cdd:PRK11248 1 MLQISHLYADYGGK--PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAErgvVFQN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2013 MGYCPQFDAIDDLLTGREhlylyarLRGVPSKEIEKVANWGIQSLGLSLYADRLAGTYSGGNKRKLSTAIALTGCPPLLL 2092
Cdd:PRK11248 79 EGLLPWRNVQDNVAFGLQ-------LAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2093 LDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGTFQCLgtiQHLKYKFGDGYIVTMKIK 2171
Cdd:PRK11248 152 LDEPFGALDAFTREQMQTLLLKLWQEtGKQVLLITHDIEEAVFMATELVLLSPGPGRVV---ERLPLNFARRFVAGESSR 228
|
....*
gi 6671495 2172 SPKDD 2176
Cdd:PRK11248 229 SIKSD 233
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
1962-2156 |
4.10e-17 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 87.80 E-value: 4.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1962 RPGECFGLLGVNGAGKTT-----TFKMLTGdtTVTSGDATVAGKSIltSISDVHQNMGYCPQFDAIDDLLTGREHLYLYA 2036
Cdd:TIGR00955 49 KPGELLAVMGSSGAGKTTlmnalAFRSPKG--VKGSGSVLLNGMPI--DAKEMRAISAYVQQDDLFIPTLTVREHLMFQA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2037 RLR---GVPSKE-IEKVANWgIQSLGLSLYADRLAGT------YSGGNKRKLSTAIALTGCPPLLLLDEPTTGMDPQARR 2106
Cdd:TIGR00955 125 HLRmprRVTKKEkRERVDEV-LQALGLRKCANTRIGVpgrvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAY 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 6671495 2107 MLWNTIVSIIREGRAVVLTSH--SMEECEaLCTRLAIMVKGTFQCLGTIQHL 2156
Cdd:TIGR00955 204 SVVQVLKGLAQKGKTIICTIHqpSSELFE-LFDKIILMAEGRVAYLGSPDQA 254
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
939-1119 |
4.15e-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: 82.16 E-value: 4.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 939 EPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIETNLDVVRQSLGMCPQHNILFHHL 1018
Cdd:cd03231 9 ERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1019 TVAEHILFYAQLKGRSweeaqlEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTSGVDPYSRR 1098
Cdd:cd03231 89 SVLENLRFWHADHSDE------QVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVA 162
|
170 180
....*....|....*....|..
gi 6671495 1099 SIWDLLLKY-RSGRTIIMSTHH 1119
Cdd:cd03231 163 RFAEAMAGHcARGGMVVLTTHQ 184
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
940-1138 |
5.12e-17 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 87.47 E-value: 5.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 940 PSGRPAVDRL---NITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIET-NLDVV----RQSLGMCPQH 1011
Cdd:PRK10535 15 PSGEEQVEVLkgiSLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATlDADALaqlrREHFGFIFQR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1012 NILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTSG 1091
Cdd:PRK10535 95 YHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGA 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 6671495 1092 VDPYSRRSIWDLLLKYRS-GRTIIMSTHHMDEADlLGDRIAIISQGRL 1138
Cdd:PRK10535 175 LDSHSGEEVMAILHQLRDrGHTVIIVTHDPQVAA-QAERVIEIRDGEI 221
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1937-2145 |
5.97e-17 |
|
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: 80.50 E-value: 5.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1937 LKLNELTKVYSGSSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-SISDVHQNMGY 2015
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDlDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2016 CPQfDAIddLLTG--REHLylyarlrgvpskeiekvanwgiqslglslyadrlagtYSGGNKRKLSTAIALTGCPPLLLL 2093
Cdd:cd03228 81 VPQ-DPF--LFSGtiRENI-------------------------------------LSGGQRQRIAIARALLRDPPILIL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 6671495 2094 DEPTTGMDPQARRMLWNTIVSiIREGRAVVLTSHSMEECEaLCTRLAIMVKG 2145
Cdd:cd03228 121 DEATSALDPETEALILEALRA-LAKGKTVIVIAHRLSTIR-DADRIIVLDDG 170
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
927-1144 |
6.53e-17 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 85.66 E-value: 6.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 927 PGVCVKNLVKVFepSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIE-TNLDVVRQSL 1005
Cdd:PRK09536 2 PMIDVSDLSVEF--GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEaLSARAASRRV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1006 GMCPQHNILFHHLTVaEHILFYAQLKGRS----WEEA-QLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDS 1080
Cdd:PRK09536 80 ASVPQDTSLSFEFDV-RQVVEMGRTPHRSrfdtWTETdRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQAT 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6671495 1081 KVVVLDEPTSGVDpySRRSIWDLLLKYR---SGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
Cdd:PRK09536 159 PVLLLDEPTASLD--INHQVRTLELVRRlvdDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPP 223
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1936-2145 |
8.40e-17 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 86.23 E-value: 8.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1936 ILKLNELTKVYSGSSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIltSISD------- 2008
Cdd:COG3845 5 ALELRGITKRFGGVV--ANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPV--RIRSprdaial 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2009 ----VHQNMGYCPQFDAIDDLLTGREHLYLYARLRGVPSKEIEKVAnwgiQSLGLSLYADRLAGTYSGGNKRKLSTAIAL 2084
Cdd:COG3845 81 gigmVHQHFMLVPNLTVAENIVLGLEPTKGGRLDRKAARARIRELS----ERYGLDVDPDAKVEDLSVGEQQRVEILKAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6671495 2085 TGCPPLLLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2145
Cdd:COG3845 157 YRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRG 217
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
957-1118 |
8.99e-17 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 81.75 E-value: 8.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 957 QITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDI-----ETNLDVVRQSLGMCPQHNILFHHLTVAEHILFYAQLK 1031
Cdd:PRK10584 37 ETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLhqmdeEARAKLRAKHVGFVFQSFMLIPTLNALENVELPALLR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1032 GRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTSGVDPYSRRSIWDLL--LKYRS 1109
Cdd:PRK10584 117 GESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLfsLNREH 196
|
....*....
gi 6671495 1110 GRTIIMSTH 1118
Cdd:PRK10584 197 GTTLILVTH 205
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1938-2152 |
9.88e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 83.24 E-value: 9.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1938 KLNELTKVYSGSSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTG-----DTTVTSGDATVAGKSILTSISDVHQN 2012
Cdd:PRK13643 6 KVNYTYQPNSPFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGllqptEGKVTVGDIVVSSTSKQKEIKPVRKK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2013 MGYCPQF--------DAIDDLLTGREHLylyarlrGVPSKEIEKVANWGIQSLGLSL-YADRLAGTYSGGNKRKLSTAIA 2083
Cdd:PRK13643 86 VGVVFQFpesqlfeeTVLKDVAFGPQNF-------GIPKEKAEKIAAEKLEMVGLADeFWEKSPFELSGGQMRRVAIAGI 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6671495 2084 LTGCPPLLLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGTFQCLGT 2152
Cdd:PRK13643 159 LAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGT 227
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
949-1144 |
1.24e-16 |
|
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: 84.01 E-value: 1.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGK---DIETNLDVV--RQSLGMCPQHNILFHHLTVAEH 1023
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRtlfDSRKGIFLPpeKRRIGYVFQEARLFPHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1024 iLFYAQLKGRSwEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTSGVDPYSRRSIWDL 1103
Cdd:TIGR02142 96 -LRYGMKRARP-SERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPY 173
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 6671495 1104 L--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
Cdd:TIGR02142 174 LerLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPI 216
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1941-2130 |
1.26e-16 |
|
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: 80.91 E-value: 1.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1941 ELTKVYsGSSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGksilTSISDVH--------QN 2012
Cdd:cd03292 5 NVTKTY-PNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNG----QDVSDLRgraipylrRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2013 MGYCPQ-FDAIDDLlTGREHLYLYARLRGVPSKEIEKVANWGIQSLGLSLYADRLAGTYSGGNKRKLSTAIALTGCPPLL 2091
Cdd:cd03292 80 IGVVFQdFRLLPDR-NVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTIL 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 6671495 2092 LLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSME 2130
Cdd:cd03292 159 IADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKE 197
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1963-2145 |
1.40e-16 |
|
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: 80.80 E-value: 1.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1963 PGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAG-------KSILTS-----ISDVHQNMGYCPQFDAIDDLLTGre 2030
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfdsrKKINLPpqqrkIGLVFQQYALFPHLNVRENLAFG-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2031 hlylyarLRGVPSKEIEKVANWGIQSLGLSLYADRLAGTYSGGNKRKLSTAIALTGCPPLLLLDEPTTGMDPQARRMLWN 2110
Cdd:cd03297 100 -------LKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLP 172
|
170 180 190
....*....|....*....|....*....|....*.
gi 6671495 2111 TIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKG 2145
Cdd:cd03297 173 ELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDG 208
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1947-2152 |
1.61e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 82.44 E-value: 1.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1947 SGSSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAG--KSILTSISDVHQNMGYCPQ------ 2018
Cdd:PRK13633 19 ESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldTSDEENLWDIRNKAGMVFQnpdnqi 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2019 FDAI--DDLLTGREHLylyarlrGVPSKEIEKVANWGIQSLGLSLYADRLAGTYSGGNKRKLSTAIALTGCPPLLLLDEP 2096
Cdd:PRK13633 99 VATIveEDVAFGPENL-------GIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEP 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 6671495 2097 TTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECeALCTRLAIMVKGTFQCLGT 2152
Cdd:PRK13633 172 TAMLDPSGRREVVNTIKELNKKyGITIILITHYMEEA-VEADRIIVMDSGKVVMEGT 227
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1936-2145 |
1.65e-16 |
|
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: 85.26 E-value: 1.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1936 ILKLNELTKVYSGSSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTG--DTTVTSGDATVAGKSILTS-------- 2005
Cdd:TIGR02633 1 LLEMKGIVKTFGGVK--ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGvyPHGTWDGEIYWSGSPLKASnirdtera 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2006 -ISDVHQNMGYCPQFDAIDDLLTGREhLYLYARLRGVPskEIEKVANWGIQSLGLSLYAD-RLAGTYSGGNKRKLSTAIA 2083
Cdd:TIGR02633 79 gIVIIHQELTLVPELSVAENIFLGNE-ITLPGGRMAYN--AMYLRAKNLLRELQLDADNVtRPVGDYGGGQQQLVEIAKA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6671495 2084 LTGCPPLLLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2145
Cdd:TIGR02633 156 LNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDG 217
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1964-2127 |
1.76e-16 |
|
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: 80.23 E-value: 1.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1964 GECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTSISDVHQNMGYCPQFDAIDDLLTGREHLYLYARLRGvpS 2043
Cdd:cd03231 26 GEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENLRFWHADHS--D 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2044 KEIEKvanwGIQSLGLSLYADRLAGTYSGGNKRKLSTAIALTGCPPLLLLDEPTTGMDPQARRMLWNTIVSIIREGRAVV 2123
Cdd:cd03231 104 EQVEE----ALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGHCARGGMVV 179
|
....
gi 6671495 2124 LTSH 2127
Cdd:cd03231 180 LTTH 183
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1937-2127 |
1.96e-16 |
|
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: 79.28 E-value: 1.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1937 LKLNELTKVYSGSSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTSISDVHQNMGYC 2016
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2017 PQfdaiddlltgREHLYlYARLRgvpskeiekvANWGIQslglslyadrlagtYSGGNKRKLSTAIALTGCPPLLLLDEP 2096
Cdd:cd03247 81 NQ----------RPYLF-DTTLR----------NNLGRR--------------FSGGERQRLALARILLQDAPIVLLDEP 125
|
170 180 190
....*....|....*....|....*....|.
gi 6671495 2097 TTGMDPQARRMLWNTIVSIIREGRAVVLTSH 2127
Cdd:cd03247 126 TVGLDPITERQLLSLIFEVLKDKTLIWITHH 156
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
957-1119 |
2.10e-16 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 79.85 E-value: 2.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 957 QITaflGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIETNLDVVRQSLgmcpqhniLF--HH------LTVAEHILFYA 1028
Cdd:PRK13538 31 QIE---GPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDL--------LYlgHQpgikteLTALENLRFYQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1029 QLKGRSWEEAqleMEAMLEDTGLHhkRNEE--AQDLSGGMQRKlsVAIA--FVGDSKVVVLDEPTSGVDPYSRRSIWDLL 1104
Cdd:PRK13538 100 RLHGPGDDEA---LWEALAQVGLA--GFEDvpVRQLSAGQQRR--VALArlWLTRAPLWILDEPFTAIDKQGVARLEALL 172
|
170
....*....|....*.
gi 6671495 1105 LKY-RSGRTIIMSTHH 1119
Cdd:PRK13538 173 AQHaEQGGMVILTTHQ 188
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1952-2152 |
2.24e-16 |
|
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: 80.85 E-value: 2.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1952 PAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIlTSISDVHQNMGYCPQFDAIDDLLTGREH 2031
Cdd:cd03296 16 VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDA-TDVPVQERNVGFVFQHYALFRHMTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2032 ----LYLYARLRGVPSKEIEKVANWGIQSLGLSLYADRLAGTYSGGNKRKLSTAIALTGCPPLLLLDEPTTGMDPQARRM 2107
Cdd:cd03296 95 vafgLRVKPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 6671495 2108 L--WntivsiIRE-----GRAVVLTSHSMEECEALCTRLAIMVKGTFQCLGT 2152
Cdd:cd03296 175 LrrW------LRRlhdelHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGT 220
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1934-2156 |
2.37e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 81.70 E-value: 2.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1934 TDILKLNELT-KVYSGSSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGK--------SILT 2004
Cdd:PRK13650 2 SNIIEVKNLTfKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDllteenvwDIRH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2005 SISDVHQNmgycP--QFDAI---DDLLTGREHlylyarlRGVPSKEIEKVANWGIQSLGLSLYADRLAGTYSGGNKRKLS 2079
Cdd:PRK13650 82 KIGMVFQN----PdnQFVGAtveDDVAFGLEN-------KGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6671495 2080 TAIALTGCPPLLLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECeALCTRLAIMVKGTFQCLGTIQHL 2156
Cdd:PRK13650 151 IAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDEV-ALSDRVLVMKNGQVESTSTPREL 227
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
927-1142 |
2.47e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 81.68 E-value: 2.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 927 PGVCVKNLVKVFepSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSG-----TVLIGGKDIETNLDVV 1001
Cdd:PRK14271 20 PAMAAVNLTLGF--AGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRDVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1002 --RQSLGMCPQHNILFHhLTVAEHILfyAQLKGRSW---EEAQLEMEAMLEDTGLHHKRNEEAQD----LSGGMQRKLSV 1072
Cdd:PRK14271 98 efRRRVGMLFQRPNPFP-MSIMDNVL--AGVRAHKLvprKEFRGVAQARLTEVGLWDAVKDRLSDspfrLSGGQQQLLCL 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1073 AIAFVGDSKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSG 1142
Cdd:PRK14271 175 ARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEG 244
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1952-2142 |
2.86e-16 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 80.17 E-value: 2.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1952 PAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATV--AGKSI-LTSISDVH------QNMGYCPQFdai 2022
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWVdLAQASPREilalrrRTIGYVSQF--- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2023 ddL-----LTGREHLYLYARLRGVPSKE-IEKVANWgIQSLGL-----SLYAdrlaGTYSGGNKRKLSTAIALTGCPPLL 2091
Cdd:COG4778 102 --LrviprVSALDVVAEPLLERGVDREEaRARAREL-LARLNLperlwDLPP----ATFSGGEQQRVNIARGFIADPPLL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 6671495 2092 LLDEPTTGMDPQARRmlwnTIVSIIRE----GRAVVLTSHSMEECEALCTRLAIM 2142
Cdd:COG4778 175 LLDEPTASLDAANRA----VVVELIEEakarGTAIIGIFHDEEVREAVADRVVDV 225
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
945-1131 |
3.01e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 80.98 E-value: 3.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSI---LTGLLPP--TSGTVLIGGKDI-ETNLDV--VRQSLGMCPQHNILFH 1016
Cdd:PRK14243 25 AVKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrLNDLIPGfrVEGKVTFHGKNLyAPDVDPveVRRRIGMVFQKPNPFP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1017 HlTVAEHILFYAQLKG----------RSWEEAQL--EMEAMLEDTGLhhkrneeaqDLSGGMQRKLSVAIAFVGDSKVVV 1084
Cdd:PRK14243 105 K-SIYDNIAYGARINGykgdmdelveRSLRQAALwdEVKDKLKQSGL---------SLSGGQQQRLCIARAIAVQPEVIL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 6671495 1085 LDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIA 1131
Cdd:PRK14243 175 MDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTA 221
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1936-2152 |
4.04e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 80.80 E-value: 4.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1936 ILKLNELTKVYSgSSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAG---------KSILTSI 2006
Cdd:PRK13644 1 MIRLENVSYSYP-DGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGidtgdfsklQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2007 SDVHQNmgycPQFDAI-----DDLLTGREHLYLyarlrgvPSKEIEKVANWGIQSLGLSLYADRLAGTYSGGNKRKLSTA 2081
Cdd:PRK13644 80 GIVFQN----PETQFVgrtveEDLAFGPENLCL-------PPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6671495 2082 IALTGCPPLLLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEAlCTRLAIMVKGTFQCLGT 2152
Cdd:PRK13644 149 GILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGE 218
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
950-1151 |
4.17e-16 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 80.06 E-value: 4.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 950 NITFY--ENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGK--DIETNLD-----VVRQSLGMCPQHNILFHHLTV 1020
Cdd:COG4161 20 DINLEcpSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfDFSQKPSekairLLRQKVGMVFQQYNLWPHLTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1021 AEHiLFYAQLK--GRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTSGVDPYSRR 1098
Cdd:COG4161 100 MEN-LIEAPCKvlGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 6671495 1099 SIWDLLLKY-RSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTplflKNCF 1151
Cdd:COG4161 179 QVVEIIRELsQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGD----ASHF 228
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
931-1139 |
5.30e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 83.58 E-value: 5.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 931 VKNLVKVFepSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGkdietnldvvRQSLGMCPQ 1010
Cdd:COG0488 1 LENLSKSF--GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK----------GLRIGYLPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1011 HNILFHHLTVAEHIL----FYAQLKGRsWEEAQLEMEAMLED----TGLHHKRNE------EAQ---------------- 1060
Cdd:COG0488 69 EPPLDDDLTVLDTVLdgdaELRALEAE-LEELEAKLAEPDEDlerlAELQEEFEAlggweaEARaeeilsglgfpeedld 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1061 ----DLSGGMQRKLSVAIAFVGDSKVVVLDEPTSGVDPYSRRsiW--DLLLKYRSgrTIIMSTH--H-MDEadlLGDRIA 1131
Cdd:COG0488 148 rpvsELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIE--WleEFLKNYPG--TVLVVSHdrYfLDR---VATRIL 220
|
....*...
gi 6671495 1132 IISQGRLY 1139
Cdd:COG0488 221 ELDRGKLT 228
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
928-1152 |
5.82e-16 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 82.09 E-value: 5.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 928 GVCVKNLVKVFEPSgrPAVDRLNITFYENQITAFLGHNGAgktttlSILTGLLP-----PTSGTVLIGGKDIETNLDVVR 1002
Cdd:NF000106 13 AVEVRGLVKHFGEV--KAVDGVDLDVREGTVLGVLGP*GA------A**RGALPahv*gPDAGRRPWRF*TWCANRRALR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1003 QSLGMC-PQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSK 1081
Cdd:NF000106 85 RTIG*HrPVR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6671495 1082 VVVLDEPTSGVDPYSRRSIWDLLLKY-RSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFLKNCFG 1152
Cdd:NF000106 165 VLYLDEPTTGLDPRTRNEVWDEVRSMvRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVG 236
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
950-1138 |
6.33e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 83.30 E-value: 6.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 950 NITFY--ENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIE--TNLDVVRQSLGMCPQH---NILFHHLTVAE 1022
Cdd:PRK09700 281 DISFSvcRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISprSPLDAVKKGMAYITESrrdNGFFPNFSIAQ 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1023 HILFYAQLKGRSW----------EEAQLEmEAMLEDTGLH-HKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTSG 1091
Cdd:PRK09700 361 NMAISRSLKDGGYkgamglfhevDEQRTA-ENQRELLALKcHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRG 439
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 6671495 1092 VDPYSRRSIWDLLLKY-RSGRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
Cdd:PRK09700 440 IDVGAKAEIYKVMRQLaDDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1938-2145 |
7.18e-16 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 81.39 E-value: 7.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1938 KLNELTKVYSGSSSP--AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSiLTSISD-----VH 2010
Cdd:PRK11153 3 ELKNISKVFPQGGRTihALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQD-LTALSEkelrkAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2011 QNMGYCPQ-FDaiddLLTGR---EHLYLYARLRGVPSKEIEKVANWGIQSLGLSLYADRLAGTYSGGNKRKLSTAIALTG 2086
Cdd:PRK11153 82 RQIGMIFQhFN----LLSSRtvfDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALAS 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2087 CPPLLLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKG 2145
Cdd:PRK11153 158 NPKVLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVIDAG 217
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
907-1138 |
8.59e-16 |
|
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: 83.26 E-value: 8.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 907 PEHPEGMndsfferELPGLVPGVCVKNLVKVFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGT 986
Cdd:COG4618 316 PAEPERM-------PLPRPKGRLSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGS 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 987 VLIGGKDIET-NLDVVRQSLGMCPQHNILFHHlTVAEHIlfyAQLKGRSWEE----AQL----EM--------EAMLEDT 1049
Cdd:COG4618 389 VRLDGADLSQwDREELGRHIGYLPQDVELFDG-TIAENI---ARFGDADPEKvvaaAKLagvhEMilrlpdgyDTRIGEG 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1050 GLHhkrneeaqdLSGG-MQRkLSVAIAFVGDSKVVVLDEPTSGVDPYSRRSIWDLL--LKYRsGRTIIMSTHHMdeaDLL 1126
Cdd:COG4618 465 GAR---------LSGGqRQR-IGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIraLKAR-GATVVVITHRP---SLL 530
|
250
....*....|....
gi 6671495 1127 G--DRIAIISQGRL 1138
Cdd:COG4618 531 AavDKLLVLRDGRV 544
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
1937-2128 |
9.50e-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: 82.79 E-value: 9.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1937 LKLNELTKVYSGSSsPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-SISDVHQNMGY 2015
Cdd:TIGR02868 335 LELRDLSAGYPGAP-PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSlDQDEVRRRVSV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2016 CPQ----FDA--IDDLLTGREHLY---LYARLRGVpskeieKVANWgIQSL--GLSLYADRLAGTYSGGNKRKLSTAIAL 2084
Cdd:TIGR02868 414 CAQdahlFDTtvRENLRLARPDATdeeLWAALERV------GLADW-LRALpdGLDTVLGEGGARLSGGERQRLALARAL 486
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 6671495 2085 TGCPPLLLLDEPTTGMDPQARRMLWNTIVSIIrEGRAVVLTSHS 2128
Cdd:TIGR02868 487 LADAPILLLDEPTEHLDAETADELLEDLLAAL-SGRTVVLITHH 529
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1957-2128 |
1.16e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 77.99 E-value: 1.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1957 LCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIltSISDVHQNMGYCPQFDAIDDLLTGREHLYLYA 2036
Cdd:PRK13539 21 LSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI--DDPDVAEACHYLGHRNAMKPALTVAENLEFWA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2037 RLRGVPSKEIEKVanwgIQSLGLSLYADRLAGTYSGGNKRKLSTAIALTGCPPLLLLDEPTTGMDPQARRMLWNTIVSII 2116
Cdd:PRK13539 99 AFLGGEELDIAAA----LEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELIRAHL 174
|
170
....*....|..
gi 6671495 2117 REGRAVVLTSHS 2128
Cdd:PRK13539 175 AQGGIVIAATHI 186
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1937-2145 |
1.18e-15 |
|
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: 76.87 E-value: 1.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1937 LKLNELTKVYSGSSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI-LTSISDVHQNMGY 2015
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADIsQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2016 CPQfdaiDDLLtgrehlylyarlrgvpskeiekvanwgiqslglslyadrLAGT-----YSGGNKRKLSTAIALTGCPPL 2090
Cdd:cd03246 81 LPQ----DDEL---------------------------------------FSGSiaeniLSGGQRQRLGLARALYGNPRI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 6671495 2091 LLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEAlCTRLAIMVKG 2145
Cdd:cd03246 118 LVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLAS-ADRILVLEDG 171
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1951-2167 |
1.30e-15 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 81.62 E-value: 1.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1951 SPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIlTSISD-------------VHQNMGYCP 2017
Cdd:PRK10070 41 SLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDI-AKISDaelrevrrkkiamVFQSFALMP 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2018 QFDAIDDLLTGREhlylyarLRGVPSKEIEKVANWGIQSLGLSLYADRLAGTYSGGNKRKLSTAIALTGCPPLLLLDEPT 2097
Cdd:PRK10070 120 HMTVLDNTAFGME-------LAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAF 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6671495 2098 TGMDPQARRMLWNTIVSI-IREGRAVVLTSHSMEECEALCTRLAIMVKGTFQCLGTIQHLKYKFGDGYIVT 2167
Cdd:PRK10070 193 SALDPLIRTEMQDELVKLqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRT 263
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
943-1138 |
1.70e-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: 77.90 E-value: 1.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 943 RPAVDRL-NITF--YENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIET-NLDVVRQSLGMCPQHNILFHHl 1018
Cdd:cd03248 24 RPDTLVLqDVSFtlHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQyEHKYLHSKVSLVGQEPVLFAR- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1019 TVAEHILFyaQLKGRSWE---EAQLEMEA----MLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTSG 1091
Cdd:cd03248 103 SLQDNIAY--GLQSCSFEcvkEAAQKAHAhsfiSELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSA 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 6671495 1092 VDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADlLGDRIAIISQGRL 1138
Cdd:cd03248 181 LDAESEQQVQQALYDWPERRTVLVIAHRLSTVE-RADQILVLDGGRI 226
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
950-1118 |
1.79e-15 |
|
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: 76.90 E-value: 1.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 950 NITFY--ENQITAFLGHNGAGKTTTLSIL-----TGLlppTSGTVLIGGKDIETNLdvvRQSLGMCPQHNILFHHLTVAE 1022
Cdd:cd03232 25 NISGYvkPGTLTALMGESGAGKTTLLDVLagrktAGV---ITGEILINGRPLDKNF---QRSTGYVEQQDVHSPNLTVRE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1023 HILFYAQLKGRSWEEaqlemeamledtglhhkrneeaqdlsggmQRKLSVAIAFVGDSKVVVLDEPTSGVDPYSRRSIWD 1102
Cdd:cd03232 99 ALRFSALLRGLSVEQ-----------------------------RKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVR 149
|
170
....*....|....*..
gi 6671495 1103 LLLKY-RSGRTIIMSTH 1118
Cdd:cd03232 150 FLKKLaDSGQAILCTIH 166
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1936-2145 |
2.57e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 78.20 E-value: 2.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1936 ILKLNELTKV-YSGSSS--PAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-------- 2004
Cdd:COG1101 1 MLELKNLSKTfNPGTVNekRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKlpeykrak 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2005 SISDVHQN--MGYCPQfdaiddlLTGREHLYL-YAR-----LR-GVPSKEIEKVANWgIQSLGLSLyADRL---AGTYSG 2072
Cdd:COG1101 81 YIGRVFQDpmMGTAPS-------MTIEENLALaYRRgkrrgLRrGLTKKRRELFREL-LATLGLGL-ENRLdtkVGLLSG 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6671495 2073 GNKRKLSTAIAlTGCPP-LLLLDEPTTGMDPQARRMLWNTIVSIIREGRavvLTS----HSMEECEALCTRLAIMVKG 2145
Cdd:COG1101 152 GQRQALSLLMA-TLTKPkLLLLDEHTAALDPKTAALVLELTEKIVEENN---LTTlmvtHNMEQALDYGNRLIMMHEG 225
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
913-1143 |
2.62e-15 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 81.93 E-value: 2.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 913 MNDSFFE-RELPGLVPGVCVKNLVkVFE------PSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSG 985
Cdd:PRK13657 312 VEDAVPDvRDPPGAIDLGRVKGAV-EFDdvsfsyDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSG 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 986 TVLIGGKDIET-NLDVVRQSLGMCPQHNILFHHlTVAEHILFyaqlkGRswEEAQL-EMEAMLE-----------DTGLH 1052
Cdd:PRK13657 391 RILIDGTDIRTvTRASLRRNIAVVFQDAGLFNR-SIEDNIRV-----GR--PDATDeEMRAAAEraqahdfierkPDGYD 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1053 HKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMD---EAdllgDR 1129
Cdd:PRK13657 463 TVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLStvrNA----DR 538
|
250
....*....|....
gi 6671495 1130 IAIISQGRLYCSGT 1143
Cdd:PRK13657 539 ILVFDNGRVVESGS 552
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1964-2146 |
2.89e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 78.39 E-value: 2.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1964 GECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTSIsdvHQNM-GYCPQFDAID---------DLLTGRehlY 2033
Cdd:PRK15056 33 GSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQAL---QKNLvAYVPQSEEVDwsfpvlvedVVMMGR---Y 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2034 LYARLRGVPSKEIEKVANWGIQSLGLSLYADRLAGTYSGGNKRK--LSTAIALTGcpPLLLLDEPTTGMDPQ--ARrmlw 2109
Cdd:PRK15056 107 GHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRvfLARAIAQQG--QVILLDEPFTGVDVKteAR---- 180
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 6671495 2110 ntIVSIIR----EGRAVVLTSHSMEECEALCTrLAIMVKGT 2146
Cdd:PRK15056 181 --IISLLRelrdEGKTMLVSTHNLGSVTEFCD-YTVMVKGT 218
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1937-2145 |
3.13e-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: 77.22 E-value: 3.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1937 LKLNELTKVYSGSSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTG-----DTTVTSGDATVAGKSILTSISDVHQ 2011
Cdd:cd03260 1 IELRDLNVYYGDKH--ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLDGKDIYDLDVDVLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2012 ---NMGYCPQ----FDAiddllTGREHLYLYARLRGV-PSKEIEKVANWGIQSLGLSLY-ADRLAGTY-SGGNKRKLSTA 2081
Cdd:cd03260 79 lrrRVGMVFQkpnpFPG-----SIYDNVAYGLRLHGIkLKEELDERVEEALRKAALWDEvKDRLHALGlSGGQQQRLCLA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6671495 2082 IALTGCPPLLLLDEPTTGMDPQARRMLWNTIVSIIREgRAVVLTSHSMEECEALCTRLAIMVKG 2145
Cdd:cd03260 154 RALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNG 216
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
931-1144 |
3.30e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 78.21 E-value: 3.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 931 VKNLVkvFEPSGRPAVDRLN---ITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIET-NLDVVRQSLG 1006
Cdd:PRK13642 7 VENLV--FKYEKESDVNQLNgvsFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAeNVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1007 MCPQH-NILFHHLTVAEHILFYAQLKGRSWEEAQLEM-EAMLEDTGLHHKRNEEAQdLSGGMQRKLSVAIAFVGDSKVVV 1084
Cdd:PRK13642 85 MVFQNpDNQFVGATVEDDVAFGMENQGIPREEMIKRVdEALLAVNMLDFKTREPAR-LSGGQKQRVAVAGIIALRPEIII 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6671495 1085 LDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEAdLLGDRIAIISQGRLYCSGTP 1144
Cdd:PRK13642 164 LDESTSMLDPTGRQEIMRVIheIKEKYQLTVLSITHDLDEA-ASSDRILVMKAGEIIKEAAP 224
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1961-2145 |
3.58e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 80.87 E-value: 3.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1961 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI--LTSISDVHQNMGYCPQfdaiDDLLTGrehLYLYARL 2038
Cdd:PRK15439 286 VRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEInaLSTAQRLARGLVYLPE----DRQSSG---LYLDAPL 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2039 R-----------GV---PSKEIEKVANWGiQSLGLSL-YADRLAGTYSGGNKRKLSTAIALTGCPPLLLLDEPTTGMDPQ 2103
Cdd:PRK15439 359 AwnvcalthnrrGFwikPARENAVLERYR-RALNIKFnHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVS 437
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 6671495 2104 ARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2145
Cdd:PRK15439 438 ARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQG 479
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
1911-2130 |
4.38e-15 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 80.96 E-value: 4.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1911 EPVFDEDDDVAEERQRVMSGGNKTDIlKLNELTkVYSGSSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTV 1990
Cdd:COG4988 312 FALLDAPEPAAPAGTAPLPAAGPPSI-ELEDVS-FSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPP 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1991 TSGDATVAGKSILT-SISDVHQNMGYCPQFDAiddLLTG--REHLYLYArlRGVPSKEIEKVAnwgiQSLGLSLYADRLA 2067
Cdd:COG4988 390 YSGSILINGVDLSDlDPASWRRQIAWVPQNPY---LFAGtiRENLRLGR--PDASDEELEAAL----EAAGLDEFVAALP 460
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6671495 2068 GTY-----------SGGNKRKLSTAIALTGCPPLLLLDEPTTGMDPQARRMLWNTIVSiIREGRAVVLTSHSME 2130
Cdd:COG4988 461 DGLdtplgeggrglSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRR-LAKGRTVILITHRLA 533
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1936-2156 |
4.59e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 77.92 E-value: 4.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1936 ILKLNELTKVYSGSSSpAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIL-TSISDVHQNMG 2014
Cdd:PRK13652 3 LIETRDLCYSYSGSKE-ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITkENIREVRKFVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2015 YCpqFDAIDDLL---TGREHLYLYARLRGVPSKEIEKVANWGIQSLGLSLYADRLAGTYSGGNKRKLSTAIALTGCPPLL 2091
Cdd:PRK13652 82 LV--FQNPDDQIfspTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6671495 2092 LLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGTFQCLGTIQHL 2156
Cdd:PRK13652 160 VLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1936-2145 |
4.84e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 77.81 E-value: 4.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1936 ILKLNELTKVYSGSSSpAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIL---TSISDVHQN 2012
Cdd:PRK13639 1 ILETRDLKYSYPDGTE-ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKydkKSLLEVRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2013 MGYCpqFDAIDDLL---TGREHLYLYARLRGVPSKEIEKVANWGIQSLGLSLYADRLAGTYSGGNKRKLSTAIALTGCPP 2089
Cdd:PRK13639 80 VGIV--FQNPDDQLfapTVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 6671495 2090 LLLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2145
Cdd:PRK13639 158 IIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDG 213
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
936-1138 |
4.96e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 80.43 E-value: 4.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 936 KVFEPSGrPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIETN-----LD--VVRQS---- 1004
Cdd:PRK10762 259 KVDNLSG-PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRspqdgLAngIVYISedrk 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1005 -----LGMCPQHNIlfhHLTVAEHilfYAQLKGRsweeaqlemeamledtgLHHKRNEEAQD------------------ 1061
Cdd:PRK10762 338 rdglvLGMSVKENM---SLTALRY---FSRAGGS-----------------LKHADEQQAVSdfirlfniktpsmeqaig 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1062 -LSGGMQRKLSVAIAFVGDSKVVVLDEPTSGVDPYSRRSIWDLLLKYRS-GRTIIMSTHHMDEadLLG--DRIAIISQGR 1137
Cdd:PRK10762 395 lLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAeGLSIILVSSEMPE--VLGmsDRILVMHEGR 472
|
.
gi 6671495 1138 L 1138
Cdd:PRK10762 473 I 473
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
938-1122 |
5.28e-15 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 76.68 E-value: 5.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 938 FEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIET-NLDVVRQSLGMCPQHNILFH 1016
Cdd:PRK10247 15 YLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTlKPEIYRQQVSYCAQTPTLFG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1017 HlTVAEHILFYAQLKGRSWEEAQLEMEAM---LEDTGLHHKRNEeaqdLSGGMQRKLSVA--IAFVgdSKVVVLDEPTSG 1091
Cdd:PRK10247 95 D-TVYDNLIFPWQIRNQQPDPAIFLDDLErfaLPDTILTKNIAE----LSGGEKQRISLIrnLQFM--PKVLLLDEITSA 167
|
170 180 190
....*....|....*....|....*....|...
gi 6671495 1092 VDPYSRRSIWDLLLKYRSGRTI--IMSTHHMDE 1122
Cdd:PRK10247 168 LDESNKHNVNEIIHRYVREQNIavLWVTHDKDE 200
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1935-2139 |
6.03e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 80.49 E-value: 6.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1935 DILKLNELTKVYSGSssPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVaGKSIltsisdvhqNMG 2014
Cdd:COG0488 314 KVLELEGLSKSYGDK--TLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV---------KIG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2015 YCPQ-FDAIDDLLTGREHLylyarLRGVPSKEIEKVANWgiqsLGLSL----YADRLAGTYSGGNKRKLSTAIALTGCPP 2089
Cdd:COG0488 382 YFDQhQEELDPDKTVLDEL-----RDGAPGGTEQEVRGY----LGRFLfsgdDAFKPVGVLSGGEKARLALAKLLLSPPN 452
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 6671495 2090 LLLLDEPTTGMDPQARRMLWNTIVSIirEGrAVVLTSHSMEECEALCTRL 2139
Cdd:COG0488 453 VLLLDEPTNHLDIETLEALEEALDDF--PG-TVLLVSHDRYFLDRVATRI 499
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
929-1137 |
6.69e-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: 73.64 E-value: 6.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 929 VCVKNLVKVFEpsGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKdietnldvvrqslgmc 1008
Cdd:cd03221 1 IELENLSKTYG--GKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST---------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1009 pqhnilfhhltvaEHILFYAQlkgrsweeaqlemeamledtglhhkrneeaqdLSGGMQRKLSVAIAFVGDSKVVVLDEP 1088
Cdd:cd03221 63 -------------VKIGYFEQ--------------------------------LSGGEKMRLALAKLLLENPNLLLLDEP 97
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 6671495 1089 TSGVDPYSRRSIWDLLLKYRsgRTIIMSTHhmDEA--DLLGDRIAIISQGR 1137
Cdd:cd03221 98 TNHLDLESIEALEEALKEYP--GTVILVSH--DRYflDQVATKIIELEDGK 144
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
938-1147 |
7.13e-15 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 77.14 E-value: 7.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 938 FEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIET-NLDVVRQSLGMCPQHNILFH 1016
Cdd:PRK10575 19 FRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESwSSKAFARKVAYLPQQLPAAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1017 HLTVAEHIL-----FYAQLkGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTSG 1091
Cdd:PRK10575 99 GMTVRELVAigrypWHGAL-GRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSA 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 6671495 1092 VDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFL 1147
Cdd:PRK10575 178 LDIAHQVDVLALVhrLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
1946-2139 |
7.19e-15 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 75.66 E-value: 7.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1946 YSGSSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTSisDVHQNMGYCPQFDAIDDL 2025
Cdd:PRK13543 19 FSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRG--DRSRFMAYLGHLPGLKAD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2026 LTGREHLYLYARLRGVPSKEIEKVAnwgIQSLGLSLYADRLAGTYSGGNKRKLSTAIALTGCPPLLLLDEPTTGMDPQAR 2105
Cdd:PRK13543 97 LSTLENLHFLCGLHGRRAKQMPGSA---LAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGI 173
|
170 180 190
....*....|....*....|....*....|....
gi 6671495 2106 RMLWNTIVSIIREGRAVVLTSHSMEECEALCTRL 2139
Cdd:PRK13543 174 TLVNRMISAHLRGGGAALVTTHGAYAAPPVRTRM 207
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1936-2152 |
7.71e-15 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 76.59 E-value: 7.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1936 ILKLNELTKVYSgsSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIlTSISD--VHQNM 2013
Cdd:PRK11231 2 TLRTENLTVGYG--TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPI-SMLSSrqLARRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2014 GYCPQFDAIDDLLTGRE--------HLYLYARLrgvpSKEIEKVANWGIQSLGLSLYADRLAGTYSGGNKRKLSTAIALT 2085
Cdd:PRK11231 79 ALLPQHHLTPEGITVRElvaygrspWLSLWGRL----SAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6671495 2086 GCPPLLLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGTFQCLGT 2152
Cdd:PRK11231 155 QDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGT 221
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1968-2133 |
8.35e-15 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 80.94 E-value: 8.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1968 GLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIltsiSD------VHQNMGYCPQfdaidDL-------LTGREHLYL 2034
Cdd:NF033858 31 GLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDM----ADarhrraVCPRIAYMPQ-----GLgknlyptLSVFENLDF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2035 YARLRGVPSKEIEkvanWGIQSL----GLSLYADRLAGTYSGGNKRKLSTAIALTGCPPLLLLDEPTTGMDPQARRMLWN 2110
Cdd:NF033858 102 FGRLFGQDAAERR----RRIDELlratGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRRQFWE 177
|
170 180
....*....|....*....|....*..
gi 6671495 2111 TIVSiIREGRA----VVLTSHsMEECE 2133
Cdd:NF033858 178 LIDR-IRAERPgmsvLVATAY-MEEAE 202
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1950-2145 |
9.64e-15 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 78.73 E-value: 9.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1950 SSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI-LTSISDVHQNMGYCPQFDAIDDLLTG 2028
Cdd:PRK09536 15 DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVeALSARAASRRVASVPQDTSLSFEFDV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2029 RE--------HLYLYARLRGVPSKEIEKvanwGIQSLGLSLYADRLAGTYSGGNKRKLSTAIALTGCPPLLLLDEPTTGM 2100
Cdd:PRK09536 95 RQvvemgrtpHRSRFDTWTETDRAAVER----AMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 6671495 2101 D-PQARRMLwNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2145
Cdd:PRK09536 171 DiNHQVRTL-ELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADG 215
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
943-1138 |
1.12e-14 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 76.28 E-value: 1.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 943 RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPP----TSGTVLIGGKDIE----------TNLDVVRQSLGmc 1008
Cdd:PRK10418 16 QPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVApcalrgrkiaTIMQNPRSAFN-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1009 PQHnilfhhlTVAEHILFYAQLKGRSWEEAQleMEAMLEDTGLhhkrnEEAQ--------DLSGGMQRKLSVAIAFVGDS 1080
Cdd:PRK10418 94 PLH-------TMHTHARETCLALGKPADDAT--LTAALEAVGL-----ENAArvlklypfEMSGGMLQRMMIALALLCEA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1081 KVVVLDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
Cdd:PRK10418 160 PFIIADEPTTDLDVVAQARILDLLesIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRI 219
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1936-2147 |
1.27e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 79.28 E-value: 1.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1936 ILKLNELTKVYSGSSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGK---------SILTSI 2006
Cdd:PRK10762 4 LLQLKGIDKAFPGVK--ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKevtfngpksSQEAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2007 SDVHQNMGYCPQFDAIDDLLTGREhlyLYARLRGVPSKEIEKVANWGIQSLGLSLYADRLAGTYSGGNKRKLSTAIALTG 2086
Cdd:PRK10762 82 GIIHQELNLIPQLTIAENIFLGRE---FVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSF 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6671495 2087 CPPLLLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGTF 2147
Cdd:PRK10762 159 ESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQF 219
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
929-1143 |
1.72e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 79.12 E-value: 1.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 929 VCVKNLVkVFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTsGTVLIGGKDI-ETNLDVVRQSLGM 1007
Cdd:PRK11174 350 IEAEDLE-ILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GSLKINGIELrELDPESWRKHLSW 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1008 CPQHNILFHHlTVAEHILfyaqLKGRSWEEAQLEmeAMLEDT-----------GLHHKRNEEAQDLSGGMQRKLSVAIAF 1076
Cdd:PRK11174 428 VGQNPQLPHG-TLRDNVL----LGNPDASDEQLQ--QALENAwvseflpllpqGLDTPIGDQAAGLSVGQAQRLALARAL 500
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6671495 1077 VGDSKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDeaDLLG-DRIAIISQGRLYCSGT 1143
Cdd:PRK11174 501 LQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLE--DLAQwDQIWVMQDGQIVQQGD 566
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
927-1142 |
1.98e-14 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 75.64 E-value: 1.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 927 PGVCVKNLVKVFepSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIETNL-------- 998
Cdd:TIGR02323 2 PLLQVSGLSKSY--GGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAELElyqlseae 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 999 --DVVRQSLGMCPQHNILFHHLTVA------EHILFYAQLK-GRSWEEAQLEMEAMLEDTGlhhKRNEEAQDLSGGMQRK 1069
Cdd:TIGR02323 80 rrRLMRTEWGFVHQNPRDGLRMRVSaganigERLMAIGARHyGNIRATAQDWLEEVEIDPT---RIDDLPRAFSGGMQQR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6671495 1070 LSVAIAFVGDSKVVVLDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSG 1142
Cdd:TIGR02323 157 LQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLrgLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESG 231
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1937-2147 |
2.46e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 78.41 E-value: 2.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1937 LKLNELTKVYSGSSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGK---------SILTSIS 2007
Cdd:PRK11288 5 LSFDGIGKTFPGVK--ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQemrfasttaALAAGVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2008 DVHQNMGYCPQFDAIDDLLTGRehlyLYARLRGVPSKEIEKVANWGIQSLGLSLYADRLAGTYSGGNKRKLSTAIALTGC 2087
Cdd:PRK11288 83 IIYQELHLVPEMTVAENLYLGQ----LPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2088 PPLLLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGTF 2147
Cdd:PRK11288 159 ARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRY 218
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
949-1151 |
2.80e-14 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 74.67 E-value: 2.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGK--DIETNLDV-----VRQSLGMCPQHNILFHHLTVA 1021
Cdd:PRK11124 21 ITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfDFSKTPSDkaireLRRNVGMVFQQYNLWPHLTVQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1022 EHiLFYAQLK--GRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTSGVDPYSRRS 1099
Cdd:PRK11124 101 QN-LIEAPCRvlGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQ 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 6671495 1100 IWDLLLKYR-SGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTplflKNCF 1151
Cdd:PRK11124 180 IVSIIRELAeTGITQVIVTHEVEVARKTASRVVYMENGHIVEQGD----ASCF 228
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1961-2145 |
3.13e-14 |
|
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: 73.72 E-value: 3.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1961 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTSISDVH---QNMGYCPQfdaiddlltgreHLYLYAR 2037
Cdd:cd03262 23 VKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINelrQKVGMVFQ------------QFNLFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2038 L-------------RGVPSKEIEKVANWGIQSLGLSLYADRLAGTYSGGNKRKLSTAIALTGCPPLLLLDEPTTGMDPQA 2104
Cdd:cd03262 91 LtvlenitlapikvKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPEL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 6671495 2105 RRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2145
Cdd:cd03262 171 VGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDG 211
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
929-1137 |
3.40e-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: 73.66 E-value: 3.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 929 VCVKNLVKVFEPSGRPAVDRL---NITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGkdietnldvvrqSL 1005
Cdd:cd03250 1 ISVEDASFTWDSGEQETSFTLkdiNLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG------------SI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1006 GMCPQHNILFHhLTVAEHILFyaqlkGRSWEEAQLE--MEA--------MLED---TGLHHK-RNeeaqdLSGGMQRKLS 1071
Cdd:cd03250 69 AYVSQEPWIQN-GTIRENILF-----GKPFDEERYEkvIKAcalepdleILPDgdlTEIGEKgIN-----LSGGQKQRIS 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1072 VAIAFVGDSKVVVLDEPTSGVDPYSRRSIWDLLL--KYRSGRTIIMSTHHMdeaDLLG--DRIAIISQGR 1137
Cdd:cd03250 138 LARAVYSDADIYLLDDPLSAVDAHVGRHIFENCIlgLLLNNKTRILVTHQL---QLLPhaDQIVVLDNGR 204
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1936-2156 |
3.42e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 75.27 E-value: 3.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1936 ILKLNELTKVYSGSSSpAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTS---ISDVHQN 2012
Cdd:PRK13636 5 ILKVEELNYNYSDGTH-ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSrkgLMKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2013 MGYCPQfDAIDDLLTGR--EHLYLYARLRGVPSKEIEKVANWGIQSLGLSLYADRLAGTYSGGNKRKLSTAIALTGCPPL 2090
Cdd:PRK13636 84 VGMVFQ-DPDNQLFSASvyQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6671495 2091 LLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGTFQCLGTIQHL 2156
Cdd:PRK13636 163 LVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEV 229
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1936-2142 |
3.68e-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: 3.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1936 ILKLNELTKVYSGSSSP--AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTG---DTTVTSGDATVAGKSILT------ 2004
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVvkAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGllpPPGITSGEILFDGEDLLKlsekel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2005 ------SISDVHQNmgycPqFDAIDDLLTGREHLY-LYARLRGVPSKEIEKVANWGIQSLGLSlYADRLAGTY----SGG 2073
Cdd:COG0444 81 rkirgrEIQMIFQD----P-MTSLNPVMTVGDQIAePLRIHGGLSKAEARERAIELLERVGLP-DPERRLDRYphelSGG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6671495 2074 NKRKLSTAIALTGCPPLLLLDEPTTGMDP--QARrmlwntIVSIIRE-----GRAVVLTSHSMEECEALCTRLAIM 2142
Cdd:COG0444 155 MRQRVMIARALALEPKLLIADEPTTALDVtiQAQ------ILNLLKDlqrelGLAILFITHDLGVVAEIADRVAVM 224
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1937-2130 |
3.73e-14 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 77.71 E-value: 3.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1937 LKLNELTKVYSGSSsPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSiLTSIS--DVHQNMG 2014
Cdd:TIGR02857 322 LEFSGVSVAYPGRR-PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVP-LADADadSWRDQIA 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2015 YCPQ----FDAiddllTGREHLYLYArlRGVPSKEIEKV-----ANWGIQSLGLSLyaDRLAGT----YSGGNKRKLSTA 2081
Cdd:TIGR02857 400 WVPQhpflFAG-----TIAENIRLAR--PDASDAEIREAleragLDEFVAALPQGL--DTPIGEggagLSGGQAQRLALA 470
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 6671495 2082 IALTGCPPLLLLDEPTTGMDPQARrmlwNTIVSIIRE---GRAVVLTSHSME 2130
Cdd:TIGR02857 471 RAFLRDAPLLLLDEPTAHLDAETE----AEVLEALRAlaqGRTVLLVTHRLA 518
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1932-2173 |
3.90e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 75.03 E-value: 3.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1932 NKTDILKLNELTKVYSGSSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI----LTSIS 2007
Cdd:PRK13632 3 NKSVMIKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITIskenLKEIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2008 D----VHQNmgycP--QFDAI---DDLLTGREHlylyarlRGVPSKEIEKVANWGIQSLGLSLYADRLAGTYSGGNKRKL 2078
Cdd:PRK13632 83 KkigiIFQN----PdnQFIGAtveDDIAFGLEN-------KKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2079 STAIALTGCPPLLLLDEPTTGMDPQARRmlwnTIVSIIREGRA-----VVLTSHSMEECeALCTRLAIMVKGTFQCLGTI 2153
Cdd:PRK13632 152 AIASVLALNPEIIIFDESTSMLDPKGKR----EIKKIMVDLRKtrkktLISITHDMDEA-ILADKVIVFSEGKLIAQGKP 226
|
250 260
....*....|....*....|.
gi 6671495 2154 QHLkykFGDGYIV-TMKIKSP 2173
Cdd:PRK13632 227 KEI---LNNKEILeKAKIDSP 244
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
932-1093 |
4.77e-14 |
|
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: 73.07 E-value: 4.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 932 KNLVKVFEPSGRPAVDRL-NITFY--ENQITAFLGHNGAGKTTTLSILTGLLPPT---SGTVLIGGKDIETNLDVVRQSL 1005
Cdd:cd03233 6 WRNISFTTGKGRSKIPILkDFSGVvkPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPGEI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1006 GMCPQHNILFHHLTVAEHILFYAQLKGrsweeaqlemeamledtglhhkrNEEAQDLSGGMQRKLSVAIAFVGDSKVVVL 1085
Cdd:cd03233 86 IYVSEEDVHFPTLTVRETLDFALRCKG-----------------------NEFVRGISGGERKRVSIAEALVSRASVLCW 142
|
....*...
gi 6671495 1086 DEPTSGVD 1093
Cdd:cd03233 143 DNSTRGLD 150
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1926-2152 |
4.79e-14 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 76.52 E-value: 4.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1926 RVMSGGNKTDILKLNELTKVYSGSssPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIlTS 2005
Cdd:PRK09452 4 LNKQPSSLSPLVELRGISKSFDGK--EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDI-TH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2006 ISDVHQNMGYCPQFDAIDDLLTGREHLYLYARLRGVPSKEIEKVANWGIQSLGLSLYADRLAGTYSGGNKRKLSTAIALT 2085
Cdd:PRK09452 81 VPAENRHVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6671495 2086 GCPPLLLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGTFQCLGT 2152
Cdd:PRK09452 161 NKPKVLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGT 228
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
932-1137 |
5.19e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 77.28 E-value: 5.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 932 KNLVKVFepSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLP--PTSGTVLIGGKDIETN--LDVVRQSLGM 1007
Cdd:PRK13549 9 KNITKTF--GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPhgTYEGEIIFEGEELQASniRDTERAGIAI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1008 CPQHNILFHHLTVAEHILFYAQL--KGR-SWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVV 1084
Cdd:PRK13549 87 IHQELALVKELSVLENIFLGNEItpGGImDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 6671495 1085 LDEPTSGVDPYSRRSIWDLL--LKyRSGRTIIMSTHHMDEADLLGDRIAIISQGR 1137
Cdd:PRK13549 167 LDEPTASLTESETAVLLDIIrdLK-AHGIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
1968-2156 |
6.26e-14 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 75.92 E-value: 6.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1968 GLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTSISDV----HQN-MGYCPQFDAIDDLLTGREHLyLYARLRGVP 2042
Cdd:TIGR02142 27 AIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIflppEKRrIGYVFQEARLFPHLSVRGNL-RYGMKRARP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2043 SkeiEKVANWG--IQSLGLSLYADRLAGTYSGGNKRKLSTAIALTGCPPLLLLDEPTTGMDPQARRMLWNTIVSIIRE-G 2119
Cdd:TIGR02142 106 S---ERRISFErvIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLERLHAEfG 182
|
170 180 190
....*....|....*....|....*....|....*..
gi 6671495 2120 RAVVLTSHSMEECEALCTRLAIMVKGTFQCLGTIQHL 2156
Cdd:TIGR02142 183 IPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEV 219
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
923-1143 |
8.19e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 77.71 E-value: 8.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 923 PGlVPGVCVKNLVKVFE-PSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPtsgtvliggkdIETNLDVV 1001
Cdd:PLN03232 610 PG-APAISIKNGYFSWDsKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSH-----------AETSSVVI 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1002 RQSLGMCPQHNILFHhLTVAEHILFYAQLKGRSWEEAqLEMEAMLEDTGLHHKRN-----EEAQDLSGGMQRKLSVAIAF 1076
Cdd:PLN03232 678 RGSVAYVPQVSWIFN-ATVRENILFGSDFESERYWRA-IDVTALQHDLDLLPGRDlteigERGVNISGGQKQRVSMARAV 755
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6671495 1077 VGDSKVVVLDEPTSGVDPYSRRSIWDLLLKYR-SGRTIIMSTHHMDEADLLgDRIAIISQGRLYCSGT 1143
Cdd:PLN03232 756 YSNSDIYIFDDPLSALDAHVAHQVFDSCMKDElKGKTRVLVTNQLHFLPLM-DRIILVSEGMIKEEGT 822
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
931-1136 |
9.53e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 76.58 E-value: 9.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 931 VKNLVKVFepSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDI---------ETNLDVV 1001
Cdd:PRK10762 7 LKGIDKAF--PGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVtfngpkssqEAGIGII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1002 RQSLGMCPQhnilfhhLTVAEHILFYAQLKGR----SWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFV 1077
Cdd:PRK10762 85 HQELNLIPQ-------LTIAENIFLGREFVNRfgriDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLS 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1078 GDSKVVVLDEPTSGVDPYSRRSIWDLLLKYRS-GRTIIMSTHHMDEADLLGDRIAIISQG 1136
Cdd:PRK10762 158 FESKVIIMDEPTDALTDTETESLFRVIRELKSqGRGIVYISHRLKEIFEICDDVTVFRDG 217
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
949-1144 |
1.02e-13 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 73.48 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIE--TNLDVVRQsLGMCPQHNILFHHLTVAEHILF 1026
Cdd:PRK10253 26 LTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQhyASKEVARR-IGLLAQNATTPGDITVQELVAR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1027 ----YAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTSGVDPYSRRSIWD 1102
Cdd:PRK10253 105 grypHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLE 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 6671495 1103 LL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
Cdd:PRK10253 185 LLseLNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAP 228
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
931-1138 |
1.23e-13 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 73.17 E-value: 1.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 931 VKNLVKVFepSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGgkdiETNLDVVRQSLGMCPQ 1010
Cdd:PRK11247 15 LNAVSKRY--GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAG----TAPLAEAREDTRLMFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1011 HNILFHHLTVAEHILFyaQLKGrSWEEAQLEMeamLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTS 1090
Cdd:PRK11247 89 DARLLPWKKVIDNVGL--GLKG-QWRDAALQA---LAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLG 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 6671495 1091 GVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
Cdd:PRK11247 163 ALDALTRIEMQDLIesLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1956-2146 |
2.12e-13 |
|
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: 71.37 E-value: 2.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1956 RLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTS------ISDVHQNMGYCPQFDAIDDLLTGR 2029
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAppadrpVSMLFQENNLFAHLTVEQNVGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2030 EHlylYARLRGVPSKEIEKVAnwgiQSLGLSLYADRLAGTYSGGNKRKLSTAIALTGCPPLLLLDEPTTGMDPQARRMLW 2109
Cdd:cd03298 96 SP---GLKLTAEDRQAIEVAL----ARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEML 168
|
170 180 190
....*....|....*....|....*....|....*...
gi 6671495 2110 NTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGT 2146
Cdd:cd03298 169 DLVLDLHAEtKMTVLMVTHQPEDAKRLAQRVVFLDNGR 206
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1936-2145 |
2.46e-13 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 75.06 E-value: 2.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1936 ILKLNELTkVYSGSSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIL-TSISDVHQN-- 2012
Cdd:COG3845 257 VLEVENLS-VRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITgLSPRERRRLgv 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2013 ---------MGYCPQFDAIDDLLTGREHLYLYARLRGVPSKEIEKVAN-----WGIQSLGlslyADRLAGTYSGGNKRKL 2078
Cdd:COG3845 336 ayipedrlgRGLVPDMSVAENLILGRYRRPPFSRGGFLDRKAIRAFAEelieeFDVRTPG----PDTPARSLSGGNQQKV 411
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6671495 2079 STAIALTGCPPLLLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2145
Cdd:COG3845 412 ILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEG 478
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1933-2133 |
5.03e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 71.75 E-value: 5.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1933 KTDILKLNELTKVYSGSSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTG--------DTTVTSGDATVAGKS--- 2001
Cdd:PRK13640 2 KDNIVEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGlllpddnpNSKITVDGITLTAKTvwd 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2002 ILTSISDVHQNmgycP--QFDAI---DDLLTGREHlylyarlRGVPSKEIEKVANWGIQSLGLSLYADRLAGTYSGGNKR 2076
Cdd:PRK13640 82 IREKVGIVFQN----PdnQFVGAtvgDDVAFGLEN-------RAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQ 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6671495 2077 KLSTAIALTGCPPLLLLDEPTTGMDPQARrmlwNTIVSIIRE-----GRAVVLTSHSMEECE 2133
Cdd:PRK13640 151 RVAIAGILAVEPKIIILDESTSMLDPAGK----EQILKLIRKlkkknNLTVISITHDIDEAN 208
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1937-2152 |
5.12e-13 |
|
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: 74.40 E-value: 5.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1937 LKLNELTKVYSGSSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-SISDVHQNMGY 2015
Cdd:COG4618 331 LSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQwDREELGRHIGY 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2016 CPQ----FDAiddllTGREHLylyARLRGVPSKEIEKVANW-GIQSLGLSL---YADRLA---GTYSGGNKRKLSTAIAL 2084
Cdd:COG4618 411 LPQdvelFDG-----TIAENI---ARFGDADPEKVVAAAKLaGVHEMILRLpdgYDTRIGeggARLSGGQRQRIGLARAL 482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2085 TGCPPLLLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMeecEAL--CTRLAIMVKGTFQCLGT 2152
Cdd:COG4618 483 YGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRP---SLLaaVDKLLVLRDGRVQAFGP 549
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
931-1138 |
5.36e-13 |
|
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: 71.37 E-value: 5.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 931 VKNLVKVFEPSG-------RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIeTNLD---- 999
Cdd:TIGR02769 5 VRDVTHTYRTGGlfgakqrAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDL-YQLDrkqr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1000 -VVRQSLGMC---------PQHNIlfhHLTVAEHILFYAQLKgrswEEAQLE-MEAMLEDTGLhhkRNEEAQ----DLSG 1064
Cdd:TIGR02769 84 rAFRRDVQLVfqdspsavnPRMTV---RQIIGEPLRHLTSLD----ESEQKArIAELLDMVGL---RSEDADklprQLSG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6671495 1065 GMQRKLSVAIAFVGDSKVVVLDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
Cdd:TIGR02769 154 GQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLrkLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1961-2145 |
7.06e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 73.79 E-value: 7.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1961 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI-LTSISD-VHQNMGYCPQ---FDAIDDLLTGREHLYLY 2035
Cdd:PRK11288 276 VRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIdIRSPRDaIRAGIMLCPEdrkAEGIIPVHSVADNINIS 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2036 ARLRGVPSKEI------EKVANWGIQSLGL-SLYADRLAGTYSGGNKRK------LSTAIALtgcpplLLLDEPTTGMDP 2102
Cdd:PRK11288 356 ARRHHLRAGCLinnrweAENADRFIRSLNIkTPSREQLIMNLSGGNQQKailgrwLSEDMKV------ILLDEPTRGIDV 429
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 6671495 2103 QARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2145
Cdd:PRK11288 430 GAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREG 472
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1961-2148 |
8.83e-13 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 70.19 E-value: 8.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1961 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSiLTSISDVH------QNMGYCPQFDAIDDLLTGREHLYL 2034
Cdd:PRK10584 33 VKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQP-LHQMDEEAraklraKHVGFVFQSFMLIPTLNALENVEL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2035 YARLRGVPSKEIEKVANWGIQSLGLSLYADRLAGTYSGGNKRKLSTAIALTGCPPLLLLDEPTTGMDPQARRMLWNTIVS 2114
Cdd:PRK10584 112 PALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFS 191
|
170 180 190
....*....|....*....|....*....|....*
gi 6671495 2115 IIRE-GRAVVLTSHSmEECEALCTRLAIMVKGTFQ 2148
Cdd:PRK10584 192 LNREhGTTLILVTHD-LQLAARCDRRLRLVNGQLQ 225
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1961-2154 |
9.09e-13 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 70.57 E-value: 9.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1961 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSiLTSIS--DVHQNMGYCPQ-------FDAIDDLLTGREH 2031
Cdd:PRK13548 25 LRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRP-LADWSpaELARRRAVLPQhsslsfpFTVEEVVAMGRAP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2032 LYL-YARLRGVPSKEIEKVanwgiqslGLSLYADRLAGTYSGGNKRKLSTAIALT------GCPPLLLLDEPTTGMDPQ- 2103
Cdd:PRK13548 104 HGLsRAEDDALVAAALAQV--------DLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSALDLAh 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 6671495 2104 -------ARRMlwntivsIIREGRAVVLTSHSMEECEALCTRLAIMVKGTFQCLGTIQ 2154
Cdd:PRK13548 176 qhhvlrlARQL-------AHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPA 226
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
943-1160 |
9.15e-13 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 73.99 E-value: 9.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 943 RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDI-ETNLDVVRQSLGMCPQHNILFHHlTVA 1021
Cdd:TIGR00958 494 VPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLvQYDHHYLHRQVALVGQEPVLFSG-SVR 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1022 EHILFYAqlkgRSWEEAQLEMEAMLE---------DTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTSGV 1092
Cdd:TIGR00958 573 ENIAYGL----TDTPDEEIMAAAKAAnahdfimefPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSAL 648
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6671495 1093 DPYSRRSIWDllLKYRSGRTIIMSTHHMDEADlLGDRIAIISQGRLYCSGTPLFLKNcfGTGFYLTLV 1160
Cdd:TIGR00958 649 DAECEQLLQE--SRSRASRTVLLIAHRLSTVE-RADQILVLKKGSVVEMGTHKQLME--DQGCYKHLV 711
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
932-1137 |
9.81e-13 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 73.23 E-value: 9.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 932 KNLVKVFepSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDI---------ETNLDVVR 1002
Cdd:PRK10982 2 SNISKSF--PGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfksskealENGISMVH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1003 QSLGMCPQHNilfhhltVAEHI-LFYAQLKGRSWEEAQL--EMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGD 1079
Cdd:PRK10982 80 QELNLVLQRS-------VMDNMwLGRYPTKGMFVDQDKMyrDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYN 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 6671495 1080 SKVVVLDEPTSGVDPYSRRSIWDLLLKYR-SGRTIIMSTHHMDEADLLGDRIAIISQGR 1137
Cdd:PRK10982 153 AKIVIMDEPTSSLTEKEVNHLFTIIRKLKeRGCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
943-1138 |
2.23e-12 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 72.16 E-value: 2.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 943 RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPT-SGTVLIGGK--DIETNLDVVRQSLGMCPQ----HNILf 1015
Cdd:TIGR02633 273 RKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKpvDIRNPAQAIRAGIAMVPEdrkrHGIV- 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1016 HHLTVAEHILFYA--QLKGRSWEEAQLEMEAMLEDTGLHHKRNEEA----QDLSGGMQRKLSVAIAFVGDSKVVVLDEPT 1089
Cdd:TIGR02633 352 PILGVGKNITLSVlkSFCFKMRIDAAAELQIIGSAIQRLKVKTASPflpiGRLSGGNQQKAVLAKMLLTNPRVLILDEPT 431
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 6671495 1090 SGVDPYSRRSIWDLLLKY-RSGRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
Cdd:TIGR02633 432 RGVDVGAKYEIYKLINQLaQEGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1936-2145 |
2.79e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 68.75 E-value: 2.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1936 ILKLNELTKVYSgsSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIL--TSISDVHQNM 2013
Cdd:PRK11614 5 MLSFDKVSAHYG--KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITdwQTAKIMREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2014 GYCPQFDAIDDLLTGREHLYL--YARLRGVPSKEIEKVANwgiqsLGLSLYADRL--AGTYSGGNKRKLSTAIALTGCPP 2089
Cdd:PRK11614 83 AIVPEGRRVFSRMTVEENLAMggFFAERDQFQERIKWVYE-----LFPRLHERRIqrAGTMSGGEQQMLAIGRALMSQPR 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 6671495 2090 LLLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2145
Cdd:PRK11614 158 LLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENG 213
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1969-2145 |
2.98e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 69.39 E-value: 2.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1969 LLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTS-----ISDVHQNMGYCPQF--------DAIDDLLTGREHLyly 2035
Cdd:PRK13649 38 FIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTsknkdIKQIRKKVGLVFQFpesqlfeeTVLKDVAFGPQNF--- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2036 arlrGVPSKEIEKVANWGIQSLGLS--LYaDRLAGTYSGGNKRKLSTAIALTGCPPLLLLDEPTTGMDPQARRMLWNTIV 2113
Cdd:PRK13649 115 ----GVSQEEAEALAREKLALVGISesLF-EKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFK 189
|
170 180 190
....*....|....*....|....*....|..
gi 6671495 2114 SIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2145
Cdd:PRK13649 190 KLHQSGMTIVLVTHLMDDVANYADFVYVLEKG 221
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1936-2145 |
3.55e-12 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 70.11 E-value: 3.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1936 ILKLNELTKVYSGSSSP--AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIlTSISD----- 2008
Cdd:COG1135 1 MIELENLSKTFPTKGGPvtALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDL-TALSErelra 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2009 VHQNMGYCPQfdaiddlltgreHLYLYAR----------LR--GVPSKEI-EKVAnwgiqSL----GLSlyaDRlAGTY- 2070
Cdd:COG1135 80 ARRKIGMIFQ------------HFNLLSSrtvaenvalpLEiaGVPKAEIrKRVA-----ELlelvGLS---DK-ADAYp 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2071 ---SGGNKRKLSTAIALTGCPPLLLLDEPTTGMDPQarrmlwnTIVSI------IRE--GRAVVLTSHSMEECEALCTRL 2139
Cdd:COG1135 139 sqlSGGQKQRVGIARALANNPKVLLCDEATSALDPE-------TTRSIldllkdINRelGLTIVLITHEMDVVRRICDRV 211
|
....*.
gi 6671495 2140 AIMVKG 2145
Cdd:COG1135 212 AVLENG 217
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
944-1138 |
5.26e-12 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 71.20 E-value: 5.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 944 PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDI-ETNLDVVRQSLGMCPQHNILFHHlTVAE 1022
Cdd:PRK11176 357 PALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLrDYTLASLRNQVALVSQNVHLFND-TIAN 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1023 HILfYAqlKGRSWEEAQLEMEAMLE---------DTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTSGVD 1093
Cdd:PRK11176 436 NIA-YA--RTEQYSREQIEEAARMAyamdfinkmDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALD 512
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 6671495 1094 PYSRRSIWDLLLKYRSGRTIIMSTHHMDEADlLGDRIAIISQGRL 1138
Cdd:PRK11176 513 TESERAIQAALDELQKNRTSLVIAHRLSTIE-KADEILVVEDGEI 556
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
957-1137 |
5.48e-12 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 71.06 E-value: 5.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 957 QITAFLGHNGAGKTTTLSILTGLLPPTS--GTVLIGGKDIETNldvVRQSLGMCPQHNILFHHLTVAEHILFYAQL---K 1031
Cdd:PLN03211 95 EILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTKQ---ILKRTGFVTQDDILYPHLTVRETLVFCSLLrlpK 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1032 GRSWEEAQLEMEAMLEDTGLHHKRNEEA-----QDLSGGMQRKLSVAIAFVGDSKVVVLDEPTSGVDPYSR-RSIWDLLL 1105
Cdd:PLN03211 172 SLTKQEKILVAESVISELGLTKCENTIIgnsfiRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAyRLVLTLGS 251
|
170 180 190
....*....|....*....|....*....|...
gi 6671495 1106 KYRSGRTIIMSTHH-MDEADLLGDRIAIISQGR 1137
Cdd:PLN03211 252 LAQKGKTIVTSMHQpSSRVYQMFDSVLVLSEGR 284
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1937-2127 |
5.62e-12 |
|
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: 65.55 E-value: 5.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1937 LKLNELTKVYSGSssPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGdatvagksILTSISDVhqNMGYC 2016
Cdd:cd03221 1 IELENLSKTYGGK--LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEG--------IVTWGSTV--KIGYF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2017 PQFdaiddlltgrehlylyarlrgvpskeiekvanwgiqslglslyadrlagtySGGNKRKLSTAIALTGCPPLLLLDEP 2096
Cdd:cd03221 69 EQL---------------------------------------------------SGGEKMRLALAKLLLENPNLLLLDEP 97
|
170 180 190
....*....|....*....|....*....|.
gi 6671495 2097 TTGMDPQARRMLWNTIVSiirEGRAVVLTSH 2127
Cdd:cd03221 98 TNHLDLESIEALEEALKE---YPGTVILVSH 125
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
931-1137 |
6.03e-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: 67.46 E-value: 6.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 931 VKNLVKVF---EPSGR--PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIggKDIETNLDVV---- 1001
Cdd:COG4778 7 VENLSKTFtlhLQGGKrlPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILV--RHDGGWVDLAqasp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1002 -------RQSLGMCPQHnilfhhL----------TVAEHILfyaqLKGRSWEEAQLEMEAMLEDTGLHhkrnEEAQDL-- 1062
Cdd:COG4778 85 reilalrRRTIGYVSQF------LrviprvsaldVVAEPLL----ERGVDREEARARARELLARLNLP----ERLWDLpp 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6671495 1063 ---SGGMQRKLSVAIAFVGDSKVVVLDEPTSGVDPYSRRSIWDLLLKY-RSGRTIIMSTHHMDEADLLGDRIAIISQGR 1137
Cdd:COG4778 151 atfSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAkARGTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1961-2145 |
6.49e-12 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 67.85 E-value: 6.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1961 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTSISD----------------VHQNMGYCPQFDAIDD 2024
Cdd:PRK11264 26 VKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLsqqkglirqlrqhvgfVFQNFNLFPHRTVLEN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2025 LLTGRehlylyARLRGVPSKEIEKVANWGIQSLGLSLYADRLAGTYSGGNKRKLSTAIALTGCPPLLLLDEPTTGMDPQA 2104
Cdd:PRK11264 106 IIEGP------VIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPEL 179
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 6671495 2105 RRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2145
Cdd:PRK11264 180 VGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQG 220
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1936-2136 |
6.98e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 70.34 E-value: 6.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1936 ILKLNELTKVYSGSssPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGdttVT-----SGDATVAGKSI-LTSISD- 2008
Cdd:PRK13549 5 LLEMKNITKTFGGV--KALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG---VYphgtyEGEIIFEGEELqASNIRDt 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2009 -------VHQNMGYCPQFDAIDDLLTGREHLY--------LYARlrgvpSKEIekvanwgIQSLGLSLYADRLAGTYSGG 2073
Cdd:PRK13549 80 eragiaiIHQELALVKELSVLENIFLGNEITPggimdydaMYLR-----AQKL-------LAQLKLDINPATPVGNLGLG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6671495 2074 NKRKLSTAIALTGCPPLLLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALC 2136
Cdd:PRK13549 148 QQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAIS 210
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
957-1138 |
7.34e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 70.33 E-value: 7.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 957 QITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGK--DIETNLDVVRQSLGMCP----QHNILFHHlTVAEHI------ 1024
Cdd:PRK11288 280 EIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKpiDIRSPRDAIRAGIMLCPedrkAEGIIPVH-SVADNInisarr 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1025 --LFYAQLKGRSWEE--AQLEMEAMLEDTglhhkRNEEaQD---LSGGMQRKLSVAIAFVGDSKVVVLDEPTSGVDPYSR 1097
Cdd:PRK11288 359 hhLRAGCLINNRWEAenADRFIRSLNIKT-----PSRE-QLimnLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAK 432
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 6671495 1098 RSIWDLLLKY-RSGRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
Cdd:PRK11288 433 HEIYNVIYELaAQGVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
931-1144 |
9.38e-12 |
|
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: 66.67 E-value: 9.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 931 VKNLVKVFEPSGRPAVDrlNITFY--ENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIET-NLDVVRQSLGM 1007
Cdd:cd03369 9 VENLSVRYAPDLPPVLK--NVSFKvkAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTiPLEDLRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1008 CPQHNILFHHlTVAEHILFYAQlkgrsWEEAQLeMEAMledtglhhKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDE 1087
Cdd:cd03369 87 IPQDPTLFSG-TIRSNLDPFDE-----YSDEEI-YGAL--------RVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDE 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 6671495 1088 PTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDE-ADLlgDRIAIISQGRLYCSGTP 1144
Cdd:cd03369 152 ATASIDYATDALIQKTIREEFTNSTILTIAHRLRTiIDY--DKILVMDAGEVKEYDHP 207
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
941-1136 |
1.22e-11 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 70.13 E-value: 1.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 941 SGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIET-NLDVVRQSLGMCPQHNILfhhlt 1019
Cdd:PRK10790 352 DDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSlSHSVLRQGVAMVQQDPVV----- 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1020 VAEHilFYAQLK-GRSWEEAQ----LEMEAMLE-----DTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEPT 1089
Cdd:PRK10790 427 LADT--FLANVTlGRDISEEQvwqaLETVQLAElarslPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEAT 504
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 6671495 1090 SGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMD---EAD--LLGDRIAIISQG 1136
Cdd:PRK10790 505 ANIDSGTEQAIQQALAAVREHTTLVVIAHRLStivEADtiLVLHRGQAVEQG 556
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1959-2156 |
1.28e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 67.74 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1959 VGVRPGECFGLLGVNGAGKTTTFKMLTG-----DTTVTSGDATVAGKSILTSISDVHQNMGYCPQFDaiddlltgrEH-L 2032
Cdd:PRK13634 28 VSIPSGSYVAIIGHTGSGKSTLLQHLNGllqptSGTVTIGERVITAGKKNKKLKPLRKKVGIVFQFP---------EHqL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2033 YLYARLR---------GVPSKEIEKVANWGIQSLGLSL-YADRLAGTYSGGNKRKLSTAIALTGCPPLLLLDEPTTGMDP 2102
Cdd:PRK13634 99 FEETVEKdicfgpmnfGVSEEDAKQKAREMIELVGLPEeLLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDP 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 6671495 2103 QARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGTFQCLGTIQHL 2156
Cdd:PRK13634 179 KGRKEMMEMFYKLHKEkGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREI 233
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
932-1137 |
1.33e-11 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 69.43 E-value: 1.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 932 KNLVKVFepSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTS--GTVLIGG-----KDI----ETNLDV 1000
Cdd:NF040905 5 RGITKTF--PGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGevcrfKDIrdseALGIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1001 VRQSLGMCPQhnilfhhLTVAEHIlFYAQLKGR----SWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAF 1076
Cdd:NF040905 83 IHQELALIPY-------LSIAENI-FLGNERAKrgviDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKAL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6671495 1077 VGDSKVVVLDEPTSGVDPYSRRSIWDLLLKYRS-GRTIIMSTHHMDEADLLGDRIAIISQGR 1137
Cdd:NF040905 155 SKDVKLLILDEPTAALNEEDSAALLDLLLELKAqGITSIIISHKLNEIRRVADSITVLRDGR 216
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
923-1148 |
1.43e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 70.54 E-value: 1.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 923 PGLvPGVCVKNLVKVFEPSG-RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLiggkdietnldVV 1001
Cdd:PLN03130 610 PGL-PAISIKNGYFSWDSKAeRPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASV-----------VI 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1002 RQSLGMCPQHNILFHhLTVAEHILFYAQLKGRSWEEAqlemeamLEDTGLHHKRN-----------EEAQDLSGGMQRKL 1070
Cdd:PLN03130 678 RGTVAYVPQVSWIFN-ATVRDNILFGSPFDPERYERA-------IDVTALQHDLDllpggdlteigERGVNISGGQKQRV 749
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1071 SVAIAFVGDSKVVVLDEPTSGVDPYSRRSIWDLLLKYR-SGRTIIMST---HHMDEAdllgDRIAIISQGRLYCSGT--- 1143
Cdd:PLN03130 750 SMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIKDElRGKTRVLVTnqlHFLSQV----DRIILVHEGMIKEEGTyee 825
|
250
....*....|
gi 6671495 1144 -----PLFLK 1148
Cdd:PLN03130 826 lsnngPLFQK 835
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
958-1142 |
1.69e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 67.22 E-value: 1.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 958 ITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIETNLdvvRQSL-GMCPQ-HNILFHHLTVAEHILFYAQLKGRSW 1035
Cdd:PRK15056 35 IAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQAL---QKNLvAYVPQsEEVDWSFPVLVEDVVMMGRYGHMGW 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1036 -----EEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTSGVDPYSRRSIWDLLLKYRS- 1109
Cdd:PRK15056 112 lrrakKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDe 191
|
170 180 190
....*....|....*....|....*....|...
gi 6671495 1110 GRTIIMSTHHMDEADLLGDRIAIIsQGRLYCSG 1142
Cdd:PRK15056 192 GKTMLVSTHNLGSVTEFCDYTVMV-KGTVLASG 223
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
949-1118 |
1.93e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 65.28 E-value: 1.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIggKDIETNlDVVRQSLGMCpQHNI-LFHHLTVAEHILFY 1027
Cdd:PRK13541 19 LSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYY--KNCNIN-NIAKPYCTYI-GHNLgLKLEMTVFENLKFW 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1028 AQLkgrsWEEAQLeMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTSGVDPYSRRSIWDLL-LK 1106
Cdd:PRK13541 95 SEI----YNSAET-LYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIvMK 169
|
170
....*....|..
gi 6671495 1107 YRSGRTIIMSTH 1118
Cdd:PRK13541 170 ANSGGIVLLSSH 181
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1937-2145 |
2.16e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 68.88 E-value: 2.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1937 LKLNELtkvysgsSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTS----------- 2005
Cdd:PRK10762 258 LKVDNL-------SGPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRspqdglangiv 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2006 -ISD------------VHQNMGycpqfdaiddlLTGREHL-YLYARLRGvpSKEIEKVANWgIQSLGLSL-YADRLAGTY 2070
Cdd:PRK10762 331 yISEdrkrdglvlgmsVKENMS-----------LTALRYFsRAGGSLKH--ADEQQAVSDF-IRLFNIKTpSMEQAIGLL 396
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6671495 2071 SGGNKRKLSTAIALTGCPPLLLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2145
Cdd:PRK10762 397 SGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEG 471
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1936-2156 |
2.63e-11 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 66.57 E-value: 2.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1936 ILKLNELTKVYSGSSS-PAVDrlcVGVRPGECFGLLGVNGAGKTTTFK----MLTGDTTVTS-----GDATVAGKSILTS 2005
Cdd:PRK09984 4 IIRVEKLAKTFNQHQAlHAVD---LNIHHGEMVALLGPSGSGKSTLLRhlsgLITGDKSAGShiellGRTVQREGRLARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2006 ISDVHQNMGYC-PQFDAIDDLlTGREHLYLYArLRGVP---------SKEIEKVANWGIQSLGLSLYADRLAGTYSGGNK 2075
Cdd:PRK09984 81 IRKSRANTGYIfQQFNLVNRL-SVLENVLIGA-LGSTPfwrtcfswfTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2076 RKLSTAIALTGCPPLLLLDEPTTGMDPQARRMLWNTIVSIIR-EGRAVVLTSHSMEECEALCTRLAIMVKGTFQCLGTIQ 2154
Cdd:PRK09984 159 QRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQnDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQ 238
|
..
gi 6671495 2155 HL 2156
Cdd:PRK09984 239 QF 240
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1964-2145 |
2.99e-11 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 65.81 E-value: 2.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1964 GECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTS-------ISDVHQNMGYCPQFDAIDDLLTGREHLyLYA 2036
Cdd:PRK11124 28 GETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSktpsdkaIRELRRNVGMVFQQYNLWPHLTVQQNL-IEA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2037 --RLRGVPSKEIEKVANWGIQSLGLSLYADRLAGTYSGGNKRKLSTAIALTGCPPLLLLDEPTTGMDPQarrmLWNTIVS 2114
Cdd:PRK11124 107 pcRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPE----ITAQIVS 182
|
170 180 190
....*....|....*....|....*....|....*
gi 6671495 2115 IIRE----GRAVVLTSHSMEECEALCTRLAIMVKG 2145
Cdd:PRK11124 183 IIRElaetGITQVIVTHEVEVARKTASRVVYMENG 217
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
931-1138 |
3.21e-11 |
|
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: 68.56 E-value: 3.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 931 VKNLVKVFEPSGR--PAVDRLNITFYENQITAFLGHNGAGKT-TTLSILtGLLPP----TSGTVLIGGKDI----ETNLD 999
Cdd:COG4172 9 VEDLSVAFGQGGGtvEAVKGVSFDIAAGETLALVGESGSGKSvTALSIL-RLLPDpaahPSGSILFDGQDLlglsERELR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1000 VVR-QSLGMC---------PQHNI-------LFHHltvaehilfyaqlKGRSWEEAQLEMEAMLEDTGLhhkRNEEAQ-- 1060
Cdd:COG4172 88 RIRgNRIAMIfqepmtslnPLHTIgkqiaevLRLH-------------RGLSGAAARARALELLERVGI---PDPERRld 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1061 ----DLSGGMQRKLSVAIAFVGDSKVVVLDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHhmdeaDL-----LGDR 1129
Cdd:COG4172 152 ayphQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLkdLQRELGMALLLITH-----DLgvvrrFADR 226
|
....*....
gi 6671495 1130 IAIISQGRL 1138
Cdd:COG4172 227 VAVMRQGEI 235
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
1962-2145 |
3.62e-11 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 69.10 E-value: 3.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1962 RPGECFGLLGVNGAGKTTTFKMLTGDTT--VTSGDATVAG----KSILTSISdvhqnmGYCPQFDAIDDLLTGREHLYLY 2035
Cdd:PLN03140 904 RPGVLTALMGVSGAGKTTLMDVLAGRKTggYIEGDIRISGfpkkQETFARIS------GYCEQNDIHSPQVTVRESLIYS 977
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2036 ARLRgVPsKEIEK-----VANWGIQSLGLSLYADRLAGT-----YSGGNKRKLSTAIALTGCPPLLLLDEPTTGMDPQAR 2105
Cdd:PLN03140 978 AFLR-LP-KEVSKeekmmFVDEVMELVELDNLKDAIVGLpgvtgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAA 1055
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 6671495 2106 RMLWNTIVSIIREGRAVVLTSH--SMEECEALcTRLAIMVKG 2145
Cdd:PLN03140 1056 AIVMRTVRNTVDTGRTVVCTIHqpSIDIFEAF-DELLLMKRG 1096
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1937-2156 |
3.81e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 68.31 E-value: 3.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1937 LKLNELTKVYSGSSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-SISDVHQNMGY 2015
Cdd:PRK11160 339 LTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADySEAALRQAISV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2016 CPQ----FDAiddllTGREHLYLYA------RLRGVpskeIEKVanwGIQSL-----GLSLYADRLAGTYSGGNKRKLST 2080
Cdd:PRK11160 419 VSQrvhlFSA-----TLRDNLLLAApnasdeALIEV----LQQV---GLEKLleddkGLNAWLGEGGRQLSGGEQRRLGI 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2081 AIALTGCPPLLLLDEPTTGMDPQARRmlwnTIVSIIRE---GRAVVLTSH---SMEECEALCtrlaIMVKGTFQCLGTIQ 2154
Cdd:PRK11160 487 ARALLHDAPLLLLDEPTEGLDAETER----QILELLAEhaqNKTVLMITHrltGLEQFDRIC----VMDNGQIIEQGTHQ 558
|
..
gi 6671495 2155 HL 2156
Cdd:PRK11160 559 EL 560
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
939-1138 |
4.12e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 68.15 E-value: 4.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 939 EPSGRP--AVDRL------NITF--YENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIeTNLDVV------- 1001
Cdd:PRK15439 262 QAAGAPvlTVEDLtgegfrNISLevRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEI-NALSTAqrlargl 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1002 ------RQSLGMCPQHNILFHHLTVAEHILFYAQLKGRswEEAQLEMEAMLEDTGLHHKrNEEAQDLSGGMQRKLSVAIA 1075
Cdd:PRK15439 341 vylpedRQSSGLYLDAPLAWNVCALTHNRRGFWIKPAR--ENAVLERYRRALNIKFNHA-EQAARTLSGGNQQKVLIAKC 417
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6671495 1076 FVGDSKVVVLDEPTSGVDPYSRRSIWDLLlkyRS----GRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
Cdd:PRK15439 418 LEASPQLLIVDEPTRGVDVSARNDIYQLI---RSiaaqNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
957-1136 |
5.31e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 68.60 E-value: 5.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 957 QITAFLGHNGAGKTTTLSIL-----TGLLppTSGTVLIGGKDIETNLdvvRQSLGMCPQHNILFHHLTVAEHILFYAQL- 1030
Cdd:TIGR00956 790 TLTALMGASGAGKTTLLNVLaervtTGVI--TGGDRLVNGRPLDSSF---QRSIGYVQQQDLHLPTSTVRESLRFSAYLr 864
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1031 ---------KGRSWEEAQ--LEMEAMLE------DTGLhhkrNEEaqdlsggmQRK-LSVAIAFVGDSKVVV-LDEPTSG 1091
Cdd:TIGR00956 865 qpksvskseKMEYVEEVIklLEMESYADavvgvpGEGL----NVE--------QRKrLTIGVELVAKPKLLLfLDEPTSG 932
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 6671495 1092 VDPYSRRSIWDLLLKY-RSGRTiIMSTHHMDEADLLG--DRIAIISQG 1136
Cdd:TIGR00956 933 LDSQTAWSICKLMRKLaDHGQA-ILCTIHQPSAILFEefDRLLLLQKG 979
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1937-2146 |
6.76e-11 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 64.39 E-value: 6.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1937 LKLNELTKVYSGssspavDRLC--VGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTS------IS- 2007
Cdd:COG3840 2 LRLDDLTYRYGD------FPLRfdLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALppaerpVSm 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2008 -----------DVHQNMGYcpqfdAIDDLLtgrehlylyaRLRGVPSKEIEKVAnwgiQSLGLSLYADRLAGTYSGGNKR 2076
Cdd:COG3840 76 lfqennlfphlTVAQNIGL-----GLRPGL----------KLTAEQRAQVEQAL----ERVGLAGLLDRLPGQLSGGQRQ 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6671495 2077 KLSTAIALTGCPPLLLLDEPTTGMDPQARR-MLwNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGT 2146
Cdd:COG3840 137 RVALARCLVRKRPILLLDEPFSALDPALRQeML-DLVDELCRErGLTVLMVTHDPEDAARIADRVLLVADGR 207
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
931-1137 |
7.44e-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: 67.16 E-value: 7.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 931 VKNLVKVFepSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLP--PTSGTVLIGGKDIETN--LDVVRQSLG 1006
Cdd:TIGR02633 4 MKGIVKTF--GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSPLKASniRDTERAGIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1007 MCPQHNILFHHLTVAEHILFYAQLK---GR-SWEEAQLEMEAMLEDTGLHHKRN-EEAQDLSGGMQRKLSVAIAFVGDSK 1081
Cdd:TIGR02633 82 IIHQELTLVPELSVAENIFLGNEITlpgGRmAYNAMYLRAKNLLRELQLDADNVtRPVGDYGGGQQQLVEIAKALNKQAR 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 6671495 1082 VVVLDEPTSGVDPYSRRSIWDLL--LKyRSGRTIIMSTHHMDEADLLGDRIAIISQGR 1137
Cdd:TIGR02633 162 LLILDEPSSSLTEKETEILLDIIrdLK-AHGVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
949-1155 |
8.81e-11 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 64.57 E-value: 8.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLpPTSGTVLIGGKDIET----NLDVVRQSLgmCPQHNILFhhltvAEHI 1024
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAwsaaELARHRAYL--SQQQTPPF-----AMPV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1025 LFYAQL---KGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGG-MQR-KLSVAIAFV-----GDSKVVVLDEPTSGVDp 1094
Cdd:PRK03695 87 FQYLTLhqpDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGeWQRvRLAAVVLQVwpdinPAGQLLLLDEPMNSLD- 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6671495 1095 YSRRSIWDLLLKY--RSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSG------TPLFLKNCFGTGF 1155
Cdd:PRK03695 166 VAQQAALDRLLSElcQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGrrdevlTPENLAQVFGVNF 234
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
931-1137 |
9.09e-11 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 65.90 E-value: 9.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 931 VKNLVKVFE-PSGR-PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPP---TSGTVLIGGKDI----ETNLDVV 1001
Cdd:PRK09473 15 VKDLRVTFStPDGDvTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREIlnlpEKELNKL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1002 R-QSLGMCPQHNI--LFHHLTVAEHILFYAQL-KGRSWEEAQLEMEAMLEDTGL--HHKR-NEEAQDLSGGMQRKLSVAI 1074
Cdd:PRK09473 95 RaEQISMIFQDPMtsLNPYMRVGEQLMEVLMLhKGMSKAEAFEESVRMLDAVKMpeARKRmKMYPHEFSGGMRQRVMIAM 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6671495 1075 AFVGDSKVVVLDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGR 1137
Cdd:PRK09473 175 ALLCRPKLLIADEPTTALDVTVQAQIMTLLneLKREFNTAIIMITHDLGVVAGICDKVLVMYAGR 239
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1951-2130 |
9.36e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 65.03 E-value: 9.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1951 SPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKS--------------ILTSISDVHQNMGYC 2016
Cdd:PRK13638 14 EPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPldyskrgllalrqqVATVFQDPEQQIFYT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2017 pqfDAIDDLLTGREHLylyarlrGVPSKEIEKVANWGIQSLGLSLYADRLAGTYSGGNKRKLSTAIALTGCPPLLLLDEP 2096
Cdd:PRK13638 94 ---DIDSDIAFSLRNL-------GVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEP 163
|
170 180 190
....*....|....*....|....*....|....
gi 6671495 2097 TTGMDPQARRMLWNTIVSIIREGRAVVLTSHSME 2130
Cdd:PRK13638 164 TAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDID 197
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
1963-2127 |
9.40e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 67.21 E-value: 9.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1963 PGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATV-AGKSILTSisDVHQNMGYCPQFDAIDDLLTGREHLYLYARLR-- 2039
Cdd:PLN03211 93 PGEILAVLGPSGSGKSTLLNALAGRIQGNNFTGTIlANNRKPTK--QILKRTGFVTQDDILYPHLTVRETLVFCSLLRlp 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2040 -GVPSKEIEKVANWGIQSLGLSLYADRLAGT-----YSGGNKRKLSTAIALTGCPPLLLLDEPTTGMDPQARRMLWNTIV 2113
Cdd:PLN03211 171 kSLTKQEKILVAESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLG 250
|
170
....*....|....
gi 6671495 2114 SIIREGRAVVLTSH 2127
Cdd:PLN03211 251 SLAQKGKTIVTSMH 264
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
931-1167 |
9.92e-11 |
|
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: 66.75 E-value: 9.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 931 VKNLVKVFEpsGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGL--LPPTSGTVL-------------------- 988
Cdd:TIGR03269 3 VKNLTKKFD--GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIyhvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 989 ----IGGKDIETNLDV----------VRQSLGMCPQHNI-LFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHH 1053
Cdd:TIGR03269 81 pcpvCGGTLEPEEVDFwnlsdklrrrIRKRIAIMLQRTFaLYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1054 KRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTSGVDPYSRRSIWDLLLK--YRSGRTIIMSTHHMDEADLLGDRIA 1131
Cdd:TIGR03269 161 RITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEavKASGISMVLTSHWPEVIEDLSDKAI 240
|
250 260 270
....*....|....*....|....*....|....*.
gi 6671495 1132 IISQGRLYCSGTPLFLKNCFGTGFylTLVRKMKNIQ 1167
Cdd:TIGR03269 241 WLENGEIKEEGTPDEVVAVFMEGV--SEVEKECEVE 274
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1963-2157 |
1.08e-10 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 64.26 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1963 PGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI-------LTSISDVHQNMGYC-------PQFDAIDDLLTG 2028
Cdd:COG4161 27 SGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsqkpsEKAIRLLRQKVGMVfqqynlwPHLTVMENLIEA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2029 RehlylyARLRGVPSKEIEKVANWGIQSLGLSLYADRLAGTYSGGNKRKLSTAIALTGCPPLLLLDEPTTGMDPQarrmL 2108
Cdd:COG4161 107 P------CKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPE----I 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 6671495 2109 WNTIVSIIRE----GRAVVLTSHSMEECEALCTRLAIMVKGTFQCLGTIQHLK 2157
Cdd:COG4161 177 TAQVVEIIRElsqtGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDASHFT 229
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1932-2130 |
1.18e-10 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 64.07 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1932 NKTDILKLNELTKVYS-GSSSPAVDR-LCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSiLTSISDV 2009
Cdd:PRK11629 1 MNKILLQCDNLCKRYQeGSVQTDVLHnVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQP-MSKLSSA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2010 ------HQNMGYCPQFDAIDDLLTGREHLYLYARLRGVPSKEIEKVANWGIQSLGLSLYADRLAGTYSGGNKRKLSTAIA 2083
Cdd:PRK11629 80 akaelrNQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 6671495 2084 LTGCPPLLLLDEPTTGMDPQARRMLWNTIVSI-IREGRAVVLTSHSME 2130
Cdd:PRK11629 160 LVNNPRLVLADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDLQ 207
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1929-2146 |
1.23e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 66.61 E-value: 1.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1929 SGGNKTDILKLNELTKVYSGSssPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSiLTSISD 2008
Cdd:PRK15439 4 SDTTAPPLLCARSISKQYSGV--EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNP-CARLTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2009 VH-QNMG-Y-CPQFDAIDDLLTGREHLylyarLRGVPSKE--IEKVANWgIQSLGLSLYADRLAGTYSGGNKRKLSTAIA 2083
Cdd:PRK15439 81 AKaHQLGiYlVPQEPLLFPNLSVKENI-----LFGLPKRQasMQKMKQL-LAALGCQLDLDSSAGSLEVADRQIVEILRG 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6671495 2084 LTGCPPLLLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGT 2146
Cdd:PRK15439 155 LMRDSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGT 217
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
931-1142 |
1.62e-10 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 63.79 E-value: 1.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 931 VKNLVKVFEPsgRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIETnLDV---------- 1000
Cdd:PRK11701 9 VRGLTKLYGP--RKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQL-RDLyalseaerrr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1001 -VRQSLGMCPQH-------------NILFHHLTV-AEHilfYAQLKGR--SWEEaQLEMEAMLEDtglhhkrneeaqDL- 1062
Cdd:PRK11701 86 lLRTEWGFVHQHprdglrmqvsaggNIGERLMAVgARH---YGDIRATagDWLE-RVEIDAARID------------DLp 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1063 ---SGGMQRKLSVAIAFVGDSKVVVLDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGR 1137
Cdd:PRK11701 150 ttfSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLrgLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGR 229
|
....*
gi 6671495 1138 LYCSG 1142
Cdd:PRK11701 230 VVESG 234
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
942-1138 |
1.68e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 66.11 E-value: 1.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 942 GRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLP-PTSGTVLIGGK--DIETNLDVVRQSLGMCP----QHNIL 1014
Cdd:PRK13549 274 HIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKpvKIRNPQQAIAQGIAMVPedrkRDGIV 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1015 fHHLTVAEHILF--YAQLKGRSWEEAQLEMEAMLEDTG-LHHKRNEEAQ---DLSGGMQRKLSVAIAFVGDSKVVVLDEP 1088
Cdd:PRK13549 354 -PVMGVGKNITLaaLDRFTGGSRIDDAAELKTILESIQrLKVKTASPELaiaRLSGGNQQKAVLAKCLLLNPKILILDEP 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 6671495 1089 TSGVDPYSRRSIWDLLLKY-RSGRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
Cdd:PRK13549 433 TRGIDVGAKYEIYKLINQLvQQGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
932-1145 |
2.13e-10 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 64.86 E-value: 2.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 932 KNLVKVFePSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIeTNLDVVRQSLGMCPQH 1011
Cdd:PRK11650 7 QAVRKSY-DGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVV-NELEPADRDIAMVFQN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1012 NILFHHLTVAEHiLFYAqLKGRSWEEAQ-----------LEMEAMLEdtglhHKRNEeaqdLSGGmQRKlSVAI--AFVG 1078
Cdd:PRK11650 85 YALYPHMSVREN-MAYG-LKIRGMPKAEieervaeaariLELEPLLD-----RKPRE----LSGG-QRQ-RVAMgrAIVR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6671495 1079 DSKVVVLDEPTSGVDPYSR--------RsiwdllLKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPL 1145
Cdd:PRK11650 152 EPAVFLFDEPLSNLDAKLRvqmrleiqR------LHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPV 220
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
1953-2189 |
2.24e-10 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 63.68 E-value: 2.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1953 AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTSIsdvhqNMGYCPQfdaiddlLTGREHL 2032
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIAI-----SAGLSGQ-------LTGIENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2033 YLYARLRGVPSKEIEKVANWGIQSLGLSLYADRLAGTYSGGNKRKLSTAIALTGCPPLLLLDEPTTGMDPQARRMLWNTI 2112
Cdd:PRK13546 107 EFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKI 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6671495 2113 VSIIREGRAVVLTSHSMEECEALCTRLAIMVKGTFQclgtiqhlkyKFGDgyivtmkikspKDDLLPDLnpvEQFFQ 2189
Cdd:PRK13546 187 YEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLK----------DYGE-----------LDDVLPKY---EAFLN 239
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
949-1138 |
2.40e-10 |
|
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: 65.59 E-value: 2.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 949 LNITFYENQITaFL-GHNGAGKTTTLSILTGLLPPTSGTVLIGGKDI-ETNLDVVRQslgmcpqhniLF------HHLtv 1020
Cdd:COG4615 351 IDLTIRRGELV-FIvGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVtADNREAYRQ----------LFsavfsdFHL-- 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1021 aehilfYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQ-----DLSGGmQRK-LSVAIAFVGDSKVVVLDEPTSGVDP 1094
Cdd:COG4615 418 ------FDRLLGLDGEADPARARELLERLELDHKVSVEDGrfsttDLSQG-QRKrLALLVALLEDRPILVFDEWAADQDP 490
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 6671495 1095 YSRRSIW-DLL--LKyRSGRTIIMSTHhmDEA--DlLGDRIAIISQGRL 1138
Cdd:COG4615 491 EFRRVFYtELLpeLK-ARGKTVIAISH--DDRyfD-LADRVLKMDYGKL 535
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
2040-2152 |
2.49e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 64.49 E-value: 2.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2040 GVPSKEIEKVANWGIQSLGL-SLYADRLAGTYSGGNKRKLSTAIALTGCPPLLLLDEPTTGMDPQARRMLWNTIVSIIRE 2118
Cdd:PRK13631 146 GVKKSEAKKLAKFYLNKMGLdDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN 225
|
90 100 110
....*....|....*....|....*....|....
gi 6671495 2119 GRAVVLTSHSMEECEALCTRLAIMVKGTFQCLGT 2152
Cdd:PRK13631 226 NKTVFVITHTMEHVLEVADEVIVMDKGKILKTGT 259
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
945-1138 |
2.60e-10 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 63.30 E-value: 2.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGtvliggkDIETNLD--VVRQSLGMCPQhnilfhhLTVAE 1022
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVG-------KVDRNGEvsVIAISAGLSGQ-------LTGIE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1023 HILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTSGVDPYSRRSIWD 1102
Cdd:PRK13546 105 NIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLD 184
|
170 180 190
....*....|....*....|....*....|....*..
gi 6671495 1103 LLLKYR-SGRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
Cdd:PRK13546 185 KIYEFKeQNKTIFFVSHNLGQVRQFCTKIAWIEGGKL 221
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1937-2131 |
2.85e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 63.69 E-value: 2.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1937 LKLNELTKVYSGSSS---PAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-----SISD 2008
Cdd:PRK13641 3 IKFENVDYIYSPGTPmekKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPetgnkNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2009 VHQNMGYCPQF--------DAIDDLLTGREHLylyarlrGVPSKEIEKVANWGIQSLGLSL-YADRLAGTYSGGNKRKLS 2079
Cdd:PRK13641 83 LRKKVSLVFQFpeaqlfenTVLKDVEFGPKNF-------GFSEDEAKEKALKWLKKVGLSEdLISKSPFELSGGQMRRVA 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 6671495 2080 TAIALTGCPPLLLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEE 2131
Cdd:PRK13641 156 IAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDD 207
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1936-2145 |
3.16e-10 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 63.02 E-value: 3.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1936 ILKLNELTKVYSGssspavDRLCVGV----RPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKS----ILTSIS 2007
Cdd:PRK11701 6 LLSVRGLTKLYGP------RKGCRDVsfdlYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDgqlrDLYALS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2008 D-------------VHQN--MGYCPQFDA---IDDLL--TGREHlylYARLRGVPSKEIEKVanwgiqslglSLYADR-- 2065
Cdd:PRK11701 80 EaerrrllrtewgfVHQHprDGLRMQVSAggnIGERLmaVGARH---YGDIRATAGDWLERV----------EIDAARid 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2066 -LAGTYSGGNKRKLSTAIALTGCPPLLLLDEPTTGMD--PQARrmLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAI 2141
Cdd:PRK11701 147 dLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDvsVQAR--LLDLLRGLVRElGLAVVIVTHDLAVARLLAHRLLV 224
|
....
gi 6671495 2142 MVKG 2145
Cdd:PRK11701 225 MKQG 228
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1953-2130 |
4.37e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 62.83 E-value: 4.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1953 AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTS-ISDVHQNMGYCPQfDAIDDLLTGR-- 2029
Cdd:PRK13647 20 ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAEnEKWVRSKVGLVFQ-DPDDQVFSSTvw 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2030 EHLYLYARLRGVPSKEIEKVANWGIQSLGLSLYADRLAGTYSGGNKRKLSTAIALTGCPPLLLLDEPTTGMDPQARRMLW 2109
Cdd:PRK13647 99 DDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLM 178
|
170 180
....*....|....*....|.
gi 6671495 2110 NTIVSIIREGRAVVLTSHSME 2130
Cdd:PRK13647 179 EILDRLHNQGKTVIVATHDVD 199
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1954-2152 |
4.69e-10 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 62.92 E-value: 4.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1954 VDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTT--VTSGDATVAGKSILTS-------ISDVHQNMGYCPQ------ 2018
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTggGAPRGARVTGDVTLNGeplaaidAPRLARLRAVLPQaaqpaf 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2019 -FDAIDDLLTGRehlYLYARLRGVPSKEIEKVANWGIQSLGLSLYADRLAGTYSGGNKRKLSTAIAL---------TGCP 2088
Cdd:PRK13547 97 aFSAREIVLLGR---YPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpphdaAQPP 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6671495 2089 PLLLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLT-SHSMEECEALCTRLAIMVKGTFQCLGT 2152
Cdd:PRK13547 174 RYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAiVHDPNLAARHADRIAMLADGAIVAHGA 238
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
909-1138 |
6.60e-10 |
|
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: 64.97 E-value: 6.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 909 HPEGMNDSFFEREL-PGLVPGVCVKNLVKVFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTV 987
Cdd:TIGR00957 616 HEELEPDSIERRTIkPGEGNSITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHV 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 988 LIGGkdietnldvvrqSLGMCPQHNILfHHLTVAEHILFYAQLKGRSWEeAQLEMEAMLED-----TGLHHKRNEEAQDL 1062
Cdd:TIGR00957 696 HMKG------------SVAYVPQQAWI-QNDSLRENILFGKALNEKYYQ-QVLEACALLPDleilpSGDRTEIGEKGVNL 761
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6671495 1063 SGGMQRKLSVAIAFVGDSKVVVLDEPTSGVDPYSRRSIWDLLLKYR---SGRTIIMSTHHMDEADLLgDRIAIISQGRL 1138
Cdd:TIGR00957 762 SGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIGPEgvlKNKTRILVTHGISYLPQV-DVIIVMSGGKI 839
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1968-2156 |
8.07e-10 |
|
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: 63.20 E-value: 8.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1968 GLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTSISDV----HQ-NMGYCPQfDAIddL---LTGREHLyLYARLR 2039
Cdd:COG4148 29 ALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARGIflppHRrRIGYVFQ-EAR--LfphLSVRGNL-LYGRKR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2040 GVPSK---EIEKVANW-GIQSLglslyADRLAGTYSGGNKRKLSTAIALTGCPPLLLLDEPTTGMDPQARRMLWNTIVSI 2115
Cdd:COG4148 105 APRAErriSFDEVVELlGIGHL-----LDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILPYLERL 179
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 6671495 2116 IREGR-AVVLTSHSMEECEALCTRLAIMVKGTFQCLGTIQHL 2156
Cdd:COG4148 180 RDELDiPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEV 221
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
1936-2145 |
9.46e-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: 9.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1936 ILKLNELTKVYSGSS-------SPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAG--------- 1999
Cdd:TIGR02769 2 LLEVRDVTHTYRTGGlfgakqrAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGqdlyqldrk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2000 --KSILTSISDVHQNmgyCPqfDAIDDLLTGR----EHLYLYARLRgvPSKEIEKVANWgIQSLGL-SLYADRLAGTYSG 2072
Cdd:TIGR02769 82 qrRAFRRDVQLVFQD---SP--SAVNPRMTVRqiigEPLRHLTSLD--ESEQKARIAEL-LDMVGLrSEDADKLPRQLSG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6671495 2073 GNKRKLSTAIALTGCPPLLLLDEPTTGMDpqarRMLWNTIVSIIRE-----GRAVVLTSHSMEECEALCTRLAIMVKG 2145
Cdd:TIGR02769 154 GQLQRINIARALAVKPKLIVLDEAVSNLD----MVLQAVILELLRKlqqafGTAYLFITHDLRLVQSFCQRVAVMDKG 227
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1937-2149 |
9.82e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 62.10 E-value: 9.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1937 LKLNELTKVYSgSSSP----AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTG-----DTTVTSGDATVAGKSILTSIS 2007
Cdd:PRK13646 3 IRFDNVSYTYQ-KGTPyehqAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINAllkptTGTVTVDDITITHKTKDKYIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2008 DVHQNMGYCPQF-------DAID-DLLTGREHLylyarlrGVPSKEIEKVANWGIQSLGLSLYADRLAG-TYSGGNKRKL 2078
Cdd:PRK13646 82 PVRKRIGMVFQFpesqlfeDTVErEIIFGPKNF-------KMNLDEVKNYAHRLLMDLGFSRDVMSQSPfQMSGGQMRKI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6671495 2079 STAIALTGCPPLLLLDEPTTGMDPQARRMLWNTIVSI-IREGRAVVLTSHSMEECEALCTRLAIMVKGT--FQC 2149
Cdd:PRK13646 155 AIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLqTDENKTIILVSHDMNEVARYADEVIVMKEGSivSQT 228
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1942-2156 |
1.02e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 62.04 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1942 LTKVYSGSSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTG-DTTVT----SGDATVAGKSILT--SISDVHQNMG 2014
Cdd:PRK14271 27 LTLGFAGKT--VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRmNDKVSgyrySGDVLLGGRSIFNyrDVLEFRRRVG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2015 YCPQ------FDAIDDLLTG-REHlylyarlRGVPSKEIEKVANWGIQSLGL-SLYADRLAGT---YSGGNKRKLSTAIA 2083
Cdd:PRK14271 105 MLFQrpnpfpMSIMDNVLAGvRAH-------KLVPRKEFRGVAQARLTEVGLwDAVKDRLSDSpfrLSGGQQQLLCLART 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6671495 2084 LTGCPPLLLLDEPTTGMDPQARRMLWNTIVSIIrEGRAVVLTSHSMEECEALCTRLAIMVKGTFQCLGTIQHL 2156
Cdd:PRK14271 178 LAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLA-DRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQL 249
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
943-1138 |
1.06e-09 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 63.58 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 943 RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIET-NLDVVRQSLGMCPQHNILFHHlTVA 1021
Cdd:PRK10789 328 HPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKlQLDSWRSRLAVVSQTPFLFSD-TVA 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1022 EHILFyaqlkGR-SWEEAQLEMEAML----EDT-----GLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTSG 1091
Cdd:PRK10789 407 NNIAL-----GRpDATQQEIEHVARLasvhDDIlrlpqGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSA 481
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 6671495 1092 VDPYSRRSIWDLLLKYRSGRTIIMSTHHMD---EAdllgDRIAIISQGRL 1138
Cdd:PRK10789 482 VDGRTEHQILHNLRQWGEGRTVIISAHRLSaltEA----SEILVMQHGHI 527
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
1953-2162 |
1.09e-09 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 63.76 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1953 AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTSISdvhqnmgycpqfDAIDDLLTGREHL 2032
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAIS------------SGLNGQLTGIENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2033 YLYARLRGVPSKEIEKVANWGIQSLGLSLYADRLAGTYSGGNKRKLSTAIALTGCPPLLLLDEPTTGMDPQARRMLWNTI 2112
Cdd:PRK13545 107 ELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKM 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 6671495 2113 VSIIREGRAVVLTSHSMEECEALCTRLAIMVKGTFQCLGTIQHLKYKFGD 2162
Cdd:PRK13545 187 NEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDHYDE 236
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
890-1143 |
1.40e-09 |
|
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: 61.41 E-value: 1.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 890 EERALEKTEPLTEEMEDPEHPEGMNDSFFERelpglvpgvcvknlvkvFEPSGRPAVDRLNITFYENQITAFLGHNGAGK 969
Cdd:cd03291 14 DEGFGELLEKAKQENNDRKHSSDDNNLFFSN-----------------LCLVGAPVLKNINLKIEKGEMLAITGSTGSGK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 970 TTTLSILTGLLPPTSGTVLIGGKdietnldvvrqsLGMCPQHNILFHHlTVAEHILF---YAQLKGRSWEEA-QLEmeam 1045
Cdd:cd03291 77 TSLLMLILGELEPSEGKIKHSGR------------ISFSSQFSWIMPG-TIKENIIFgvsYDEYRYKSVVKAcQLE---- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1046 lED-TGLHHKRN----EEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTSGVDPYSRRSIWD-LLLKYRSGRTIIMSTHH 1119
Cdd:cd03291 140 -EDiTKFPEKDNtvlgEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFEsCVCKLMANKTRILVTSK 218
|
250 260
....*....|....*....|....
gi 6671495 1120 MDEADlLGDRIAIISQGRLYCSGT 1143
Cdd:cd03291 219 MEHLK-KADKILILHEGSSYFYGT 241
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1937-2145 |
1.60e-09 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 60.37 E-value: 1.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1937 LKLNELTKVYSGSSSpavdRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGK------------SILT 2004
Cdd:PRK10771 2 LKLTDITWLYHHLPM----RFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQdhtttppsrrpvSMLF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2005 SISD------VHQNMGycpqfdaiddlltgrehLYLYA--RLRGVPSKEIEKVAnwgiQSLGLSLYADRLAGTYSGGNKR 2076
Cdd:PRK10771 78 QENNlfshltVAQNIG-----------------LGLNPglKLNAAQREKLHAIA----RQMGIEDLLARLPGQLSGGQRQ 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6671495 2077 KLSTAIALTGCPPLLLLDEPTTGMDPQARR-MLwnTIVSIIREGRAVVL--TSHSMEECEALCTRLAIMVKG 2145
Cdd:PRK10771 137 RVALARCLVREQPILLLDEPFSALDPALRQeML--TLVSQVCQERQLTLlmVSHSLEDAARIAPRSLVVADG 206
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1932-2154 |
1.72e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 60.92 E-value: 1.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1932 NKTDILKLNELTKVYSGSSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-SISDVH 2010
Cdd:PRK13648 3 DKNSIIVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDdNFEKLR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2011 QNMGYCpqFDAIDDLLTGREHLYLYA---RLRGVPSKEIEKVANWGIQSLGLSLYADRLAGTYSGGNKRKLSTAIALTGC 2087
Cdd:PRK13648 83 KHIGIV--FQNPDNQFVGSIVKYDVAfglENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALN 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6671495 2088 PPLLLLDEPTTGMDPQARRMLWNtIVSIIREGRAVVLTSHSMEECEAL-CTRLAIMVKGTFQCLGTIQ 2154
Cdd:PRK13648 161 PSVIILDEATSMLDPDARQNLLD-LVRKVKSEHNITIISITHDLSEAMeADHVIVMNKGTVYKEGTPT 227
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1964-2154 |
2.89e-09 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 61.25 E-value: 2.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1964 GECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIltsiSDVH---QNMGYCPQ----------FDAIDDLLTgre 2030
Cdd:PRK10851 28 GQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDV----SRLHardRKVGFVFQhyalfrhmtvFDNIAFGLT--- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2031 hlYLYARLRgvPSKEI--EKVANWgIQSLGLSLYADRLAGTYSGGNKRKLSTAIALTGCPPLLLLDEPTTGMDPQARRML 2108
Cdd:PRK10851 101 --VLPRRER--PNAAAikAKVTQL-LEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKEL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 6671495 2109 WNTIVSIIREGR-AVVLTSHSMEECEALCTRLAIMVKGTFQCLGTIQ 2154
Cdd:PRK10851 176 RRWLRQLHEELKfTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPD 222
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1937-2134 |
3.08e-09 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 59.03 E-value: 3.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1937 LKLNELTkVYSGSSsPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTtvtSGDATVAGKSIL--TSISD--VHQ- 2011
Cdd:COG4136 2 LSLENLT-ITLGGR-PLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTL---SPAFSASGEVLLngRRLTAlpAEQr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2012 NMGYCPQfdaiDDLLTgrEHLYLYARL-----RGVPSKEIEKVANWGIQSLGLSLYADRLAGTYSGGNKRKLSTAIALTG 2086
Cdd:COG4136 77 RIGILFQ----DDLLF--PHLSVGENLafalpPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 6671495 2087 CPPLLLLDEPTTGMDP----QARRMLWNTivsIIREGRAVVLTSHSMEECEA 2134
Cdd:COG4136 151 EPRALLLDEPFSKLDAalraQFREFVFEQ---IRQRGIPALLVTHDEEDAPA 199
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
929-1119 |
3.17e-09 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 57.93 E-value: 3.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 929 VCVKNLvKVFEPSGRPAVDRLNITFYENQ---ITaflGHNGAGKTTTLSILTGLLPPTSGTVliggkdietnldvvrqsl 1005
Cdd:cd03223 1 IELENL-SLATPDGRVLLKDLSFEIKPGDrllIT---GPSGTGKSSLFRALAGLWPWGSGRI------------------ 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1006 GMCPQHNILFhhltVAEH----------ILFYAqlkgrsWEEAqlemeamledtglhhkrneeaqdLSGGMQRKLSVAIA 1075
Cdd:cd03223 59 GMPEGEDLLF----LPQRpylplgtlreQLIYP------WDDV-----------------------LSGGEQQRLAFARL 105
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 6671495 1076 FVGDSKVVVLDEPTSGVDPYSRRSIWDLLLKYrsGRTIIMSTHH 1119
Cdd:cd03223 106 LLHKPKFVFLDEATSALDEESEDRLYQLLKEL--GITVISVGHR 147
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
963-1121 |
3.79e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 58.81 E-value: 3.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 963 GHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIETNLDVVRQSLGMCPQHNILFHHLTVAEHILFYAQlkgrsWEEAQLEM 1042
Cdd:PRK13540 34 GSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGHRSGINPYLTLRENCLYDIH-----FSPGAVGI 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6671495 1043 EAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMD 1121
Cdd:PRK13540 109 TELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSHQD 187
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
943-1144 |
3.84e-09 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 59.74 E-value: 3.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 943 RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLiggKDIETNLDVVRQSLGMCPQHNilfhhLTVAE 1022
Cdd:PRK09544 17 RRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK---RNGKLRIGYVPQKLYLDTTLP-----LTVNR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1023 HILFYAQLKgrsweeaQLEMEAMLEDTGLHHKRNEEAQDLSGG-MQRKLsVAIAFVGDSKVVVLDEPTSGVDPYSRRSIW 1101
Cdd:PRK09544 89 FLRLRPGTK-------KEDILPALKRVQAGHLIDAPMQKLSGGeTQRVL-LARALLNRPQLLVLDEPTQGVDVNGQVALY 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 6671495 1102 DLLLKYRS--GRTIIMSTHHMDEADLLGDRIAIISQgRLYCSGTP 1144
Cdd:PRK09544 161 DLIDQLRRelDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGTP 204
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1969-2127 |
5.08e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 58.42 E-value: 5.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1969 LLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTSISDVHQNMGYCPQFDAIDDLLTGREHLYLYARLRGvpskeiek 2048
Cdd:PRK13540 32 LKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGHRSGINPYLTLRENCLYDIHFSP-------- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2049 vANWGIQSL----GLSLYADRLAGTYSGGNKRKLSTAIALTGCPPLLLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVL 2124
Cdd:PRK13540 104 -GAVGITELcrlfSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQEHRAKGGAVLL 182
|
...
gi 6671495 2125 TSH 2127
Cdd:PRK13540 183 TSH 185
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1961-2145 |
5.44e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 61.34 E-value: 5.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1961 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTS------------ISDVHQNMGYCPQFDAIDDLLTG 2028
Cdd:PRK09700 286 VCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRspldavkkgmayITESRRDNGFFPNFSIAQNMAIS 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2029 REhLYLyARLRG----VPSKEIEKVANWGIQSLGLSLYA-DRLAGTYSGGNKRKLSTAIALTGCPPLLLLDEPTTGMDPQ 2103
Cdd:PRK09700 366 RS-LKD-GGYKGamglFHEVDEQRTAENQRELLALKCHSvNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVG 443
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 6671495 2104 ARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2145
Cdd:PRK09700 444 AKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEG 485
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
945-1139 |
5.60e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 61.14 E-value: 5.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDI-ETNLDVVRQslgmcpqhniLFHHLTVAEH 1023
Cdd:PRK10522 338 SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVtAEQPEDYRK----------LFSAVFTDFH 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1024 iLFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQ-----DLSGGMQRKLSVAIAFVGDSKVVVLDEPTSGVDPYSRR 1098
Cdd:PRK10522 408 -LFDQLLGPEGKPANPALVEKWLERLKMAHKLELEDGrisnlKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRR 486
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 6671495 1099 SIWDLLLKY--RSGRTIIMSTHHmDEADLLGDRIAIISQGRLY 1139
Cdd:PRK10522 487 EFYQVLLPLlqEMGKTIFAISHD-DHYFIHADRLLEMRNGQLS 528
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1966-2128 |
5.61e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 59.09 E-value: 5.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1966 CFGLLGVNGAGKTT---TFKMLT--GDTTVTSGDATVAGKSILTSISD---VHQNMGYCPQFDAIDDLLTGREHLYLYAR 2037
Cdd:PRK14267 32 VFALMGPSGCGKSTllrTFNRLLelNEEARVEGEVRLFGRNIYSPDVDpieVRREVGMVFQYPNPFPHLTIYDNVAIGVK 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2038 LRGV--PSKEIEKVANWGIQSLGL-SLYADRL---AGTYSGGNKRKLSTAIALTGCPPLLLLDEPTTGMDPQARRMLWNT 2111
Cdd:PRK14267 112 LNGLvkSKKELDERVEWALKKAALwDEVKDRLndyPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEEL 191
|
170
....*....|....*..
gi 6671495 2112 IVSiIREGRAVVLTSHS 2128
Cdd:PRK14267 192 LFE-LKKEYTIVLVTHS 207
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1961-2127 |
7.18e-09 |
|
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: 57.92 E-value: 7.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1961 VRPGECFGLLGVNGAGKTTTFKMLTG--DTTVTSGDATVAGKSILTSISDVHQNMGycpqfdaiddlltgrehLYLY--- 2035
Cdd:cd03217 23 IKKGEVHALMGPNGSGKSTLAKTIMGhpKYEVTEGEILFKGEDITDLPPEERARLG-----------------IFLAfqy 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2036 -ARLRGVpskeieKVANWgIQSLGLSLyadrlagtySGGNKRKLSTAIALTGCPPLLLLDEPTTGMDPQARRMLWNTIVS 2114
Cdd:cd03217 86 pPEIPGV------KNADF-LRYVNEGF---------SGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINK 149
|
170
....*....|...
gi 6671495 2115 IIREGRAVVLTSH 2127
Cdd:cd03217 150 LREEGKSVLIITH 162
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1946-2108 |
7.32e-09 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 58.40 E-value: 7.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1946 YSGSSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-SISDVHQNMGYCPQfDAIdd 2024
Cdd:cd03251 10 YPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDyTLASLRRQIGLVSQ-DVF-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2025 LLTG--REHLyLYARlRGVPSKEIEKVAnwgiQSLGLSLYADRLAGTY-----------SGGNKRKLSTAIALTGCPPLL 2091
Cdd:cd03251 87 LFNDtvAENI-AYGR-PGATREEVEEAA----RAANAHEFIMELPEGYdtvigergvklSGGQRQRIAIARALLKDPPIL 160
|
170
....*....|....*..
gi 6671495 2092 LLDEPTTGMDPQARRML 2108
Cdd:cd03251 161 ILDEATSALDTESERLV 177
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1933-2156 |
7.62e-09 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 60.12 E-value: 7.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1933 KTDILKLNELTKVYSgsSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTS------I 2006
Cdd:PRK11432 3 QKNFVVLKNITKRFG--SNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRsiqqrdI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2007 SDVHQNMGYCPQFDAIDDLLTGrehlylyARLRGVPSKEIEKVANWGIQSLGLSLYADRLAGTYSGGNKRKLSTAIALTG 2086
Cdd:PRK11432 81 CMVFQSYALFPHMSLGENVGYG-------LKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALIL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6671495 2087 CPPLLLLDEPTTGMDPQARRMLWNTivsiIRE-GRAVVLTS----HSMEECEALCTRLAIMVKGTFQCLGTIQHL 2156
Cdd:PRK11432 154 KPKVLLFDEPLSNLDANLRRSMREK----IRElQQQFNITSlyvtHDQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1937-2130 |
8.42e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 59.33 E-value: 8.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1937 LKLNELTKVYSGSSS---PAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGD------------ATVAGKS 2001
Cdd:PRK13651 3 IKVKNIVKIFNKKLPtelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTiewifkdeknkkKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2002 ILTS-------------ISDVHQNMGYCPQFdAIDDLL--TGREHLYLYARLRGVPSKEIEKVANWGIQSLGLSL-YADR 2065
Cdd:PRK13651 83 VLEKlviqktrfkkikkIKEIRRRVGVVFQF-AEYQLFeqTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDEsYLQR 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6671495 2066 LAGTYSGGNKRKLSTAIALTGCPPLLLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSME 2130
Cdd:PRK13651 162 SPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLD 226
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1961-2107 |
8.99e-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: 58.57 E-value: 8.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1961 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIltsisdvhqnmGYCPQFDAIDDLLTGREHLYLYARLRG 2040
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV-----------SYKPQYIKADYEGTVRDLLSSITKDFY 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6671495 2041 VPSKEIEKVANwgiqSLGLSLYADRLAGTYSGGNKRKLSTAIALTGCPPLLLLDEPTTGMDPQARRM 2107
Cdd:cd03237 91 THPYFKTEIAK----PLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLM 153
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1952-2145 |
9.85e-09 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 58.56 E-value: 9.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1952 PAVDRLCVGVRPGECFGLLGVNGAGKTTT----FKMLTGDTTVTSGDATVAGKSILTS------ISDVHQNmgycPQfDA 2021
Cdd:PRK10418 17 PLVHGVSLTLQRGRVLALVGGSGSGKSLTcaaaLGILPAGVRQTAGRVLLDGKPVAPCalrgrkIATIMQN----PR-SA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2022 IDDLLTGREHLYLYARLRGVPSKEIEKVAnwGIQSLGLSlYADRLAGTY----SGGNKRKLSTAIALTGCPPLLLLDEPT 2097
Cdd:PRK10418 92 FNPLHTMHTHARETCLALGKPADDATLTA--ALEAVGLE-NAARVLKLYpfemSGGMLQRMMIALALLCEAPFIIADEPT 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 6671495 2098 TGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKG 2145
Cdd:PRK10418 169 TDLDVVAQARILDLLESIVQKrALGMLLVTHDMGVVARLADDVAVMSHG 217
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
927-1137 |
9.87e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 60.49 E-value: 9.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 927 PGVCVKNLVKVFEPSG--RPAVDRLNITFYENQITAFLGHNGAGKT-TTLSILtGLLPP-----TSGTVLIGGKDI---- 994
Cdd:PRK15134 4 PLLAIENLSVAFRQQQtvRTVVNDVSLQIEAGETLALVGESGSGKSvTALSIL-RLLPSppvvyPSGDIRFHGESLlhas 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 995 ETNLDVVR-QSLGMC---------PQHNI---LFHHLTVaeHilfyaqlKGRSWEEAQLEMEAMLEDTGLHH--KR-NEE 1058
Cdd:PRK15134 83 EQTLRGVRgNKIAMIfqepmvslnPLHTLekqLYEVLSL--H-------RGMRREAARGEILNCLDRVGIRQaaKRlTDY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1059 AQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQG 1136
Cdd:PRK15134 154 PHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLreLQQELNMGLLFITHNLSIVRKLADRVAVMQNG 233
|
.
gi 6671495 1137 R 1137
Cdd:PRK15134 234 R 234
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
903-1142 |
1.04e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 60.95 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 903 EMEDPEHPEGMNDSFFErelpgLVPGVCVKNlVKVFEPSGRpavdrlnitfyenqITAFLGHNGAGKTTTLSILTGLLPP 982
Cdd:PTZ00243 653 SERSAKTPKMKTDDFFE-----LEPKVLLRD-VSVSVPRGK--------------LTVVLGATGSGKSTLLQSLLSQFEI 712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 983 TSGTVLiggkdietnldvVRQSLGMCPQHNILFHhLTVAEHILFYAQLKGRSWEEA----QLEMEAMLEDTGLHHKRNEE 1058
Cdd:PTZ00243 713 SEGRVW------------AERSIAYVPQQAWIMN-ATVRGNILFFDEEDAARLADAvrvsQLEADLAQLGGGLETEIGEK 779
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1059 AQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTSGVDPY-SRRSIWDLLLKYRSGRTIIMSTHHMDEADlLGDRIAIISQGR 1137
Cdd:PTZ00243 780 GVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHvGERVVEECFLGALAGKTRVLATHQVHVVP-RADYVVALGDGR 858
|
....*
gi 6671495 1138 LYCSG 1142
Cdd:PTZ00243 859 VEFSG 863
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
1873-2127 |
1.08e-08 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 60.36 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1873 LIGKNLVA---MAIEGVVYF--LLTLLIQH-----HFFLTRWIAEPAREPVFDEDDDVA--EERQRVMSGGNKTDILKLN 1940
Cdd:PRK13657 259 VLGAALVQkgqLRVGEVVAFvgFATLLIGRldqvvAFINQVFMAAPKLEEFFEVEDAVPdvRDPPGAIDLGRVKGAVEFD 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1941 ELTKVYSGSSsPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKML-------TGDTTVTSGD-ATVAGKSILTSISDVHQN 2012
Cdd:PRK13657 339 DVSFSYDNSR-QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLqrvfdpqSGRILIDGTDiRTVTRASLRRNIAVVFQD 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2013 MGYcpqFD-AI-DDLLTGR-----EHLYLYARlRGVPSKEIEKvanwgiQSLGLSLYADRLAGTYSGGNKRKLSTAIALT 2085
Cdd:PRK13657 418 AGL---FNrSIeDNIRVGRpdatdEEMRAAAE-RAQAHDFIER------KPDGYDTVVGERGRQLSGGERQRLAIARALL 487
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 6671495 2086 GCPPLLLLDEPTTGMDPQARRMLwNTIVSIIREGRAVVLTSH 2127
Cdd:PRK13657 488 KDPPILILDEATSALDVETEAKV-KAALDELMKGRTTFIIAH 528
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1954-2148 |
1.51e-08 |
|
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: 59.84 E-value: 1.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1954 VDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGD-TTVTSGDATVAGK--SILTSISDVHQNMGYCPQ----FDAIDDLL 2026
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKpvDIRNPAQAIRAGIAMVPEdrkrHGIVPILG 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2027 TGRE----HLYLYARLRGVPSKEIEKVANWGIQSLGLSLYADRLA-GTYSGGNKRKLSTAIALTGCPPLLLLDEPTTGMD 2101
Cdd:TIGR02633 356 VGKNitlsVLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVD 435
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 6671495 2102 PQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGTFQ 2148
Cdd:TIGR02633 436 VGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLK 482
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1963-2127 |
1.58e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 59.80 E-value: 1.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1963 PGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAgKSIltsisdvhqNMGYCPQfdaiddlltgreHLYLYARLRGVP 2042
Cdd:PRK10636 337 PGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLA-KGI---------KLGYFAQ------------HQLEFLRADESP 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2043 SKEIEKVANWGI-QSL-----GLSLYADRLA---GTYSGGNKRKLSTAIALTGCPPLLLLDEPTTGMDPQARRMLWNTIV 2113
Cdd:PRK10636 395 LQHLARLAPQELeQKLrdylgGFGFQGDKVTeetRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALI 474
|
170
....*....|....
gi 6671495 2114 SIirEGrAVVLTSH 2127
Cdd:PRK10636 475 DF--EG-ALVVVSH 485
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
943-1136 |
1.66e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 57.28 E-value: 1.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 943 RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLP--PTSGTVLIGGKDIETNldvvrqslgmcpqhnilfhhLTV 1020
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVPDNQFGRE--------------------ASL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1021 AEHILfyaqLKGRSWEEAQLEMEAMLEDTGLHHKRNEEaqdLSGGMQRKLSVAIAFVGDSKVVVLDEPTSGVDP-YSRR- 1098
Cdd:COG2401 103 IDAIG----RKGDFKDAVELLNAVGLSDAVLWLRRFKE---LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRqTAKRv 175
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 6671495 1099 -SIWDLLLKyRSGRTIIMSTHHMD-EADLLGDRIAIISQG 1136
Cdd:COG2401 176 aRNLQKLAR-RAGITLVVATHHYDvIDDLQPDLLIFVGYG 214
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1946-2129 |
1.66e-08 |
|
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: 57.50 E-value: 1.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1946 YSGSSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTSISD-VHQNMGYCPQfdaiDD 2024
Cdd:cd03252 10 YKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAwLRRQVGVVLQ----EN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2025 LL---TGREHLYLyarlrGVPSKEIEKVanwgiqslglsLYADRLAGTY---------------------SGGNKRKLST 2080
Cdd:cd03252 86 VLfnrSIRDNIAL-----ADPGMSMERV-----------IEAAKLAGAHdfiselpegydtivgeqgaglSGGQRQRIAI 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 6671495 2081 AIALTGCPPLLLLDEPTTGMDPQARRMLWNTIVSIIrEGRAVVLTSHSM 2129
Cdd:cd03252 150 ARALIHNPRILIFDEATSALDYESEHAIMRNMHDIC-AGRTVIIIAHRL 197
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1953-2145 |
1.98e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 59.48 E-value: 1.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1953 AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT----SISDVHQNMGYCPQ--FDAIDDLL 2026
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTlspgKLQALRRDIQFIFQdpYASLDPRQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2027 TGREHLYLYARLRGV-PSKEIEKVANWGIQSLGL-SLYADRLAGTYSGGNKRKLSTAIALTGCPPLLLLDEPTTGMDPQA 2104
Cdd:PRK10261 419 TVGDSIMEPLRVHGLlPGKAAAARVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSI 498
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 6671495 2105 RRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKG 2145
Cdd:PRK10261 499 RGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLG 540
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
938-1156 |
2.25e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 59.99 E-value: 2.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 938 FEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDI-ETNLDVVRQSLGMCPQHNILFH 1016
Cdd:PLN03232 1244 YRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVaKFGLTDLRRVLSIIPQSPVLFS 1323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1017 HlTVAEHI-LFYAQLKGRSWEEAQlemEAMLEDT------GLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEPT 1089
Cdd:PLN03232 1324 G-TVRFNIdPFSEHNDADLWEALE---RAHIKDVidrnpfGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEAT 1399
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6671495 1090 SGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEAdLLGDRIAIISQGRLYCSGTPLFLKNCFGTGFY 1156
Cdd:PLN03232 1400 ASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTI-IDCDKILVLSSGQVLEYDSPQELLSRDTSAFF 1465
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
655-856 |
2.47e-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: 58.17 E-value: 2.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 655 FPIFMVLAWIYSVSMTVKGIVLEKELRLKETLKNQGVSNAVIWCTWFLdSFSIMALSIFLLTLFIMHGRILHYSDPFILF 734
Cdd:pfam12698 164 VGLILMIIILIGAAIIAVSIVEEKESRIKERLLVSGVSPLQYWLGKIL-GDFLVGLLQLLIILLLLFGIGIPFGNLGLLL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 735 LFLLAFATATIMQSFLLSTLFSKASLAaacSGVIYFTLYLPHVLCFA--WQDRMTADLKTTVSLLSSVAFGFGteylvrF 812
Cdd:pfam12698 243 LLFLLYGLAYIALGYLLGSLFKNSEDA---QSIIGIVILLLSGFFGGlfPLEDPPSFLQWIFSIIPFFSPIDG------L 313
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 6671495 813 EEQGLGLQWSNIgksplegdefsfLLSMKMMLLDAALYGLLAWY 856
Cdd:pfam12698 314 LRLIYGDSLWEI------------APSLIILLLFAVVLLLLALL 345
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
938-1143 |
2.62e-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: 59.54 E-value: 2.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 938 FEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKdietnldvvrqsLGMCPQHNILFHH 1017
Cdd:TIGR01271 434 FSLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR------------ISFSPQTSWIMPG 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1018 lTVAEHILF---YAQLKGRSWEEA-QLEmeamlEDTGLHHKRN-----EEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEP 1088
Cdd:TIGR01271 502 -TIKDNIIFglsYDEYRYTSVIKAcQLE-----EDIALFPEKDktvlgEGGITLSGGQRARISLARAVYKDADLYLLDSP 575
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 6671495 1089 TSGVDPYSRRSIWD-LLLKYRSGRTIIMST---HHMDEAdllgDRIAIISQGRLYCSGT 1143
Cdd:TIGR01271 576 FTHLDVVTEKEIFEsCLCKLMSNKTRILVTsklEHLKKA----DKILLLHEGVCYFYGT 630
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
1915-2106 |
3.07e-08 |
|
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: 58.96 E-value: 3.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1915 DEDDDVAEERQRVmsggnkTDILKLNELTKVYSGSSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGD 1994
Cdd:TIGR02203 315 PEKDTGTRAIERA------RGDVEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQ 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1995 ATVAG--------KSILTSISDVHQNMGYcpqfdaIDDLLTGRehlYLYARLRGVPSKEIEKVAnwgiQSLGLSLYADRL 2066
Cdd:TIGR02203 389 ILLDGhdladytlASLRRQVALVSQDVVL------FNDTIANN---IAYGRTEQADRAEIERAL----AAAYAQDFVDKL 455
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 6671495 2067 -----------AGTYSGGNKRKLSTAIALTGCPPLLLLDEPTTGMDPQARR 2106
Cdd:TIGR02203 456 plgldtpigenGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESER 506
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1936-2145 |
3.28e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 57.41 E-value: 3.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1936 ILKLNELTKVYSGSSS-PAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-SISDVHQNM 2013
Cdd:PRK13642 4 ILEVENLVFKYEKESDvNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAeNVWNLRRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2014 GYCpqFDAIDDLLTG---REHLYLYARLRGVPSKEIEKVANWGIQSLGLSLYADRLAGTYSGGNKRKLSTAIALTGCPPL 2090
Cdd:PRK13642 84 GMV--FQNPDNQFVGatvEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 6671495 2091 LLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLT-SHSMEECeALCTRLAIMVKG 2145
Cdd:PRK13642 162 IILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSiTHDLDEA-ASSDRILVMKAG 216
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1952-2131 |
3.48e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 58.49 E-value: 3.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1952 PAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVT-SGDATVAGK---SILTsISDVHQNMGYCPQ--------- 2018
Cdd:PRK10938 274 PILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPQGySNDLTLFGRrrgSGET-IWDIKKHIGYVSSslhldyrvs 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2019 -----------FDAIDdlltgrehlyLYarlRGVPSKEIEKVANWgIQSLGLSlyaDRLAG----TYSGGNKRKLSTAIA 2083
Cdd:PRK10938 353 tsvrnvilsgfFDSIG----------IY---QAVSDRQQKLAQQW-LDILGID---KRTADapfhSLSWGQQRLALIVRA 415
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 6671495 2084 LTGCPPLLLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVL-TSHSMEE 2131
Cdd:PRK10938 416 LVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLfVSHHAED 464
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
906-1138 |
3.51e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 58.71 E-value: 3.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 906 DPEHPEGMNDSFFERElpglvPGVCVKNLVKVFEPSGR---------PAVDRLNITFYENQITAFLGHNGAGKTTTLSIL 976
Cdd:PRK10261 296 AKQEPPIEQDTVVDGE-----PILQVRNLVTRFPLRSGllnrvtrevHAVEKVSFDLWPGETLSLVGESGSGKSTTGRAL 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 977 TGLLPPTSGTVLIGGKDIETNLDVVRQSL-------------GMCPQHNILFhhlTVAEHILFYAQLKGrswEEAQLEME 1043
Cdd:PRK10261 371 LRLVESQGGEIIFNGQRIDTLSPGKLQALrrdiqfifqdpyaSLDPRQTVGD---SIMEPLRVHGLLPG---KAAAARVA 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1044 AMLEDTGLhhkRNEEA----QDLSGGMQRKLSVAIAFVGDSKVVVLDEPTSGVDPYSRRSIWDLLLKYRS--GRTIIMST 1117
Cdd:PRK10261 445 WLLERVGL---LPEHAwrypHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRdfGIAYLFIS 521
|
250 260
....*....|....*....|.
gi 6671495 1118 HHMDEADLLGDRIAIISQGRL 1138
Cdd:PRK10261 522 HDMAVVERISHRVAVMYLGQI 542
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
940-1093 |
4.25e-08 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 57.41 E-value: 4.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 940 PSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDI----ETNLDVVRQSLGMCPQHNI-- 1013
Cdd:PRK15079 31 PKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLlgmkDDEWRAVRSDIQMIFQDPLas 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1014 LFHHLTVAEHI-----LFYAQLkgrSWEEAQLEMEAMLEDTGL-HHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDE 1087
Cdd:PRK15079 111 LNPRMTIGEIIaeplrTYHPKL---SRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDE 187
|
....*.
gi 6671495 1088 PTSGVD 1093
Cdd:PRK15079 188 PVSALD 193
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1961-2146 |
4.33e-08 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 56.66 E-value: 4.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1961 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGdatvagksilTSISDVHQNMGYCPQ---FDAIDDLLTGRehlylYAR 2037
Cdd:PRK09544 27 LKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEG----------VIKRNGKLRIGYVPQklyLDTTLPLTVNR-----FLR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2038 LR-GVPSKEI---------EKVANWGIQSLglslyadrlagtySGGNKRKLSTAIALTGCPPLLLLDEPTTGMDPQARRM 2107
Cdd:PRK09544 92 LRpGTKKEDIlpalkrvqaGHLIDAPMQKL-------------SGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 6671495 2108 LWNTIVSIIRE-GRAVVLTSHSM-----EECEALCTRLAIMVKGT 2146
Cdd:PRK09544 159 LYDLIDQLRRElDCAVLMVSHDLhlvmaKTDEVLCLNHHICCSGT 203
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1969-2152 |
5.14e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 56.94 E-value: 5.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1969 LLGVNGAGKTTTFKMLTGDTTVTSGDATV------AGKSILTSISDVHQNMGYCPQF-------DAID-DLLTGREHLyl 2034
Cdd:PRK13645 42 VIGTTGSGKSTMIQLTNGLIISETGQTIVgdyaipANLKKIKEVKRLRKEIGLVFQFpeyqlfqETIEkDIAFGPVNL-- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2035 yarlrGVPSKEIEKVANWGIQSLGLSL-YADRLAGTYSGGNKRKLSTA--IALTGcpPLLLLDEPTTGMDPQARRMLWNT 2111
Cdd:PRK13645 120 -----GENKQEAYKKVPELLKLVQLPEdYVKRSPFELSGGQKRRVALAgiIAMDG--NTLVLDEPTGGLDPKGEEDFINL 192
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 6671495 2112 IVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGTFQCLGT 2152
Cdd:PRK13645 193 FERLNKEyKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGS 234
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
931-1138 |
5.85e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 57.82 E-value: 5.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 931 VKNLVKVFEPSGRpavdrlNITF--YENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIE--TNLDVV----- 1001
Cdd:PRK10982 253 VRNLTSLRQPSIR------DVSFdlHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINnhNANEAInhgfa 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1002 -----RQSLGMCPQHNILFHHL--TVAEHILFYAQLKGRSWE-EAQLEMEAMLEDTGLHHKrneEAQDLSGGMQRKLSVA 1073
Cdd:PRK10982 327 lvteeRRSTGIYAYLDIGFNSLisNIRNYKNKVGLLDNSRMKsDTQWVIDSMRVKTPGHRT---QIGSLSGGNQQKVIIG 403
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6671495 1074 IAFVGDSKVVVLDEPTSGVDPYSRRSIWDLLLKY-RSGRTIIMSTHHMDEadLLG--DRIAIISQGRL 1138
Cdd:PRK10982 404 RWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELaKKDKGIIIISSEMPE--LLGitDRILVMSNGLV 469
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
931-1121 |
5.94e-08 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 58.38 E-value: 5.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 931 VKNLVKVFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPpTSGTVLIGGKDIET-NLDVVRQSLGMCP 1009
Cdd:TIGR01271 1220 VQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSvTLQTWRKAFGVIP 1298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1010 QHNILFHHlTVAEHILFYAQLKGRS-WEEA-QLEMEAMLEDtgLHHKRNEEAQD----LSGGMQRKLSVAIAFVGDSKVV 1083
Cdd:TIGR01271 1299 QKVFIFSG-TFRKNLDPYEQWSDEEiWKVAeEVGLKSVIEQ--FPDKLDFVLVDggyvLSNGHKQLMCLARSILSKAKIL 1375
|
170 180 190
....*....|....*....|....*....|....*...
gi 6671495 1084 VLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMD 1121
Cdd:TIGR01271 1376 LLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVE 1413
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
931-1143 |
5.95e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 57.94 E-value: 5.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 931 VKNLVKVFEPSGR--PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGG----KDIETNLDVVRQS 1004
Cdd:PRK10261 15 VENLNIAFMQEQQkiAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrRRSRQVIELSEQS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1005 -----------LGMCPQH-----NILFhhlTVAEHILFYAQL-KGRSWEEAQLEMEAMLEDTglhhkRNEEAQ------- 1060
Cdd:PRK10261 95 aaqmrhvrgadMAMIFQEpmtslNPVF---TVGEQIAESIRLhQGASREEAMVEAKRMLDQV-----RIPEAQtilsryp 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1061 -DLSGGMQRKLSVAIAFVGDSKVVVLDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGR 1137
Cdd:PRK10261 167 hQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIkvLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGE 246
|
....*.
gi 6671495 1138 LYCSGT 1143
Cdd:PRK10261 247 AVETGS 252
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1937-2138 |
6.16e-08 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 56.22 E-value: 6.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1937 LKLNELTKVYSGSSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDaTVAGKSILTSISD----VHQN 2012
Cdd:PRK11247 13 LLLNAVSKRYGERT--VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGE-LLAGTAPLAEAREdtrlMFQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2013 MGYCPQFDAIDDLLTGrehlylyarLRGvpskeiekvaNW------GIQSLGLSLYADRLAGTYSGGNKRKLSTAIALTG 2086
Cdd:PRK11247 90 ARLLPWKKVIDNVGLG---------LKG----------QWrdaalqALAAVGLADRANEWPAALSGGQKQRVALARALIH 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 6671495 2087 CPPLLLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTR 2138
Cdd:PRK11247 151 RPGLLLLDEPLGALDALTRIEMQDLIESLWQQhGFTVLLVTHDVSEAVAMADR 203
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1964-2130 |
6.50e-08 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 56.13 E-value: 6.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1964 GECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIltsiSDVHQNMGYCPQFDAID-DLLTGR-----EHLYLYAR 2037
Cdd:PRK10619 31 GDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTI----NLVRDKDGQLKVADKNQlRLLRTRltmvfQHFNLWSH 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2038 LrgvpsKEIEKVANWGIQSLGLS---------LYADRLA------GTY----SGGNKRKLSTAIALTGCPPLLLLDEPTT 2098
Cdd:PRK10619 107 M-----TVLENVMEAPIQVLGLSkqeareravKYLAKVGideraqGKYpvhlSGGQQQRVSIARALAMEPEVLLFDEPTS 181
|
170 180 190
....*....|....*....|....*....|..
gi 6671495 2099 GMDPQARRMLWNTIVSIIREGRAVVLTSHSME 2130
Cdd:PRK10619 182 ALDPELVGEVLRIMQQLAEEGKTMVVVTHEMG 213
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1961-2127 |
6.62e-08 |
|
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: 55.69 E-value: 6.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1961 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-SISDVHQNMGYCPQfdaiDDLL---TGREHLyLYA 2036
Cdd:cd03254 26 IKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDiSRKSLRSMIGVVLQ----DTFLfsgTIMENI-RLG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2037 RLRgVPSKEIEKVAnwgiQSLGLSLYADRLAGTY-----------SGGNKRKLSTAIALTGCPPLLLLDEPTTGMDPQAR 2105
Cdd:cd03254 101 RPN-ATDEEVIEAA----KEAGAHDFIMKLPNGYdtvlgenggnlSQGERQLLAIARAMLRDPKILILDEATSNIDTETE 175
|
170 180
....*....|....*....|..
gi 6671495 2106 RMLWNTIVSiIREGRAVVLTSH 2127
Cdd:cd03254 176 KLIQEALEK-LMKGRTSIIIAH 196
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1936-2145 |
1.08e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 55.55 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1936 ILKLNELTKVYSgsSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLT--GD---TTVTSGDATVAGKSIL---TSIS 2007
Cdd:PRK14239 5 ILQVSDLSVYYN--KKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDlnpEVTITGSIVYNGHNIYsprTDTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2008 DVHQNMGYCPQ------FDAIDDLLTGrehlylyARLRGVPSKEI--EKVANwgiqSL-GLSLY---ADRL---AGTYSG 2072
Cdd:PRK14239 83 DLRKEIGMVFQqpnpfpMSIYENVVYG-------LRLKGIKDKQVldEAVEK----SLkGASIWdevKDRLhdsALGLSG 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6671495 2073 GNKRKLSTAIALTGCPPLLLLDEPTTGMDPQARRMLWNTIVSiIREGRAVVLTSHSMEECEALCTRLAIMVKG 2145
Cdd:PRK14239 152 GQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLG-LKDDYTMLLVTRSMQQASRISDRTGFFLDG 223
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
932-1093 |
1.14e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 57.44 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 932 KNLVKVFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIET-NLDVVRQSLGMCPQ 1010
Cdd:PLN03130 1241 EDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKfGLMDLRKVLGIIPQ 1320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1011 HNILFHHlTV-------AEHilFYAQLkgrsWEeaQLEmEAMLEDT------GLHHKRNEEAQDLSGGMQRKLSVAIAFV 1077
Cdd:PLN03130 1321 APVLFSG-TVrfnldpfNEH--NDADL----WE--SLE-RAHLKDVirrnslGLDAEVSEAGENFSVGQRQLLSLARALL 1390
|
170
....*....|....*.
gi 6671495 1078 GDSKVVVLDEPTSGVD 1093
Cdd:PLN03130 1391 RRSKILVLDEATAAVD 1406
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1937-2101 |
1.17e-07 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 55.38 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1937 LKLNELTKVYsGSSSPAVDrLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTSIS-DVHQNMGY 2015
Cdd:PRK10253 8 LRGEQLTLGY-GKYTVAEN-LTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASkEVARRIGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2016 CPQFDAIDDLLTGRE--------HLYLYARLRgvpsKEIEKVANWGIQSLGLSLYADRLAGTYSGGNKRKLSTAIALTGC 2087
Cdd:PRK10253 86 LAQNATTPGDITVQElvargrypHQPLFTRWR----KEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQE 161
|
170
....*....|....
gi 6671495 2088 PPLLLLDEPTTGMD 2101
Cdd:PRK10253 162 TAIMLLDEPTTWLD 175
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1948-2127 |
1.23e-07 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 57.10 E-value: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1948 GSSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-SISDVHQNMGYCPQfDAIddLL 2026
Cdd:COG1132 350 PGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDlTLESLRRQIGVVPQ-DTF--LF 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2027 TG--REHLyLYARLrGVPSKEIEKVA------NWgIQSL-----------GLSLyadrlagtySGGNKRKLSTAIALTGC 2087
Cdd:COG1132 427 SGtiRENI-RYGRP-DATDEEVEEAAkaaqahEF-IEALpdgydtvvgerGVNL---------SGGQRQRIAIARALLKD 494
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 6671495 2088 PPLLLLDEPTTGMDPQARRMLWNTIVSiIREGRAVVLTSH 2127
Cdd:COG1132 495 PPILILDEATSALDTETEALIQEALER-LMKGRTTIVIAH 533
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1967-2145 |
1.32e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 55.05 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1967 FGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKsILTSISDVHQnmgycpqfdaIDDLLTGRE------------HLYL 2034
Cdd:PRK14246 39 FGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGK-VLYFGKDIFQ----------IDAIKLRKEvgmvfqqpnpfpHLSI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2035 YARL------RGVPSK-EIEKVANWGIQSLGL-SLYADRL---AGTYSGGNKRKLSTAIALTGCPPLLLLDEPTTGMDPQ 2103
Cdd:PRK14246 108 YDNIayplksHGIKEKrEIKKIVEECLRKVGLwKEVYDRLnspASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIV 187
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 6671495 2104 ARRMLWNTIVSIIREgRAVVLTSHSMEECEALCTRLAIMVKG 2145
Cdd:PRK14246 188 NSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNG 228
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
943-1140 |
1.43e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 56.56 E-value: 1.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 943 RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPP--TSGTVLIGGK--------DIETNLDVVRQSLGM----- 1007
Cdd:PRK10938 273 RPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPQgySNDLTLFGRRrgsgetiwDIKKHIGYVSSSLHLdyrvs 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1008 CPQHNIL----FHHLTVAEHILFYAQLKGRSWEeAQLEMEAMLEDTGLHhkrneeaqDLSGGMQRKLSVAIAFVGDSKVV 1083
Cdd:PRK10938 353 TSVRNVIlsgfFDSIGIYQAVSDRQQKLAQQWL-DILGIDKRTADAPFH--------SLSWGQQRLALIVRALVKHPTLL 423
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6671495 1084 VLDEPTSGVDPYSR---RSIWDLLLkyRSGRT--IIMSTHHMDEADLLGDRIAIISQGRLYC 1140
Cdd:PRK10938 424 ILDEPLQGLDPLNRqlvRRFVDVLI--SEGETqlLFVSHHAEDAPACITHRLEFVPDGDIYR 483
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1953-2145 |
1.55e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 56.66 E-value: 1.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1953 AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI---------LTSISDVHQNMGYCPQFDAID 2023
Cdd:PRK10982 13 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfksskealENGISMVHQELNLVLQRSVMD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2024 DLLTGR--------EHLYLYarlrgvpsKEIEKVanwgIQSLGLSLYADRLAGTYSGGNKRKLSTAIALTGCPPLLLLDE 2095
Cdd:PRK10982 93 NMWLGRyptkgmfvDQDKMY--------RDTKAI----FDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 6671495 2096 PTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2145
Cdd:PRK10982 161 PTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDG 210
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
952-1130 |
1.77e-07 |
|
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: 54.72 E-value: 1.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 952 TFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGtvliggkDIETNLDVVRQSlgmcPQHNILFHHLTVAEhiLFYAQLK 1031
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEG-------DIEIELDTVSYK----PQYIKADYEGTVRD--LLSSITK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1032 GrSWEEAQLEMEAMlEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTSGVDPYSR----RSIWDLLLKY 1107
Cdd:cd03237 88 D-FYTHPYFKTEIA-KPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRlmasKVIRRFAENN 165
|
170 180
....*....|....*....|...
gi 6671495 1108 RSgrTIIMSTHHMDEADLLGDRI 1130
Cdd:cd03237 166 EK--TAFVVEHDIIMIDYLADRL 186
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
956-1139 |
1.77e-07 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 52.76 E-value: 1.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 956 NQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIggKDIETNLDVVRQSLgmcpqhnilfhhltvaehilfyaqlkgrsw 1035
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIY--IDGEDILEEVLDQL------------------------------ 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1036 eeaqlemeamledtgLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTSGVDPYSRRSIWDLL-------LKYR 1108
Cdd:smart00382 50 ---------------LLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEelrllllLKSE 114
|
170 180 190
....*....|....*....|....*....|.
gi 6671495 1109 SGRTIIMSTHhmDEADLLGDRIAIISQGRLY 1139
Cdd:smart00382 115 KNLTVILTTN--DEKDLGPALLRRRFDRRIV 143
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
1937-2101 |
1.93e-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: 56.67 E-value: 1.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1937 LKLNELTKVYsGSSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-SISDVHQNMGY 2015
Cdd:TIGR01193 474 IVINDVSYSY-GYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDiDRHTLRQFINY 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2016 CPQ----FDA--IDDLLTG-REHLYLYARLRGVPSKEIEKVANWGIQSLGLSLYADrlAGTYSGGNKRKLSTAIALTGCP 2088
Cdd:TIGR01193 553 LPQepyiFSGsiLENLLLGaKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEE--GSSISGGQKQRIALARALLTDS 630
|
170
....*....|...
gi 6671495 2089 PLLLLDEPTTGMD 2101
Cdd:TIGR01193 631 KVLILDESTSNLD 643
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
963-1094 |
1.97e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 54.08 E-value: 1.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 963 GHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIeTNLDVVR--QSLGMCPQhniLFHHLTVAEHILFYAQLKGRsweEAQL 1040
Cdd:PRK13543 44 GDNGAGKTTLLRVLAGLLHVESGQIQIDGKTA-TRGDRSRfmAYLGHLPG---LKADLSTLENLHFLCGLHGR---RAKQ 116
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 6671495 1041 EMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTSGVDP 1094
Cdd:PRK13543 117 MPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
941-1120 |
2.08e-07 |
|
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: 53.87 E-value: 2.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 941 SGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTV-----LIGGKDIETNLDVVRQSLGMCPQHNILF 1015
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnkNESEPSFEATRSRNRYSVAYAAQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1016 HhLTVAEHILFYAQLKGRSW----EEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTSG 1091
Cdd:cd03290 92 N-ATVEENITFGSPFNKQRYkavtDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSA 170
|
170 180 190
....*....|....*....|....*....|..
gi 6671495 1092 VDPY-SRRSIWDLLLKY--RSGRTIIMSTHHM 1120
Cdd:cd03290 171 LDIHlSDHLMQEGILKFlqDDKRTLVLVTHKL 202
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
949-1120 |
2.23e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 56.58 E-value: 2.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGG----KDIetNLDVVRQSLGMCPQHNILF--------- 1015
Cdd:PTZ00265 404 LNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDshnlKDI--NLKWWRSKIGVVSQDPLLFsnsiknnik 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1016 ---HHLTVAEHILFYAQLKGRSWEEAQ---------------LEMEAMLEDTGLHHKRNEE------------------- 1058
Cdd:PTZ00265 482 yslYSLKDLEALSNYYNEDGNDSQENKnkrnscrakcagdlnDMSNTTDSNELIEMRKNYQtikdsevvdvskkvlihdf 561
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6671495 1059 ---------------AQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHM 1120
Cdd:PTZ00265 562 vsalpdkyetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTInnLKGNENRITIIIAHRL 640
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1946-2112 |
2.28e-07 |
|
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: 54.04 E-value: 2.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1946 YSGSSSPAVDRLCVGVRPGECFGLLGVNGAGKTTT----FKMLtgdtTVTSGDATVAGKSILT-SISDVHQNMGYCPQfD 2020
Cdd:cd03244 12 YRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLllalFRLV----ELSSGSILIDGVDISKiGLHDLRSRISIIPQ-D 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2021 AIddLLTG--REHL---------YLYARLRGVPSKEIekvanwgIQSLGLSLYADRLAG--TYSGGNKRKLSTAIALTGC 2087
Cdd:cd03244 87 PV--LFSGtiRSNLdpfgeysdeELWQALERVGLKEF-------VESLPGGLDTVVEEGgeNLSVGQRQLLCLARALLRK 157
|
170 180
....*....|....*....|....*
gi 6671495 2088 PPLLLLDEPTTGMDPQARRMLWNTI 2112
Cdd:cd03244 158 SKILVLDEATASVDPETDALIQKTI 182
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1933-2145 |
2.40e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 55.89 E-value: 2.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1933 KTDILKLNELTKVysgsSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTSISDVHQN 2012
Cdd:PRK10982 247 GEVILEVRNLTSL----RQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAIN 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2013 MGYCpqfdaiddLLTG-REHLYLYARL------------------RGVPSKEIEKVANWGIQSLGLSLYADRLA-GTYSG 2072
Cdd:PRK10982 323 HGFA--------LVTEeRRSTGIYAYLdigfnslisnirnyknkvGLLDNSRMKSDTQWVIDSMRVKTPGHRTQiGSLSG 394
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6671495 2073 GNKRKLSTAIALTGCPPLLLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2145
Cdd:PRK10982 395 GNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNG 467
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1961-2124 |
2.86e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 55.97 E-value: 2.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1961 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKsiltsISdvhqnmgYCPQFDAIDDLLTgrehlyLYARLRG 2040
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELK-----IS-------YKPQYIKPDYDGT------VEDLLRS 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2041 VPSK--------EIekvanwgIQSLGLSLYADRLAGTYSGGNKRKLSTAIALTGCPPLLLLDEPTTGMDPQARRMLWNTI 2112
Cdd:PRK13409 424 ITDDlgssyyksEI-------IKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAI 496
|
170
....*....|..
gi 6671495 2113 VSIIREGRAVVL 2124
Cdd:PRK13409 497 RRIAEEREATAL 508
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1931-2127 |
3.68e-07 |
|
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: 55.33 E-value: 3.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1931 GNKtdILKLNELTKVYSGSssPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVaGKSIltsisdvh 2010
Cdd:TIGR03719 319 GDK--VIEAENLTKAFGDK--LLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV-------- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2011 qNMGYCPQF-DAIDDLLT-------GREHLylyarlrgvpskeieKVANWGIQSLGlslYADR----------LAGTYSG 2072
Cdd:TIGR03719 386 -KLAYVDQSrDALDPNKTvweeisgGLDII---------------KLGKREIPSRA---YVGRfnfkgsdqqkKVGQLSG 446
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 6671495 2073 GNKRKLSTAIALTGCPPLLLLDEPTTGMDPQARRMLWNTIVSIirEGRAVVLtSH 2127
Cdd:TIGR03719 447 GERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNF--AGCAVVI-SH 498
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
891-1119 |
4.41e-07 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 55.20 E-value: 4.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 891 ERALEKTEPLTEEMEDPEHPEGmndsfferelpglvPGVCVKNLvKVFEPSGRPAVDRLNITFYENQ---ITaflGHNGA 967
Cdd:COG4178 339 EEALEAADALPEAASRIETSED--------------GALALEDL-TLRTPDGRPLLEDLSLSLKPGErllIT---GPSGS 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 968 GKTTTLSILTGLLPPTSGTVLiggkdietnldvvrqslgmCPQHnilfhhltvaEHILFYAQ--------LKG------- 1032
Cdd:COG4178 401 GKSTLLRAIAGLWPYGSGRIA-------------------RPAG----------ARVLFLPQrpylplgtLREallypat 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1033 -RSWEEAQLEmeAMLEDTGLHH--KRNEEAQD----LSGGMQRKLSVAIAFVGDSKVVVLDEPTSGVDPYSRRSIWDLLL 1105
Cdd:COG4178 452 aEAFSDAELR--EALEAVGLGHlaERLDEEADwdqvLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLR 529
|
250
....*....|....
gi 6671495 1106 KYRSGRTIIMSTHH 1119
Cdd:COG4178 530 EELPGTTVISVGHR 543
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
943-1137 |
4.79e-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: 52.61 E-value: 4.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 943 RPAVDRLNITFYENqITAFLGHNGAGKTTTLS----ILTGLLPP----------------TSGTVLIGGKDIETNLDVVR 1002
Cdd:cd03240 10 RSFHERSEIEFFSP-LTLIVGQNGAGKTTIIEalkyALTGELPPnskggahdpkliregeVRAQVKLAFENANGKKYTIT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1003 QSLGMCpqHNILFHHltvaehilfyaqlkgrsweeaQLEMEAMLEDtglHHKRneeaqdLSGGMQRKLSVAI------AF 1076
Cdd:cd03240 89 RSLAIL--ENVIFCH---------------------QGESNWPLLD---MRGR------CSGGEKVLASLIIrlalaeTF 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6671495 1077 VGDSKVVVLDEPTSGVDPYSRR-SIWDLLLKYRS--GRTIIMSTHHMDEADLLGDRIAIISQGR 1137
Cdd:cd03240 137 GSNCGILALDEPTTNLDEENIEeSLAEIIEERKSqkNFQLIVITHDEELVDAADHIYRVEKDGR 200
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
946-1138 |
5.04e-07 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 53.54 E-value: 5.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 946 VDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIETnLD-------------VVRQSLGMC-PQH 1011
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAK-LNraqrkafrrdiqmVFQDSISAVnPRK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1012 NI-------LFHHLTVAEhilfyaqlkgrswEEAQLEMEAMLEDTGLhhkRNEEA----QDLSGGMQRKLSVAIAFVGDS 1080
Cdd:PRK10419 107 TVreiirepLRHLLSLDK-------------AERLARASEMLRAVDL---DDSVLdkrpPQLSGGQLQRVCLARALAVEP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1081 KVVVLDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
Cdd:PRK10419 171 KLLILDEAVSNLDLVLQAGVIRLLkkLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
955-1133 |
5.25e-07 |
|
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: 54.79 E-value: 5.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 955 ENQITAFLGHNGAGKTTTLSILTGLL---------PPT--------SGTVLiggKD-----IETNLDVVR--QSLGMCPQ 1010
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELkpnlgdydeEPSwdevlkrfRGTEL---QDyfkklANGEIKVAHkpQYVDLIPK 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1011 hnilFHHLTVAEhILFYAQLKGRSWEEA-QLEMEAMLedtglhhkrNEEAQDLSGG-MQRkLSVAIAFVGDSKVVVLDEP 1088
Cdd:COG1245 175 ----VFKGTVRE-LLEKVDERGKLDELAeKLGLENIL---------DRDISELSGGeLQR-VAIAAALLRDADFYFFDEP 239
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 6671495 1089 TSGVDPYSR----RSIWDLLlkyRSGRTIIMSTHHMDEADLLGDRIAII 1133
Cdd:COG1245 240 SSYLDIYQRlnvaRLIRELA---EEGKYVLVVEHDLAILDYLADYVHIL 285
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1963-2101 |
6.28e-07 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 53.25 E-value: 6.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1963 PGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTSISDVH-QNMGYCPQFDAIDDLLTGREHLYL-----YA 2036
Cdd:PRK10575 36 AGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFaRKVAYLPQQLPAAEGMTVRELVAIgrypwHG 115
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6671495 2037 RLRGVPSKEIEKVANwGIQSLGLSLYADRLAGTYSGGNKRKLSTAIALTGCPPLLLLDEPTTGMD 2101
Cdd:PRK10575 116 ALGRFGAADREKVEE-AISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALD 179
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1934-2127 |
6.31e-07 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 54.73 E-value: 6.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1934 TDILKLNELTKVY-SGSSSPAV-DRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTSISDV-- 2009
Cdd:PRK10535 2 TALLELKDIRRSYpSGEEQVEVlKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADAla 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2010 ---HQNMGYCPQFDAIDDLLTGREHLYLYARLRGVPSKEIEKVANWGIQSLGLSLYADRLAGTYSGGNKRKLSTAIALTG 2086
Cdd:PRK10535 82 qlrREHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMN 161
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 6671495 2087 CPPLLLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSH 2127
Cdd:PRK10535 162 GGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTH 202
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
955-1144 |
7.55e-07 |
|
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: 52.75 E-value: 7.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 955 ENQITAFLGHNGAGKTTTLSILTGLLPPTsgtvlIGGKDIETNLD-VVRQSLGMCPQH---NILFHHLTVAEHI----LF 1026
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLKPN-----LGKFDDPPDWDeILDEFRGSELQNyftKLLEGDVKVIVKPqyvdLI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1027 YAQLKGRSWE--EAQLE---MEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTSGVDPYSR---- 1097
Cdd:cd03236 100 PKAVKGKVGEllKKKDErgkLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRlnaa 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 6671495 1098 RSIWDLLlkyRSGRTIIMSTHHMDEADLLGDRIAIisqgrLYcsGTP 1144
Cdd:cd03236 180 RLIRELA---EDDNYVLVVEHDLAVLDYLSDYIHC-----LY--GEP 216
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1961-2168 |
7.84e-07 |
|
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: 52.54 E-value: 7.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1961 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-SISDVHQNMGYCPQ----FDAiddllTGREHLyLY 2035
Cdd:cd03249 26 IPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDlNLRWLRSQIGLVSQepvlFDG-----TIAENI-RY 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2036 ARLRGVPSKEIE--KVANwgIQSLGLSL---YaDRLAGTY----SGGNKRKLSTAIALTGCPPLLLLDEPTTGMDPQARR 2106
Cdd:cd03249 100 GKPDATDEEVEEaaKKAN--IHDFIMSLpdgY-DTLVGERgsqlSGGQKQRIAIARALLRNPKILLLDEATSALDAESEK 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6671495 2107 MLWNTIVSiIREGRAVVLTSHsmeecealctRLAimvkgtfqclgTIQH--LKYKFGDGYIVTM 2168
Cdd:cd03249 177 LVQEALDR-AMKGRTTIVIAH----------RLS-----------TIRNadLIAVLQNGQVVEQ 218
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1932-2131 |
8.31e-07 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 52.41 E-value: 8.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1932 NKTDILKLNELTkvYSGSSSPAVDRLCVGVRPGEcFGLL-GVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-SISDV 2009
Cdd:PRK10247 3 ENSPLLQLQNVG--YLAGDAKILNNISFSLRAGE-FKLItGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTlKPEIY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2010 HQNMGYCPQFDAI--DdllTGREHLYLYARLRGV---PSKEIEKVANWGIQSLGLSLYADRLagtySGGNKRKLSTAIAL 2084
Cdd:PRK10247 80 RQQVSYCAQTPTLfgD---TVYDNLIFPWQIRNQqpdPAIFLDDLERFALPDTILTKNIAEL----SGGEKQRISLIRNL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 6671495 2085 TGCPPLLLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEE 2131
Cdd:PRK10247 153 QFMPKVLLLDEITSALDESNKHNVNEIIHRYVREqNIAVLWVTHDKDE 200
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
931-1136 |
1.32e-06 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 52.10 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 931 VKNLVK-------VFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIETNLDVVR- 1002
Cdd:PRK15112 7 VRNLSKtfryrtgWFRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRs 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1003 QSLGMCPQ--HNILFHHLTVAEHILFYAQLK-GRSWEEAQLEMEAMLEDTGLhhkRNEEA----QDLSGGMQRKLSVAIA 1075
Cdd:PRK15112 87 QRIRMIFQdpSTSLNPRQRISQILDFPLRLNtDLEPEQREKQIIETLRQVGL---LPDHAsyypHMLAPGQKQRLGLARA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6671495 1076 FVGDSKVVVLDEPTSGVDPYSRRSIWDLLLKY--RSGRTIIMSTHHMDEADLLGDRIAIISQG 1136
Cdd:PRK15112 164 LILRPKVIIADEALASLDMSMRSQLINLMLELqeKQGISYIYVTQHLGMMKHISDQVLVMHQG 226
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
947-1118 |
1.68e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 53.70 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 947 DRLNI------TFYENQITAFLGHNGAGKTTTLSILTGLLPP--TSGTVLIGG--KDIETnldVVRQSlGMCPQHNILFH 1016
Cdd:PLN03140 891 DRLQLlrevtgAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGgyIEGDIRISGfpKKQET---FARIS-GYCEQNDIHSP 966
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1017 HLTVAEHILFYAQLkgRSWEEAQLEMEAMLEDTGLHHKRNEEAQD----------LSGGMQRKLSVAIAFVGDSKVVVLD 1086
Cdd:PLN03140 967 QVTVRESLIYSAFL--RLPKEVSKEEKMMFVDEVMELVELDNLKDaivglpgvtgLSTEQRKRLTIAVELVANPSIIFMD 1044
|
170 180 190
....*....|....*....|....*....|....*.
gi 6671495 1087 EPTSGVDPysrRSIWDLLLKYR----SGRTIIMSTH 1118
Cdd:PLN03140 1045 EPTSGLDA---RAAAIVMRTVRntvdTGRTVVCTIH 1077
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1961-2104 |
1.68e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 53.25 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1961 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKsilTSISDVHQNMgycPQFD--AIDDLLTG-REHLYLYAR 2037
Cdd:PRK10636 24 INPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGN---WQLAWVNQET---PALPqpALEYVIDGdREYRQLEAQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2038 LRGVPSK-----------EIEKVANWGIQSLGLSLYA---------DRLAGTYSGGNKRKLSTAIALTGCPPLLLLDEPT 2097
Cdd:PRK10636 98 LHDANERndghaiatihgKLDAIDAWTIRSRAASLLHglgfsneqlERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPT 177
|
....*..
gi 6671495 2098 TGMDPQA 2104
Cdd:PRK10636 178 NHLDLDA 184
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1932-2124 |
2.75e-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: 52.48 E-value: 2.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1932 NKTDILKLNELTKVYSGSSspavdrLCVG---VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKsiltsISd 2008
Cdd:COG1245 337 EEETLVEYPDLTKSYGGFS------LEVEggeIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLK-----IS- 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2009 vhqnmgYCPQFDAIDDLLTGREHLYlYARLRGVPSK----EIekvanwgIQSLGLS-LYaDRLAGTYSGGNKRKLSTAIA 2083
Cdd:COG1245 405 ------YKPQYISPDYDGTVEEFLR-SANTDDFGSSyyktEI-------IKPLGLEkLL-DKNVKDLSGGELQRVAIAAC 469
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 6671495 2084 LTGCPPLLLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVL 2124
Cdd:COG1245 470 LSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAM 510
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1950-2127 |
3.11e-06 |
|
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: 50.69 E-value: 3.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1950 SSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIltsiSDVHQN-----MGYCPQ----FD 2020
Cdd:cd03253 13 GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDI----REVTLDslrraIGVVPQdtvlFN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2021 aiDDLLtgreHLYLYARLrGVPSKEIEKVANWG-IQSLGLSL---YADRLA--GTY-SGGNKRKLSTAIALTGCPPLLLL 2093
Cdd:cd03253 89 --DTIG----YNIRYGRP-DATDEEVIEAAKAAqIHDKIMRFpdgYDTIVGerGLKlSGGEKQRVAIARAILKNPPILLL 161
|
170 180 190
....*....|....*....|....*....|....
gi 6671495 2094 DEPTTGMDPQARRMLWNTIVSIIReGRAVVLTSH 2127
Cdd:cd03253 162 DEATSALDTHTEREIQAALRDVSK-GRTTIVIAH 194
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1954-2145 |
3.66e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 52.24 E-value: 3.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1954 VDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGD-TTVTSGDATVAGK--SILTSISDVHQNMGYCPQ---FDAIDDLLT 2027
Cdd:PRK13549 278 VDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAyPGRWEGEIFIDGKpvKIRNPQQAIAQGIAMVPEdrkRDGIVPVMG 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2028 GREHLYL--YARL--RGVPSKEIE-KVANWGIQSLGLSLYADRLA-GTYSGGNKRKLSTAIALTGCPPLLLLDEPTTGMD 2101
Cdd:PRK13549 358 VGKNITLaaLDRFtgGSRIDDAAElKTILESIQRLKVKTASPELAiARLSGGNQQKAVLAKCLLLNPKILILDEPTRGID 437
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 6671495 2102 PQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2145
Cdd:PRK13549 438 VGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEG 481
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1954-2147 |
4.59e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 51.71 E-value: 4.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1954 VDRLCVGVRPGECFGLLGVNGAGKTTtFKM-LTGDT--TVTSGDATVAGKSIltSISDVHqnmgycpqfDAIDDLLT--- 2027
Cdd:NF040905 276 VDDVSLNVRRGEIVGIAGLMGAGRTE-LAMsVFGRSygRNISGTVFKDGKEV--DVSTVS---------DAIDAGLAyvt 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2028 -GREHLYL-----------YARLRGVPS-------KEIeKVANWGIQSLGL---SLYAdrLAGTYSGGNKRKLSTAIALT 2085
Cdd:NF040905 344 eDRKGYGLnliddikrnitLANLGKVSRrgvidenEEI-KVAEEYRKKMNIktpSVFQ--KVGNLSGGNQQKVVLSKWLF 420
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6671495 2086 GCPPLLLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGTF 2147
Cdd:NF040905 421 TDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMNEGRI 482
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
944-1093 |
7.81e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 51.10 E-value: 7.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 944 PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIggkdiETNLDVVRqsLGMCPQHNI---LFHHLT- 1019
Cdd:PRK11147 17 PLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIY-----EQDLIVAR--LQQDPPRNVegtVYDFVAe 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1020 ----VAEHILFYAQLkgrSWEEAQLEMEAMLEDTG-----LHH-----------------KRNEEAQ--DLSGGMQRKLS 1071
Cdd:PRK11147 90 gieeQAEYLKRYHDI---SHLVETDPSEKNLNELAklqeqLDHhnlwqlenrinevlaqlGLDPDAAlsSLSGGWLRKAA 166
|
170 180
....*....|....*....|..
gi 6671495 1072 VAIAFVGDSKVVVLDEPTSGVD 1093
Cdd:PRK11147 167 LGRALVSNPDVLLLDEPTNHLD 188
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
931-1131 |
7.85e-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: 51.09 E-value: 7.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 931 VKNLVKVFEpsGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGgkdiET-NLDVVRQSL-GMC 1008
Cdd:TIGR03719 325 AENLTKAFG--DKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIG----ETvKLAYVDQSRdALD 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1009 PQHnilfhhlTVAEHI---LFYAQLKGRsweeaqlEMEAMLEDTGLHHKRNEEAQ---DLSGGMQRKLSVAIAFVGDSKV 1082
Cdd:TIGR03719 399 PNK-------TVWEEIsggLDIIKLGKR-------EIPSRAYVGRFNFKGSDQQKkvgQLSGGERNRVHLAKTLKSGGNV 464
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 6671495 1083 VVLDEPTSGVDPYSRRSIWDLLLKYrSGRTIIMStHhmDEADLlgDRIA 1131
Cdd:TIGR03719 465 LLLDEPTNDLDVETLRALEEALLNF-AGCAVVIS-H--DRWFL--DRIA 507
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1937-2160 |
9.17e-06 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 50.96 E-value: 9.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1937 LKLNELTKVYSGSSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGdttvTSGDATVAGKSILtsisdvhqNMGYC 2016
Cdd:TIGR03269 1 IEVKNLTKKFDGKE--VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRG----MDQYEPTSGRIIY--------HVALC 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2017 PQ---------------------------FDAIDDLLTGR----------EHLYLYARLR------------GVPSKEIE 2047
Cdd:TIGR03269 67 EKcgyverpskvgepcpvcggtlepeevdFWNLSDKLRRRirkriaimlqRTFALYGDDTvldnvlealeeiGYEGKEAV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2048 KVANWGIQSLGLSLYADRLAGTYSGGNKRKLSTAIALTGCPPLLLLDEPTTGMDPQARRMLWNTIVS-IIREGRAVVLTS 2126
Cdd:TIGR03269 147 GRAVDLIEMVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEaVKASGISMVLTS 226
|
250 260 270
....*....|....*....|....*....|....
gi 6671495 2127 HSMEECEALCTRLAIMVKGTFQCLGTIQHLKYKF 2160
Cdd:TIGR03269 227 HWPEVIEDLSDKAIWLENGEIKEEGTPDEVVAVF 260
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1964-2127 |
9.67e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 50.74 E-value: 9.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1964 GECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIltSISDVHQnmgYCPQFDAI--DdlltgrehLYLYARLRGV 2041
Cdd:PRK10522 349 GELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPV--TAEQPED---YRKLFSAVftD--------FHLFDQLLGP 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2042 PSKEIEK--VANWgIQSLG----LSLYADRLAGT-YSGGNKRKLSTAIALTGCPPLLLLDEPTTGMDPQARRMLWNTIVS 2114
Cdd:PRK10522 416 EGKPANPalVEKW-LERLKmahkLELEDGRISNLkLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQVLLP 494
|
170
....*....|....
gi 6671495 2115 IIRE-GRAVVLTSH 2127
Cdd:PRK10522 495 LLQEmGKTIFAISH 508
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
2064-2128 |
1.04e-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: 48.09 E-value: 1.04e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6671495 2064 DRLAGTYSGGNKR--KLSTAIALTGCPPLLLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHS 2128
Cdd:cd03238 82 GQKLSTLSGGELQrvKLASELFSEPPGTLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHN 148
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1961-2145 |
1.05e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 49.14 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1961 VRPGECFGLLGVNGAGKTTTFKMLTGDTTV-----TSGDATVAGKSILT-SISDVHQNMGYCPQFDAIDDLLTGREHLYL 2034
Cdd:PRK14247 26 IPDNTITALMGPSGSGKSTLLRVFNRLIELypearVSGEVYLDGQDIFKmDVIELRRRVQMVFQIPNPIPNLSIFENVAL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2035 YARL-RGVPSK-EIEKVANWGIQSLGL-SLYADRL---AGTYSGGNKRKLSTAIALTGCPPLLLLDEPTTGMDPQARRML 2108
Cdd:PRK14247 106 GLKLnRLVKSKkELQERVRWALEKAQLwDEVKDRLdapAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKI 185
|
170 180 190
....*....|....*....|....*....|....*..
gi 6671495 2109 WNTIVSIIREgRAVVLTSHSMEECEALCTRLAIMVKG 2145
Cdd:PRK14247 186 ESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKG 221
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
954-1130 |
1.13e-05 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 50.55 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 954 YENQITAFLGHNGAGKTTTLSILTGLLPPTSGtvliggkDIETNLDVVRQslgmcPQHNILFHHLTVAEhiLFYAQLKGR 1033
Cdd:COG1245 364 REGEVLGIVGPNGIGKTTFAKILAGVLKPDEG-------EVDEDLKISYK-----PQYISPDYDGTVEE--FLRSANTDD 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1034 ---SWEEAQLemeamLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTSGVDPYSRRSIWDLLLKY--R 1108
Cdd:COG1245 430 fgsSYYKTEI-----IKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFaeN 504
|
170 180
....*....|....*....|..
gi 6671495 1109 SGRTIIMSTHHMDEADLLGDRI 1130
Cdd:COG1245 505 RGKTAMVVDHDIYLIDYISDRL 526
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1961-2145 |
1.84e-05 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 48.91 E-value: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1961 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-----------SISDVHQNM--GYCPQFDAIDDLLT 2027
Cdd:PRK10419 35 LKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKlnraqrkafrrDIQMVFQDSisAVNPRKTVREIIRE 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2028 GREHLY-LYARLRGVPSKEIekvanwgIQSLGLSL-YADRLAGTYSGGNKRKLSTAIALTGCPPLLLLDEPTTGMDpqar 2105
Cdd:PRK10419 115 PLRHLLsLDKAERLARASEM-------LRAVDLDDsVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLD---- 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 6671495 2106 RMLWNTIVSIIRE-----GRAVVLTSHSMEECEALCTRLAIMVKG 2145
Cdd:PRK10419 184 LVLQAGVIRLLKKlqqqfGTACLFITHDLRLVERFCQRVMVMDNG 228
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
960-1093 |
2.11e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 49.19 E-value: 2.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 960 AFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIETNLDVVRQSLGMCPQhnilfhhltvaehILF---YAQLKGRSWE 1036
Cdd:PRK11308 45 AVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLLRQKIQ-------------IVFqnpYGSLNPRKKV 111
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6671495 1037 EAQLE-----------------MEAMLEDTGLhhkRNEEAQD----LSGGMQRKLSVAIAFVGDSKVVVLDEPTSGVD 1093
Cdd:PRK11308 112 GQILEepllintslsaaerrekALAMMAKVGL---RPEHYDRyphmFSGGQRQRIAIARALMLDPDVVVADEPVSALD 186
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1963-2101 |
2.38e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 49.35 E-value: 2.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1963 PGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVaGKSIltsisdvhqNMGYCPQF-DAIDDLLT-------GREHLYL 2034
Cdd:PRK11819 349 PGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV---------KLAYVDQSrDALDPNKTvweeisgGLDIIKV 418
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6671495 2035 YArlRGVPSKEiekvanwgiqslglslYADR----------LAGTYSGGNKRKLSTAIALTGCPPLLLLDEPTTGMD 2101
Cdd:PRK11819 419 GN--REIPSRA----------------YVGRfnfkggdqqkKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLD 477
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
922-1164 |
2.65e-05 |
|
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: 48.37 E-value: 2.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 922 LPGLVPGVCVKNLVKVFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDI-ETNLDV 1000
Cdd:cd03288 13 LVGLGGEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDIsKLPLHT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1001 VRQSLGMCPQHNILFhhltvAEHILFYAQLK-----GRSWEE---AQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSV 1072
Cdd:cd03288 93 LRSRLSIILQDPILF-----SGSIRFNLDPEckctdDRLWEAleiAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1073 AIAFVGDSKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEAdLLGDRIAIISQGRLYCSGTP--LFLKNc 1150
Cdd:cd03288 168 ARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTI-LDADLVLVLSRGILVECDTPenLLAQE- 245
|
250
....*....|....
gi 6671495 1151 fgTGFYLTLVRKMK 1164
Cdd:cd03288 246 --DGVFASLVRTDK 257
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
984-1120 |
3.04e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 49.64 E-value: 3.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 984 SGTVLIGGKDI-ETNLDVVRQSLGMCPQHNILFHhLTVAEHILFyaqlkGRswEEAQLE----------MEAMLEDTGLH 1052
Cdd:PTZ00265 1276 SGKILLDGVDIcDYNLKDLRNLFSIVSQEPMLFN-MSIYENIKF-----GK--EDATREdvkrackfaaIDEFIESLPNK 1347
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6671495 1053 HKRN--EEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHM 1120
Cdd:PTZ00265 1348 YDTNvgPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIvdIKDKADKTIITIAHRI 1419
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1929-2133 |
3.22e-05 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 49.52 E-value: 3.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1929 SGGNKTdilkLNELTKVYSGSSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTgDTTVTSGDATVAGKSILT-SIS 2007
Cdd:TIGR01271 1214 SGGQMD----VQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALL-RLLSTEGEIQIDGVSWNSvTLQ 1288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2008 DVHQNMGYCPQFDAIddlLTG--REHLYLYARLRgvpSKEIEKVAN-WGIQSLgLSLYADRLA-----GTY--SGGNKRK 2077
Cdd:TIGR01271 1289 TWRKAFGVIPQKVFI---FSGtfRKNLDPYEQWS---DEEIWKVAEeVGLKSV-IEQFPDKLDfvlvdGGYvlSNGHKQL 1361
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 6671495 2078 LSTAIALTGCPPLLLLDEPTTGMDPQARRMLWNTIVSIIREGrAVVLTSHSME---ECE 2133
Cdd:TIGR01271 1362 MCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNC-TVILSEHRVEallECQ 1419
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
943-1093 |
4.20e-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: 49.17 E-value: 4.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 943 RPAVD----RLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDI-ETNLDVVRQSLGMCPQHNILFHH 1017
Cdd:TIGR00957 1295 REDLDlvlrHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIaKIGLHDLRFKITIIPQDPVLFSG 1374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1018 lTVAEHILFYAQLkgrSWEEAQLEME-AMLED------TGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTS 1090
Cdd:TIGR00957 1375 -SLRMNLDPFSQY---SDEEVWWALElAHLKTfvsalpDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATA 1450
|
...
gi 6671495 1091 GVD 1093
Cdd:TIGR00957 1451 AVD 1453
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
925-1118 |
4.43e-05 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 48.59 E-value: 4.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 925 LVPGVC----VKNLVKvFE------PSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLiggKDI 994
Cdd:TIGR00954 438 LVPGRGiveyQDNGIK-FEniplvtPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLT---KPA 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 995 ETNLDVVRQ----SLGmcpqhnilfhhlTVAEHILF---YAQLKGRSWEEAQLEmeAMLEDTGLHH--KRN---EEAQD- 1061
Cdd:TIGR00954 514 KGKLFYVPQrpymTLG------------TLRDQIIYpdsSEDMKRRGLSDKDLE--QILDNVQLTHilEREggwSAVQDw 579
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1062 ---LSGGMQRKLSVAIAFVGDSKVVVLDEPTSGVDPYSRRSIWDLLLKYrsGRTIIMSTH 1118
Cdd:TIGR00954 580 mdvLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREF--GITLFSVSH 637
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
957-1093 |
7.06e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 48.57 E-value: 7.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 957 QITAFLGHNGAGKTTTLSILT----GLLPPTSGTVLIGGKDIEtnlDVVRQSLG---MCPQHNILFHHLTVAEHILFYAQ 1029
Cdd:TIGR00956 88 ELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGITPE---EIKKHYRGdvvYNAETDVHFPHLTVGETLDFAAR 164
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6671495 1030 LK-------GRSWEE-AQLEMEAMLEDTGLHHKRNEEAQD-----LSGGMQRKLSVAIAFVGDSKVVVLDEPTSGVD 1093
Cdd:TIGR00956 165 CKtpqnrpdGVSREEyAKHIADVYMATYGLSHTRNTKVGNdfvrgVSGGERKRVSIAEASLGGAKIQCWDNATRGLD 241
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
1062-1118 |
7.28e-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: 45.43 E-value: 7.28e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6671495 1062 LSGGMQRKLSVAIAF----VGDSKVVVLDEPTSGVDPYSRRSIWDLLLKYR-SGRTIIMSTH 1118
Cdd:cd03227 78 LSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLvKGAQVIVITH 139
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
931-1143 |
9.72e-05 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 47.10 E-value: 9.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 931 VKNLVKVFEPSGRP--AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGL---------------------LPPTSGTV 987
Cdd:PRK15093 6 IRNLTIEFKTSDGWvkAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVtkdnwrvtadrmrfddidllrLSPRERRK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 988 LIGgkdieTNLDVVRQSLGMC--PQHNIlFHHLTVAEHILFYaqlKGRSWEEAQLEMEAMLEDtgLHHKRNEEAQD---- 1061
Cdd:PRK15093 86 LVG-----HNVSMIFQEPQSCldPSERV-GRQLMQNIPGWTY---KGRWWQRFGWRKRRAIEL--LHRVGIKDHKDamrs 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1062 ----LSGGMQRKLSVAIAFVGDSKVVVLDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIisq 1135
Cdd:PRK15093 155 fpyeLTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLtrLNQNNNTTILLISHDLQMLSQWADKINV--- 231
|
....*...
gi 6671495 1136 grLYCSGT 1143
Cdd:PRK15093 232 --LYCGQT 237
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
1961-2164 |
1.08e-04 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 47.41 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1961 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAG--------KSILTSISDVHQ-----------NMGYCPQFDA 2021
Cdd:TIGR00958 504 LHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGvplvqydhHYLHRQVALVGQepvlfsgsvreNIAYGLTDTP 583
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2022 IDDLLTGREHLYLYARLRGVPSKEIEKVANWGIQslglslyadrlagtYSGGNKRKLSTAIALTGCPPLLLLDEPTTGMD 2101
Cdd:TIGR00958 584 DEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQ--------------LSGGQKQRIAIARALVRKPRVLILDEATSALD 649
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6671495 2102 PQARRMLWNtivSIIREGRAVVLTSHSMEECEAlCTRLAIMVKGTFQCLGTIQHLkYKFGDGY 2164
Cdd:TIGR00958 650 AECEQLLQE---SRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQL-MEDQGCY 707
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1969-2104 |
1.23e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.55 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1969 LLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTSISDVHqnmgycpqFDAIDdlLTGREHLYLYARLRGVPSKEIEK 2048
Cdd:PLN03073 540 MVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMAVFSQHH--------VDGLD--LSSNPLLYMMRCFPGVPEQKLRA 609
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 6671495 2049 -VANWGIQ-SLGL-SLYadrlagTYSGGNKRKLSTAIALTGCPPLLLLDEPTTGMDPQA 2104
Cdd:PLN03073 610 hLGSFGVTgNLALqPMY------TLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDA 662
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2071-2131 |
1.40e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 46.18 E-value: 1.40e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6671495 2071 SGGNKRKLSTAIALTGCPPLLLLDEPTTGMDPQARRMLWNTIVSI-IREGRAVVLTSHSMEE 2131
Cdd:PRK14258 152 SGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLrLRSELTMVIVSHNLHQ 213
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
2071-2130 |
1.49e-04 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 46.23 E-value: 1.49e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6671495 2071 SGGNKRKLSTAIALTGCPP---LLLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSME 2130
Cdd:pfam13304 238 SDGTKRLLALLAALLSALPkggLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTHSPL 300
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
2071-2127 |
2.03e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 43.89 E-value: 2.03e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6671495 2071 SGGNKRKLSTAIALTGCP----PLLLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSH 2127
Cdd:cd03227 79 SGGEKELSALALILALASlkprPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITH 139
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
931-990 |
2.42e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 46.27 E-value: 2.42e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 931 VKNLVKVFEpsGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIG 990
Cdd:PRK11819 327 AENLSKSFG--DRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIG 384
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
931-1118 |
2.88e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 46.04 E-value: 2.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 931 VKNLVKVFEpsGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVliggKDIETNldvvrqSLGMCPQ 1010
Cdd:PRK15064 322 VENLTKGFD--NGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV----KWSENA------NIGYYAQ 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1011 -HNILFHH-LTVAEHILFYAQLKgrsweEAQLEMEAML-------EDTglhhkrNEEAQDLSGGMQRKLSVAIAFVGDSK 1081
Cdd:PRK15064 390 dHAYDFENdLTLFDWMSQWRQEG-----DDEQAVRGTLgrllfsqDDI------KKSVKVLSGGEKGRMLFGKLMMQKPN 458
|
170 180 190
....*....|....*....|....*....|....*..
gi 6671495 1082 VVVLDEPTSGVDPYSRRSIWDLLLKYRSgrTIIMSTH 1118
Cdd:PRK15064 459 VLVMDEPTNHMDMESIESLNMALEKYEG--TLIFVSH 493
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
950-1122 |
3.11e-04 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 46.04 E-value: 3.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 950 NITFY--ENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVliggkDIETNLDVVRQSLGMCPQhnilfhhLTVAEHILFY 1027
Cdd:PRK13545 42 NISFEvpEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV-----DIKGSAALIAISSGLNGQ-------LTGIENIELK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1028 AQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTSGVDPYSRRSIWDLLLKY 1107
Cdd:PRK13545 110 GLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNEF 189
|
170
....*....|....*.
gi 6671495 1108 R-SGRTIIMSTHHMDE 1122
Cdd:PRK13545 190 KeQGKTIFFISHSLSQ 205
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1937-2145 |
3.35e-04 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 44.33 E-value: 3.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1937 LKLNELTKVYSGSSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-SISDVHQNMGY 2015
Cdd:cd03369 7 IEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTiPLEDLRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2016 CPQfDAIddLLTG--REHLYLYARLrgvpsKEIEKVANWGIQSLGLSLyadrlagtySGGNKRKLSTAIALTGCPPLLLL 2093
Cdd:cd03369 87 IPQ-DPT--LFSGtiRSNLDPFDEY-----SDEEIYGALRVSEGGLNL---------SQGQRQLLCLARALLKRPRVLVL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 6671495 2094 DEPTTGMDPQARRMlwntIVSIIRE---GRAVVLTSHSMEECeALCTRLAIMVKG 2145
Cdd:cd03369 150 DEATASIDYATDAL----IQKTIREeftNSTILTIAHRLRTI-IDYDKILVMDAG 199
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1953-2159 |
5.18e-04 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 44.72 E-value: 5.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1953 AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTG---DTTVTSGDATVAGKSILT------------SISDVHQN-MGYC 2016
Cdd:PRK09473 31 AVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGllaANGRIGGSATFNGREILNlpekelnklraeQISMIFQDpMTSL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2017 PQFDAIDDLLTgrEHLYLYAR-------------LRGVPSKEIEKvanwgiqslGLSLYADRlagtYSGGNKRKLSTAIA 2083
Cdd:PRK09473 111 NPYMRVGEQLM--EVLMLHKGmskaeafeesvrmLDAVKMPEARK---------RMKMYPHE----FSGGMRQRVMIAMA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2084 LTGCPPLLLLDEPTTGMDP--QARRM-LWNtivSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGTFQCLGTIQHLKYK 2159
Cdd:PRK09473 176 LLCRPKLLIADEPTTALDVtvQAQIMtLLN---ELKREfNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQ 252
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
962-1120 |
5.19e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 45.16 E-value: 5.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 962 LGHNGAGKTTTLSILTGLLPPTSGTVLIgGKDIEtnldvvrqsLGMCPQHNILFhhLTVAEHILFY-AQLkgrsweeAQL 1040
Cdd:PRK10636 344 LGRNGAGKSTLIKLLAGELAPVSGEIGL-AKGIK---------LGYFAQHQLEF--LRADESPLQHlARL-------APQ 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1041 EMEAMLEDT----GLH-HKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIM 1115
Cdd:PRK10636 405 ELEQKLRDYlggfGFQgDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGALVVVS 484
|
....*
gi 6671495 1116 STHHM 1120
Cdd:PRK10636 485 HDRHL 489
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1964-2105 |
5.70e-04 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 44.64 E-value: 5.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1964 GECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI------LTSISDVHQNMGYCPQFDAIDDLLTGrehlylyAR 2037
Cdd:PRK11000 29 GEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMndvppaERGVGMVFQSYALYPHLSVAENMSFG-------LK 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6671495 2038 LRGVPSKEIEKVANWGIQSLGLSLYADRLAGTYSGGNKRKLSTAIALTGCPPLLLLDEPTTGMDPQAR 2105
Cdd:PRK11000 102 LAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALR 169
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1937-2156 |
8.46e-04 |
|
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: 43.69 E-value: 8.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1937 LKLNELTKVYSGSSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTF----KMLTgdttvTSGDATVAGKSILT-SISDVHQ 2011
Cdd:cd03289 3 MTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLsaflRLLN-----TEGDIQIDGVSWNSvPLQKWRK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2012 NMGYCPQFDAIddlLTG--REHLYLYARLRgvpSKEIEKVAnwgiQSLGLSLYADRLAG-----------TYSGGNKRKL 2078
Cdd:cd03289 78 AFGVIPQKVFI---FSGtfRKNLDPYGKWS---DEEIWKVA----EEVGLKSVIEQFPGqldfvlvdggcVLSHGHKQLM 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2079 STAIALTGCPPLLLLDEPTTGMDPQARRMLWNTIVSIIrEGRAVVLTSHSMeecEAL--CTRLAIMVKGTFQCLGTIQHL 2156
Cdd:cd03289 148 CLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQAF-ADCTVILSEHRI---EAMleCQRFLVIEENKVRQYDSIQKL 223
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
1971-2127 |
9.14e-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: 42.98 E-value: 9.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1971 GVNGAGKTTTF---KM-LTGDTTVTS----GDATVAGK-SILTSIS-----------------DVHQNMGYCPQFDaIDD 2024
Cdd:cd03240 29 GQNGAGKTTIIealKYaLTGELPPNSkggaHDPKLIREgEVRAQVKlafenangkkytitrslAILENVIFCHQGE-SNW 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2025 LLTgrehlylyarlrgvpskeiekvanwgiqslglslyadRLAGTYSGGNKRKLSTAIAL-------TGCpPLLLLDEPT 2097
Cdd:cd03240 108 PLL-------------------------------------DMRGRCSGGEKVLASLIIRLalaetfgSNC-GILALDEPT 149
|
170 180 190
....*....|....*....|....*....|....*
gi 6671495 2098 TGMDPQARRmlwNTIVSIIRE-----GRAVVLTSH 2127
Cdd:cd03240 150 TNLDEENIE---ESLAEIIEErksqkNFQLIVITH 181
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1946-2131 |
9.61e-04 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 43.60 E-value: 9.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1946 YSGSSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI----LTSISDVHQNMGYCPQFDA 2021
Cdd:PRK11831 15 FTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamsRSRLYTVRKRMSMLFQSGA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2022 IDDLLTG--------REHLYLyarlrgvPSKEIEKVANWGIQSLGLSLYADRLAGTYSGGNKRK--LSTAIALTgcPPLL 2091
Cdd:PRK11831 95 LFTDMNVfdnvayplREHTQL-------PAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRaaLARAIALE--PDLI 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 6671495 2092 LLDEPTTGMDPqarrMLWNTIVSIIRE-----GRAVVLTSHSMEE 2131
Cdd:PRK11831 166 MFDEPFVGQDP----ITMGVLVKLISElnsalGVTCVVVSHDVPE 206
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1057-1138 |
1.01e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 44.01 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1057 EEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTSGVD---PYSRRSIWDLLLKyrSGRTIIMSTHHMDEadLLG--DRIA 1131
Cdd:NF040905 400 QKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDvgaKYEIYTIINELAA--EGKGVIVISSELPE--LLGmcDRIY 475
|
....*..
gi 6671495 1132 IISQGRL 1138
Cdd:NF040905 476 VMNEGRI 482
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1961-2101 |
1.24e-03 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 44.33 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1961 VRPGECFGLLGVNGAGKTTTFKMLTGDTtvtsgDATVAGKSILTSISDVHQN---------MGYCPQFDAIDDLLTGREH 2031
Cdd:TIGR00956 84 IKPGELTVVLGRPGSGCSTLLKTIASNT-----DGFHIGVEGVITYDGITPEeikkhyrgdVVYNAETDVHFPHLTVGET 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2032 LYLYARLRGVP------SKE--IEKVANWGIQSLGLSLYADRLAGT-----YSGGNKRKLSTAIALTGCPPLLLLDEPTT 2098
Cdd:TIGR00956 159 LDFAARCKTPQnrpdgvSREeyAKHIADVYMATYGLSHTRNTKVGNdfvrgVSGGERKRVSIAEASLGGAKIQCWDNATR 238
|
...
gi 6671495 2099 GMD 2101
Cdd:TIGR00956 239 GLD 241
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1937-2101 |
1.88e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 43.34 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 1937 LKLNELTKVYSGSssPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSiltsisdvhqNMGYC 2016
Cdd:PRK15064 320 LEVENLTKGFDNG--PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENA----------NIGYY 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671495 2017 PQfDAIDDL---LTGREHLYLYAR-------LRGVpskeiekvanwgiqsLGLSLY----ADRLAGTYSGGNKRKLSTAI 2082
Cdd:PRK15064 388 AQ-DHAYDFendLTLFDWMSQWRQegddeqaVRGT---------------LGRLLFsqddIKKSVKVLSGGEKGRMLFGK 451
|
170
....*....|....*....
gi 6671495 2083 ALTGCPPLLLLDEPTTGMD 2101
Cdd:PRK15064 452 LMMQKPNVLVMDEPTNHMD 470
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
2071-2125 |
2.24e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 43.48 E-value: 2.24e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 6671495 2071 SGGNKRKLSTAIALTGCPPLLLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLT 2125
Cdd:PTZ00265 1360 SGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIIT 1414
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
2088-2130 |
3.21e-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: 42.30 E-value: 3.21e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 6671495 2088 PPLLLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSME 2130
Cdd:COG3593 188 NPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTHSPH 230
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
2057-2127 |
7.43e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 41.54 E-value: 7.43e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6671495 2057 LGLS-LYADRLAGTYSGGNKRK--LSTAI--ALTGCppLLLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSH 2127
Cdd:TIGR00630 475 VGLDyLSLSRAAGTLSGGEAQRirLATQIgsGLTGV--LYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEH 548
|
|
| |
