ID A0A0V0TE82_9BILA Unreviewed; 2099 AA.
AC A0A0V0TE82;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE SubName: Full=ATP-binding cassette sub-family B member 6, mitochondrial {ECO:0000313|EMBL:KRX37265.1};
GN Name=Abcb6 {ECO:0000313|EMBL:KRX37265.1};
GN ORFNames=T05_5731 {ECO:0000313|EMBL:KRX37265.1};
OS Trichinella murrelli.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=144512 {ECO:0000313|EMBL:KRX37265.1, ECO:0000313|Proteomes:UP000055048};
RN [1] {ECO:0000313|EMBL:KRX37265.1, ECO:0000313|Proteomes:UP000055048}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS417 {ECO:0000313|EMBL:KRX37265.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRX37265.1}.
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DR EMBL; JYDJ01000317; KRX37265.1; -; Genomic_DNA.
DR STRING; 144512.A0A0V0TE82; -.
DR Proteomes; UP000055048; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003682; F:chromatin binding; IEA:InterPro.
DR CDD; cd18581; ABC_6TM_ABCB6; 1.
DR CDD; cd00200; WD40; 1.
DR Gene3D; 1.20.1560.10; ABC transporter type 1, transmembrane domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011527; ABC1_TM_dom.
DR InterPro; IPR036640; ABC1_TM_sf.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR006595; CTLH_C.
DR InterPro; IPR009269; NKAP_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR InterPro; IPR040067; WDR47.
DR PANTHER; PTHR19863; NEMITIN (NEURONAL ENRICHED MAP INTERACTING PROTEIN) HOMOLOG; 1.
DR PANTHER; PTHR19863:SF5; WD REPEAT-CONTAINING PROTEIN 47; 1.
DR Pfam; PF00664; ABC_membrane; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR Pfam; PF06047; Nkap_C; 1.
DR Pfam; PF00400; WD40; 5.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00668; CTLH; 1.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF90123; ABC transporter transmembrane region; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS50929; ABC_TM1F; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
DR PROSITE; PS50897; CTLH; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 5.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000313|EMBL:KRX37265.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000055048};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; WD repeat {ECO:0000256|PROSITE-ProRule:PRU00221}.
FT TRANSMEM 1500..1519
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1624..1646
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1652..1673
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 148..205
FT /note="CTLH"
FT /evidence="ECO:0000259|PROSITE:PS50897"
FT REPEAT 774..804
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 885..925
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 930..971
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 972..1006
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 1018..1049
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT DOMAIN 1507..1799
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 1831..2075
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 78..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 511..580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 625..702
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1138..1250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..95
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..547
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 552..569
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 644..702
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1138..1157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1181..1201
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1202..1236
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2099 AA; 238007 MW; F7AD41577A63EFEC CRC64;
MDVKIAEVDV IKLILEFLEK RHLHIAQQIQ HIGVMKCQGG AAACLLAHAP SLRRVVEEED
SDLSTGPTKQ LHMFEFHSNR KREREGRDTQ NIEEQGEAEN TRASIVGKSK FTLRNLHLSR
LILCDSYVFF SCVRFSLERE SGVINGRYSD DMLFLRQLIL DGQWDTTIDF VEPLKATPGF
DYKRVHYFIY KYKYYELLCI KLEPGPMQNN EFTVNEVVEC LRLLKDVCPS VEEYNKLYAL
LTLSKLGDDE EFRHWNPSSA RMECFQKIHP LVEAFLPVSV EQAESLIASE HDRLVQLVVK
GLLYECGVQY CQKKALEMNK DEVQAEPISV GSLFDSHPLE DVDSSLLAWL TSIPDEMFKM
PFEALALKMH LQRLQRPKLR ACWTQEILAA PIVPEIFPNA AVSHIRLKSA EKMSRSMIPQ
YEGLVHGLEA DQSRLGSRFG SVGLKHRNNA SLSQSMLAGF QISSRPFDEM QRSTLDLLLL
DRGQESQALP VGEPAVVGQA TDGLLKLAKK DPFDQQLPSP IREEDENDSP MPTLNCSNNS
TKQGGRLLSR ISRLESSRRR NDKLSVEQHP HPHQQQQQHP TAYQMMHMSY CAIEKTDKEN
NPATFGSNLP IASAVSTPTI ASVTPITSSC RPTKNGPHRH SLDTGQAELS SDGSSKPSVL
SRSRGSKEIN RSQDIISTST TTGSMGSSSI DGSAKRCSAD TGDLSQGGVN TRFVAVSRLE
DQQAIRCTAF HPSGRFYAVG TNSRQLHICR YPLLKNLKLR DHVAKGPELL LSRPKQHRGS
VYCASFNPTG ELLATGSNDK TIRLMQFNAD SCTVGMHAFV YFVEKIANFP LPGVEHDLNV
HNGTVRDLVF MEDTSNHTSL LISGGAGNCN IQITDCASGT SVRQLQGHTA PVLGMYTWGG
CMFVSCSQDR TIRFWDLRCT KAVNLLSAGN QFYSSPVTSI CVDPSGRLLV SGHEDASVML
YDIHGARLVQ LYRPHVDEVR AVRFSPGTYY LLSGSYDKKV AITDMRGDLM APLKYLPVVE
HQDKVIQCRW HPHDFTFVST SADRSAVLWA LPPPEDETLF EISLQNDKLT PTKIFDRLAQ
FSQCQRESRF FERFLHLSAM KIAQIAAVFR RTAVAVFRCQ RSEFSLSRAN FITRGRLSSS
RSSSCSSRSS SSSRSSSPSY RRRRKRSPKR YYERSWDSGK YRRKSPRRRS RSSSRDRRKK
YRSSSRKDEK KYYSRRSESG SRDSESFRRH GKSRSPNPER YPSPTSSYFK NMYSSRNSTL
LDLSNLSRRI KDRIKIAEEG VPEIWNSSPV VSDLNSYGEE TEIVKDVVVE QETKKKKKKH
RKHKHSDSDE NDVEWIEVTK ETLLNKNENK SKISDEEDVV GPLPSTSDAG GDIAKRVDYG
RNLLPGEGAA MAAYIAEGKR IPRRGEIGLT SEEIQKFEEV GFVMSGTRHR RMEATRLRKE
NQIYSAEEKR MLSMFSKEEQ LFKNNEAKTH DGEKHLGFTV RHMWHKVRFL IPFIWPSENL
YLQFAFVFSF LLLVLGRVVN LFAPIYHKHI VDSLNYNNGT IAFRSDLIII YVLLMFCQGG
SASNGLLNNI RNYFWIGVQQ HSSRQISLRL YEHLHKLSYQ WHMDRKIGEV IEIMDRGVDS
VNQLIIYMVF NIAPVIMDIV IAIIYFCVTF NYIFGLIVLT TMAIYLIATF FITEWRTAFR
REMLKRENEL QAVAVDSLMN FETIKFCNAE KDETNRYGHA FESYQKEECK SLASLIVLSF
GQNVIISIGL LSGSLLCAYF ISVEQFDLTP GDYVLYAAYI LQLYQPLNWM GTYYRLIHQS
FIDMENMFAL FSIAPEAQGS DEILTVNKGK LEFRNVSFGY VPERRILKDI SFIVPPGQTV
AVVGPSGSGK TTLLRLVLRF YDCVQGSILI DDQNIAKFTP SSVRSHIAVV PQDTILFNQT
IKFNIAFAKS NATDEEIFEA AKLAEIHDLI LKLPNGYDSV VGERGLKMSG GEKQRIAIAR
AMIKVPSVMI LDEVTDLSLN FFLATSSLDV ETERLIQASL DKVCKGKTTL IVTHRLSTVV
NANQILVMRN GRIEEFGTHA ELLNKDGLYS NMWKQQMTEW QPSPIADNVI GNEIFRENM
//
