ID A0A0K9PLA4_ZOSMR Unreviewed; 1610 AA.
AC A0A0K9PLA4;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=ABC transporter B family member 20 {ECO:0008006|Google:ProtNLM};
GN ORFNames=ZOSMA_205G00190 {ECO:0000313|EMBL:KMZ69843.1};
OS Zostera marina (Eelgrass).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Zosteraceae; Zostera.
OX NCBI_TaxID=29655 {ECO:0000313|EMBL:KMZ69843.1, ECO:0000313|Proteomes:UP000036987};
RN [1] {ECO:0000313|Proteomes:UP000036987}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Finnish {ECO:0000313|Proteomes:UP000036987};
RX PubMed=26814964; DOI=10.1038/nature16548;
RA Olsen J.L., Rouze P., Verhelst B., Lin Y.-C., Bayer T., Collen J.,
RA Dattolo E., De Paoli E., Dittami S., Maumus F., Michel G., Kersting A.,
RA Lauritano C., Lohaus R., Toepel M., Tonon T., Vanneste K., Amirebrahimi M.,
RA Brakel J., Bostroem C., Chovatia M., Grimwood J., Jenkins J.W.,
RA Jueterbock A., Mraz A., Stam W.T., Tice H., Bornberg-Bauer E., Green P.J.,
RA Pearson G.A., Procaccini G., Duarte C.M., Schmutz J., Reusch T.B.H.,
RA Van de Peer Y.;
RT "The genome of the seagrass Zostera marina reveals angiosperm adaptation to
RT the sea.";
RL Nature 530:331-335(2016).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:KMZ69843.1}.
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DR EMBL; LFYR01000744; KMZ69843.1; -; Genomic_DNA.
DR STRING; 29655.A0A0K9PLA4; -.
DR OrthoDB; 5487044at2759; -.
DR Proteomes; UP000036987; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR CDD; cd18578; ABC_6TM_Pgp_ABCB1_D2_like; 1.
DR CDD; cd08771; DLP_1; 1.
DR Gene3D; 1.20.1560.10; ABC transporter type 1, transmembrane domain; 3.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
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; IPR022812; Dynamin.
DR InterPro; IPR001401; Dynamin_GTPase.
DR InterPro; IPR045063; Dynamin_N.
DR InterPro; IPR000375; Dynamin_stalk.
DR InterPro; IPR030381; G_DYNAMIN_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR039421; Type_1_exporter.
DR PANTHER; PTHR43394:SF11; ALPHA-FACTOR-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR43394; ATP-DEPENDENT PERMEASE MDL1, MITOCHONDRIAL; 1.
DR Pfam; PF00664; ABC_membrane; 2.
DR Pfam; PF00005; ABC_tran; 2.
DR Pfam; PF01031; Dynamin_M; 1.
DR Pfam; PF00350; Dynamin_N; 1.
DR PRINTS; PR00195; DYNAMIN.
DR SMART; SM00382; AAA; 2.
DR SMART; SM00053; DYNc; 1.
DR SUPFAM; SSF90123; ABC transporter transmembrane region; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 3.
DR PROSITE; PS50929; ABC_TM1F; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
DR PROSITE; PS51718; G_DYNAMIN_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000036987};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 437..461
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 514..541
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 556..580
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1035..1063
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1083..1105
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1161..1181
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1187..1208
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1257..1284
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1304..1325
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 36..309
FT /note="Dynamin-type G"
FT /evidence="ECO:0000259|PROSITE:PS51718"
FT DOMAIN 413..582
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 615..850
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 1039..1297
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 1361..1598
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 875..922
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 962..1002
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 877..891
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 962..989
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1610 AA; 178148 MW; 453FD002B259A09D CRC64;
MAEEASVSAA SPIGRTVIPI VNKLQDIFSQ LGSSSTIDLP QVAVVGSQSS GKSSVLEALV
GRDFLPRGRD ICTRRPLVLQ LVHTPVRSGD GGDEWGEFLH FPGKKFFDFH AIRSEIQAET
DREAGENKGV SKKQIRLKIF SPNVLNITLV DLPGITRVPV GDQPSDIEAK IRTIILEYIK
HETCIILAVS PANSDLANSD ALQMARVADP DGSRTIGVIT KLDIMDRGTD ARQFLLGNVI
PLRLGYVGIV NRSQEDITFN RSIKDALVHE ESFFRERLVY RGLSDRCGVP QLAMKLNQIL
VQHIKAVLPG LKARISGQLV TVAKEHAAYG EITESKAGQG ALLLNILTKF CEAFSSMVEG
KNEEMSTSEL SGGARIHYIF QSIFVKSLEW SGFGGKWKLL SSIPSYQLTM QRTLVGNYIH
NMATFFSGLV IGFLNCWQIA LLTLGTGPFI VAAGGISNIF LHKLAESIQD AYAEAANIAE
QAISCIRTVY AFSNETLAKY SYAASLQETL RYGILISLVQ GLGLGFTYGL AICSCSLQLW
VGRFLVSKGN ANGGEIIIAL FAIILSGLGL NQAATNFYSF EQGKIATFRL YEMISRSASS
VNQEGNTLVS VIGNIDFRNV YFSYLSRPEI PILSGFYLSV PARKTVALVG RNGSGKSSII
PLMERFYDPT LGEVLLDGEN IKTFKLEWLR NQIGLVTQEP ALLSLSIRDN IAYGRAATPH
QIEEAAKTAH AHSFITSFEH GYDTKVGKAG ISLNEEQKIK LAVARAVLSN PSILLLDEVT
GGLDFEAEKA VQEALDILML GRSTIIIARR LSLIRNADYI AVMDGGKLIQ MGTHDELLST
EGLYAELIRC EEAEKLPKRT PMRNYAGVIP FQIEKDCQNR QDPSSPKMIK SSSLRRGHGF
HDHHPADSNL NSQESQIQST PSEQLMENGM SLHTTESIPP CIKRQHSLEK GLPGLLKIEV
RNGSQSSSND PGPESPISPF LTSDPQNERS HSRTFNRPPE NLDDYLSTKH KYADVLLHHK
SPSFWRLFEL NLAEWLYALL GSTGAAIFGS FNPILAFTIS LVVVEYYAKI DSVMQQNVNR
WCLLIACTGI VTVLANFLQH FYFGIMGEKM TERVRRMMFL AMLRNEVGWF DDEENCAETL
SMRLANDATF VRAAFSNRLS ILIQDTAAVI AALLIGCLLQ WRLALVALAT IPVLIASAFT
QKMWITGFSR RIQNMHRKAS VVLEDAVRNI YTVVAFCSSN KVIELYRIQL DIIFKRSLSY
GITIGFVFGL SRFLLFACNA LILWYTGLSI KEGRFSIRTA MKEYIVFSFV TFALVEPFGL
APYILKRRKS LTAVFDIIDR VPKIDPDDNT GLKPPNLYGS IEFKNVGFYY PSRPEAMILS
NFSLKVNGGQ TVALVGVTGS GKSTIISLIE RFYDPVSGQV FLDGRELSLF NLKWLRNHMG
LIPQEPIIFA TSIRENIIYA RHNATDTEMK EAAIIANANH FISSLPHGYD THVGMRGVDL
TPGQKQRIAI ARVVLKNAPI LLIDESSSSI ESESSRVVQE ALGTLTMGNK TSILIAHRAA
MMKNVDNIVV VNGGQIVEEG GHDKLLQMDG LYAQLMQPHF GTRRRQHRFL
//