ID W1QH87_OGAPD Unreviewed; 756 AA.
AC W1QH87;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Protein SEY1 {ECO:0000313|EMBL:ESW99715.1};
DE EC=3.6.5.- {ECO:0000313|EMBL:ESW99715.1};
GN Name=SEY1 {ECO:0000256|HAMAP-Rule:MF_03109};
GN ORFNames=HPODL_03587 {ECO:0000313|EMBL:ESW99715.1};
OS Ogataea parapolymorpha (strain ATCC 26012 / BCRC 20466 / JCM 22074 / NRRL
OS Y-7560 / DL-1) (Yeast) (Hansenula polymorpha).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Pichiaceae; Ogataea.
OX NCBI_TaxID=871575 {ECO:0000313|EMBL:ESW99715.1, ECO:0000313|Proteomes:UP000008673};
RN [1] {ECO:0000313|EMBL:ESW99715.1, ECO:0000313|Proteomes:UP000008673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 26012 / BCRC 20466 / JCM 22074 / NRRL Y-7560 / DL-1
RC {ECO:0000313|Proteomes:UP000008673};
RX PubMed=24279325; DOI=10.1186/1471-2164-14-837;
RA Ravin N.V., Eldarov M.A., Kadnikov V.V., Beletsky A.V., Schneider J.,
RA Mardanova E.S., Smekalova E.M., Zvereva M.I., Dontsova O.A., Mardanov A.V.,
RA Skryabin K.G.;
RT "Genome sequence and analysis of methylotrophic yeast Hansenula polymorpha
RT DL1.";
RL BMC Genomics 14:837-837(2013).
RN [2] {ECO:0000313|Proteomes:UP000008673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 26012 / BCRC 20466 / JCM 22074 / NRRL Y-7560 / DL-1
RC {ECO:0000313|Proteomes:UP000008673};
RA Ravin N.V., Mardanov A.V., Eldarov M.A., Kadnikov V.V., Beletsky A.V.,
RA Zvereva M.I., Smekalova E.M., Dontsova O.A., Skryabin K.G.;
RT "Genome sequence of the methylotrophic yeast Hansenula polymorpha DL1.";
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|HAMAP-Rule:MF_03109}; Multi-pass membrane protein
CC {ECO:0000256|HAMAP-Rule:MF_03109}. Note=Enriched in the cortical ER.
CC Concentrated in punctae along the ER tubules. {ECO:0000256|HAMAP-
CC Rule:MF_03109}.
CC -!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
CC superfamily. GB1/RHD3 GTPase family. RHD3 subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_03109}.
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:ESW99715.1}.
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DR EMBL; AEOI02000007; ESW99715.1; -; Genomic_DNA.
DR RefSeq; XP_013935387.1; XM_014079912.1.
DR AlphaFoldDB; W1QH87; -.
DR STRING; 871575.W1QH87; -.
DR GeneID; 25773024; -.
DR KEGG; opa:HPODL_03587; -.
DR eggNOG; KOG2203; Eukaryota.
DR HOGENOM; CLU_011270_0_0_1; -.
DR OMA; YAEGVWD; -.
DR OrthoDB; 1606at2759; -.
DR Proteomes; UP000008673; Chromosome IV.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0007029; P:endoplasmic reticulum organization; IEA:UniProtKB-UniRule.
DR CDD; cd01851; GBP; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_03109; Sey1; 1.
DR InterPro; IPR030386; G_GB1_RHD3_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR008803; RHD3/Sey1.
DR InterPro; IPR046758; Sey1/RHD3-like_3HB.
DR PANTHER; PTHR45923; PROTEIN SEY1; 1.
DR PANTHER; PTHR45923:SF2; PROTEIN SEY1; 1.
DR Pfam; PF05879; RHD3_GTPase; 1.
DR Pfam; PF20428; Sey1_3HB; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51715; G_GB1_RHD3; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|HAMAP-Rule:MF_03109};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824, ECO:0000256|HAMAP-
KW Rule:MF_03109}; GTP-binding {ECO:0000256|HAMAP-Rule:MF_03109};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_03109, ECO:0000313|EMBL:ESW99715.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_03109};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03109};
KW Reference proteome {ECO:0000313|Proteomes:UP000008673};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_03109};
KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_03109,
KW ECO:0000256|SAM:Phobius}.
FT TOPO_DOM 1..664
FT /note="Cytoplasmic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03109"
FT TRANSMEM 665..682
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TOPO_DOM 686..688
FT /note="Lumenal"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03109"
FT TRANSMEM 689..708
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TOPO_DOM 710..756
FT /note="Cytoplasmic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03109"
FT DOMAIN 32..262
FT /note="GB1/RHD3-type G"
FT /evidence="ECO:0000259|PROSITE:PS51715"
FT COILED 425..452
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03109"
FT COILED 725..756
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03109"
FT BINDING 42..49
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03109"
SQ SEQUENCE 756 AA; 87734 MW; EB5EDB43ED85831C CRC64;
MSSLQLIDEN KTFNEHLLPY IQRYYDGKDD NGLNYHIVSV FGSQSTGKST LLNRLFGTEF
EVMDEAKRQQ TTKGIWISHA KYIASSKAES GRTENTNHVF VLDVEGVDGR EKADDKDFER
KSALFALSTS EILIVNIWEH QVGLYQGANM ELLKTVFEVN LSLFHSNRQK CLLLFVVRDF
TGVTPLENLE ENLKTDLNKI WDSLSRPENC EGVKITDFFD LGFVSISHKH FQKERFEEDI
RLLGDKFASD SLFKQEYHRN IPIDAWTIYM DQIWQQIELN KDLDLPTQQI LVARFRCDEI
MQQAYDIFEE QYQMVDFGKL EDSQDFADAL KELRSEALAP YDSSASRYNQ SVYLERREQL
IKKIDLRLTE TNSQRLNSVI KKLVSEFSEQ VQIAKKKRDA KFSDILAAQS AAIVTQFRED
ASKCIFDHSR ELEQLKKELS DVSEQLRHKE KNLLLSRLTK KFQTQFKEKL AEITGDPSTD
LWDRVLNEFN QITQSLESKY VSDDQYDYQL GMTEQENKDT HVELLQSFWT KFKDIIHDYV
TEDTVSRILR NKFEDLFRYD DNDVPRVWLN TLEIDQQYNR ARDTVLSLLP VFSKMVLTKT
NEEIVPPVNI STTDSEELDE DDKETTFAEL LSIKQQNGVL SRVKKEMDAI YIEAKRSVMA
NTTSIPFWMY ALVLVLGWNE FMAVLRNPLL FMLIIILATG AYFAHYMGLL RPMLSVAGAT
LTHTKTVAKQ KLRELVEEAE SAKADVKAEV DEAKTK
//
