SEY1_PICGU
ID SEY1_PICGU Reviewed; 850 AA.
AC A5DB26;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 3.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Protein SEY1 {ECO:0000255|HAMAP-Rule:MF_03109};
DE EC=3.6.5.- {ECO:0000255|HAMAP-Rule:MF_03109};
GN Name=SEY1 {ECO:0000255|HAMAP-Rule:MF_03109}; ORFNames=PGUG_00481;
OS Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX NCBI_TaxID=294746;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324;
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA Birren B.W., Kellis M., Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
CC -!- FUNCTION: Cooperates with the reticulon proteins and tubule-shaping DP1
CC family proteins to generate and maintain the structure of the tubular
CC endoplasmic reticulum network. Has GTPase activity, which is required
CC for its function in ER organization. {ECO:0000255|HAMAP-Rule:MF_03109}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000255|HAMAP-Rule:MF_03109}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_03109}. Note=Enriched in the cortical ER.
CC Concentrated in punctae along the ER tubules. {ECO:0000255|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:0000255|PROSITE-ProRule:PRU01052}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EDK36383.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CH408155; EDK36383.2; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_001487104.1; XM_001487054.1.
DR AlphaFoldDB; A5DB26; -.
DR SMR; A5DB26; -.
DR STRING; 4929.XP_001487104.1; -.
DR PRIDE; A5DB26; -.
DR EnsemblFungi; EDK36383; EDK36383; PGUG_00481.
DR GeneID; 5129416; -.
DR KEGG; pgu:PGUG_00481; -.
DR eggNOG; KOG2203; Eukaryota.
DR HOGENOM; CLU_011270_0_0_1; -.
DR InParanoid; A5DB26; -.
DR OrthoDB; 418635at2759; -.
DR Proteomes; UP000001997; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 Gene3D; 3.40.50.300; -; 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 PANTHER; PTHR45923; PTHR45923; 1.
DR Pfam; PF05879; RHD3; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51715; G_GB1_RHD3; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; GTP-binding; Hydrolase; Membrane;
KW Nucleotide-binding; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..850
FT /note="Protein SEY1"
FT /id="PRO_0000384995"
FT TOPO_DOM 1..741
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TRANSMEM 742..762
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TOPO_DOM 763..765
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TRANSMEM 766..786
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TOPO_DOM 787..850
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT DOMAIN 64..297
FT /note="GB1/RHD3-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01052"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 816..850
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 816..841
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 74..81
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
SQ SEQUENCE 850 AA; 96739 MW; 8176141A64E7A092 CRC64;
MSDLPPPDLG SEEISVSPTS SSSSFVPIDK NQLQDAVQVV SEAKEFNSLI LDYVRKATPA
SEVNNNYHIV SVFGSQSTGK STLLNRLFNT NFDVMDESNR SQTTKGIWMA YSSIITTSQG
PVPSKGGENI FVMDVEGTDG RERGEDQDFE RKAALFALST SEVLIINVWE HQIGLYQGAN
MGLLKTVFEV NLSLFGRTKL EMNEHKVLLL FVIRDHIGTT SKESLAATVT QDLIKMWDSL
SKPQELAHLQ FSDFFDIQFH TLRHKILQPG EFTTDVQLLG DRFTDHKNED FLFKKYYHHD
IPIDGWTMYA ENCWDQIDKN KDLDLPTQQI LVAKFKCDEI LTSVFEEFRS KFEERHAKYA
PTDIKEEVDY EELGGSLGDL KEDTLENYDM MASRYNQSVY LQKRKTLEQK ITDVYQDLVD
QHGAHMVSKL SAKFASSLSS KKLPKDVSFA LATEALRKDI VHQFLKNCSC ITLNGSLDHA
KHVTSFTRKL DSILSKQRFV ELNSILAKSL KKVESAVAKA ITQEISEPSE STWDRVLEKF
KGAQDEYFYS KYETATGVDF GLGTSASVNE RALEKFQFRA WSLLHLQMRK LISKDNLVII
LKDRFEDKFR YDENGIPRLY QNSHELELNF TAAKEHALKA LPILTLATLS DGTTIVPKYD
VRDKRLQKKL GAAFDTTGEV DLKDEDVESD TDEEDEDENE PKCFAEAISE TDKASVLSKF
KKETDATFVE SKRALIQHVT HIPYYIYIVI LVLGWNEFMA VLRNPFFFTL LLMLGAGTYV
LYHLNLLKPA MVVVQRMFDE CLVIAKQKLK EFIDEQPQEH AKRLSKMAGI TEDKPEEIEM
SDLTPPGEGS
