SEY1_PARBA
ID SEY1_PARBA Reviewed; 873 AA.
AC C1GWM2;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 04-FEB-2015, sequence version 2.
DT 03-AUG-2022, entry version 62.
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=PAAG_02917;
OS Paracoccidioides lutzii (strain ATCC MYA-826 / Pb01) (Paracoccidioides
OS brasiliensis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX NCBI_TaxID=502779;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-826 / Pb01;
RX PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT "Comparative genomic analysis of human fungal pathogens causing
RT paracoccidioidomycosis.";
RL PLoS Genet. 7:E1002345-E1002345(2011).
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}.
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DR EMBL; KN293997; EEH40941.2; -; Genomic_DNA.
DR RefSeq; XP_002795441.2; XM_002795395.2.
DR AlphaFoldDB; C1GWM2; -.
DR SMR; C1GWM2; -.
DR STRING; 502779.C1GWM2; -.
DR EnsemblFungi; EEH40941; EEH40941; PAAG_02917.
DR GeneID; 9098658; -.
DR KEGG; pbl:PAAG_02917; -.
DR VEuPathDB; FungiDB:PAAG_02917; -.
DR eggNOG; KOG2203; Eukaryota.
DR HOGENOM; CLU_011270_0_0_1; -.
DR OMA; TNFDVMD; -.
DR OrthoDB; 418635at2759; -.
DR Proteomes; UP000002059; Partially assembled 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..873
FT /note="Protein SEY1"
FT /id="PRO_0000384989"
FT TOPO_DOM 1..750
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TRANSMEM 751..771
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TOPO_DOM 772..774
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TRANSMEM 775..795
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TOPO_DOM 796..873
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT DOMAIN 50..308
FT /note="GB1/RHD3-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01052"
FT REGION 677..701
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 841..873
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 60..67
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
SQ SEQUENCE 873 AA; 98729 MW; B05969692CD7793F CRC64;
MVANGHFFAG VGDVLDGKNY EHGVQVVDEE KEFNPNLSNY LTYENVTPAG FNYHLISVFG
SQSTGKSTLL NSLFGTHFSV MSETERRQTT KGIWLSKNKG LKSDKGQDNQ TKMADNILVM
DVEGTDGRER GEDQDFERKS ALFALATSEV LIVNIWEHQV GLYQGANMGL LKTVFEVNLE
LFLKDKRSNP RSLLFFVIRD FLGTTPLQNL QNTLLQDLNR IWNSLSKPAG LENSSITDYF
DFAFAGLPHK NFQPEKFVDE VQKLSTRFCD GHRDPNKTDA KGTGSIEGGI FLPEYHRRIP
ADGFAVYAEG IWDQIVNNKD LDLPTQQELL AQFRCDEISR EVLVAFDEAI SPFEAKQAEA
VQAGNPQVLG GLGSAMRNAR MKSVKNFDTE ASRYHKRVYQ MKKSELQDKI DFRLKALFLG
QLSAAHRSGI QEFTESVTAA VKAGQKRGAS YDFAEIVKKE RKLAIEKFEQ EARATVVEDT
QWSNYQQELS LYQKDLEIIG GQLRRDEMRR LATRVERWVR SRLGESIDLE FNAIGSGRSG
SGAPEFGDKP SEKSLWDRVW TLFIDIVLDA ERRFTERASS FDASIDEVDV GLWRLRRKSW
GVLRAKIDEE MMEGNILLKL RENFEDKFRY DDAGVPRIWR PNDDIESIYT RARESTLTLI
PLLSRFRLSE TNAPPPLDKW IGHTPSSATP ADEEDLTPIG GVDEDEGKSL EEEMTMIGEA
KKQDLTVRFK KTADGVYVEA KRSAIGGITQ VPLYFYGLLL ALGWNEIVAV LRNPAYFLLL
FVCAVTAYVT YQLNLWGPII KMTEAASQQA LMEGKRRLRE FLEASDTGLQ TMAMSEGRNA
EGYDMSNMKN RKSAGGYQNN RSHIDDADDD DDF
