SEY1_PODAN
ID SEY1_PODAN Reviewed; 852 AA.
AC B2B1M4; A0A090D8K9;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 54.
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}; OrderedLocusNames=Pa_6_3800;
GN ORFNames=PODANS_6_3800;
OS Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383)
OS (Pleurage anserina).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Podosporaceae; Podospora;
OC Podospora anserina.
OX NCBI_TaxID=515849;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383;
RX PubMed=18460219; DOI=10.1186/gb-2008-9-5-r77;
RA Espagne E., Lespinet O., Malagnac F., Da Silva C., Jaillon O., Porcel B.M.,
RA Couloux A., Aury J.-M., Segurens B., Poulain J., Anthouard V.,
RA Grossetete S., Khalili H., Coppin E., Dequard-Chablat M., Picard M.,
RA Contamine V., Arnaise S., Bourdais A., Berteaux-Lecellier V., Gautheret D.,
RA de Vries R.P., Battaglia E., Coutinho P.M., Danchin E.G.J., Henrissat B.,
RA El Khoury R., Sainsard-Chanet A., Boivin A., Pinan-Lucarre B., Sellem C.H.,
RA Debuchy R., Wincker P., Weissenbach J., Silar P.;
RT "The genome sequence of the model ascomycete fungus Podospora anserina.";
RL Genome Biol. 9:R77.1-R77.22(2008).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383;
RX PubMed=24558260; DOI=10.1534/genetics.113.159988;
RA Grognet P., Bidard F., Kuchly C., Tong L.C.H., Coppin E., Benkhali J.A.,
RA Couloux A., Wincker P., Debuchy R., Silar P.;
RT "Maintaining two mating types: Structure of the mating type locus and its
RT role in heterokaryosis in Podospora anserina.";
RL Genetics 197:421-432(2014).
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; CU638744; CAP71009.1; -; Genomic_DNA.
DR EMBL; FO904941; CDP30408.1; -; Genomic_DNA.
DR RefSeq; XP_001909875.1; XM_001909840.1.
DR AlphaFoldDB; B2B1M4; -.
DR SMR; B2B1M4; -.
DR STRING; 5145.XP_001909875.1; -.
DR EnsemblFungi; CAP71009; CAP71009; PODANS_6_3800.
DR GeneID; 6194414; -.
DR KEGG; pan:PODANSg6912; -.
DR VEuPathDB; FungiDB:PODANS_6_3800; -.
DR eggNOG; KOG2203; Eukaryota.
DR HOGENOM; CLU_011270_0_0_1; -.
DR OrthoDB; 418635at2759; -.
DR Proteomes; UP000001197; Chromosome 6.
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 Coiled coil; Endoplasmic reticulum; GTP-binding; Hydrolase; Membrane;
KW Nucleotide-binding; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..852
FT /note="Protein SEY1"
FT /id="PRO_0000384998"
FT TOPO_DOM 1..738
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TRANSMEM 739..759
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TOPO_DOM 760..762
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TRANSMEM 763..783
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TOPO_DOM 784..852
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT DOMAIN 47..294
FT /note="GB1/RHD3-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01052"
FT COILED 475..500
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT BINDING 57..64
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
SQ SEQUENCE 852 AA; 95401 MW; DF1F5A606A61BE59 CRC64;
MNGHFAAIGN GPTAKQYDHG IQVIDEDKSF NTNLNDYLTE THVAESGFNY HLISVFGSQS
TGKSTLLNHL FGTQFSVMSE TERRQTTKGI WLSKNKRDSA NGSPMADNIL VMDVEGTDGR
ERGEDQDFER KSALFALATS EVLIVNIWEH QVGLYQGANM GLLKTVFEVN LQLFLKDRQS
QTRSLLFFVI RDFVGNTPLE NLRTTLITDL SKIWSSISKP QGLEDSKIED YFDFAFSALP
HKIYQPEKFL AEVDRLGARF TTGHRSTKDQ EFGGGVFLPE YHRRIPADGL SVYAGGVWDQ
IVNNKDLDLP TQQELLAQFR CDEIAREVLV GFDTVIAPLE EQQVEAIRLG KPAAVLADLG
AQGAGAREKC IKAFETQASR YHKGVYTMKR GELESKIDTR LKALYQAQLT AAHKAGVAAF
SEAVSGAVKA GQKAGGSYEF AEIVAKQKAK TLQIFKTEAK SLSIPGVAWS NFKPQYKLFE
KELDEVSARL RKEEMRRLAI RVERWVRSRL GDAIGLEFNK LGSGRGGSVS PEGGEKPATE
KDLWDRVWNA FIGIVKEAET RFAERAKSFE ASPEEVEVGL WRLRRKSWVA LREKIEEEVM
ESNILMKLRE NFEDKFRYDE DGVPRIWRPT DDIEGIYTKA RESTLGLVPL LSRFRLSETY
APPDLPAFIG VQPAGVEPED EEDLLPIGGI DEEEGKSLEE ETTVLGESKR QDLVVRFKKM
ADGVYVEAKR SAIGGITQVP LYFYVILLIL GWNEILMVLR NPFLILLILV MGGGTYIAYS
LNLLGPMMQM SNAAFNQAVD IGKDRLRDFL VNNETARQAL AVPARQMGAD ISLDRLDSRG
KKAQDISDDD DI
