ID   SEY1_ASPFN              Reviewed;         859 AA.
AC   B8NJL4;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 68.
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; ORFNames=AFLA_067350;
OS   Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS   / JCM 12722 / SRRC 167).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=332952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC   167;
RX   PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA   Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA   Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT   "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT   aflatoxin contamination of food and feed.";
RL   Genome Announc. 3:E0016815-E0016815(2015).
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; EQ963479; EED49913.1; -; Genomic_DNA.
DR   RefSeq; XP_002380294.1; XM_002380253.1.
DR   AlphaFoldDB; B8NJL4; -.
DR   SMR; B8NJL4; -.
DR   STRING; 5059.CADAFLAP00008159; -.
DR   PRIDE; B8NJL4; -.
DR   EnsemblFungi; EED49913; EED49913; AFLA_067350.
DR   VEuPathDB; FungiDB:AFLA_067350; -.
DR   eggNOG; KOG2203; Eukaryota.
DR   HOGENOM; CLU_011270_0_0_1; -.
DR   OMA; TNFDVMD; -.
DR   Proteomes; UP000001875; Unassembled WGS sequence.
DR   GO; GO:0032541; C:cortical endoplasmic reticulum; IEA:EnsemblFungi.
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:0048309; P:endoplasmic reticulum inheritance; IEA:EnsemblFungi.
DR   GO; GO:0016320; P:endoplasmic reticulum membrane fusion; IEA:EnsemblFungi.
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; Transmembrane; Transmembrane helix.
FT   CHAIN           1..859
FT                   /note="Protein sey1"
FT                   /id="PRO_0000384970"
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..859
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   DOMAIN          50..299
FT                   /note="GB1/RHD3-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01052"
FT   REGION          817..859
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          442..500
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   BINDING         60..67
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
SQ   SEQUENCE   859 AA;  96554 MW;  C7937AE4C5ECF499 CRC64;
     MATNGHFASI GNSASDTTAY EHGVQVIDEN KEFNPNLSQY LSLENVTPSG FNYHLISVFG
     SQSTGKSTLL NHLFGTHFSV MSELERRQTT KGIWMSKNKN ESSSMASNIL VMDVEGTDGR
     ERGEDQDFER KSALFALATS EVLIVNIWEH QVGLYQGANM GLLKTVFEVN LQLFLKDKNT
     THRSLLFFVI RDYSGMTPLQ NLQKTLMEDM ARLWDSISKP GGLENSNVHD YFDFQFYGLP
     HKGYQPEKFV EETQKLSLRF CDGQRDPNLD ARKGEFSDGG VFLPEYHRRI PADGFSRYAE
     GIWDQIVNNK DLDLPTQQEL LAQFRCDEIL REVMVAFDET IVPFEDKQSQ AARLGEPEIL
     GGLGAAMRSS RTKAVKAFES EASRYHKGVY QRKRAELESK ADTRLKTLFQ GQLNAAHKSG
     ISEFSEAVTA AVKSGQKKGT GYDFAEIVNE EAKKAVDKFE EVARATVVDG TSWSDYKQEL
     ALYEKELAEV SARLRRDEMR RLASRVERWV QSRLGESVGL EFNALGSGRA GGGAPEKGDQ
     PTEKKFWDRV WNVFVETVLD AERRFTDRAS SFDASLEEVD VGLWRLRRKS WGVLRAKIDE
     EMIEGNLLLK LRENFEDKFR YDDAGVPRIW RPTDDIEGIY TRARESTLTL IPLLSKFRLD
     ETSAPPPLDR WIGHTPSSAT SADEEDLAPI GGVDEEEGKS LEEEMTIVSD AKRQELTVRF
     KKAADGVYVE AKRSAIGGMT QVPLYFYGLL LALGWNEIIA VLRNPAYFFL LFVCAVGAYI
     TYQLNLWGPI IKMTEAASNQ AVTEGKKRLR EFLESSDTGR QAIAMSTPGG SGRGGEEHEM
     SRLNQQGKSA AADEDVDDL