ID   SEY1_CHAGB              Reviewed;         852 AA.
AC   Q2GUT7;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-SEP-2009, sequence version 2.
DT   03-AUG-2022, entry version 56.
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=CHGG_08267;
OS   Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS   NRRL 1970) (Soil fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX   NCBI_TaxID=306901;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970;
RX   PubMed=25720678; DOI=10.1128/genomea.00021-15;
RA   Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT   "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL   Genome Announc. 3:E0002115-E0002115(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; CH408033; EAQ87014.1; -; Genomic_DNA.
DR   RefSeq; XP_001225923.1; XM_001225922.1.
DR   AlphaFoldDB; Q2GUT7; -.
DR   SMR; Q2GUT7; -.
DR   STRING; 38033.XP_001225923.1; -.
DR   PRIDE; Q2GUT7; -.
DR   EnsemblFungi; EAQ87014; EAQ87014; CHGG_08267.
DR   GeneID; 4394192; -.
DR   eggNOG; KOG2203; Eukaryota.
DR   HOGENOM; CLU_011270_0_0_1; -.
DR   InParanoid; Q2GUT7; -.
DR   OrthoDB; 418635at2759; -.
DR   Proteomes; UP000001056; 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   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_0000384979"
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..283
FT                   /note="GB1/RHD3-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01052"
FT   REGION          825..852
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          475..500
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   COMPBIAS        832..846
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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;  95967 MW;  4FDF4A2CE0A184E2 CRC64;
     MNGHFAAVGN GPTAQQYEHG IQVIDEDKAF NTNLNDYLGE TRVAEAGFNY HLISVFGSQS
     TGKSTLLNHL FKTEFSVMSE SARRQTTKGI WMSKNKRAGA NGDAATMADN ILVMDVEGTD
     GRERGEDQDF ERKSALFALA TSEVLIVNIW EHQIGLYQGA NMGLLKTVFE VNLQLFLKDR
     QSQTRSLLFF VIRDHVGNTP LANLRDTLVQ DLTKIWSTLS KPQGLEDSKI EDYFDFAFAA
     LPHKILQPEK FLEEADKLST RFTTGHRSAK DQEFVGGVFL PEYHRRIPAD GLSVYAEGVW
     DQIVNNKDLD LPTQQELLAQ FRCDEISREV FVGFDSVIVP LEEQQAEATR LGKATVLPDL
     GVTGAGTREK CVKAFETQAS RYHKGVYSVK RGELESKIDA RLKALYQTQL SAAHKSGVAA
     FSDAVTNAVK AGQKAGGYEF AEIVDKQKKK TLEFFKKEAQ SLLIQGVAWT NFKPQYRLFE
     KELDEVSARL RKEEMRRLAI RVERWVKSRL GDSIGVEFNK LGSGRGGSGA PENGEKPATE
     KDLWDRIWNT FSGIIREAET RFADRAKSFE ASPEEVEVGL WRLRRKSWVA LREKIEEEMM
     ESNILMKLRE NFEDKFRYDE EGVPRIWRPT DDIEGIYTRA RESTLGLIPL LARFRLAETY
     APPDLPTFVG PQPAGAEPED EEDLAPIGGV DEEEGKSLEE EMTVLSESKR QDLVVRFKKM
     ADGVYVEAKR SAIGGITQVP LYFYIVLLIF GWNEIVMVLR NPMLFMLLLV MGGGTYVAYT
     LNLLGPMMQM ANAASNQAVE IGKEKLRDFL ENNQTMRQAI AMPPRSQDNG IGMDRLDSRG
     KKAQEVEEDD DI