SEY1_PYRTR
ID SEY1_PYRTR Reviewed; 862 AA.
AC B2W244;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 2.
DT 03-AUG-2022, entry version 49.
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=PTRG_03492;
OS Pyrenophora tritici-repentis (strain Pt-1C-BFP) (Wheat tan spot fungus)
OS (Drechslera tritici-repentis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Pyrenophora.
OX NCBI_TaxID=426418;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pt-1C-BFP;
RX PubMed=23316438; DOI=10.1534/g3.112.004044;
RA Manning V.A., Pandelova I., Dhillon B., Wilhelm L.J., Goodwin S.B.,
RA Berlin A.M., Figueroa M., Freitag M., Hane J.K., Henrissat B., Holman W.H.,
RA Kodira C.D., Martin J., Oliver R.P., Robbertse B., Schackwitz W.,
RA Schwartz D.C., Spatafora J.W., Turgeon B.G., Yandava C., Young S., Zhou S.,
RA Zeng Q., Grigoriev I.V., Ma L.-J., Ciuffetti L.M.;
RT "Comparative genomics of a plant-pathogenic fungus, Pyrenophora tritici-
RT repentis, reveals transduplication and the impact of repeat elements on
RT pathogenicity and population divergence.";
RL G3 (Bethesda) 3:41-63(2013).
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=EDU46330.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; DS231617; EDU46330.1; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_001933825.1; XM_001933790.1.
DR AlphaFoldDB; B2W244; -.
DR SMR; B2W244; -.
DR STRING; 45151.EDU46330; -.
DR GeneID; 6341723; -.
DR eggNOG; KOG2203; Eukaryota.
DR InParanoid; B2W244; -.
DR OrthoDB; 418635at2759; -.
DR Proteomes; UP000001471; 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..862
FT /note="Protein sey1"
FT /id="PRO_0000384999"
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..862
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT DOMAIN 48..298
FT /note="GB1/RHD3-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01052"
FT REGION 524..543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 821..862
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 473..499
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT COMPBIAS 834..862
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 58..65
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
SQ SEQUENCE 862 AA; 96787 MW; 9151AFBCA759DDA0 CRC64;
MMNAHFAGVG DNADNAAYEH GIQVIDEDKM FNGNVSTYLN IEKVIPAGFN YHLISVFGSQ
STGKSTLLNH LFGTQFGVMS EQERRQTTKG IWMSKNKRES GGSSMAENIL VMDVEGTDGR
ERGEDQDFER KSALFALATS EVLIVNIWEH QVGLYQGANM GLLKTVFEVN LQLFVKDSQS
TPRSLLFFVI RDHLGTTPLK NLQNTLVQDL SKLWSTISKP AGLENSRIED YFDFAFVALP
HKILQPEKFD EAVTQLSTRF KEGYNDPRKS GLIDEATAPI FLPQYHRRIP ADGFSAYAEG
VWDQIVNNKD LDLPTQQELL AQFRCDEISR EVQVAFDETI TPLEDKQAED ARAGTHSLIP
DLGPKMNAAR QKVLKDFDVN ASRYHKGVYK RKQAELEGKV DTRLKALFQK QLTAAHKSGI
EGFTEAVSAA VKNGQKKNAS YDFAQIVDSE KKKALTKFEE DATAMAIEGA AWSSHENELK
IYKKELDDVS GRLRKEEMRR LATRIERWVR TRLDESIGLE FNKLGSGRGG SGAPEHGDRP
PTEKDLWDRV WTIFTDTVKM AEKRFTDRAS SFDASADEVE VGLWRLRRKS WGVLRAKIDE
EVMEGNILLK LRENFEDKFR YDDLGVPRIW RPTDDIDGLY TKARESTITV IPLLAHFKLA
KTSKPPPLDA WIGEAPASVS PADEEDLSPI GGVDDDEDKT LEDEMTILSD GKQADLLVRF
KKTADGVYVE AKRGAIGGLS QIPFWLYPAM LALGWNEIVA VLRNPIYFIF LILLAVAAYV
TYTLNLWGPI MRVANAASQQ GLEVGKERLR AFLENSDAGR QAMAMSGSGD SNSTRRYEDV
KMDRLNGDGK KSKSMEEDLD DI
