SEY1_PARBP
ID SEY1_PARBP Reviewed; 872 AA.
AC C0S6S4;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 47.
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=PABG_03379;
OS Paracoccidioides brasiliensis (strain Pb03).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX NCBI_TaxID=482561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pb03;
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; KN305534; EEH21148.1; -; Genomic_DNA.
DR AlphaFoldDB; C0S6S4; -.
DR SMR; C0S6S4; -.
DR EnsemblFungi; EEH21148; EEH21148; PABG_03379.
DR VEuPathDB; FungiDB:PABG_03379; -.
DR HOGENOM; CLU_011270_0_0_1; -.
DR InParanoid; C0S6S4; -.
DR Proteomes; UP000002740; 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; Transmembrane; Transmembrane helix.
FT CHAIN 1..872
FT /note="Protein SEY1"
FT /id="PRO_0000384990"
FT TOPO_DOM 1..749
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TRANSMEM 750..770
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TOPO_DOM 771..773
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TRANSMEM 774..794
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TOPO_DOM 795..872
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT DOMAIN 49..294
FT /note="GB1/RHD3-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01052"
FT REGION 676..704
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 849..872
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 482..504
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT BINDING 59..66
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
SQ SEQUENCE 872 AA; 98480 MW; 73BBBAE6EC5EB7F2 CRC64;
MVANGHFAGV GDVLDAKNYE HGVQVIDEEK EFNPNLSNYL SYENVTPAGF NYHLISVFGS
QSTGKSTLLN SLFGTHFSVM SETERRQTTK GIWLSKNKRL KSDKGQDNQT KMADNILVMD
VEGTDGRERG EDQDFERKSA LFALATSEVL IVNIWEHQVG LYQGANMGLL KTVFEVNLEL
FLKDKRSNPR SLLFFVIRDF LGTTPLQNLQ NTLLQDLNRI WNSLSKPAGL ENSSITDYFD
FAFAGLPHKN FQPEKFVDEV RKLSTRFCDG HRDPNKTDAK GTSSIEGGIF LPEYHRRIPA
DGFAVYAEGI WDQIVNNKDL DLPTQQELLA QFRCDEISRE VLVAFDEAIS PFEAKQAEAV
QAGNPQVLGG LGSAMCNARM KSVKNFDTEA SRYHKRVYQM KKSELQDKID SRLKALFLGQ
LSAAHRSGIQ EFTESVTAAV KAGQKRGASY DFAEIVTKER KLAIEKFEKE ARAAVVEDTQ
WSNYQQELSL YQKDLENIGG QLRRDEMRRL ATRVGRWVRS RLGESIDLEF NAIGSGRGGS
GAPEFGDKPS EKSLWDRVWT LFVDTVLDAE RRFTERASSF DASIDEVDVG LWRLRRKSWG
VLRAKIEEEM MEGNILLKLR ENFEDKFRYD DAGVPRIWRP NDDIESIYTR ARESTLTLIP
LLSRFRLAET NAPPPLDKWI GHTPSSATPA DEEDLTPIGG VDEDEGKSLE EEMTMIGEAK
KQDLTVRFKK TADGVYVEAK RSAIGGITQV PLYFYGLLLA LGWNEIVAVL RNPAYFLLLF
VCAVTAYVTY QLNLWGPIIK MTEAASQQAL MEGKRRLREF LEASDTGLQA MAMSEGRNAE
EYDMSNMKNR KSAGGFQNNR SHIDDADDDD DF
