SEY1_AJECN
ID SEY1_AJECN Reviewed; 873 AA.
AC A6R1D5;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 60.
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=HCAG_03442;
OS Ajellomyces capsulatus (strain NAm1 / WU24) (Darling's disease fungus)
OS (Histoplasma capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma;
OC unclassified Histoplasma.
OX NCBI_TaxID=2059318;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NAm1 / WU24;
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(2009).
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; CH476657; EDN06912.1; -; Genomic_DNA.
DR RefSeq; XP_001541345.1; XM_001541295.1.
DR AlphaFoldDB; A6R1D5; -.
DR SMR; A6R1D5; -.
DR STRING; 339724.A6R1D5; -.
DR EnsemblFungi; EDN06912; EDN06912; HCAG_03442.
DR GeneID; 5447647; -.
DR KEGG; aje:HCAG_03442; -.
DR VEuPathDB; FungiDB:HCAG_03442; -.
DR HOGENOM; CLU_011270_0_0_1; -.
DR OMA; TNFDVMD; -.
DR OrthoDB; 418635at2759; -.
DR Proteomes; UP000009297; 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..873
FT /note="Protein SEY1"
FT /id="PRO_0000384966"
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..873
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT DOMAIN 49..307
FT /note="GB1/RHD3-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01052"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 677..703
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 828..873
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 482..506
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT COMPBIAS 840..864
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 59..66
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
SQ SEQUENCE 873 AA; 98816 MW; 60A32A270E882EC2 CRC64;
MVANGHFAGS ADGQHSSSYE HGVQVIDEDK EFNPNVSKYL TYENVTPAGF NYHLISVFGS
QSTGKSTLLN NLFGTHFSVM SETERRQTTK GIWLSKNKRL ELRKDRDPQA KMADNILVMD
VEGTDGRERG EDQDFERKSA LFALATSEVL IVNIWEHQVG LYQGANMGLL KTVFEVNLEL
FLKDNKSTPR SLLFFVIRDF LGTTPLQNLQ NTLLQDLNRI WSSLSKPAGL ENSTINDYFD
FAFAGLPHKN FQPDKFMDEV QKLSTRFREG HRDPNSLDRK GTGSIEGGIF LPEYHRRIPA
DGFAVYAEGV WDQIVNNKDL DLPTQQELLA QFRCDEISRE ALVAFDEAIS PFELKQAEAV
QAGYPEVLGG LGPAMRNARM KAVKNFDTEA CRYHKRVYQM KKAELQDKID TRLKALFLGQ
LGAAHRSGVQ EFSESVSAAV KAGQKKGASY DFAEIVRKQR KLAIEKFEQE ARSTLVEDAP
WSNYQQELSL YQKDLERTSG QLRRDEMRRL ATRVERWVRS RLGESVDLEF NALGSGRGGS
GAPEFGDKPS EKTIWDRVWT LFVDTVLDAE RRFTERASSF DASLDEVDVG LWRLRRKSWG
VLRAKIDEEM MEGNLLLKLR ENFEDKFRYD DAGVPRIWRP TDDIESVYSQ ARESTLTLIP
LLARFKLAET NAPPPLDKWI GHTPSSATPA DEEDLTPIGG VDDDEGKSLE EEMTLIGEAK
KQDITVRFKK TADGVYVEAK RSAIGGITQV PLYFYGLLFA LGWNEILAVL RNPVYFLLLF
VCAIGAYITY QLNLWGPIIK MTEAASHQAV EEGKRRLREF LEASDTGRQA MAMSGARNAT
EEHEMSRLSR KPAERGGRKN RADEDVDDDD DDF
