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HSV2_EMENI
ID   HSV2_EMENI              Reviewed;         317 AA.
AC   Q5B464; C8VB13;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   25-MAY-2022, entry version 102.
DE   RecName: Full=SVP1-like protein 2;
GN   Name=hsv2; ORFNames=AN4666;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
CC   -!- FUNCTION: Involved in mitochondrial or peroxisomal functions and amino
CC       acid signaling pathways. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000250}; Peripheral
CC       membrane protein {ECO:0000250}. Cytoplasmic vesicle membrane
CC       {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC       Note=Vesicular and vacuolar. {ECO:0000250}.
CC   -!- DOMAIN: May contain a beta-propeller domain involved in specific
CC       binding to phosphatidylinositol 3,5-bisphosphate (PIP2), leading to the
CC       association of the protein to the membrane. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the WD repeat PROPPIN family. {ECO:0000305}.
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DR   EMBL; AACD01000080; EAA60708.1; -; Genomic_DNA.
DR   EMBL; BN001303; CBF77040.1; -; Genomic_DNA.
DR   RefSeq; XP_662270.1; XM_657178.1.
DR   AlphaFoldDB; Q5B464; -.
DR   SMR; Q5B464; -.
DR   STRING; 162425.CADANIAP00005767; -.
DR   EnsemblFungi; CBF77040; CBF77040; ANIA_04666.
DR   EnsemblFungi; EAA60708; EAA60708; AN4666.2.
DR   GeneID; 2872463; -.
DR   KEGG; ani:AN4666.2; -.
DR   eggNOG; KOG2111; Eukaryota.
DR   HOGENOM; CLU_025895_0_0_1; -.
DR   InParanoid; Q5B464; -.
DR   OMA; MGTTNYL; -.
DR   OrthoDB; 966922at2759; -.
DR   Proteomes; UP000000560; Chromosome III.
DR   Proteomes; UP000005890; Unassembled WGS sequence.
DR   GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0019898; C:extrinsic component of membrane; IBA:GO_Central.
DR   GO; GO:0034045; C:phagophore assembly site membrane; IBA:GO_Central.
DR   GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; IBA:GO_Central.
DR   GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IBA:GO_Central.
DR   GO; GO:0000422; P:autophagy of mitochondrion; IBA:GO_Central.
DR   GO; GO:0044804; P:autophagy of nucleus; IBA:GO_Central.
DR   GO; GO:0006497; P:protein lipidation; IBA:GO_Central.
DR   GO; GO:0034497; P:protein localization to phagophore assembly site; IBA:GO_Central.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   Gene3D; 2.130.10.10; -; 1.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   SMART; SM00320; WD40; 2.
DR   SUPFAM; SSF50978; SSF50978; 1.
PE   3: Inferred from homology;
KW   Cytoplasmic vesicle; Membrane; Protein transport; Reference proteome;
KW   Repeat; Transport; Vacuole; WD repeat.
FT   CHAIN           1..317
FT                   /note="SVP1-like protein 2"
FT                   /id="PRO_0000051028"
FT   REPEAT          119..159
FT                   /note="WD 1"
FT   REPEAT          164..203
FT                   /note="WD 2"
SQ   SEQUENCE   317 AA;  34192 MW;  920DC2982616E3C0 CRC64;
     MLGQSNYLAL VGGGRQPKFP QNKLVIWDDA KQKVVITLEF RTSVLGVRLS KSRIVVALLN
     SIHTFVFSSP PKKLAVFETT DNPLGLACLG QKVLAFPGRS PGQVQLVELE TGNVSIIPAH
     STPLRAMALS PDGEVLATAS EAGTLVRIFA TSNCAKMAEL RRGVDHAIIF SLAISPSNNL
     LAVTSDKSTL HVFNLPHPRN APYSNQQASS SDDGVNKKWG ILGKIPLLPR VFSDVYSFAS
     AHFELGEEEP GPTYAPPLGT VLGRPPKGVI GWSNDNTILV VGSGSDGRWE KFVLRDDEEG
     KKHCIREGWK KYLGSGS
 
 
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