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Database: UniProt
Entry: G0VER4_NAUCC
LinkDB: G0VER4_NAUCC
Original site: G0VER4_NAUCC 
ID   G0VER4_NAUCC            Unreviewed;       594 AA.
AC   G0VER4;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   24-JAN-2024, entry version 59.
DE   RecName: Full=Actin-binding protein {ECO:0008006|Google:ProtNLM};
GN   Name=NCAS0D04740 {ECO:0000313|EMBL:CCC70055.1};
GN   OrderedLocusNames=NCAS_0D04740 {ECO:0000313|EMBL:CCC70055.1};
OS   Naumovozyma castellii (strain ATCC 76901 / BCRC 22586 / CBS 4309 / NBRC
OS   1992 / NRRL Y-12630) (Yeast) (Saccharomyces castellii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Naumovozyma.
OX   NCBI_TaxID=1064592 {ECO:0000313|EMBL:CCC70055.1, ECO:0000313|Proteomes:UP000001640};
RN   [1] {ECO:0000313|EMBL:CCC70055.1, ECO:0000313|Proteomes:UP000001640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 76901 / BCRC 22586 / CBS 4309 / NBRC 1992 / NRRL Y-12630
RC   {ECO:0000313|Proteomes:UP000001640};
RX   PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA   Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA   Wolfe K.H.;
RT   "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT   accidents.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Type strain:CBS 4309;
RA   Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA   Wolfe K.H.;
RT   "Genome sequence of Naumovozyma castellii.";
RL   Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; HE576755; CCC70055.1; -; Genomic_DNA.
DR   RefSeq; XP_003676416.1; XM_003676368.1.
DR   AlphaFoldDB; G0VER4; -.
DR   STRING; 1064592.G0VER4; -.
DR   GeneID; 11528394; -.
DR   KEGG; ncs:NCAS_0D04740; -.
DR   eggNOG; KOG3655; Eukaryota.
DR   HOGENOM; CLU_459326_0_0_1; -.
DR   InParanoid; G0VER4; -.
DR   OMA; FKEPRGA; -.
DR   OrthoDB; 101008at2759; -.
DR   Proteomes; UP000001640; Chromosome 4.
DR   GO; GO:0003779; F:actin binding; IEA:InterPro.
DR   CDD; cd11819; SH3_Cortactin_like; 1.
DR   Gene3D; 3.40.20.10; Severin; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   InterPro; IPR002108; ADF-H.
DR   InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   PANTHER; PTHR10829; CORTACTIN AND DREBRIN; 1.
DR   PANTHER; PTHR10829:SF25; DREBRIN-LIKE PROTEIN; 1.
DR   Pfam; PF00241; Cofilin_ADF; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   SMART; SM00102; ADF; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF55753; Actin depolymerizing proteins; 1.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   PROSITE; PS51263; ADF_H; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000001640};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}.
FT   DOMAIN          7..136
FT                   /note="ADF-H"
FT                   /evidence="ECO:0000259|PROSITE:PS51263"
FT   DOMAIN          534..594
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   REGION          142..289
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          310..545
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        176..195
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        230..245
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        255..272
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        320..353
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        371..389
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        440..455
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        490..506
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        526..541
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   594 AA;  67322 MW;  D56865A035A8AB13 CRC64;
     MALEPINCTT HSREIEEQYL KIVRGSDADT TWLIISPNSK KEYFPESTGA DFAEFLQSFD
     ETKVQFGLAR VSPPGSDVEK LILVGWCPDS APMKPRASFA SNFATVANQV LKGYHIQVTA
     RDEDDLDEDE LLSRVSNASG ARYSIQTSSG ANAKPKPKQH TIPKKQTPPP SKPAVHEKPI
     VEKFERAAKQ NSNEDDWDEP EVEERDFDKQ PLKPNQSTYK PVGKIDLQKV IQEENAKEDP
     RLVHSVANGK IDPKSDIANL KEQSKLKRDA EFNNFLGKSP LPVNEFKKDD DKVIKGFKTE
     KTPAQLWAEK KAAANKNKAP VEQNREDDEK HDTNEQDDED EHDVRDLKSK FESMATTTDE
     PQIIHPKPFS KPTPAREEQE VEPPKKKDIK QFGTPLPGMH TEVSEDEQQN DDNDDDWSDD
     EDQGNARKPA PLPARNIPPV RANKEEEEEE KKRASPPPPS LPTRNEEPEE EEEEPTPSLP
     KRNNIARAEP EEEEEEEEEE EEKEEEPTPS LPSRNTEAVP PPPPRRSAEP EKKKEEPWAI
     AEYDYEAGED NELTFSENDK IINIEFVDDD WWLGELESSG EKGLFPSNYV SLGN
//
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