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Database: UniProt
Entry: S8A7V4_DACHA
LinkDB: S8A7V4_DACHA
Original site: S8A7V4_DACHA 
ID   S8A7V4_DACHA            Unreviewed;       895 AA.
AC   S8A7V4;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=ZZ-type domain-containing protein {ECO:0000259|PROSITE:PS50135};
GN   ORFNames=H072_7107 {ECO:0000313|EMBL:EPS39100.1};
OS   Dactylellina haptotyla (strain CBS 200.50) (Nematode-trapping fungus)
OS   (Monacrosporium haptotylum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC   Orbiliales; Orbiliaceae; Dactylellina.
OX   NCBI_TaxID=1284197 {ECO:0000313|EMBL:EPS39100.1, ECO:0000313|Proteomes:UP000015100};
RN   [1] {ECO:0000313|EMBL:EPS39100.1, ECO:0000313|Proteomes:UP000015100}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 200.50 {ECO:0000313|EMBL:EPS39100.1,
RC   ECO:0000313|Proteomes:UP000015100};
RX   PubMed=24244185;
RA   Meerupati T., Andersson K.M., Friman E., Kumar D., Tunlid A., Ahren D.;
RT   "Genomic mechanisms accounting for the adaptation to parasitism in
RT   nematode-trapping fungi.";
RL   PLoS Genet. 9:E1003909-E1003909(2013).
RN   [2] {ECO:0000313|Proteomes:UP000015100}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 200.50 {ECO:0000313|Proteomes:UP000015100};
RA   Ahren D.G.;
RT   "Genomic mechanisms accounting for the adaptation to parasitism in
RT   nematode-trapping fungi.";
RL   Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EPS39100.1}.
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DR   EMBL; AQGS01000489; EPS39100.1; -; Genomic_DNA.
DR   RefSeq; XP_011112879.1; XM_011114577.1.
DR   AlphaFoldDB; S8A7V4; -.
DR   eggNOG; ENOG502SZFB; Eukaryota.
DR   HOGENOM; CLU_327312_0_0_1; -.
DR   OMA; RFANICG; -.
DR   OrthoDB; 70376at2759; -.
DR   Proteomes; UP000015100; Unassembled WGS sequence.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd02249; ZZ; 1.
DR   Gene3D; 3.30.60.90; -; 1.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000433; Znf_ZZ.
DR   InterPro; IPR043145; Znf_ZZ_sf.
DR   PANTHER; PTHR48182; PROTEIN SERAC1; 1.
DR   PANTHER; PTHR48182:SF2; PROTEIN SERAC1; 1.
DR   Pfam; PF00569; ZZ; 1.
DR   SMART; SM00291; ZnF_ZZ; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS50135; ZF_ZZ_2; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015100};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00228}.
FT   DOMAIN          518..575
FT                   /note="ZZ-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50135"
FT   REGION          326..414
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          433..516
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          773..809
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          838..865
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        326..351
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        352..367
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        381..414
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        433..499
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        500..516
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   895 AA;  99211 MW;  2D563E4F1929492C CRC64;
     MQAPEFNRQD ALGLRLVRTP PSEIGYTCDI IILHGLNGGP AKSFRHPEGG NIWFADFLPV
     DIVDVDSWTN ARIWTYGYEA DKAFGAANSS ALDFARSLLY QVDRIREGNE KFKIIWVCHS
     LGGIVAKTAL VEAQIIPQYQ PILTQTAGVI FLGTPHTGSA VMTVADIGAK IAGVMLPDTI
     VSKNRKLINC VRKDSGRLFE TAGRFANICG DMKIFNMYEA PSVTGSRTVE RDSAVMNLGK
     IETQFMLDGT NHRTMCIYKD RMDQNYLSVL DAIKKLTRST STLYEPLDLP AAPATRAQSN
     SYFNPSASTT SFGGLNGFGS SYASDNRSQA SYNSTSTYSN ASQTSTAPTS NYSSPQPPPP
     RPPAKEPVAA QWPHYFNQDQ DRRYPPSTIY GDQGQQPNSQ NSRPDNYAPP SYSATARDMN
     YSSAASVFSA TSSSSLYDSP SAPAYRTPSG STSQTPNTQI SPSTNFSPYR PSGSTPTSPE
     PNRSIRTPVQ EIRSAPSAPS PSKPTEPEPK PTLPPPESPH WICDGCKNPI YPFESRIHCL
     DCPDYDLCGP CHAKGTATKG HKGYHKEEFI IKARQITQEQ SELVIPSEVH PEVTPGRLFR
     NWTIQDERRV HHLSCNDDHA RYLISSLEPG NYRVSFHLDL FLIKEFTEEH IKQLGKEPLG
     KLRIAVGYIK NKKSFFKEKF PEDKNLISRI FEFGWYDDFN VNPQSGTIAV DLKCILSIEG
     NEDRDDVGIL FQWSEFRKFQ SSDKALISFA LISARFEDLM EFDPDFGGAI DKAKPVDRYT
     HPPSQEAARA PVQTPAQAPA QAQTQASSAE SGISALSLDD IFQAIMEVAQ EERDRQEREA
     FQQAIAEELA RRRRAQAEAQ EREAAAQLMA NYMVATQATV EFALLNEYLK HLTGG
//
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