ID A0A2G4SPE0_RHIZD Unreviewed; 882 AA.
AC A0A2G4SPE0;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Transcription factor {ECO:0008006|Google:ProtNLM};
GN ORFNames=RHIMIDRAFT_205380 {ECO:0000313|EMBL:PHZ10641.1};
OS Rhizopus microsporus ATCC 52813.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX NCBI_TaxID=1340429 {ECO:0000313|EMBL:PHZ10641.1, ECO:0000313|Proteomes:UP000242254};
RN [1] {ECO:0000313|EMBL:PHZ10641.1, ECO:0000313|Proteomes:UP000242254}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 52813 {ECO:0000313|EMBL:PHZ10641.1,
RC ECO:0000313|Proteomes:UP000242254};
RX PubMed=27956601; DOI=10.1073/pnas.1615148113;
RA Lastovetsky O.A., Gaspar M.L., Mondo S.J., LaButti K.M., Sandor L.,
RA Grigoriev I.V., Henry S.A., Pawlowska T.E.;
RT "Lipid metabolic changes in an early divergent fungus govern the
RT establishment of a mutualistic symbiosis with endobacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:15102-15107(2016).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR017179}.
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DR EMBL; KZ303854; PHZ10641.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G4SPE0; -.
DR STRING; 1340429.A0A2G4SPE0; -.
DR OrthoDB; 375531at2759; -.
DR Proteomes; UP000242254; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016442; C:RISC complex; IEA:UniProtKB-UniRule.
DR GO; GO:0004518; F:nuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0031047; P:regulatory ncRNA-mediated gene silencing; IEA:InterPro.
DR CDD; cd00175; SNc; 3.
DR Gene3D; 2.30.30.140; -; 1.
DR Gene3D; 2.40.50.90; -; 5.
DR InterPro; IPR016685; Silence_cplx_Nase-comp_TudorSN.
DR InterPro; IPR035437; SNase_OB-fold_sf.
DR InterPro; IPR016071; Staphylococal_nuclease_OB-fold.
DR InterPro; IPR002999; Tudor.
DR PANTHER; PTHR12302; EBNA2 BINDING PROTEIN P100; 1.
DR PANTHER; PTHR12302:SF2; STAPHYLOCOCCAL NUCLEASE DOMAIN-CONTAINING PROTEIN 1; 1.
DR Pfam; PF00565; SNase; 5.
DR Pfam; PF00567; TUDOR; 1.
DR PIRSF; PIRSF017179; RISC-Tudor-SN; 1.
DR SMART; SM00318; SNc; 5.
DR SMART; SM00333; TUDOR; 1.
DR SUPFAM; SSF50199; Staphylococcal nuclease; 5.
DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 1.
DR PROSITE; PS50830; TNASE_3; 4.
DR PROSITE; PS50304; TUDOR; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|PIRNR:PIRNR017179};
KW Reference proteome {ECO:0000313|Proteomes:UP000242254};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 1..142
FT /note="TNase-like"
FT /evidence="ECO:0000259|PROSITE:PS50830"
FT DOMAIN 168..308
FT /note="TNase-like"
FT /evidence="ECO:0000259|PROSITE:PS50830"
FT DOMAIN 318..467
FT /note="TNase-like"
FT /evidence="ECO:0000259|PROSITE:PS50830"
FT DOMAIN 496..629
FT /note="TNase-like"
FT /evidence="ECO:0000259|PROSITE:PS50830"
FT DOMAIN 697..755
FT /note="Tudor"
FT /evidence="ECO:0000259|PROSITE:PS50304"
FT COILED 111..138
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 882 AA; 98753 MW; 5E56903F68DD645D CRC64;
MVNKAIVKNV LSGDTVILRG KPRPNGPPAE RLLALSNVQA PRLGSTTRSD EPFGFESREF
LRKLLVGKEV SFVPEYTTTT QREYGSIYLA NGENVQELGV KAGWLKVREG GKTTSEDKQD
VLNRLEQLQE EAQAAKVGMW NDAEKGTRDI FFTFEKDPHA FLNKYKGKPL NAIIEQVRDG
STFRVLLLLP DNTQQIITLS LSGIKAPTCK RDNAEDGVVS EPFGEEAKYF VESRLLQRGV
KVILEGLSQG QTFVGSIQHP AGNIAELLLS QGLAKCIDWS ITLATSGPTP LRNAEKLAKE
KKLRLWRNFV VKAPTETNEF DAAVIRIISG DMILVKTKNG GIEKKIQFAS IKQPPRGAGS
TAPTSKSKDV KEVGYQFEAR EYLRKKLIGK QVHVAIDYHK PAQEGFEAKD CATVIQGSQN
VAEQLVLRGL ATVIRHRKDD DNRARHYDQL LLAEKKAEEQ QKGVHSPKEL PVTRIVDASE
SAAKARQFFT FLKRAGKLSA VVEYVSNGSR LALWIPKENC RVSFVLSGVR APRVGRTPTD
KSEPFGQEAL DYVSQKCLQH DVEVEIENVD KVGSFVGSLF IQSENLAVSL LERGLATIHE
YSADESHYVN QLYGAERQAK NEKRGLWAEG VNEEVEQTST NTSTGPNREY IDVVVSEILS
GSHFYVQKVT DEIQKLEALM KELDEYYSSR PADPAFKPRV GDLVCAKFTE DDGWYRAKVR
RISHEGIEVH YIDYGNSETL SSARVRALAD KFKALKPQAH EAVLSFVKSP ERDQDYGIEA
YERFRQLTAN KQLVANVDAR EGNTLCLTLY DFRKSTSAEV SVNLDMVQDG QAYVTPKVRY
THGNETIIKT LQEAQEQAIR RRLGMFEYGD ITGDDDIRDT YY
//
