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Database: UniProt
Entry: A0A3R7N8S5_PENVA
LinkDB: A0A3R7N8S5_PENVA
Original site: A0A3R7N8S5_PENVA 
ID   A0A3R7N8S5_PENVA        Unreviewed;       624 AA.
AC   A0A3R7N8S5;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   08-NOV-2023, entry version 17.
DE   SubName: Full=Putative peptidyl-prolyl cis-trans isomerase G {ECO:0000313|EMBL:ROT80336.1};
GN   ORFNames=C7M84_000915 {ECO:0000313|EMBL:ROT80336.1};
OS   Penaeus vannamei (Whiteleg shrimp) (Litopenaeus vannamei).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC   Malacostraca; Eumalacostraca; Eucarida; Decapoda; Dendrobranchiata;
OC   Penaeoidea; Penaeidae; Penaeus.
OX   NCBI_TaxID=6689 {ECO:0000313|EMBL:ROT80336.1, ECO:0000313|Proteomes:UP000283509};
RN   [1] {ECO:0000313|EMBL:ROT80336.1, ECO:0000313|Proteomes:UP000283509}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Muscle {ECO:0000313|EMBL:ROT80336.1};
RA   Zhang X., Yuan J., Li F., Xiang J.;
RL   Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ROT80336.1, ECO:0000313|Proteomes:UP000283509}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Muscle {ECO:0000313|EMBL:ROT80336.1};
RA   Sun Y., Gao Y., Yu Y.;
RT   "The decoding of complex shrimp genome reveals the adaptation for benthos
RT   swimmer, frequently molting mechanism and breeding impact on genome.";
RL   Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:ROT80336.1}.
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DR   EMBL; QCYY01001128; ROT80336.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3R7N8S5; -.
DR   STRING; 6689.A0A3R7N8S5; -.
DR   EnsemblMetazoa; XM_027362072.1; XP_027217873.1; LOC113810378.
DR   Proteomes; UP000283509; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004402; F:histone acetyltransferase activity; IEA:InterPro.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   Gene3D; 3.40.630.30; -; 1.
DR   Gene3D; 4.10.320.30; -; 1.
DR   Gene3D; 3.30.60.60; N-acetyl transferase-like; 1.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR002717; HAT_MYST-type.
DR   InterPro; IPR040706; Zf-MYST.
DR   InterPro; IPR002515; Znf_C2H2C.
DR   InterPro; IPR036060; Znf_C2H2C_sf.
DR   PANTHER; PTHR10615; HISTONE ACETYLTRANSFERASE; 1.
DR   PANTHER; PTHR10615:SF210; HISTONE ACETYLTRANSFERASE KAT7; 1.
DR   Pfam; PF01853; MOZ_SAS; 1.
DR   Pfam; PF01530; zf-C2HC; 1.
DR   Pfam; PF17772; zf-MYST; 1.
DR   SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR   SUPFAM; SSF103637; CCHHC domain; 1.
DR   PROSITE; PS51726; MYST_HAT; 1.
DR   PROSITE; PS51802; ZF_CCHHC; 1.
PE   4: Predicted;
KW   Isomerase {ECO:0000313|EMBL:ROT80336.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000283509};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          478..624
FT                   /note="MYST-type HAT"
FT                   /evidence="ECO:0000259|PROSITE:PS51726"
FT   REGION          1..334
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          390..448
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        29..43
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        64..83
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        99..133
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        134..148
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        153..177
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        191..222
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        245..261
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        274..291
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        401..417
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        418..448
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   624 AA;  69599 MW;  EA93049351A4400F CRC64;
     MCCRSRARSR AASTDRDSPQ KPSIPTQAPK GGKEPPPAKP PQTRPHTRGS SESEPDIGTA
     PSKRGPKTSA TTVPKSSAVP PPGNQRKNGP KPAARPQQAA TQKPPNKTQQ QKVSGSNATA
     QQKKTAQSKK TIENSTDSES EAKKPVPKKA AQSKSQPKPQ SKPQPKSTAS QKAIVHQRKG
     TTKVVEKSSE KSSESSTNSS SASSESDSDS SSDSSASVKS SDKPVVAQIV RRKSQTKSTP
     ATTESEKEEE EEEEEEDEDE EDTPRKHITR SSSVRTKRGS LLGIQKGTES DSENNGKVRR
     GARNGGPKKP AGPPSKSGAR AKTKKPIPLD ILENIPLPPI ENRKCPVEGC DSTGHLGGLY
     EKHFSVEACP VFHNITKEES KMNRQIREAE MKEREKATQA VGNKSPRNGP NSEQRNYCNK
     IRDSRDKLSE PRPGEDEMAD RDRQPSLRGF TPEWDLKLFL EAQSAASEKI EDDLRGLPDT
     KGIRYIEMGR YEMEAWYQSQ YPDDYNQQPK IYICEFCLKY MRSKTILSRH AAKCVWKHPP
     GDEIYRKDKL SVWEVDGKKY KIYCQNLCLL AMLFLDHKTL YYDVEPFLFY IMTQADGEGC
     HIIGYFSKVS ETLFIFFFFY RIVL
//
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