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
//