ID A0A4D9F2W2_9SAUR Unreviewed; 1026 AA.
AC A0A4D9F2W2;
DT 03-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 03-JUL-2019, sequence version 1.
DT 24-JAN-2024, entry version 13.
DE SubName: Full=BMP and activin membrane-bound inhibitor-like protein {ECO:0000313|EMBL:TFK12284.1};
GN ORFNames=DR999_PMT04335 {ECO:0000313|EMBL:TFK12284.1};
OS Platysternon megacephalum (big-headed turtle).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Testudinoidea; Platysternidae; Platysternon.
OX NCBI_TaxID=55544 {ECO:0000313|EMBL:TFK12284.1, ECO:0000313|Proteomes:UP000297703};
RN [1] {ECO:0000313|EMBL:TFK12284.1, ECO:0000313|Proteomes:UP000297703}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DO16091913 {ECO:0000313|EMBL:TFK12284.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:TFK12284.1};
RA Gong S.;
RT "Draft genome of the big-headed turtle Platysternon megacephalum.";
RL Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:TFK12284.1, ECO:0000313|Proteomes:UP000297703}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DO16091913 {ECO:0000313|EMBL:TFK12284.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:TFK12284.1};
RA Gong S.;
RT "The genome sequence of big-headed turtle.";
RL Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-
CC lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752,
CC Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930;
CC Evidence={ECO:0000256|ARBA:ARBA00000636};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. ECO subfamily.
CC {ECO:0000256|ARBA:ARBA00005816}.
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:TFK12284.1}.
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DR EMBL; QXTE01000024; TFK12284.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4D9F2W2; -.
DR STRING; 55544.A0A4D9F2W2; -.
DR Proteomes; UP000297703; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR InterPro; IPR028005; AcTrfase_ESCO_Znf_dom.
DR InterPro; IPR028009; ESCO_Acetyltransf_dom.
DR PANTHER; PTHR45884; N-ACETYLTRANSFERASE ECO; 1.
DR PANTHER; PTHR45884:SF1; N-ACETYLTRANSFERASE ESCO1; 1.
DR Pfam; PF13880; Acetyltransf_13; 1.
DR Pfam; PF13878; zf-C2H2_3; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000297703};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 790..829
FT /note="N-acetyltransferase ESCO zinc-finger"
FT /evidence="ECO:0000259|Pfam:PF13878"
FT DOMAIN 949..1017
FT /note="N-acetyltransferase ESCO acetyl-transferase"
FT /evidence="ECO:0000259|Pfam:PF13880"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 78..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 230..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 455..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 638..739
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..39
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..142
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..187
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 230..257
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..297
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..315
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..471
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 638..653
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 680..694
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 698..716
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1026 AA; 114796 MW; B7FFFA1D0D4B5235 CRC64;
MAAQKRKSAI AESSAKRRKL DKNSKSSTKK EREVSATKHV LNKSKPNKSA MQKKAVLKIS
VKPNRSVVNK AINNCARRSS HSKLVQKHSK QSELQLKKRS SKTVPMKKSS LKSLGRVSTT
KTPSRSSKIN RTTFLKSTKT SSKTGPEGKD KCALQTKVSV ESKRQQLKST SDIKKNSSKP
QSIRQSVLQS VKTLNETTLR NIHVDMKSVK GNSTESNYST STKAVKITDK NLGIQVQSPK
KNLAKKSTSQ DAEQPSIKSF GDNKREPELG MRMSTRSSGT NTKITVKDPQ QQPKATKNKE
VCQKKSVEDI PKPRHIIIPD EQLTRRSHRL QQLSDMSARS LRNREIKEGK ASEVQQGTQT
KGCIQGTRVE TVKPLKQKTE QKNKKTKSNF ISGDEEITVG ITSSLPEKKC KMDHKTNDSN
SSQHSLHGSR LFLDHKKVEM VSPLQPTSVT INKEKQPVHQ NVKSSVKAKR VSQPPVNEKD
LANQPENVVK SKRVSILELC EEIAGEIESD TVEVKRDSPN TEYRKGEEKH AETQLSQTVM
LTQKEPNQST QCKRFFPSKK GIPVKCVLNG RNSPANKNSK WTKIKLMKAN NIHQNKLNSA
SVPKLDLLET KTKVPESSQA TGAEIQLSKA QGKLSVTKPC ENKSATHVQE KLGAVSSETV
RAKDVTPETK QPTKKVAENG LLDNRTKHVP EPTLDESFSL HLDTSPESTP VKSTTAAAPP
PKQAKKEIES ESQGSAPKQL VRTLFTNQTS ETSEKRVPLP NHSLASRCSS FLSSEQHIQK
LREAGKDDKQ LIIDAGQKRF GAISCNICGM LYTASNPEDE TQHLLFHNQF ISAVKYVGWK
KERILAEYPD GKIIMVLPDD PKYALKKVEE IREMVDNDLG FQQAPLMCYS RTKTLLFISN
DKKVTGCLIA EHIQSGYRVI EEKIPEVSSE NEKIIFERQK AWCCSTSPEP ALCGISRIWV
FSMMRRKKIA SRMIECLRSN FIYGSYLRKE EIAFSDPTPD GKLFATQYCG TGQFLVYNFL
NGQYHT
//
