ID A0A3Q3BB98_KRYMA Unreviewed; 2490 AA.
AC A0A3Q3BB98;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 18-JUN-2025, entry version 33.
DE RecName: Full=histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184};
DE EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
OS Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000026436.1, ECO:0000313|Proteomes:UP000264800};
RN [1] {ECO:0000313|Ensembl:ENSKMAP00000026436.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2025) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-lactoyl-CoA + L-lysyl-[protein] = N(6)-[(S)-lactoyl]-L-
CC lysyl-[protein] + CoA + H(+); Xref=Rhea:RHEA:61996, Rhea:RHEA-
CC COMP:9752, Rhea:RHEA-COMP:19466, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:231527,
CC ChEBI:CHEBI:231528; Evidence={ECO:0000256|ARBA:ARBA00047411};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61997;
CC Evidence={ECO:0000256|ARBA:ARBA00047411};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR STRING; 37003.ENSKMAP00000026436; -.
DR Ensembl; ENSKMAT00000026775.1; ENSKMAP00000026436.1; ENSKMAG00000019617.1.
DR GeneTree; ENSGT00940000155364; -.
DR OrthoDB; 899at2759; -.
DR Proteomes; UP000264800; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000123; C:histone acetyltransferase complex; IEA:InterPro.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-ARBA.
DR GO; GO:0005667; C:transcription regulator complex; IEA:TreeGrafter.
DR GO; GO:0031490; F:chromatin DNA binding; IEA:TreeGrafter.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IEA:UniProtKB-ARBA.
DR GO; GO:0004402; F:histone acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0003713; F:transcription coactivator activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:TreeGrafter.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR CDD; cd05495; Bromo_cbp_like; 1.
DR CDD; cd20910; NCBD_CREBBP-p300_like; 1.
DR CDD; cd15647; PHD_CBP; 1.
DR CDD; cd15802; RING_CBP-p300; 1.
DR CDD; cd02337; ZZ_CBP; 1.
DR FunFam; 1.10.246.20:FF:000001; E1A binding protein p300; 1.
DR FunFam; 1.20.1020.10:FF:000001; E1A binding protein p300; 1.
DR FunFam; 1.20.1020.10:FF:000002; E1A binding protein p300; 1.
DR FunFam; 2.10.110.40:FF:000001; E1A binding protein p300; 1.
DR FunFam; 3.30.60.90:FF:000003; E1A binding protein p300; 1.
DR FunFam; 1.20.920.10:FF:000001; Histone acetyltransferase p300; 1.
DR FunFam; 3.30.40.10:FF:000034; Histone acetyltransferase p300; 1.
DR Gene3D; 2.10.110.40; -; 1.
DR Gene3D; 3.30.60.90; -; 1.
DR Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR Gene3D; 1.10.246.20; Coactivator CBP, KIX domain; 1.
DR Gene3D; 1.10.1630.10; Nuclear receptor coactivator, CREB-bp-like, interlocking domain; 1.
DR Gene3D; 1.20.1020.10; TAZ domain; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR031162; CBP_P300_HAT.
DR InterPro; IPR013178; Histone_AcTrfase_Rtt109/CBP.
DR InterPro; IPR003101; KIX_dom.
DR InterPro; IPR036529; KIX_dom_sf.
DR InterPro; IPR009110; Nuc_rcpt_coact.
DR InterPro; IPR014744; Nuc_rcpt_coact_CREBbp.
DR InterPro; IPR037073; Nuc_rcpt_coact_CREBbp_sf.
DR InterPro; IPR056484; PHD_P300.
DR InterPro; IPR010303; RING_CBP-p300.
DR InterPro; IPR038547; RING_CBP-p300_sf.
DR InterPro; IPR035898; TAZ_dom_sf.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR000197; Znf_TAZ.
DR InterPro; IPR000433; Znf_ZZ.
DR InterPro; IPR043145; Znf_ZZ_sf.
DR PANTHER; PTHR13808; CBP/P300-RELATED; 1.
DR PANTHER; PTHR13808:SF34; CREB-BINDING PROTEIN; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF09030; Creb_binding; 1.
DR Pfam; PF08214; HAT_KAT11; 1.
DR Pfam; PF02172; KIX; 1.
DR Pfam; PF23570; PHD_P300; 1.
DR Pfam; PF06001; RING_CBP-p300; 1.
DR Pfam; PF02135; zf-TAZ; 2.
DR Pfam; PF00569; ZZ; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM01250; KAT11; 1.
DR SMART; SM00551; ZnF_TAZ; 2.
DR SMART; SM00291; ZnF_ZZ; 1.
DR SUPFAM; SSF47370; Bromodomain; 1.
DR SUPFAM; SSF47040; Kix domain of CBP (creb binding protein); 1.
DR SUPFAM; SSF69125; Nuclear receptor coactivator interlocking domain; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF57933; TAZ domain; 2.
DR PROSITE; PS00633; BROMODOMAIN_1; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS51727; CBP_P300_HAT; 1.
DR PROSITE; PS50952; KIX; 1.
DR PROSITE; PS50134; ZF_TAZ; 2.
DR PROSITE; PS01357; ZF_ZZ_1; 1.
DR PROSITE; PS50135; ZF_ZZ_2; 1.
PE 4: Predicted;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Biological rhythms {ECO:0000256|ARBA:ARBA00023108};
KW Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW ProRule:PRU00035}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00203}; Methylation {ECO:0000256|ARBA:ARBA00022481};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000264800};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00203};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00228}.
FT DOMAIN 360..446
FT /note="TAZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50134"
FT DOMAIN 603..682
FT /note="KIX"
FT /evidence="ECO:0000259|PROSITE:PS50952"
FT DOMAIN 1101..1173
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 1321..1698
FT /note="CBP/p300-type HAT"
FT /evidence="ECO:0000259|PROSITE:PS51727"
FT DOMAIN 1700..1748
FT /note="ZZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50135"
FT DOMAIN 1763..1844
FT /note="TAZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50134"
FT ZN_FING 360..446
FT /note="TAZ-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00203"
FT ZN_FING 1763..1844
FT /note="TAZ-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00203"
FT REGION 1..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 104..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 228..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 453..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 509..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 697..724
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 818..1086
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1554..1612
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1872..1965
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2145..2205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2237..2294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2328..2476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..85
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..124
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..167
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..265
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..305
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..471
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..490
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 697..717
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 842..863
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 887..897
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 899..912
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 926..963
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1003..1013
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1023..1059
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1554..1566
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1567..1577
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1583..1593
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1884..1914
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1942..1953
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1954..1964
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2150..2170
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2237..2250
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2271..2294
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2328..2346
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2361..2373
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2378..2388
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2393..2408
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2418..2429
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2490 AA; 271061 MW; FA339DCED33C6B27 CRC64;
MAENLLDVGP PSSKRPKLNS PALSASDGQD LGSLPWDDLE NDLPDELIPN GGDMSLMGGM
PSNGGAAPGA GGPGGTPAGL GGGGASVVQD AAAKHKQLSE LLRPTGTGLN SASAQPGSMG
SQLGNPLGKS PLGQASPNSH SSPQAQKPGT PTGVAAQNSN SNTAAMGLSS TGFSQAMINN
SQGHAGLLAQ GGQPQPGQVM NGGLVPGAGR GRGNGVAGMQ YQGQTIQGAA SGPGGSGSAL
VETLTPGGQQ MGAHTTLSAA QQAGNMSKMG LGTNGSPFGA QPYGQGAAGP GQQLNPQQQQ
QLQNKAALAN SLPPFPNELK GAAVTSVPNM QLQQQQQQAA MLPLAGSGGV AVPSAGPTAD
PEKRKLIQQQ LVLLLHAHKC QRREQANGEV RACALPHCRT MKNVLNHMTH CQAGKSCQVA
HCASSRQIIS HWKNCTRHDC PVCLPLKNAS DKRTQQPMLN SPNSGLQNPM SSVGMGQPSA
PTINASTPID PSSMQRAYAA LGLPYSSQAT GQATAQQPSG QTAGAQNSQG QQQLPQQMRS
INTIGNQMTL GGGTMGVTTS EQTNLHTDSL PNTLNTNNPL LSDGSAVGSM GNLPTAAPVS
ATGTRKAWHE HVTQDLRNHL VHKLVQAIFP TPDPAALKDR RMENLVAYAR KVEGDMYESA
NSRDEYYHFL AEKIYKIQKE LEEKRRSRLQ RQINNQAPMA AQGAQQPGLP QPNALGPRPQ
NGPVSLPNMP NQIMNRMQVS QGINQFNHMT LPNTQMSPAT MGARAVSPMN HPQQMNISSV
PAVGMSPSRM PQAQGMMPGH SNLVAQTPSQ GQFMPQTQFP PGSGAVAPSN AMNVTVGPGM
GQPPAQAAVS QQQQQNANLP MNALGPQLGP QLASSQTPLH STPPPTASSA STAGGATNLP
HTQSSSRSST PTLPGPVPAP AQGATPXXXX XXXXXXXXXX XXXXXPRPTQ PQPQAELPAA
AQTQPPPQPP TTPLSQPGAS LENRVPTPAS AASAELHPQH VGTEVKTETH TDQQEFEAAG
GKIEPKTEPE DESVKKEPPD EKPEPMEVED KKPEMKTESK EEEEGGSNGT TSSSPTQSRR
KIFKPEELRQ ALMPTLESLY RQDPESLPFR QPVDPMLLGI PDYFDIVKNP IDLSTIKRKL
DTGQYQEPWQ YVDDVWLMFN NAWLYNRKTS RVYKYCSKLA EVFESEIDPV MQGLGYCCGR
KYEFSPQTLC CYGKQLCTIP TGGTYYSYQN RYHFCEKCFN EIQGDSVTLG DDPAQPQTMI
SKDQFERKKN DVLDPEPFVE CKDCGRKMHQ ICVLHYEVIW PSGFICDNCL KKSVKTRKEN
KFTAKRLQST RLGMYIEDRV NKYLKRQNHP EAGEVFVRVV ASSDKTVEVK PGMKTRFVDT
GEMPEAFPYR TKALFAFEEI DGVDVCFFGM HVQEYGSECP FPNTRRVYIS YLDSIHFFRP
RILRTAVYHE ILIGYLEYVK KLGYTQGHIW ACPPSEGDDY IFHCHPPEQK IPKPKRLQEW
YRKMLDKAFA ERILHDYKDI FKQATEDRLT SANELPYFEG DFWPNVLEES IKELEQEEEE
RKKEENTAAS ETPEGTPSDS KNAKKKNNKK TNKNKSSVSR ANKKKPGMPN VANDLSQKLY
ATMEKHKEVF FVIHLHSGPM ANTLPPIVDP DPLISCDLMD GRDAFLTLAR DKHWEFSSLR
RCKWSTMCML VELHNQGQDR FVYTCNECKH HVETRWHCTV CEDFDLCINC YNTKGHEHPM
VKWGLGLDDD SNSQSGEASK SPQESRRLSI QRCIQSLVHA CQCRNANCAL PSCQKMKRVV
QHTKGCKRKT NGGCPVCKQL IALCCYHAKH CQENKCPVPF CLNIKHKLRQ QQLQHRLQQA
QLIRRRMATM QGRTMPLPSP PASAAPSTPT SHTQPNTPQT PQQPLSNQPQ TPNSAGVMSP
SFPNAPRSVQ PQAPVSQGKP GPQASPLHQQ QSPLPQPPQP PQQRPPLAAL RMAHQIERMA
QAQQNQQNYR VNMNGLAMNP QQPQQRMAGP MQPAMQMVPG PHGPQVMQPN MAPGQWPATT
GPMQAAQTQQ PGLVPNQSPQ QVMAMQRPMM APGQQASQVQ RMLIPQQPGA RPQTPQRPST
IPPTALQDLL RTLKSPSSPQ QQQQVLNILK SNPQLMAAFI KQRTAKYANQ PQQQPPAGQQ
QQPGMPTMQT ISMPGGPVPR AGMQPQQPQQ PPVQGMASLG PQGQLMNTAH NNQQIQDLYR
RQLLRQQQQQ QQQQQQQQQQ QQQQQPQQQQ HLGQFPAQTQ GNPAMYAHLR MQQQQQQQQQ
QQQQMAMQAG TGAAAGVPMG QLPPMAQMTQ SSMGMDSTQN LLHQRLLQQQ QQAQLPQQQQ
AVLKQQMGSP AQPSPMSPQT HLLAGQAQGA AHLPSQPGLA NTLSSQVLSP APVQSPCPPT
QAQPPHSSPS PHVQNQPQPS PQHPPPPHSS SPHPGLGGPL QSMEQGHLGT PEQSAMLPQL
NTPNRGGLNN DLGMVGDATG DTLEKFVEGL
//
