ID A0A3B4ZUT1_9TELE Unreviewed; 2612 AA.
AC A0A3B4ZUT1;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Microtubule-associated protein futsch-like {ECO:0000313|Ensembl:ENSSPAP00000005462.1, ECO:0000313|RefSeq:XP_008289024.1};
GN Name=LOC103363860 {ECO:0000313|RefSeq:XP_008289024.1};
OS Stegastes partitus (bicolor damselfish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Stegastes.
OX NCBI_TaxID=144197 {ECO:0000313|Ensembl:ENSSPAP00000005462.1, ECO:0000313|Proteomes:UP000261400};
RN [1] {ECO:0000313|Ensembl:ENSSPAP00000005462.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_008289024.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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}.
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DR RefSeq; XP_008289024.1; XM_008290802.1.
DR STRING; 144197.ENSSPAP00000005462; -.
DR Ensembl; ENSSPAT00000005574.1; ENSSPAP00000005462.1; ENSSPAG00000004240.1.
DR GeneID; 103363860; -.
DR CTD; 114799; -.
DR GeneTree; ENSGT00940000157762; -.
DR OrthoDB; 22809at2759; -.
DR Proteomes; UP000261400; Unplaced.
DR Proteomes; UP000694891; Unplaced.
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:UP000694891};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 2370..2409
FT /note="N-acetyltransferase ESCO zinc-finger"
FT /evidence="ECO:0000259|Pfam:PF13878"
FT DOMAIN 2528..2596
FT /note="N-acetyltransferase ESCO acetyl-transferase"
FT /evidence="ECO:0000259|Pfam:PF13880"
FT REGION 1..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 380..425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 559..578
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1053..1084
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1346..1373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1564..1598
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1654..1726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1807..1866
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1937..2350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..26
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..81
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..167
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..204
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..224
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..249
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..265
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..283
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..314
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..361
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..425
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1055..1075
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1346..1364
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1676..1693
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1702..1726
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1944..1963
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1974..2003
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2079..2097
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2118..2161
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2179..2215
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2225..2249
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2261..2297
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2318..2335
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2612 AA; 281301 MW; 1B2507FF7CB17B60 CRC64;
MPAPKRGPAP HDSQPKIRKL EDDGEALPSK TAPATNNQSL KTGNMQEKTA APRTKKKLSV
EGVHKPAKSS TQSSPPKDSS KTISDPPVKK AKLLKATSAS CGDAPAQRAN SKASLKRTAS
TESDDELSSD GSKVDFFRER DDEDKARCIR KYSNRVKAKR RAEESTSDPQ ENLPTAPVDP
VQMDHNYGRF SDSASIQSVD DANQSEQKES AEPLTERERQ DISDNATQEV SQETSASVKG
STNVSIKCES TAEESKHEEL QKLDSQNLID NETPASSRQT LDPVTAAAPE LPVTSEDNEK
DQAESIKIQK DVDNEAQVET LCSVTGEVSP SCGDEEQADG KTDSSDSQTD LNTQTKTNQT
TEFVSEDDKL NIRVSAAHSN VILHEAPSKE TNSAPEQLLV ESSNPESQDG ENLTTAESVG
SSDTQTDLSV KIQVTFKQES KSVHVQDQVS DTVTSSCDDV NKTVIQPEEK CEESDRKRVD
FHSTQAAACP GALVEVQLSS GSLTTDSCTE ILTPDCEAVH EQNQRELLSE CFTLPEGQIA
PGVEIHNQEN HKLYGNTAEK AAEAKEDSST EKEKDVSIEC STAPDSQIKM DIQEVSHPAV
TVETESQKGE DVSEPATNVS TNFHEDHVGE RCKTMENTVN YECVSGAEIQ NKLETRTVET
SEISNPGPAV EVQEHQEVCE PTTVISAEVP GCVTADKSNN MENFEFVSRA ESKMEMHTAA
ALEFSNPAAE VEVQSQERAE VSELTTDVPA PLEAAQCESS EDAECVAAAE NQIEVDTQTA
ATSEEVCNIA PAVGAHGQTS QVVSEPTTGV SSEFHQDHEV QNVKTVESDR VNFESVTVPE
SRSEVEQRTA VTMQVSNPAP SVEIQKNQTE VGKQTATSAP AVEMQHSDGK SKEVHRDLMI
ENCQNVKNEG KMHVECAAVQ ENLIKMEMQV TSTSEISNAA PSVEMQSEKS QNEVDMEAAS
TSEVVSNMEP AVEIQNQEIQ DVSEHATHTY TQSETVAENQ DKIEISIQSQ EVISDISEKV
QEGISIPTND CKEIKNDALI ECVSAERPVK VETQEEVTKP TTTVETQSQE GGQEVRELSA
DTEEQKDFIN AEGEDDEVRA GCVSATENQS NMDVQTTVTP GEIPEGEIQN QRCQEVSEVN
NVERDVMTSS CESEQNEDKA ASECVNVPQI QSNMETTAES SNPAAVAEQQ NHVTEDVGKH
TTVLSNEIPL ENKENDRRTE PGAEDEQVDM DAISGSIERA ASALGEETGR QVINEVKADK
SVSNIEGEGA ESNEVIVFVC GQPDDNDIVI QAAEEQIKTV NQSAAELHED QIVYEPISSP
ESNDEREVCA AERHDGLSLL DIQSADGQQT ENNASNFSDN AEDRESANPQ LDDEREICVS
DSQAVVEMEV QAMSVPESPV PAQLEQNNAT VDVKQVAVIS SSDDVSVPDG RSEDVAKKSE
RNGFPECVSA TEFSEQVRED AGVQEVADVT VTTTTAATEA EMPDSASEEY VILEPVPESD
IHFDILTQAA AESGLSASLS EEVSPDSEVE NERILIGSQQ TVSLEAEVQQ CETTDGVTDA
AVTSSGEVSQ QETGSNISPL EGDFQNIQNS NQQTSSGIMD VNTPEVEVTN SCAPGTNEDC
NEVVIENAES NLDLQEVQIL EDIEIGREIV VAEEENEEDS DITIIEKPQQ TPEAGPPKKP
EEKVNEKIKD GTNGTDLKQN STAEKTVDEK TGQEVEKPKK QEMNTQARTK ARLAALAEQK
AAASKRTANR QQLNLLALCQ EIAEDIATDS MLLKRIEEEK QAAAAAAAAT AAAAAAAAAA
AAAAAKSEAS KKERPPVSTQ DADTVNVATP AGPEGCSASA PPAEEAPDAA RSSTADPAEA
KPTAEAQKRR FFITQVSVPL KAHEKKKLTR YQRLRQVELQ REKMSWARVK KLKSDQANQM
FSDMDWQSPL SAASLFSVSP VSTTPPPAAS PSKTPPPSPA TSSKPATPKT DAPKAETPKV
EPDNTEPSKT EPTKTETPKT EPIKAEPSKT PTAKTEASKT EPPSTETRRS TRQSKAQTSK
AAAAPGPAPK VTRSAAKRTL PAVPPPMPNG LNSQKQKPEV EYKPYRPRPK YSIDDFELDD
DPLPVAPTKP NPQAAAKQLP RPSLQSNPAA QSKLLSKPTV SSQPTNQAKL KAQTIPAQSK
PTAAAPAQLK PAAPQSKAAA SSKPASSAPV KPPVSTAPQS KAVSAAGQSK PAASASPLLK
TAGASVAQLK QSTPAAAQPS VSTTSETKPA ALKADAASVP QKQPNLPSRE DGTCKATTDP
LTSASASSVA PEENSTVSDD KQQCEEKPAV TAVDPSPEKK AETVKTAEKT LEKPCQDGAA
KPQDGGTPLS DACLQKEVKK LKEADKDGTQ TIIDAGQKHF GAVACNVCGM LYSAANPEDE
SQHLLFHNQF ISAVKYVGWK KERILGEYPD GKIILVLPDD PKYALKKVEE IREMVDNDLG
FQQVETKCPS QTKTFLFISN DKKVAGCLIA EHIQEGYRVI EEPVPEGSEG EKVMFERQRA
WCCSTTPEPA ICGISRIWVV NMMRRQGIAS RMIECLRNNF IYGSYLSKDE IAFSDPTPDG
KLFATQYFGT SQFLVYNFVS GTRSSQPKTD AV
//
