ID A0A3Q2CQJ7_CYPVA Unreviewed; 3604 AA.
AC A0A3Q2CQJ7;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Microtubule-associated protein futsch-like {ECO:0000313|Ensembl:ENSCVAP00000007861.1};
OS Cyprinodon variegatus (Sheepshead minnow).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Cyprinodontidae;
OC Cyprinodon.
OX NCBI_TaxID=28743 {ECO:0000313|Ensembl:ENSCVAP00000007861.1, ECO:0000313|Proteomes:UP000265020};
RN [1] {ECO:0000313|Ensembl:ENSCVAP00000007861.1}
RP IDENTIFICATION.
RG Ensembl;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_015231167.1; XM_015375681.1.
DR STRING; 28743.ENSCVAP00000007861; -.
DR Ensembl; ENSCVAT00000002597.1; ENSCVAP00000007861.1; ENSCVAG00000009558.1.
DR GeneID; 107085392; -.
DR KEGG; cvg:107085392; -.
DR GeneTree; ENSGT00940000157762; -.
DR OMA; METPENC; -.
DR OrthoDB; 22809at2759; -.
DR Proteomes; UP000265020; 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:UP000265020};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 3366..3401
FT /note="N-acetyltransferase ESCO zinc-finger"
FT /evidence="ECO:0000259|Pfam:PF13878"
FT DOMAIN 3520..3588
FT /note="N-acetyltransferase ESCO acetyl-transferase"
FT /evidence="ECO:0000259|Pfam:PF13880"
FT REGION 1..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 153..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 376..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 603..647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 689..720
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1072..1095
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1794..1824
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2097..2126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2486..2564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2616..2666
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2697..2790
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2821..2894
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2955..3372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..28
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..62
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..134
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..210
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..231
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..270
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..295
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..325
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 383..408
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 614..647
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 694..720
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1081..1095
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2486..2511
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2512..2540
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2709..2767
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2855..2884
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2982..2997
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3039..3063
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3132..3280
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3309..3338
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3339..3372
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3604 AA; 394519 MW; 286E4C777E13337B CRC64;
MPASKRESSP HEPQSKMRKV EEDGEELQSK TGPTTNALQT GVEQEKTGTP RAKKKRSSSV
EDGNELLKPS SPSSDSIATP SDPPLKKAKL LKATSASCGE VLSQRENSKG SLKRSASTES
DEEPSSDRSK VDFFREREDV DKTCCIKKYS NKAKRTVEEG SFDPPDTSHD SSSPPPDSVQ
IEHNYGRYSE SASSKSLSDT DEKKETSVEA LQRASTDVLT SETGRLDSTT EEMQQLELKH
QHHETSLTET VGRAASEDEE KRDKVRSAEI PKGQNNETLS SSEETLGSFP GDVISSSGRE
NLEPRRTDSS HRLEDHTHHT QTTVGLKESE TRSLIETNFS SLQVEICSPA AEEMVTKAES
FAVSETRLKK ESNPVANKHN FPVRDDCLGE DLNKTNENSE EKLKESSGEK IDFQYPQSVT
DSDISVKEQQ NHSFVIQGTQ SDIQNTLVKN ETEELSENII VPATQITSGE DIHSQENHTV
QESMFQMDSS NRDKNNITIL HQAVVPKIKD EEILLASNPS ATIVSQIQDS TANLSTNFQS
EENVKIVANK ETFSEAEGGS KTEIQIGITS EILNPDPPEE MQKLELHVRE SPTLVSIQIH
HHVTDGDSEN METPGGGEKN QGQSGMETRP AATSELFEQE SDVQQDSECT TAVLDESGKD
SNSTKSAEGF SAMGENLPEV DIQTLNVSKQ ASDRTLMEES HSPIKHLASE PSTDTPDEAQ
RDLEKANCAG GTLIEVLGKN TAMSEPELAK ATIEETEPQL SDKLTSDRLN EAKTTNDPAP
TQIQDVEAAG SMEEISNIAS VEERQRQLFI EPITEIGDEA YRDQGGLGAD QTQINVNTFS
ETPEEVPKIA AKQEMQTQCV RERTTDMPEE IHKDHHGQTG TIETQIQVDA SSEKTPFTEE
MQTQQVTGPI NQEKDHVNLE NANCRISVDL AAAESHRTDN TEVLASSQTG FTFTSIEMET
QMVNETPTDI PKEAMEELSN MSGASQGQME DGLEASGSKD GVCNVSVAEM ENQLFTEIPI
EAYRDQGGPC VTQAQIAVNE LSLTKSEEVS NIAPIEEIQN QSVRESFIEI PAKSPKDQDG
PNGTAKMQSQ VDSPSEETVL FKEMQAHLIS EPTIDDKAHE NLKNAHCGIS IHAASESDRE
GGTEALATSH TVSTVIEEME TQAVNEQLIE APIEAEKSLE TEQYAAQTEV EVTSEKIPND
ARVEETQTQD KPNIDVSNEI HNHLGNADSR SSENVACVST QAKLEAAEEI VATPNEGSTD
VHIEGIQRQL VSETTSDISY MVHEDVDTNF AAQTLVEVQA MSQKVTNVSP VEEMQTQLVS
KCIISIQDEA NENLENPNSA AEEDVQCGST AGQSRIQPDR EVLCTSVNIS ISSSVEEMQT
QPVFETTTGI PCEPNEYQGN LSHESILDFK CISAAEQSEL QADRKVASNC PLTEEIQTQL
VSEPDKTQKE VAETSEMPAQ LVSEPATSLP PRAQIDLGDI KCAVETQVGV DVTSEKRSNI
GSFEEMQTQL VSEPFVGTLN EAHQVHKTLG HPNSLDVTYG PNTVQNIAEP DGEVLVPSSK
VSDLSHIEKM QMQTVYEPTT EISSEAPEIA TCSALLAEAA DSTREVCTIA LRDEIQSQTI
LEPNPEIATQ HLIENENKVK VEIMTATKRQ IEVDTTVTKE SPVSPSPSDT NKDQTEFVME
TPENCSHIGS VVEPLSEENH NLSEQTAGED FDAHDAMMIE TDQNVKKEEN GCKEHLSVQD
DTVQSEIQLI SAPEDFTETP LVEMQREKSK NEIEILNTVS PAVEIQNQMW KDKNTDSTPV
TVTDNEMDTI SDSLPKTFTP PSASETNKQI QLMIDATESE SNTNKGNQDE TETVKRIFID
GNPVEMVKHT TQPLEEMFQP TTIIDTKTQK SLDASETAQD SNMCDENLSK TFEEPVGIEG
NLTQTELQTP TSLEDISNAA AKVQTENQKA QQDIGLSFLP ATPETNNQRG LEVTEVAKRV
KDGEKKAVEE YSGIVDNPVE MQAVPHEEIF QQTSKGKTEN QKCIDVTNPV TLISENIPES
FRIPTNECEE NENWVSEEYV SISKSPDEMK IQTPAEKICD ENNKNVIESL RSIAPEEQEM
QTTEGPEEIS PSTVTEQRHS WRSQEVPELT SYTRSLVSSL PPEAELQQSL NADEENDDRV
FRENLAISET PEEMEKNSQV PEGNYHQSFI ENTQSQRVQV SELPQDTKAG DDTIPAESEQ
SIICVNGQIS RPFYASETPS ETYFQESDVH LQQQRNKEAD KECKEENKVT SLCENVQEAE
TKMETSAETV EIPPLATVAE QRNHLSEEIH DTKDISNEEP LPVFNLENNA NASKLEAIAE
DVETRRQLTD EAIVERSVTN PQEGAALVDG QHDEFGSIIQ ASEDEIRTVN DTEVRFSDSQ
VVYEPISSPE SNSGGEVYTK IDLGESISVL DIQNTESPLL LGAKGDFSTQ EVKVVVHPQL
EDKEEITVPD SQVTVEMEVQ TVSEAKGATH AQLEQSNATS NASSVDISTT DGKSEDSAHK
SERSAIPDYR SEELLENSKQ VQEEDGLQGA PPQSEVEIPD GASEEYVILE PVPVGEFHLD
ILTQAAAESG LSSSLSDSGL VGKDSDESIL NVSQKRGLEE ANDGFKNAAV DRSGEVLPQD
LKNAQNSEHK NAEMSNAEAK HSAEDGKAVV LENAEVNLDL QEVQMLQDIE IGREIVVAEE
DDEEDDDVKI IKPSEQATED PPKKSEEKVE DKNKEEISST LKEKAKTEDD KKGPEVEKPK
KQEMNTQART KARLAALAEQ KAAESKRAAQ RQQLNLLALC QEIAEDIATD SMLLKRIEEE
KQAAVAAAAK AEATKREQPA VNLQDAEPDN VATPAGLEAS STSVIPAPES SAPHPSSTDS
SETKPAAEPP KRRFFISQVS VPLKAHEKKK LTRYQRLRQV ELQREKMSWA RVKKLKSDQA
NQMFSDIDWQ APFSSSFLMG PVTTPPPPAA ASQSTSSPAS PAPASKPAPP KPETPKAEPV
ATEPAKMENS PTPSPEPETA KTKPSKKGAA KAPPVKAETT KPATQTVETR RSTRQSKAQA
SQAAAAATVP APKVTRSTAK RSLPAVPPPM PNGLKAQKPK PVEYTPYKPR PKYSPDDFEL
DDDDMLLVAP KKPNQPSQQL RPGIPAQRPI TSLKPTASPQ LPNQAKLKAQ TALPGQSKPS
AATQAQIKPA QTKPTVTAPQ SKATTAVTSK LAPSVGTVPK SISTAAQPKP AAPSSMLSKA
ASTSVTKSKQ PATRGVQLSE SKHSVTSAPQ KSQSPQTQEE NKPKDAADSS SPVPASAVAP
EDSAKLSNRT CEEIPSVSTA DSIPGSNTEL AMTEEKTSTE PSKSGEEKPP DGASPQEGDK
EGTEKDAEQK HFGPDACSIC GMLYSPANPE DESQHLLFHN QFISAVKYVG WKKERIMAEY
PDGKIILVLP DDPKYALKKV EEIREMVDND LGFQQVETKY PSKTKTFLFI SIDKKVAGCL
IAEHIQEGYR VIEEAPPEGS EGEKVMFERQ RAWCCSTTPE PAICGISRIW VVGMMRRRAI
ATRMIECLRN NFIYGSYLSK DEIAFSDPTP DGKLFATHYF GTSQFLVYNF VSGTRSIQPK
TGSV
//