ID A0A1B8XVI4_XENTR Unreviewed; 1445 AA.
AC A0A1B8XVI4;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=UBP-type domain-containing protein {ECO:0000259|PROSITE:PS50271};
GN ORFNames=XENTR_v90026096mg {ECO:0000313|EMBL:OCA14674.1};
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364 {ECO:0000313|EMBL:OCA14674.1};
RN [1] {ECO:0000313|EMBL:OCA14674.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Nigerian {ECO:0000313|EMBL:OCA14674.1};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Ottilar R., Schmutz J., Salamov A., Cheng J.F., Lucas S., Pitluck S.,
RA Gundlach H., Guo Y., Haberer G., Nasrallah J., Mayer K.F.X.,
RA van de Peer Y., Weigel D., Grigoriev I.V.;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:OCA14674.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nigerian {ECO:0000313|EMBL:OCA14674.1};
RX PubMed=20431018; DOI=10.1126/science.1183670;
RA Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J.,
RA Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., Blitz I.L.,
RA Blumberg B., Dichmann D.S., Dubchak I., Amaya E., Detter J.C., Fletcher R.,
RA Gerhard D.S., Goodstein D., Graves T., Grigoriev I.V., Grimwood J.,
RA Kawashima T., Lindquist E., Lucas S.M., Mead P.E., Mitros T., Ogino H.,
RA Ohta Y., Poliakov A.V., Pollet N., Robert J., Salamov A., Sater A.K.,
RA Schmutz J., Terry A., Vize P.D., Warren W.C., Wells D., Wills A.,
RA Wilson R.K., Zimmerman L.B., Zorn A.M., Grainger R., Grammer T.,
RA Khokha M.K., Richardson P.M., Rokhsar D.S.;
RT "The genome of the Western clawed frog Xenopus tropicalis.";
RL Science 328:633-636(2010).
RN [3] {ECO:0000313|EMBL:OCA14674.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Nigerian {ECO:0000313|EMBL:OCA14674.1};
RA Sessions A., Jenkins J., Mitros T., Lyons J.T., Dichmann D.S., Robert J.,
RA Harland R.M., Rokhsar D.S.;
RT "WGS assembly of Xenopus tropicalis.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(6)-(2E)-butenoyl-L-lysyl-[protein] = (2E)-2-butenoate
CC + L-lysyl-[protein]; Xref=Rhea:RHEA:69172, Rhea:RHEA-COMP:9752,
CC Rhea:RHEA-COMP:13707, ChEBI:CHEBI:15377, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:35899, ChEBI:CHEBI:137954;
CC Evidence={ECO:0000256|ARBA:ARBA00029357};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69173;
CC Evidence={ECO:0000256|ARBA:ARBA00029357};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(6)-acetyl-L-lysyl-[histone] = acetate + L-lysyl-
CC [histone]; Xref=Rhea:RHEA:58196, Rhea:RHEA-COMP:9845, Rhea:RHEA-
CC COMP:11338, ChEBI:CHEBI:15377, ChEBI:CHEBI:29969, ChEBI:CHEBI:30089,
CC ChEBI:CHEBI:61930; EC=3.5.1.98;
CC Evidence={ECO:0000256|ARBA:ARBA00029372};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58197;
CC Evidence={ECO:0000256|ARBA:ARBA00029372};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(6)-acetyl-L-lysyl-[protein] = acetate + L-lysyl-
CC [protein]; Xref=Rhea:RHEA:58108, Rhea:RHEA-COMP:9752, Rhea:RHEA-
CC COMP:10731, ChEBI:CHEBI:15377, ChEBI:CHEBI:29969, ChEBI:CHEBI:30089,
CC ChEBI:CHEBI:61930; Evidence={ECO:0000256|ARBA:ARBA00029349};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58109;
CC Evidence={ECO:0000256|ARBA:ARBA00029349};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; KV461323; OCA14674.1; -; Genomic_DNA.
DR RefSeq; XP_012810564.1; XM_012955110.2.
DR RefSeq; XP_012810565.1; XM_012955111.2.
DR RefSeq; XP_012810566.1; XM_012955112.2.
DR AGR; Xenbase:XB-GENE-5873935; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd10003; HDAC6-dom2; 1.
DR Gene3D; 3.40.800.20; Histone deacetylase domain; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR000286; His_deacetylse.
DR InterPro; IPR023801; His_deacetylse_dom.
DR InterPro; IPR037138; His_deacetylse_dom_sf.
DR InterPro; IPR023696; Ureohydrolase_dom_sf.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR001607; Znf_UBP.
DR PANTHER; PTHR10625:SF22; HISTONE DEACETYLASE 6; 1.
DR PANTHER; PTHR10625; HISTONE DEACETYLASE HDAC1-RELATED; 1.
DR Pfam; PF00850; Hist_deacetyl; 2.
DR Pfam; PF02148; zf-UBP; 2.
DR PRINTS; PR01270; HDASUPER.
DR SMART; SM00290; ZnF_UBP; 2.
DR SUPFAM; SSF52768; Arginase/deacetylase; 2.
DR SUPFAM; SSF57850; RING/U-box; 2.
DR PROSITE; PS50271; ZF_UBP; 2.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00502};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00502};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00502}.
FT DOMAIN 1062..1160
FT /note="UBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50271"
FT DOMAIN 1342..1440
FT /note="UBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50271"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 440..461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 870..1020
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1165..1185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1197..1234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1278..1297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 940..967
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 982..999
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1445 AA; 157282 MW; D36578AC8A255AF1 CRC64;
MASPQEPKPV APRGMRGASR SPVTPASNMG KPKKKGASPQ GSQSLQEVKK RGHRMRRTPE
KELCDQLEGL NLVAEAAVQG TGLVYDEQMA QTCCLWDENF PECPARIWAV RDKMAEYGLA
ERCVAVQARE ASEEEISLIH SPQYVALMGS TQNMNVEELQ ALSDRYDSVY LHPTSFTCAS
LAVGSVLQLV DKVLRREIRN GLAVVRPPGH HAHVDQMNGY CMFNQLAIAA RYAQRTYGAK
RVLIVDWDVH HGQGTQFLFE NDPSVLYFSV HRYENGGFWP HLRESASSAV GKERGERFNV
NVAWNKTRMS DADYIHVFLN ILLPIAYEFQ PHLVLVAAGF DSVVGDPKGE MSATPGCFSH
LTHLLMSLAQ GRLILSLEGG YNQRSLAEGV CACLKALLGD PCPKLPLPSA PCQSALDSIS
DTLSAHCRLW KVLQDYESEG EAIDEPQSAE EQPPDGADEP PLEKVLEQSM MEVMREVPAQ
RTALVYDEQM MEHHNMWDSC HPESPQRINQ IFKRHKDLGL LDRCSRIPSR LATQKELQMC
HSLSYIQKIE ASAHMKPRDL HRLGNEYNSI YINSRSYHSA RLAAGSTFSV VEAVVTGKAQ
NGVCIVRPPG HHAEPAEACG FCFFNTVALA ARYAQRLRSR SEDPLRVMIL DWDVHHGNGT
QHIFQEDASV LYVSLHRYDE GLFFPNSEDA SHDKVGIGKG AGFNVNIPWN GSKMGDPEYL
MAFHRVVMPI AYEFNPQLVL ISAGFDAARG DPLGGCQVSP EGYAHMTHLL MGLAGGRVIL
VLEGGYNLTS ISESMVMCTH SLLGDPPPTL SDLRPPKPSA FNSVRKVRQA HRKYWRSLRL
NVAPQGAHNL QHSPVRNPSQ EGRFATEAGP SAMISPQGAS PPNRIPSEET AIPLASPQRP
DSVAETPRPL VPESRFSPEE VAGPFTDPLA APQHVMPTEE VSPQKLTSPK GTSSQLVSNQ
EEPEPTATTE SPGIMLHGWQ HGTPKSPTST GTQTELMGAE SRADTAPERG ATGEKGVTPT
KQELLGEAAG GSEAGNPHIG FETLMESMAN ESGEGFAVTP LPWCPHLGSV SAVPPAGLDV
RQLCAQCASE LENWVCLTCY QVLCGRYVSQ HMLCHGLASG HHLVLSFSDL SVWCYGCESY
VHHQALFPAK SAAYSSKFGA NSQLECSQEG SAHGTPKSPP STGSQRVLMG ELEAADIAPQ
PEGDPLDVLS PGQRIGSGKE GKAPGPPSST PGERSLEQIL KDLQLSDHAG NNPTIAPANE
THLDPVGGAR RKEFISTGRD AREEEQKEGR SIQAKGVTPT KQELLGEAAG GSEAGNPHIG
FETLMESMAN ESGEGFAVTP LPWCPHLGSV SAVPPAGLDV RQLCAQCASE LENWVCLTCY
QVLCGRYVSQ HMLCHGLASG HHLVLSFSDL SVWCYGCESY VHHQALFPAK SAAYSSKFGE
EMQSM
//
