ID A0A5J4ZDM7_9ASTE Unreviewed; 993 AA.
AC A0A5J4ZDM7;
DT 11-DEC-2019, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 1.
DT 27-MAR-2024, entry version 12.
DE RecName: Full=BACK domain-containing protein {ECO:0000259|SMART:SM00875};
GN ORFNames=F0562_016801 {ECO:0000313|EMBL:KAA8516693.1};
OS Nyssa sinensis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; Cornales; Nyssaceae; Nyssa.
OX NCBI_TaxID=561372 {ECO:0000313|EMBL:KAA8516693.1, ECO:0000313|Proteomes:UP000325577};
RN [1] {ECO:0000313|EMBL:KAA8516693.1, ECO:0000313|Proteomes:UP000325577}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J267 {ECO:0000313|EMBL:KAA8516693.1};
RC TISSUE=Leaf {ECO:0000313|EMBL:KAA8516693.1};
RA Yang X., Kang M., Yang Y., Xiong H., Wang M., Zhang Z., Wang Z., Wu H.,
RA Ma T., Liu J., Xi Z.;
RT "A chromosome-level genome assembly of the Chinese tupelo Nyssa sinensis.";
RL Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May act as a substrate-specific adapter of an E3 ubiquitin-
CC protein ligase complex (CUL3-RBX1-BTB) which mediates the
CC ubiquitination and subsequent proteasomal degradation of target
CC proteins. {ECO:0000256|ARBA:ARBA00002668}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the BUD31 (G10) family.
CC {ECO:0000256|ARBA:ARBA00005287}.
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 EMBL; CM018051; KAA8516693.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5J4ZDM7; -.
DR Proteomes; UP000325577; Miscellaneous, Linkage group lg8.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR CDD; cd18186; BTB_POZ_ZBTB_KLHL-like; 1.
DR Gene3D; 1.25.40.420; -; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 2.
DR InterPro; IPR011705; BACK.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR001748; BUD31.
DR InterPro; IPR006553; Leu-rich_rpt_Cys-con_subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR PANTHER; PTHR19411:SF0; PROTEIN BUD31 HOMOLOG; 1.
DR PANTHER; PTHR19411; PROTEIN BUD31-RELATED; 1.
DR Pfam; PF07707; BACK; 1.
DR Pfam; PF00651; BTB; 1.
DR Pfam; PF01125; BUD31; 1.
DR PRINTS; PR00322; G10.
DR SMART; SM00875; BACK; 1.
DR SMART; SM00367; LRR_CC; 8.
DR SUPFAM; SSF54695; POZ domain; 1.
DR SUPFAM; SSF52047; RNI-like; 2.
PE 3: Inferred from homology;
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000325577};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 146..254
FT /note="BACK"
FT /evidence="ECO:0000259|SMART:SM00875"
SQ SEQUENCE 993 AA; 111667 MW; 39B3EF57EE12E9B3 CRC64;
MTWWFSNVSI LSKRNQRPIS RRLSVSTAEI SSWDLPTILC HQIVKIKANR NRLIEQSSYF
NGLLGGSFRE SYLDHISIQW NLETLMSVLK FMFGYPDDVT RDNFLPLFEG ALFFGVEMLI
LKCKIWLSEV TSSRGLGSMQ IQLYDLIRIW KFGLEHANDF IPELCTSYLA KNFMWAMSCN
SFGDVPYNLL LSCIKHSQLT VDSERHLCDA LQVWLASDTE RSESLSSPKG DCMDILKQIR
LSLLPLWFAA GQRQCCYFSK FADESIDNVL GIMKYPCTSS LTALGDGDLC HLRIRLTEYT
KKVDLSGCPQ FKPAILLLSM LPLSYSMDTK LRETFEQSSI NLEHLDGDQY QISWGLWSTS
SFDAVQEKCP LLSEVDLTVD ISPVIPSQVS IVSSCPATMQ RISTVNFGIN NYPSNATLSY
MSRPLLSNIT KLTLEGRIDV SDSDLQNIAE FCVSLCYLNL KGCTSVTDAG ISVLLLRCME
LHSIVACDTS FGQNSILALC STTPTVDNCA ASQIEKKHSQ SLAYKLQTLH MGGCKGINET
SLSELMSQTH MLKSLCLREI QLVDNALYSF SGSSLEMLNI SSTKVSDAAL AHIVRGNPGL
KCLKARDCHN LFQNESKTQG GEFPSSSYSC TELFFELGKT CKLEEIALGW GLSGFSMEVL
KPAIAMLRAM TVGLGGSLGH DVLKLLPTVC PFLESLILYY QVISDCIIIN IVESLRHLQV
LALCYCLGEI SSLSFKFSMP NLRKLRLERV TPWMSSDDLV ILTQNCANLI KLSLLGCRLL
NSDSQQIISN GWPGLISIHL EDCGEVTKNG VASLFNCRAI EDLLLRHNGP GIQRNFIVDA
ASKMPMLRKL SLDLCDASEG DFEIPTCEGE IMPKVKTNRV KYPEGWELIE PTLSELQAKM
REAENDPHDG KRKCEALWPI FKIVHQKSRY IFDLYHRRKE ISKELYEFCL EQSYADRNLI
AKWKKPGYER LCCLRCMQPR DHNFQTTCVC PSS
//