ID A0A2A9NH10_9AGAR Unreviewed; 415 AA.
AC A0A2A9NH10;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=CTLH domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=AMATHDRAFT_147869 {ECO:0000313|EMBL:PFH49348.1};
OS Amanita thiersii Skay4041.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Pluteineae; Amanitaceae; Amanita.
OX NCBI_TaxID=703135 {ECO:0000313|EMBL:PFH49348.1, ECO:0000313|Proteomes:UP000242287};
RN [1] {ECO:0000313|EMBL:PFH49348.1, ECO:0000313|Proteomes:UP000242287}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SKay4041 {ECO:0000313|EMBL:PFH49348.1,
RC ECO:0000313|Proteomes:UP000242287};
RG DOE Joint Genome Institute;
RA Hess J., Skrede I., Wolfe B., LaButti K., Ohm R.A., Grigoriev I.V.,
RA Pringle A.;
RT "Transposable element dynamics among asymbiotic and ectomycorrhizal Amanita
RT fungi.";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in the proteasome-dependent degradation of fructose-
CC 1,6-bisphosphatase. {ECO:0000256|ARBA:ARBA00002343}.
CC -!- SIMILARITY: Belongs to the FYV10 family.
CC {ECO:0000256|ARBA:ARBA00010615}.
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DR EMBL; KZ302032; PFH49348.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A9NH10; -.
DR STRING; 703135.A0A2A9NH10; -.
DR OrthoDB; 1429623at2759; -.
DR Proteomes; UP000242287; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0045721; P:negative regulation of gluconeogenesis; IEA:UniProt.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR CDD; cd16659; RING-Ubox_Emp; 1.
DR InterPro; IPR013144; CRA_dom.
DR InterPro; IPR024964; CTLH/CRA.
DR InterPro; IPR006595; CTLH_C.
DR InterPro; IPR045098; Fyv10_fam.
DR InterPro; IPR044063; ZF_RING_GID.
DR PANTHER; PTHR12170:SF2; E3 UBIQUITIN-PROTEIN TRANSFERASE MAEA; 1.
DR PANTHER; PTHR12170; MACROPHAGE ERYTHROBLAST ATTACHER-RELATED; 1.
DR Pfam; PF10607; CTLH; 1.
DR SMART; SM00757; CRA; 1.
DR SMART; SM00668; CTLH; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50897; CTLH; 1.
DR PROSITE; PS51867; ZF_RING_GID; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000242287};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU01215}.
FT DOMAIN 164..230
FT /note="CTLH"
FT /evidence="ECO:0000259|PROSITE:PS50897"
FT DOMAIN 326..400
FT /note="RING-Gid-type"
FT /evidence="ECO:0000259|PROSITE:PS51867"
FT ZN_FING 326..400
FT /note="RING-Gid-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01215"
SQ SEQUENCE 415 AA; 46986 MW; A5F39617421838DF CRC64;
MANKLNVDGV LLLEQPFARV PYENYRKIFR TSQKYIEKEL GALQATSAEF VKNNAAASVR
MGDVEESVKT IECMIGRVEN LKRKLSNLQE TAARPTQDVM RERLQHLATI DAAPSSCSPD
FSRWAETRLD RWLVDWSLRN GKEKTARQLA KEKDIETLVD IDLFTDIRRI EEALRHHSCT
EALAWCNENK ASLRKMKASF LPPPPSSLTL EFDLRLQEYI ELTRARKSME AISYAKRHLV
QWQETHYNEI LHANALIAFD PSTTCLPYKR LFDPSRWSTL IQSFRQTAYS LNTLPTEPLL
NLALYAGLAS LKTPACYDPS TKNVDCPVCD GETRDAGIGS HHGEVPLSHH ENSTIVCRIS
GKIMDDVNMP MAFPDGQVYS REALEEMAAR DGGIVTCPRS GNKCEFSALR KVFIS
//
