ID N1QIH4_SPHMS Unreviewed; 397 AA.
AC N1QIH4;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE SubName: Full=Protein FYV10 {ECO:0000313|EMBL:EMF16985.1};
GN ORFNames=SEPMUDRAFT_137717 {ECO:0000313|EMBL:EMF16985.1};
OS Sphaerulina musiva (strain SO2202) (Poplar stem canker fungus) (Septoria
OS musiva).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Sphaerulina.
OX NCBI_TaxID=692275 {ECO:0000313|EMBL:EMF16985.1, ECO:0000313|Proteomes:UP000016931};
RN [1] {ECO:0000313|EMBL:EMF16985.1, ECO:0000313|Proteomes:UP000016931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SO2202 {ECO:0000313|EMBL:EMF16985.1,
RC ECO:0000313|Proteomes:UP000016931};
RX PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA Grigoriev I.V.;
RT "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT genomes of eighteen Dothideomycetes fungi.";
RL PLoS Pathog. 8:E1003037-E1003037(2012).
CC -!- SIMILARITY: Belongs to the FYV10 family.
CC {ECO:0000256|ARBA:ARBA00010615}.
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DR EMBL; KB456260; EMF16985.1; -; Genomic_DNA.
DR RefSeq; XP_016765106.1; XM_016902852.1.
DR AlphaFoldDB; N1QIH4; -.
DR STRING; 692275.N1QIH4; -.
DR GeneID; 27899989; -.
DR eggNOG; KOG0396; Eukaryota.
DR HOGENOM; CLU_027445_2_0_1; -.
DR OMA; CHDNRSK; -.
DR OrthoDB; 1429623at2759; -.
DR Proteomes; UP000016931; 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 InterPro; IPR024964; CTLH/CRA.
DR InterPro; IPR006595; CTLH_C.
DR InterPro; IPR045098; Fyv10_fam.
DR InterPro; IPR006594; LisH.
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; SM00668; CTLH; 1.
DR SMART; SM00667; LisH; 1.
DR PROSITE; PS50897; CTLH; 1.
DR PROSITE; PS50896; LISH; 1.
DR PROSITE; PS51867; ZF_RING_GID; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000016931};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU01215}.
FT DOMAIN 162..219
FT /note="CTLH"
FT /evidence="ECO:0000259|PROSITE:PS50897"
FT DOMAIN 320..381
FT /note="RING-Gid-type"
FT /evidence="ECO:0000259|PROSITE:PS51867"
FT ZN_FING 320..381
FT /note="RING-Gid-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01215"
FT COILED 26..98
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 397 AA; 44816 MW; A69A728567BF40C6 CRC64;
MAEMSTTKLE PDTHMLLDQP LLRLTHELCR KNLKAAQRHI EQASKNVQKE VQGAATAVAG
GQPPAQTLAA LEATLAKAQT LKRKLEALHA EEQHLHRQQR ARIQHLQELH EIPNLADVKY
DNWAHARLDR LLVDYLLRQG YTQSARELAA EKEVTDLVDV DVFEDCGRIE RSLRTGRTQE
CLSWCSDNKQ ALKKLNSKLE LELRLQQFIE LARSGSQVEA IVHARKYLAS DQDPSFGLRA
AGLLAHPADT PVEPYQDMYN TDRYGYLAEH FIRTHHELFN LPTQPLIHIA LSAGLSALKT
PTCHSQFALQ ASANTGAPVC PICSTELNEL ARNVPYAHHT KSHIEDDPVV LPNGRVFGRE
RLKRLNEKLG TRSGCIKDPT NLEDEWDEKD LKKVYIS
//
