ID A0A0D1C349_USTMA Unreviewed; 836 AA.
AC A0A0D1C349;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KIS68117.1};
GN ORFNames=UMAG_03696 {ECO:0000313|EMBL:KIS68117.1};
OS Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX NCBI_TaxID=237631 {ECO:0000313|EMBL:KIS68117.1, ECO:0000313|Proteomes:UP000000561};
RN [1] {ECO:0000313|EMBL:KIS68117.1, ECO:0000313|Proteomes:UP000000561}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=521 / FGSC 9021 {ECO:0000313|Proteomes:UP000000561};
RX PubMed=17080091; DOI=10.1038/nature05248;
RA Kamper J., Kahmann R., Bolker M., Ma L.J., Brefort T., Saville B.J.,
RA Banuett F., Kronstad J.W., Gold S.E., Muller O., Perlin M.H., Wosten H.A.,
RA de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G., Snetselaar K., McCann M.,
RA Perez-Martin J., Feldbrugge M., Basse C.W., Steinberg G., Ibeas J.I.,
RA Holloman W., Guzman P., Farman M., Stajich J.E., Sentandreu R.,
RA Gonzalez-Prieto J.M., Kennell J.C., Molina L., Schirawski J.,
RA Mendoza-Mendoza A., Greilinger D., Munch K., Rossel N., Scherer M.,
RA Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B., Meng S.,
RA Ho E.C., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J., Deelstra H.J.,
RA Ortiz-Castellanos L., Li W., Sanchez-Alonso P., Schreier P.H.,
RA Hauser-Hahn I., Vaupel M., Koopmann E., Friedrich G., Voss H., Schluter T.,
RA Margolis J., Platt D., Swimmer C., Gnirke A., Chen F., Vysotskaia V.,
RA Mannhaupt G., Guldener U., Munsterkotter M., Haase D., Oesterheld M.,
RA Mewes H.W., Mauceli E.W., DeCaprio D., Wade C.M., Butler J., Young S.,
RA Jaffe D.B., Calvo S., Nusbaum C., Galagan J., Birren B.W.;
RT "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT maydis.";
RL Nature 444:97-101(2006).
RN [2] {ECO:0000313|Proteomes:UP000000561}
RP GENOME REANNOTATION.
RC STRAIN=521 / FGSC 9021 {ECO:0000313|Proteomes:UP000000561};
RA Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Protein modification; protein sumoylation.
CC {ECO:0000256|ARBA:ARBA00004718}.
CC -!- SIMILARITY: Belongs to the PIAS family.
CC {ECO:0000256|ARBA:ARBA00005383}.
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DR EMBL; CM003149; KIS68117.1; -; Genomic_DNA.
DR RefSeq; XP_011390170.1; XM_011391868.1.
DR AlphaFoldDB; A0A0D1C349; -.
DR SMR; A0A0D1C349; -.
DR STRING; 237631.A0A0D1C349; -.
DR EnsemblFungi; KIS68117; KIS68117; UMAG_03696.
DR GeneID; 23564086; -.
DR KEGG; uma:UMAG_03696; -.
DR VEuPathDB; FungiDB:UMAG_03696; -.
DR eggNOG; KOG2169; Eukaryota.
DR InParanoid; A0A0D1C349; -.
DR OrthoDB; 20246at2759; -.
DR UniPathway; UPA00886; -.
DR Proteomes; UP000000561; Chromosome 10.
DR GO; GO:0061665; F:SUMO ligase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016925; P:protein sumoylation; IBA:GO_Central.
DR CDD; cd16792; SP-RING_Siz-like; 1.
DR Gene3D; 2.60.120.780; PINIT domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR023321; PINIT.
DR InterPro; IPR038654; PINIT_sf.
DR InterPro; IPR031141; SIZ1/2_SP-RING.
DR InterPro; IPR004181; Znf_MIZ.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR10782:SF97; SUPPRESSOR OF VARIEGATION 2-10, ISOFORM I; 1.
DR PANTHER; PTHR10782; ZINC FINGER MIZ DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF14324; PINIT; 1.
DR Pfam; PF02891; zf-MIZ; 1.
DR PROSITE; PS51466; PINIT; 1.
DR PROSITE; PS51044; ZF_SP_RING; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000000561};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00452}.
FT DOMAIN 161..323
FT /note="PINIT"
FT /evidence="ECO:0000259|PROSITE:PS51466"
FT DOMAIN 352..437
FT /note="SP-RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51044"
FT REGION 144..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 435..539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 579..600
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 613..679
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 776..836
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..484
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 515..539
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 579..593
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 661..679
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 776..796
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 836 AA; 88811 MW; 799E8CDBA051BD6F CRC64;
MATEVASGGF AEYALLVEAL RSLTVAQAKA LIKDLNNEPE AVCGYIALSG NKIDLINRLI
AALTERRNQG DIRGYQKFHA LILRYKGPPI PAYRNGSFPL PPIPRSATTN ASAGTYGGYS
ATGAYAAHPQ RLGVTPTNRA PSITPSYHSP PISTATTTTA TASLPSRPVG PAGSTRINFR
PSPFYEIKQF VSSIVQCPEA PTQSDRKNVP FFVNLTTEQA DQLRTSKYQL RLFCTTVEAH
AASLSGRNPA TVEFPLTCEV RVNSQPLSIN LRGSKKQAGR VPPPNLNKDS MLALKAGRPN
RIDLTYTNAP KRHVLVAAIC EITTVETLVE HLRSRQLRSK EEVLLKMRRE AEDDDIEQGA
ATMSLKCPFS YMRITTPCRS VNCLHVQCFD AYSFFSINEQ TPSWACPVCQ KTIKPEDLLM
DGYVDEILKK VPHDEESVII EPDGSWRTSD GKISSSGSAQ ATPAADGTSL VEDRSQTQSL
EDVKPGNAKP NGAGRASRDD IVVLDSPSPP PETTVPSISA STSATGPTQP PVVAASSSSC
SVETRTAPSV QASTLAVGAT TAPSVLTSSA AMGVNASTSN APPSHNGVVP TPSASHSAGG
LALAPRCEHT ETLDSSTTMG AHNAPTVGVG EGGVIDLTLD SDDEDSEPSV PRRPAPSIDA
HPNPLSNSMN SGYLGHHSIS SNNNRGGGFA NYASKATSMS ARIDPFASAM SRVEATPEDE
QIRRPGKRPR IEAIPTPNDP RLVKGVRPVE RERRSSLDAL PASYLDVGIN GINGSQSNGR
GYEAANTTSN GGGTRADGNS AAARGASGED DGDDSWMDNA NTSDHDQYIN EEDWWA
//
