ID K1X760_MARBU Unreviewed; 718 AA.
AC K1X760;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=RING finger domain containing protein {ECO:0000313|EMBL:EKD20931.1};
GN ORFNames=MBM_00044 {ECO:0000313|EMBL:EKD20931.1};
OS Marssonina brunnea f. sp. multigermtubi (strain MB_m1) (Marssonina leaf
OS spot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Drepanopezizaceae; Drepanopeziza.
OX NCBI_TaxID=1072389 {ECO:0000313|EMBL:EKD20931.1, ECO:0000313|Proteomes:UP000006753};
RN [1] {ECO:0000313|EMBL:EKD20931.1, ECO:0000313|Proteomes:UP000006753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MB_m1 {ECO:0000313|EMBL:EKD20931.1,
RC ECO:0000313|Proteomes:UP000006753};
RX PubMed=22876864; DOI=10.1186/1471-2164-13-382;
RA Zhu S., Cao Y.-Z., Jiang C., Tan B.-Y., Wang Z., Feng S., Zhang L.,
RA Su X.-H., Brejova B., Vinar T., Xu M., Wang M.-X., Zhang S.-G.,
RA Huang M.-R., Wu R., Zhou Y.;
RT "Sequencing the genome of Marssonina brunnea reveals fungus-poplar co-
RT evolution.";
RL BMC Genomics 13:382-382(2012).
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DR EMBL; JH921428; EKD20931.1; -; Genomic_DNA.
DR RefSeq; XP_007287933.1; XM_007287871.1.
DR AlphaFoldDB; K1X760; -.
DR STRING; 1072389.K1X760; -.
DR GeneID; 18755979; -.
DR KEGG; mbe:MBM_00044; -.
DR eggNOG; KOG2164; Eukaryota.
DR HOGENOM; CLU_011811_1_0_1; -.
DR InParanoid; K1X760; -.
DR OMA; PKQELWP; -.
DR OrthoDB; 125113at2759; -.
DR Proteomes; UP000006753; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd16536; RING-HC_RNF10; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR039739; MAG2/RNF10.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR12983; RING FINGER 10 FAMILY MEMBER; 1.
DR PANTHER; PTHR12983:SF9; RING FINGER PROTEIN 10; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000006753};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 185..235
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 541..561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 567..586
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 598..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 688..718
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 718 AA; 80216 MW; B56CCA91F8768A62 CRC64;
MNPAPPNVSS SGGKSLNISS SHSPTQPQNN QIASPGFDSG SRRASSYSAP INASARNNQS
NRKQHKNSRK PRLADEDVMA ESGVMRNVNS RRGQTSITHL MSFALPPRPQ DHRNTFIRGT
GRANTYGIGS GHHSSDKARY IHANYRFIVK PNGDYKRQAA NADQHLDWND VLQILASSVS
QEASCPICLS HPVAPRMAKC GHIFCLPCLI RYMHSTDDTN PLPEKKARCK KCPICWDLVF
ISETRPVRWY TGQESPQPRE GDDVVLRLVM RQPGSTLALP RDGAESLPKT EDIPWYFAAE
VTDYARIMKG SEDYMQEQYD AEIEDLQRQE NEDELMFGEE PEWTRKAVNA VREAKKLVDG
IGHPPAIVKQ PSEKKPKKLP PIHFTEMKEE APEMYFVQNA SQLGPSMVLG PTQHSAEPPT
GPFEPHAKPS HLELKRMGQN ESHHPDAPYY FYQALLHYYL APLDIRILKS AFGNFASFPS
TLLPRVERVS TGHIMDHDLR KKTKYLSHLP DGCEVGFLEC NWTDVVSPEI LNQFKVEIER
RRQRNREKEN KEERDRVRAE KMEDDARWAN ARRKRPSTTT DTVPANSFSA FSAEDFAPSS
LDASNASPPW PTRQGSSFGP LASPSTSPSA PRTVWGTAIV SAASPETHAQ HVDHDGDDGW
LQSWEQELHA ENAQNELIAQ VQAASLNSAG DSAKQGTPGK KKKAKKITLM STTARRAA
//