ID K5VQN7_PHACS Unreviewed; 540 AA.
AC K5VQN7;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=RING-type domain-containing protein {ECO:0000259|PROSITE:PS50089};
GN ORFNames=PHACADRAFT_154728 {ECO:0000313|EMBL:EKM49055.1};
OS Phanerochaete carnosa (strain HHB-10118-sp) (White-rot fungus) (Peniophora
OS carnosa).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Phanerochaetaceae; Phanerochaete.
OX NCBI_TaxID=650164 {ECO:0000313|EMBL:EKM49055.1, ECO:0000313|Proteomes:UP000008370};
RN [1] {ECO:0000313|EMBL:EKM49055.1, ECO:0000313|Proteomes:UP000008370}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB-10118-sp {ECO:0000313|EMBL:EKM49055.1,
RC ECO:0000313|Proteomes:UP000008370};
RX PubMed=22937793; DOI=10.1186/1471-2164-13-444;
RA Suzuki H., MacDonald J., Syed K., Salamov A., Hori C., Aerts A.,
RA Henrissat B., Wiebenga A., vanKuyk P.A., Barry K., Lindquist E.,
RA LaButti K., Lapidus A., Lucas S., Coutinho P., Gong Y., Samejima M.,
RA Mahadevan R., Abou-Zaid M., de Vries R.P., Igarashi K., Yadav J.S.,
RA Grigoriev I.V., Master E.R.;
RT "Comparative genomics of the white-rot fungi, Phanerochaete carnosa and P.
RT chrysosporium, to elucidate the genetic basis of the distinct wood types
RT they colonize.";
RL BMC Genomics 13:444-444(2012).
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DR EMBL; JH930572; EKM49055.1; -; Genomic_DNA.
DR RefSeq; XP_007402393.1; XM_007402331.1.
DR AlphaFoldDB; K5VQN7; -.
DR STRING; 650164.K5VQN7; -.
DR GeneID; 18908999; -.
DR KEGG; pco:PHACADRAFT_154728; -.
DR HOGENOM; CLU_030109_1_0_1; -.
DR InParanoid; K5VQN7; -.
DR OrthoDB; 4593171at2759; -.
DR Proteomes; UP000008370; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR047126; RNF141-like.
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; PTHR12109:SF3; RING FINGER PROTEIN 141; 1.
DR PANTHER; PTHR12109; RING FINGER PROTEIN 141-RELATED; 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:UP000008370};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 238..296
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 204..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 515..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 520..540
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 540 AA; 60571 MW; AAE420AE2C1B7E48 CRC64;
MSSFVHRRTT TARLRENPNT TSGSSSGARR PKSTASDAAV DDAPARVEPH ALRRKKSVAH
PAASGSGTQA GSVRPQRGPA PITELGEHGR KSGHRPLSRS SDVEVQVMLD PPRSQRKHGK
SKRKDRSHSR GPSDRPSVRS FNPNAQTADD AAELRHLHGS AGIEEYLKLK EELETMKKQV
SSFKKNIGKQ SKIIDDLKKE LVSAQQSHQE ERKQVKELQS RSKKHDEAIS TIEANMNCQI
CMDMLLKPYG LSPCGHVLCL SCLQNWFRTA PIADDDMHDD DPHVLLFRKK TCPVCRTAVL
GRPIPVFLIK SIAAALEKVR DNGSSSPRSS PLPEGDPWAG IFPELMSADD MWVDDEDDYL
DDDAGQDSEG EVFADAWGSD DGGDWPFDGY GTDEDEAPYE GEYLPARWAP PILDVHSDDY
PFDDINDEML SMLRRGATMP MIEIFEMSYS HDEGLRAIIG DNIVFLGWNI DLHPTDETGE
EYMEWVGADV YNHPERWDKE SNFDGTWTAW KLTREDEDVE YQPTDSDEYE PYEDTVDDLD
//