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Database: UniProt
Entry: A0A176VY36_MARPO
LinkDB: A0A176VY36_MARPO
Original site: A0A176VY36_MARPO 
ID   A0A176VY36_MARPO        Unreviewed;       613 AA.
AC   A0A176VY36;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=RING-type domain-containing protein {ECO:0000259|PROSITE:PS50089};
GN   ORFNames=AXG93_4368s1780 {ECO:0000313|EMBL:OAE25718.1};
OS   Marchantia polymorpha subsp. ruderalis.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC   Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX   NCBI_TaxID=1480154 {ECO:0000313|EMBL:OAE25718.1, ECO:0000313|Proteomes:UP000077202};
RN   [1] {ECO:0000313|EMBL:OAE25718.1, ECO:0000313|Proteomes:UP000077202}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Tak-1 and cv. Tak-2 {ECO:0000313|Proteomes:UP000077202};
RC   TISSUE=Whole gametophyte {ECO:0000313|EMBL:OAE25718.1};
RA   Honkanen S., Jones V.A., Morieri G., Champion C., Hetherington A.J.,
RA   Kelly S., Saint-Marcoux D., Proust H., Prescott H., Dolan L.;
RT   "Mechanisms controlling the formation of the plant cell surface in tip-
RT   growing cells are functionally conserved among land plants.";
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OAE25718.1}.
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DR   EMBL; LVLJ01002295; OAE25718.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A176VY36; -.
DR   OrthoDB; 460116at2759; -.
DR   Proteomes; UP000077202; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd16531; RING-HC_RING1-like; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR044592; RING1A/B.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR46537; OS11G0578200 PROTEIN; 1.
DR   PANTHER; PTHR46537:SF3; RING-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF13923; zf-C3HC4_2; 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:UP000077202};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          133..173
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          252..376
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        311..353
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   613 AA;  68828 MW;  27FD723113CD794F CRC64;
     MLSGGVRGRA GGLEGPGRDV EARNAAERNV GMRGLSRPVG RWTLAGAGSG LSQPKKNWLD
     RVYIACFITR GRIAMAAQKL FGAYREQSRF RSSISWARVE LHDMADHLDS FSNGTPNEYV
     TVCLSEIRKE MQCPICLGII RKTRTVMECL HRFCRECIDK SMRLGNNECP ACRTHCASRR
     SLRDDPKFDS LIAALYPDLE KYEEEEMALL EDETRRNKQI QASIAETFKR QSEAVARRRV
     TAKATAAAIV RKAHGKFRSV QSRNRGPAPP RNSRARGSNL NGPLSPQEDS EKEVPLPDLP
     SQPPSSSADE VYKEPPKESL KDVTKEPVKE APKDRAGWRK RRRPRHVEPE NSDDEPINTQ
     NWPEEESHQE EQKLETKIVD DVSPANKGGV PSWARAGARS QTRYGSVSVG NSNVRHVNRC
     VRATALLDYL TSTARKEDED EYDIHLHLQP LTGESDDEDV LPNLERPYLC CSPNMTVHNL
     CKHLVNRLSL APGGELELLV ERISGLVVDQ VLPAKVANSR LNKLARGKTW ASRPEGGKIV
     EVLPAKYTLK YILSHCWDKR GFTVSTQVMN MSQQQRYIKE TSTDTWGSLT ELGTKFPYIG
     IMQATVGKFQ ECK
//
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