ID A0A176VFB2_MARPO Unreviewed; 958 AA.
AC A0A176VFB2;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=C3H1-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=AXG93_2742s1090 {ECO:0000313|EMBL:OAE19540.1};
OS Marchantia polymorpha subsp. ruderalis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX NCBI_TaxID=1480154 {ECO:0000313|EMBL:OAE19540.1, ECO:0000313|Proteomes:UP000077202};
RN [1] {ECO:0000313|EMBL:OAE19540.1, 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:OAE19540.1};
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:OAE19540.1}.
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DR EMBL; LVLJ01003836; OAE19540.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A176VFB2; -.
DR OrthoDB; 50760at2759; -.
DR Proteomes; UP000077202; Unassembled WGS sequence.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd00072; GYF; 1.
DR CDD; cd10567; SWIB-MDM2_like; 1.
DR Gene3D; 3.30.1490.40; -; 1.
DR Gene3D; 3.90.70.200; Plus-3 domain; 1.
DR Gene3D; 1.10.245.10; SWIB/MDM2 domain; 1.
DR InterPro; IPR003169; GYF.
DR InterPro; IPR035445; GYF-like_dom_sf.
DR InterPro; IPR004343; Plus-3_dom.
DR InterPro; IPR036128; Plus3-like_sf.
DR InterPro; IPR019835; SWIB_domain.
DR InterPro; IPR036885; SWIB_MDM2_dom_sf.
DR InterPro; IPR003121; SWIB_MDM2_domain.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR PANTHER; PTHR46695:SF5; RNA POLYMERASE-ASSOCIATED PROTEIN RTF1 HOMOLOG; 1.
DR PANTHER; PTHR46695; ZINC FINGER CCCH DOMAIN-CONTAINING PROTEIN 44-RELATED; 1.
DR Pfam; PF02213; GYF; 1.
DR Pfam; PF03126; Plus-3; 1.
DR Pfam; PF02201; SWIB; 1.
DR Pfam; PF00642; zf-CCCH; 1.
DR SMART; SM00444; GYF; 1.
DR SMART; SM00719; Plus3; 1.
DR SMART; SM00151; SWIB; 1.
DR SUPFAM; SSF90229; CCCH zinc finger; 1.
DR SUPFAM; SSF55277; GYF domain; 1.
DR SUPFAM; SSF159042; Plus3-like; 1.
DR SUPFAM; SSF47592; SWIB/MDM2 domain; 1.
DR PROSITE; PS50829; GYF; 1.
DR PROSITE; PS51360; PLUS3; 1.
DR PROSITE; PS51925; SWIB_MDM2; 1.
DR PROSITE; PS50103; ZF_C3H1; 1.
PE 4: Predicted;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00723}; Reference proteome {ECO:0000313|Proteomes:UP000077202};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00723};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00723}.
FT DOMAIN 157..240
FT /note="DM2"
FT /evidence="ECO:0000259|PROSITE:PS51925"
FT DOMAIN 301..434
FT /note="Plus3"
FT /evidence="ECO:0000259|PROSITE:PS51360"
FT DOMAIN 659..713
FT /note="GYF"
FT /evidence="ECO:0000259|PROSITE:PS50829"
FT DOMAIN 933..958
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT ZN_FING 933..958
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 43..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 477..532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 756..793
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 807..941
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..102
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 490..518
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 756..791
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 826..845
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 895..926
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 927..941
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 958 AA; 106852 MW; 055D66C75E947072 CRC64;
MIENNETTNA EGVEVDFEDQ ETYECLFKDY WVDLKQRLQL TPAELDKDKQ AAGSGGLYLE
NGESDAEDKG DVEDYNTGSD SGASGEGDDK MDTSDEAKKR KRGKAKASTI PASGDDAVMG
ADSEPYILPE EEDVMEDVEE DDVEEYTEED GDQKSDVQLR EGWASKELID FVKFMDEDPK
KPLTKFEVTK LLWAYIKSHK LQDPRKKTQI LCDERLQTLF GKKTVNQYDM IKHVQSHYTL
KGAKSRRPNM VSDEVLKMDE DPNEEGVDDK YSKIRDVKDK RRRRKGDDDK FERPSVNEYA
AITPKNINLI YLRRQLLEEL LDDPEFDSKV CSTFVRIRVP GMVSKSEMCY RLVQVVGTRL
QAEAYKAGRK TTNIVLEILN LQKREDVTVD LVSNHEFSEE ECQRLRQSIK CGLIKTLTVG
DIEDKAKDLQ EAKVNDWFET ERQRLVNLRD RANGSATILE RSPSAIGMGD KLATASNLKS
SQLESGSRPE WDSARNKHSA WVENTRNREV ERGGFESGRS GDKMAYGRVP SYSIEDTNER
GYDERDRGWD KEWVMDERDT GVGTGWMGNG RNIRSAPAER WTEKVNNISA GIDGGRAGRS
DYRGSTSLTG LTTPVYDGKA DWNKPRELPT APSMQSTFPL ASQLTSTLSK AALEAAEKEK
VWHYMDPTGT IQGPFSMEQL RKWNTTGYFP LDLRIWRTNQ PRDESVLLTD ALAGRVQKER
IDSWGSATVR AVDIASQPAL SVSALASGYN INKTSADGWR DNAGGSSSSW VDRGSSADVA
GRSTTSWGVD NGSRLGRDII SVPAVRDSSS DLKWKAGPAE TGSWDTYGVG RSNNSYGTSP
TRNSRAEAAA RFDPANWGSR SDTVRTSEKD SWTSPSPGAD GGYSKPGGGG GRSSWGRGSS
HNFRDSGGSW NSFNEDSGGG HDNSRPMKTS RGSKKDVPCR FHQKGWCKRG DSCDFWHG
//
