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Database: UniProt
Entry: A0A176W7T4_MARPO
LinkDB: A0A176W7T4_MARPO
Original site: A0A176W7T4_MARPO 
ID   A0A176W7T4_MARPO        Unreviewed;       452 AA.
AC   A0A176W7T4;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   22-FEB-2023, entry version 22.
DE   RecName: Full=Arf-GAP domain-containing protein {ECO:0000259|PROSITE:PS50115};
GN   ORFNames=AXG93_2515s1440 {ECO:0000313|EMBL:OAE28206.1};
OS   Marchantia polymorpha subsp. ruderalis.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC   Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX   NCBI_TaxID=1480154 {ECO:0000313|EMBL:OAE28206.1, ECO:0000313|Proteomes:UP000077202};
RN   [1] {ECO:0000313|EMBL:OAE28206.1, 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:OAE28206.1};
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:OAE28206.1}.
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DR   EMBL; LVLJ01001764; OAE28206.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A176W7T4; -.
DR   OrthoDB; 389572at2759; -.
DR   Proteomes; UP000077202; Unassembled WGS sequence.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   CDD; cd08831; ArfGap_ArfGap2_3_like; 1.
DR   Gene3D; 1.10.220.150; Arf GTPase activating protein; 1.
DR   InterPro; IPR037278; ARFGAP/RecO.
DR   InterPro; IPR001164; ArfGAP_dom.
DR   InterPro; IPR038508; ArfGAP_dom_sf.
DR   PANTHER; PTHR45686:SF4; ADP-RIBOSYLATION FACTOR GTPASE ACTIVATING PROTEIN 3, ISOFORM H; 1.
DR   PANTHER; PTHR45686; ADP-RIBOSYLATION FACTOR GTPASE ACTIVATING PROTEIN 3, ISOFORM H-RELATED; 1.
DR   Pfam; PF01412; ArfGap; 1.
DR   PRINTS; PR00405; REVINTRACTNG.
DR   SMART; SM00105; ArfGap; 1.
DR   SUPFAM; SSF57863; ArfGap/RecO-like zinc finger; 1.
DR   PROSITE; PS50115; ARFGAP; 1.
PE   4: Predicted;
KW   GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00288}; Reference proteome {ECO:0000313|Proteomes:UP000077202};
KW   Zinc {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-ProRule:PRU00288};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00288}.
FT   DOMAIN          10..140
FT                   /note="Arf-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50115"
FT   REGION          191..258
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          275..324
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          367..388
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        275..319
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   452 AA;  48804 MW;  A45E6DDA3EB57BE7 CRC64;
     MASEEPLDRD ALFRKLRAKS ENKVNEAFAS RYSYEALMCF DCNAKNPTWA SVTYGVFICL
     DCSALHRSLG VHISFVRSTS LDSWNQDQLK LMSFGGNGRG RVFFKQHGWT DGGKIESKYT
     SRAAELYRQL LIKEVQKSSS LSAAAFAAAA ASSAVSEPDF FPSFDSPKQV NGHNDERKGE
     ERELFFEQAA SAPAPVARPT PSSATRKPPV LGARKLTGGK VGGGLGVRKL TTKSSDSIYD
     QKPVEPPPEP VVSSTNSVVQ SAPRASRFVY TDDQVSNTSS SATGHVSAPS TAGDFFNEFG
     SNSDNRRQTG SSSRAKVQIE DSGEAQKKFA NAKSISSAQY FGDQNKAGDS ESQVRLQKFA
     SSNAISSDDF FDRDEGGGSP SAVDLSPSEL MNKLTQQDSK AGRQNVSSEL KNFTAFQASQ
     DMSTLKNLAG ETGKKLTSIA SSLMADLQDR IR
//
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