ID A0A176VYV6_MARPO Unreviewed; 636 AA.
AC A0A176VYV6;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 03-MAY-2023, entry version 26.
DE RecName: Full=Calponin-homology (CH) domain-containing protein {ECO:0000259|PROSITE:PS50021};
GN ORFNames=AXG93_1712s1050 {ECO:0000313|EMBL:OAE25927.1};
OS Marchantia polymorpha subsp. ruderalis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX NCBI_TaxID=1480154 {ECO:0000313|EMBL:OAE25927.1, ECO:0000313|Proteomes:UP000077202};
RN [1] {ECO:0000313|EMBL:OAE25927.1, 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:OAE25927.1};
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 -!- SUBUNIT: Interacts with F-actin. {ECO:0000256|ARBA:ARBA00011385}.
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:OAE25927.1}.
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DR EMBL; LVLJ01002271; OAE25927.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A176VYV6; -.
DR OrthoDB; 5475188at2759; -.
DR Proteomes; UP000077202; Unassembled WGS sequence.
DR GO; GO:0051015; F:actin filament binding; IEA:InterPro.
DR GO; GO:0051017; P:actin filament bundle assembly; IEA:InterPro.
DR Gene3D; 1.10.418.10; Calponin-like domain; 4.
DR Gene3D; 1.10.238.10; EF-hand; 1.
DR InterPro; IPR001589; Actinin_actin-bd_CS.
DR InterPro; IPR001715; CH_dom.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR039959; Fimbrin/Plastin.
DR PANTHER; PTHR19961:SF18; FI19014P1; 1.
DR PANTHER; PTHR19961; FIMBRIN/PLASTIN; 1.
DR Pfam; PF00307; CH; 4.
DR SMART; SM00033; CH; 4.
DR SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1.
DR SUPFAM; SSF47473; EF-hand; 1.
DR PROSITE; PS00019; ACTININ_1; 1.
DR PROSITE; PS50021; CH; 3.
PE 4: Predicted;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW Reference proteome {ECO:0000313|Proteomes:UP000077202};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 95..212
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 240..343
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 444..552
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT REGION 562..636
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 580..626
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 636 AA; 70071 MW; A5EAF7DC07E5E88E CRC64;
MEQFDAWNVG KSGVITAAEL EAGMENLNLA KPLTTAEVAK LVEEHDVDHK GGLEFESFLR
VQLELQKNGR SPAVSPQKSA FLTTAQFANV HHISASEKRA YVDHINTYLD NDPAMVKYLP
IDPTTDDLFN IAKDGVLLCK LINLAVTGTI DERAMNIKDK LNPWERNENH TLCLNSAKAI
GCSVVNIGTQ DLVEGRPHLV LGLITQIVKV QLLADINLKK TPELAELLDD MEEFEELLRL
PAEKLLLRWM NYHLKKAGYT KVVSNYSSDV KDGTAYAMLL HKLAPESCTL EPLSISDPLE
RAQAVLAQAS RIGSSKYLSA KDIVDGSPNL NLAFVAHLFR IRSGLSTDSS KFTFAELIES
DDEQDSREER AFRMWINSLG IEYVSSLFED VRDGWVLLEV LDKVSPGSVN WKGATKPPIK
MPFKKLMRYH MFYLLKNLRL KGKEVSEADI VQWANLKVRN VGKTSKMESF KDKSLASGVF
FLDLLGAVEP RVVNWNIVTS GLTEEDRKKN AMYIISVARK IGCSIFLLWD DLVEVRPKMI
LTLAASIMLW SLSSKAKVAD ASASPEKSPS VKSESAPSSP PTAPASPPPG EDVLPPLDTP
SSPPLDPPSS PPVDEPSSPP SAPPPEIAEN GHDTPS
//
