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Database: UniProt
Entry: A0A176VVV1_MARPO
LinkDB: A0A176VVV1_MARPO
Original site: A0A176VVV1_MARPO 
ID   A0A176VVV1_MARPO        Unreviewed;       723 AA.
AC   A0A176VVV1;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   13-SEP-2023, entry version 18.
DE   RecName: Full=Actin-related protein 8 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=AXG93_2931s1300 {ECO:0000313|EMBL:OAE24887.1};
OS   Marchantia polymorpha subsp. ruderalis.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC   Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX   NCBI_TaxID=1480154 {ECO:0000313|EMBL:OAE24887.1, ECO:0000313|Proteomes:UP000077202};
RN   [1] {ECO:0000313|EMBL:OAE24887.1, 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:OAE24887.1};
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   -!- SIMILARITY: Belongs to the actin family.
CC       {ECO:0000256|RuleBase:RU000487}.
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:OAE24887.1}.
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DR   EMBL; LVLJ01002458; OAE24887.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A176VVV1; -.
DR   OrthoDB; 11729at2759; -.
DR   Proteomes; UP000077202; Unassembled WGS sequence.
DR   Gene3D; 3.30.420.40; -; 3.
DR   InterPro; IPR004000; Actin.
DR   InterPro; IPR043129; ATPase_NBD.
DR   PANTHER; PTHR11937; ACTIN; 1.
DR   PANTHER; PTHR11937:SF13; ACTIN-RELATED PROTEIN 8; 1.
DR   Pfam; PF00022; Actin; 1.
DR   SMART; SM00268; ACTIN; 1.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000077202}.
FT   REGION          134..245
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        147..162
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        163..184
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        185..217
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        218..245
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   723 AA;  79928 MW;  9B27B58345A67581 CRC64;
     MDIKSVVPSQ LISERGSDVV VINFGSANLR VGIATQQTPV VVPHCIAHHL LVKEQGIDGE
     EARAKGAVGE RLEAPPAAAR RPERDEICQM VELQLKMKPL NPDFEALSKD DGLRSRSIEV
     DDDKFFHWTQ VMGEESDDEV DGPLASTKAS PATTNVVKDE SESSSLASEE KGEGENGQEL
     EEDKSVKAEE DEEEVEDEEE EEDEEEVEDE EEELEEKRDI VEQPVPDEND DSVKESPDDK
     EIPDDVPAEI AASEKGSQEG SDSGIHVEVL DDMFFIWNWV LTEKLSLDAE TRQQFSVVLV
     IPDTLDNREI KELLTIVLKD LKFRAAVIHQ ECVTATFGNG ISSACVVNMG AQITSIVCIE
     DGVALPSTRI VLPFGGEDIS RCLLWVQRRW QTWPRIDTDP LHDSLDLQML ERIKEERCVI
     VEGEQQAVVD IYYRQAGHPT RAYKAYLKAL CVPVMGLFYP TLLAPEEYPS LRPWFYVDHE
     DVLDDSFHAE TFKRPEAVES APVVFGNNGG GLAMASKPDF PMEDVDGKAA LRTDEPSHGL
     AQAVVISILS TGRADIQKKL FASIQLVGGV ALTRGLVDAV EERVLHGIPA HEAVDTVAVL
     QNRTDAPLTC WKGGAVLGIL DFQREAWVQS DEWITGGVRI GSGRKYRDSV TLQSQAFCPS
     CIMEHCGPGS VIFHVVATVN GHCHQDSSTL AQRERERAVL MTAISVRHFR VDCGDGWPMM
     GLD
//
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