ID   A0A176WHA3_MARPO        Unreviewed;       512 AA.
AC   A0A176WHA3;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   RecName: Full=AB hydrolase-1 domain-containing protein {ECO:0000259|Pfam:PF12697};
GN   ORFNames=AXG93_4421s1360 {ECO:0000313|EMBL:OAE31983.1};
OS   Marchantia polymorpha subsp. ruderalis.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC   Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX   NCBI_TaxID=1480154 {ECO:0000313|EMBL:OAE31983.1, ECO:0000313|Proteomes:UP000077202};
RN   [1] {ECO:0000313|EMBL:OAE31983.1, 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:OAE31983.1};
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 peptidase S33 family. ABHD4/ABHD5 subfamily.
CC       {ECO:0000256|ARBA:ARBA00038097}.
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:OAE31983.1}.
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DR   EMBL; LVLJ01000930; OAE31983.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A176WHA3; -.
DR   OrthoDB; 276964at2759; -.
DR   Proteomes; UP000077202; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   PANTHER; PTHR42886:SF29; PUMMELIG, ISOFORM A; 1.
DR   PANTHER; PTHR42886; RE40534P-RELATED; 1.
DR   Pfam; PF12697; Abhydrolase_6; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077202};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        200..222
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          168..456
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000259|Pfam:PF12697"
SQ   SEQUENCE   512 AA;  57133 MW;  152A926AA1CCB776 CRC64;
     MTRGKHELCR RVVPELKEAS EAGSKLPEFS LPAEASVSSF YGVFVATVVG DSGKSKPLDF
     VPQVLKRMAE KNSLQHTAAE LSADANSKSW LNAWRQCLRW SPTSKEDTVQ SEKRLLTSLV
     KTPYIQQQVN IGSGAPGARV HWFRSQSSED RFINTVTFDK GAPDTPTLVM VHGYGAAQGF
     FFRNFDALAE KFRVHAIDQI GYKVVLIQSS ILIGVGTAFV IVKRLRWGAS SRPDFTCKST
     EETESWFVDS LEEWRKEMKL GKFILLGHSL GGYVAARYAL KHPENVEHLI LVGSAGFSSE
     LDQRVLEFRS TWKGAFINYL WESNVTPQKF VRFIGPWGPQ IVRGYTGARF GTRAVGTVLD
     DNESKLLSDY IFHTLAARPS GEYCLKYIFA FGAAARLPLT QSAPDWKVPT SFIYGTEDWM
     DWKGAQKASE LMNVPTEIIR VPQGGHFVFM DNARDFHSAV FYACRKFLAT ARTSGSLSED
     VVNHLSPFVY PEKGILMKFT LACLILLSSA AV
//