ID A0A176VG14_MARPO Unreviewed; 605 AA.
AC A0A176VG14;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OAE19322.1};
GN ORFNames=AXG93_1860s1320 {ECO:0000313|EMBL:OAE19322.1};
OS Marchantia polymorpha subsp. ruderalis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX NCBI_TaxID=1480154 {ECO:0000313|EMBL:OAE19322.1, ECO:0000313|Proteomes:UP000077202};
RN [1] {ECO:0000313|EMBL:OAE19322.1, 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:OAE19322.1};
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the OXA1/ALB3/YidC (TC 2.A.9.2) family.
CC {ECO:0000256|ARBA:ARBA00010583}.
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:OAE19322.1}.
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DR EMBL; LVLJ01003902; OAE19322.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A176VG14; -.
DR OrthoDB; 1215197at2759; -.
DR Proteomes; UP000077202; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032977; F:membrane insertase activity; IEA:InterPro.
DR GO; GO:0051205; P:protein insertion into membrane; IEA:UniProt.
DR CDD; cd20069; 5TM_Oxa1-like; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR InterPro; IPR001708; YidC/ALB3/OXA1/COX18.
DR PANTHER; PTHR12428:SF67; ALBINO3-LIKE PROTEIN 2, CHLOROPLASTIC; 1.
DR PANTHER; PTHR12428; OXA1; 1.
DR Pfam; PF14559; TPR_19; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS50005; TPR; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000077202};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 208..231
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 277..300
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 320..344
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 365..390
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REPEAT 478..511
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
SQ SEQUENCE 605 AA; 67540 MW; FB1E3644D513DE42 CRC64;
MSGIASRHAR RLLAAGLFPA HHLSRTTGFC ALADQRRLYR GNAEREKVCR NRHYSYASRI
LIPQQCSSMD AAFWFVPIRG FAWWSRGSGY NSETGADSKI KSDHHLESVT GSLHRSQPDQ
SEMLTDDSSV NTLLTGEDLD ANTWERAGEV PKLDIPAESL KTSQAGAELL ETVTNESLAT
SIWSILRLPA DGVVVLVDGV HNMTGAPWWL TIVGSTLAFR ATIFPFTITY IKKSAQFASS
ISLLPPIRPP PESGKTFAEQ YRVFTKRRLE LGVPSPFWAI AGLAQAPLFL YWIIALRGMA
MASHPGFETG GVLWFSNLTV PVQGALGALF PTLVALTYFI NVQVSFRTMK PSNDVTGFFM
KIYQWWLEAM TIPLFLMGFY LPQGVFMYWL TNNTFNLLQS LALQNESFRS TFGLPLLSEM
EKLRSKQQSQ SAESESINPE LLDLDGLLSA ATQCVANDRD LEAVNLLKFA LEKYPDEPEA
YNVYGMLHIK KRQWSEALEY YSLVISKARD DPPRITALMG SGIALYNQGR RGEAVDVMRP
LMDMNVPEEP VLRVKYLRAL VTLSSAMSQE GLKDEALSVL EAAAKWDSSI NVYVEELKKE
VLSSK
//