ID A0A1Y2CXC9_9FUNG Unreviewed; 454 AA.
AC A0A1Y2CXC9;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Presenilin-domain-containing protein {ECO:0000313|EMBL:ORY51546.1};
GN ORFNames=BCR33DRAFT_712578 {ECO:0000313|EMBL:ORY51546.1};
OS Rhizoclosmatium globosum.
OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC Chytridiomycota incertae sedis; Chytridiomycetes; Chytridiales;
OC Chytriomycetaceae; Rhizoclosmatium.
OX NCBI_TaxID=329046 {ECO:0000313|EMBL:ORY51546.1, ECO:0000313|Proteomes:UP000193642};
RN [1] {ECO:0000313|EMBL:ORY51546.1, ECO:0000313|Proteomes:UP000193642}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEL800 {ECO:0000313|EMBL:ORY51546.1,
RC ECO:0000313|Proteomes:UP000193642};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004477}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the peptidase A22A family.
CC {ECO:0000256|ARBA:ARBA00008604}.
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:ORY51546.1}.
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DR EMBL; MCGO01000005; ORY51546.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2CXC9; -.
DR STRING; 329046.A0A1Y2CXC9; -.
DR OrthoDB; 205653at2759; -.
DR Proteomes; UP000193642; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-KW.
DR GO; GO:0042500; F:aspartic endopeptidase activity, intramembrane cleaving; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016485; P:protein processing; IEA:InterPro.
DR Gene3D; 6.10.140.2220; -; 1.
DR Gene3D; 1.10.472.100; Presenilin; 1.
DR InterPro; IPR001108; Peptidase_A22A.
DR InterPro; IPR006639; Preselin/SPP.
DR InterPro; IPR042524; Presenilin_C.
DR InterPro; IPR002893; Znf_MYND.
DR PANTHER; PTHR10202; PRESENILIN; 1.
DR PANTHER; PTHR10202:SF13; PRESENILIN-2; 1.
DR Pfam; PF01080; Presenilin; 2.
DR Pfam; PF01753; zf-MYND; 1.
DR SMART; SM00730; PSN; 1.
DR SUPFAM; SSF144232; HIT/MYND zinc finger-like; 1.
DR PROSITE; PS50865; ZF_MYND_2; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Notch signaling pathway {ECO:0000256|ARBA:ARBA00022976};
KW Reference proteome {ECO:0000313|Proteomes:UP000193642};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00134}.
FT TRANSMEM 116..134
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 187..210
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 222..244
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 272..291
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 297..321
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 391..415
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 421..444
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 6..48
FT /note="MYND-type"
FT /evidence="ECO:0000259|PROSITE:PS50865"
FT REGION 47..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 348..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..370
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 454 AA; 50358 MW; 277FB71DEECB8B37 CRC64;
MSSVPCSTCG NPALFVCSLC PSDDLASAAK YCSEACQRSH WPTHRQEHAS ATAATPAAAS
PSNQTNDYDP DCDSTALSRQ RLQQRKEPPK QEEEEAAIRV LDSDTIDDLK YYLSQIYSIV
KPVVACIIFA ILWVKLLNPP SQYYDHAYTS PPDIYALNYG GGNVNSNVTN TVINPGRETT
EQQHADLLMA LKTLGSVVAA TVVIFVLFYF NCMKVYSVWN LWFHYSWYLG LFTYSVSVSL
LWLYLVPFDY ITFFFLLWNF VAGPLILQQS YLVVMSSLMV CFIFLCIHVD NPAVPPITSW
ILLALLAVWD LIAVLCPYGP LRLLIEASQK HNREIPAILY SAGPTTMMAS PDPSRSSQGK
NQQQPNNNNT NDNDDDDEDG NGGMKLALSD WISTSSVTIA LLTGLNFTIF LLVIWRKALP
ALPFSIAFGL LFYFSTGVCL VPFYGNEARA ASSG
//