ID A0A1Y1XQB2_9FUNG Unreviewed; 1086 AA.
AC A0A1Y1XQB2;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Presenilin-domain-containing protein {ECO:0000313|EMBL:ORX87923.1};
GN ORFNames=BCR32DRAFT_289038 {ECO:0000313|EMBL:ORX87923.1};
OS Anaeromyces robustus.
OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC Chytridiomycota incertae sedis; Neocallimastigomycetes; Neocallimastigales;
OC Neocallimastigaceae; Anaeromyces.
OX NCBI_TaxID=1754192 {ECO:0000313|EMBL:ORX87923.1, ECO:0000313|Proteomes:UP000193944};
RN [1] {ECO:0000313|EMBL:ORX87923.1, ECO:0000313|Proteomes:UP000193944}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S4 {ECO:0000313|EMBL:ORX87923.1,
RC ECO:0000313|Proteomes:UP000193944};
RG DOE Joint Genome Institute;
RA Haitjema C.H., Gilmore S.P., Henske J.K., Solomon K.V., De Groot R.,
RA Kuo A., Mondo S.J., Salamov A.A., Labutti K., Zhao Z., Chiniquy J.,
RA Barry K., Brewer H.M., Purvine S.O., Wright A.T., Boxma B., Van Alen T.,
RA Hackstein J.H., Baker S.E., Grigoriev I.V., O'Malley M.A.;
RT "A Parts List for Fungal Cellulosomes Revealed by Comparative Genomics.";
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ORX87923.1, ECO:0000313|Proteomes:UP000193944}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S4 {ECO:0000313|EMBL:ORX87923.1,
RC ECO:0000313|Proteomes:UP000193944};
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 (AUG-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:ORX87923.1}.
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DR EMBL; MCFG01000004; ORX87923.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y1XQB2; -.
DR STRING; 1754192.A0A1Y1XQB2; -.
DR OrthoDB; 205653at2759; -.
DR Proteomes; UP000193944; 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:UP000193944};
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 450..469
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 515..535
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 542..560
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 575..594
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 603..620
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 626..651
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1002..1022
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1028..1043
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 203..240
FT /note="MYND-type"
FT /evidence="ECO:0000259|PROSITE:PS50865"
FT REGION 52..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 315..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 400..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 673..695
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 791..872
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 886..966
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..339
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 791..821
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 829..872
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 930..958
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1086 AA; 122255 MW; 3D184CB1D85C58C7 CRC64;
MSQQINSPDK FKKRNDNENV FINIYNTNNK ATVNTASTSN SINIKELSSL SNSNKVNFNS
PSSYPSSPKN IKNKSKNNTT STVKEEIVNI NALNLSPNTT SNINTNLNIK HNSFNNSFNN
NNIANSTSST PITTPKLTPK PIPKQINQYE NINKEEAYTS LPRKKGKTVI TFNLDKKELI
PNVEKETEES NGKESNNEVS KYCPVCKAKA SFMCASCGPV IFYCSQSCQI AHWPEHQLVC
KGVKRKKSII KHKKAETILG EIIDPVVGTN VVGARNIAQI INLKRTMTLS NKSKSNLNHT
NSMTRLMDDI GEIGKDEKNE ENKENEGIGI GKGKEKENNG TDTQGTSPLI NIKTDNSYYI
IKGKGKNNDD DDNDDDILSP FNIPLSPIQK ASYKSLTNDE MNINQPLNSS ETKNNQPKKK
RRHRTSVLLA KIAEDEDFIK DLKFFFQQTY MLLKPVCLCI ILTALLIKFT RVKSGNAYPP
YVTQNAKGHY TYNDNNENEK NEYRMNMIKQ SVIDALKTIG QLILMTIIVL TLFVFNYIKT
ITGILIFMVV VVLAYFTYYA TEMLSLANNI AIDRITLAFL IWNLIIVGIM VIFWKGPLKM
QQGYLILVSI LMAFNLLSFF ETWHIIILLA LLCIWDMFAV LSPVGPLKLL LKTTESKKQE
MPALLFSLMA APPTNNNNNN NNNNNNDNNN KENKNININA NINTTNKSQK INNNILSQQK
SNSNTISNKP NLFQNIDSIE SLSRIESLNR IESLKRIENL KRNNSRGSSN PRTIKVIQTP
SEKRINRNLN HVNNSNTTLS PPQTLNVTSP ANLSPSLTSS EDDKIITEDT SYSSSAPLIN
RKKSNRNNKN SIYNIKTIHN PKNRSSYSIN PSSFQNISQI SQIQANNNSN NTNTNTNNKD
KNKDKNSLTL GPSGDIFTGV EEQERLNKRR NKNKNKNNNK NKIRRFKLFK KNKNKKKKSK
KEIMEDQEEE IQREGIKLGL GDFVFYSVLV GTAAKIDIVT TINCFVAVVT GLTMTIILLA
IFRKALPALP ISIIFGLIAY ILSDKVNMLI ISLTSTYNDV MNDITKAIVG GYYLEVGNIG
TGYYYI
//
