ID A0A178AQT9_9PLEO Unreviewed; 851 AA.
AC A0A178AQT9;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Phospholipase D/nuclease {ECO:0000313|EMBL:OAL00186.1};
GN ORFNames=IQ06DRAFT_317269 {ECO:0000313|EMBL:OAL00186.1};
OS Stagonospora sp. SRC1lsM3a.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Massarinaceae; Stagonospora.
OX NCBI_TaxID=765868 {ECO:0000313|EMBL:OAL00186.1, ECO:0000313|Proteomes:UP000077206};
RN [1] {ECO:0000313|EMBL:OAL00186.1, ECO:0000313|Proteomes:UP000077206}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRC1lsM3a {ECO:0000313|EMBL:OAL00186.1,
RC ECO:0000313|Proteomes:UP000077206};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KV441713; OAL00186.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A178AQT9; -.
DR STRING; 765868.A0A178AQT9; -.
DR InParanoid; A0A178AQT9; -.
DR OrthoDB; 930461at2759; -.
DR Proteomes; UP000077206; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:InterPro.
DR GO; GO:0008081; F:phosphoric diester hydrolase activity; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR CDD; cd09122; PLDc_Tdp1_1; 1.
DR Gene3D; 3.30.870.10; Endonuclease Chain A; 2.
DR InterPro; IPR010347; Tdp1.
DR InterPro; IPR003903; UIM_dom.
DR PANTHER; PTHR12415; TYROSYL-DNA PHOSPHODIESTERASE 1; 1.
DR PANTHER; PTHR12415:SF4; TYROSYL-DNA PHOSPHODIESTERASE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF06087; Tyr-DNA_phospho; 1.
DR Pfam; PF02809; UIM; 2.
DR SMART; SM00726; UIM; 2.
DR SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
DR PROSITE; PS50330; UIM; 2.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000077206};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..37
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 49..69
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 75..93
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 113..133
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 158..180
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 192..214
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 220..245
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 282..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 321..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 367..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..349
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..406
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 509
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR610347-1"
FT ACT_SITE 744
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR610347-1"
FT BINDING 511
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR610347-2"
FT BINDING 746
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR610347-2"
FT SITE 771
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|PIRSR:PIRSR610347-3"
SQ SEQUENCE 851 AA; 94686 MW; EE0B18AC72F34271 CRC64;
MTAHDILPSH VDPSLRNVNE VLLGTGGIGY TICYVLMTRQ SLRDRTYAMP VFSLAFNFAW
EIIFAMYVAD EAREKAIFAI WMLIDLGLVY AVVQYGANEW KHAPAVARNI GKIFAAMLAW
WCIILYAVSG WWLNPANPIN PKEGKIHKGV KGIDTDELGF WTALVAQVVL SISSLAQIMI
RGDSRGSSYG IWLTRFVGSI AGLNANYGYC WWVWPEAHGY VAYPVAVVMM VTWVLADLGY
LVVLLNIGKS HQSSLGFWLH MANLDDDDDL KMALALSMRQ SPAGGSAKDA IDLTSENEIE
DDDDDMRRAI ALSLQASRKS SSPEVASVSK SVLQPAMSHT PSATTLTRPF GISGIDRKAM
EEERLARLSK RKREQSPDRP LKQTTKMQAA QKTKPSQSSR AALPQNATLQ YPKGAIKRTF
AKGYPRTDDV TIEEVLQAGS LNIAVISSFM WDAEWLNKKL NPITVKQIWI MNAKGQDVQQ
RWRREMDEAG YPKTLRIHFP PMDGVQHMHS KLMLLFGKDK LRVVVPTANM IPFDWGEVKN
DWQPGVMENT VFILDLPRRR DGSVGDKSEL SNFGQNLVCF LEKQQLDQKV IQGVLKFDFS
ETTHLAFVHA MQLTRSSGGS HKGGLQQPTG LPGLAKAVRD LGLGEAKAVE LEYASASLGA
INDNFLQRLY LAAKGESFTT ESENTEVRGH VRVYFPTNET VDKSVGGPDS AGIISLSRQY
YNAATFPKEC LRDYDSTRRG MLSHNKLLLA RGTKKNGKAF AWVYTGSANM SESAWGGQKV
LKSGQMGSLN VRNWECGIVM PVPDDKLANF EGTIPPMTVF QDTVEVPFVY PGQVYGDREP
WFLRRGWSEA A
//