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Database: UniProt
Entry: A0A178AQT9_9PLEO
LinkDB: A0A178AQT9_9PLEO
Original site: A0A178AQT9_9PLEO 
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.
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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
//
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