ID A0A179EWX7_METCM Unreviewed; 877 AA.
AC A0A179EWX7;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 2.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=DDE superfamily endonuclease {ECO:0000313|EMBL:OAQ57671.2};
GN ORFNames=VFPPC_12103 {ECO:0000313|EMBL:OAQ57671.2};
OS Pochonia chlamydosporia 170.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Pochonia.
OX NCBI_TaxID=1380566 {ECO:0000313|EMBL:OAQ57671.2, ECO:0000313|Proteomes:UP000078397};
RN [1] {ECO:0000313|EMBL:OAQ57671.2, ECO:0000313|Proteomes:UP000078397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=170 {ECO:0000313|EMBL:OAQ57671.2};
RX PubMed=27416025;
RA Wang G., Liu Z., Lin R., Li E., Mao Z., Ling J., Yang Y., Yin W.B., Xie B.;
RT "Biosynthesis of antibiotic leucinostatins in bio-control fungus
RT Purpureocillium lilacinum and their inhibition on phytophthora revealed by
RT genome mining.";
RL PLoS Pathog. 12:E1005685-E1005685(2016).
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:OAQ57671.2}.
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DR EMBL; LSBJ02000020; OAQ57671.2; -; Genomic_DNA.
DR AlphaFoldDB; A0A179EWX7; -.
DR OrthoDB; 2554849at2759; -.
DR Proteomes; UP000078397; Unassembled WGS sequence.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR InterPro; IPR004875; DDE_SF_endonuclease_dom.
DR InterPro; IPR008906; HATC_C_dom.
DR InterPro; IPR006600; HTH_CenpB_DNA-bd_dom.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR PANTHER; PTHR19303:SF62; HTH CENPB-TYPE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR19303; TRANSPOSON; 1.
DR Pfam; PF03184; DDE_1; 1.
DR Pfam; PF05699; Dimer_Tnp_hAT; 1.
DR SUPFAM; SSF57756; Retrovirus zinc finger-like domains; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR PROSITE; PS51253; HTH_CENPB; 1.
DR PROSITE; PS50158; ZF_CCHC; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Endonuclease {ECO:0000313|EMBL:OAQ57671.2};
KW Hydrolase {ECO:0000313|EMBL:OAQ57671.2};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Nuclease {ECO:0000313|EMBL:OAQ57671.2};
KW Reference proteome {ECO:0000313|Proteomes:UP000078397};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00047}.
FT DOMAIN 415..484
FT /note="HTH CENPB-type"
FT /evidence="ECO:0000259|PROSITE:PS51253"
FT DOMAIN 847..862
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT REGION 797..856
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 769..796
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 826..850
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 877 AA; 101119 MW; A919563DF58E2B21 CRC64;
MGYFTLLNAY NNDTMMHTVA ETCGFNSTHR RLRCNGHIIN LAVQAFLFGK NKEASDEALR
QVSRLSRREQ EGAVGRAETA TAWRQYGALG MLHNLVVWIR SSTQRYQAFL QAAGRMIPQD
NSTRWNSWYR MIHVAIALRK ELNSFMDDRY SESDIRFDYL HPEHWQELQE IHDFLQPFYE
ITKDTQWDKT SLDEVICSMD FLVTHYKAAM EQFQHNTTMV DRIMTSWYKF DDYYTRTDDT
PVYAAAILLH PSLREAHLKE AWKDQPQYIG PAIAAVRKLW DDFKPQQEPE IEEDLSAYEA
YKKRIYQKSS CHDEFSRFIE GPTLPIGDSS ALSWWLEPTQ QTSYPSLYHL AINIFSIPAM
SAEAERVFSG ARRTVSWDRG RLSAQIVEYT ECLKHWIKSG LLDQPYMIPE PMDAELDSRD
IEMLSEEETE IIKYILDLDS RSFPPRLSGV QDMANRLLAD RHAPPVGVNW ASNFVRRRKE
LSTRFTRRYD YQRALCEDPK IIKPWFELVR NTVAKYGIQD EDFHNFDETG FMMGVISTTM
VVTSSERRGK PSLAQPGDRK WVSVLQSINS QGEAIPPFII AAGQFHLGNW YEDSALPKDW
VISTTHNGWT TNEKAVDWIR HFEKHTKPKS RGAYRLLILD GHESHHSTEF EVFCRDHKII
TLCMPSHSSH ILQPLDVGCF GPLKKAYGKE IEGLMRAHIT HITQADFFPA FCTAFKAAMT
KENIQGAFRG AGLVPFNPNS VLSRLDVRLR TPTPVEEAPE LPNPLQREHA EFMHQVALLK
AEVNQLREAN ALLSKRRRAK KTRLRQGGSM TIAEGQALQD QNDVEDQIQQ EDRKTRGRKP
RDETKGRRCG VCGKTGHNAR TCQIDVEASN EDDSSED
//
