ID A0A1F5LHE6_9EURO Unreviewed; 1465 AA.
AC A0A1F5LHE6;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=3'-5' exonuclease domain-containing protein {ECO:0000259|SMART:SM00474};
GN ORFNames=PENARI_c010G11419 {ECO:0000313|EMBL:OGE52371.1};
OS Penicillium arizonense.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1835702 {ECO:0000313|EMBL:OGE52371.1, ECO:0000313|Proteomes:UP000177622};
RN [1] {ECO:0000313|EMBL:OGE52371.1, ECO:0000313|Proteomes:UP000177622}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 141311 {ECO:0000313|EMBL:OGE52371.1,
RC ECO:0000313|Proteomes:UP000177622};
RX PubMed=27739446; DOI=10.1038/srep35112;
RA Grijseels S., Nielsen J.C., Randelovic M., Nielsen J., Nielsen K.F.,
RA Workman M., Frisvad J.C.;
RT "Penicillium arizonense, a new, genome sequenced fungal species, reveals a
RT high chemical diversity in secreted metabolites.";
RL Sci. Rep. 6:35112-35112(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:OGE52371.1}.
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DR EMBL; LXJU01000010; OGE52371.1; -; Genomic_DNA.
DR STRING; 1835702.A0A1F5LHE6; -.
DR OrthoDB; 318506at2759; -.
DR Proteomes; UP000177622; Unassembled WGS sequence.
DR GO; GO:0008408; F:3'-5' exonuclease activity; IEA:InterPro.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006139; P:nucleobase-containing compound metabolic process; IEA:InterPro.
DR CDD; cd06141; WRN_exo; 1.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR InterPro; IPR002562; 3'-5'_exonuclease_dom.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR PANTHER; PTHR13620; 3-5 EXONUCLEASE; 1.
DR PANTHER; PTHR13620:SF104; EXONUCLEASE 3'-5' DOMAIN-CONTAINING PROTEIN 2; 1.
DR Pfam; PF01612; DNA_pol_A_exo1; 1.
DR SMART; SM00474; 35EXOc; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Reference proteome {ECO:0000313|Proteomes:UP000177622}.
FT DOMAIN 1240..1430
FT /note="3'-5' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00474"
FT REGION 755..814
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 838..867
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 913..1141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1156..1176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 839..867
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 919..936
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 986..1001
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1008..1022
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1029..1043
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1065..1107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1119..1133
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1465 AA; 165655 MW; 39F0EFC33F7EA982 CRC64;
MGLSGDPEVG LRACSDGELL YYFTIGLLLA NCLLAHRQSH ALTRTDQVFV NSFANLLASR
KSRSIITTLS SQLARSISQS DHGWHPCILR DANTCTRFPS SLRHETPPAS RFHSPGPLKT
YKVRPFSTTV RRRGAWDDEE EVVPTPKKKP LRFVGPKSRS SRGPPVHRDV GSLLRAQFYA
KQNQLEAKEL SRQHALLEKA FNNLPSVDRY IDMFLMLKYF DFEVMIQYID RECERYQAMF
RTLLSWENER ILAITSSVED SVLRAEETTQ KLVAEWEGLS FSILNRLATE VSRITDRVAQ
AESVTQEYVA AVTDLSYKLR LSQVDIAVTE AEKAIQLMDH DFCLVVFFGT PELTRKVEEL
DRNLEPWQRE LLNVATSLLT HQVNISRLSI HDMEDTIQDG FLIPRQSARR RIDEITVAFD
KIHHDYKQLQ AKANVVLDAR VHIICTELSY DPDLSHRQRS MLGQLGRALS LTRNSLMAAL
HSHRSAWRKR VMQSHSLREA QLWELSDLSK VYRMHNNNNN NARERLFEAF ALGPRHGGKL
AQHLAGNSRD MASALRSIYL PRYRRQPARS PLQNFYWQQL DVVWPMYHLD TLCWLLSSEV
WYLQHTLKGS CGPLWEGIPA IGRRLSATKI AEWNFKFQVH RNELRQELDE FYNINWMRLQ
SESKLYAMGE RAYLSGRFEV PNPMSQDRGR FKEWAMHFAR ICSEAWITGF ALHQSPEFWN
RLYQKLEANR KADNDLGQGH LLAEFGSDPV RKKAVATPPL PRTGSFKTTK RSNFVRSRKL
NAPRKTQGKG AAAPEHRLPT PNAQPEAVSE QSEALPLADQ KFQKKIQGTG RPWWMRSRET
AETRTTNPKA VTPGPKNAPI ASNQNKVSQP WTMAQKIQEI FGFSNDLNVH QPPLTKTHSQ
PTEDASLDMA EYKPSAKSKR FQNMFTGRSY SSPSVEAKDD PQGPKADLPD KTPPHQPYPQ
NLPETTGMTK AGIRRRRRRE QRRNATDYYS LPQSGGVSEG SLPKQSLEHD ISPITPTKIE
SPPSGEPSDV LPGKRPPPQP YSQSLPGMGT SKYAIKRRLR KQSSSETTDP TSYHSLPQSS
GVSEGSPPKQ SLEHDTSPIT PTKIDSPPSG EPSDIFPGQT PPNGLQLQSR PGKAISKQAR
RRRLLRSVFG RSYTTDASSY QTSFRHSSGV SNGSLPEQSL EHAISPIPLT KGHGSDSLDK
ASLDETVPAS DIDLNVSVSA APKFWSHSSQ HSPGGEKLIV HYCRTLHNTE EIAQHFLGSK
VLGFDMEWKS SASAWDSIQN NVSVIQIANE ERIAIFQIAS FKPSRSLKDL VSPTLKQIIE
SPDITKVGVS IKADCTRLRK YLGIDAKATF ELSHLFKLVK YGQDNPKLVN KRGVNLSEQM
EEHFGLPLEK NEDVRCGDWA RALSYRQVQY AATDPYACIR LFNAMEAKRL AMDPVPPRPA
FAELNRPIIL PLGQAVNSEE KEPPL
//
