ID A0A2K1QRX9_9PEZI Unreviewed; 1997 AA.
AC A0A2K1QRX9;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=3'-5' exonuclease domain-containing protein {ECO:0000259|SMART:SM00474};
GN ORFNames=CAC42_3196 {ECO:0000313|EMBL:PNS17801.1};
OS Sphaceloma murrayae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Myriangiales; Elsinoaceae; Sphaceloma.
OX NCBI_TaxID=2082308 {ECO:0000313|EMBL:PNS17801.1, ECO:0000313|Proteomes:UP000243797};
RN [1] {ECO:0000313|EMBL:PNS17801.1, ECO:0000313|Proteomes:UP000243797}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CQ-2017a {ECO:0000313|EMBL:PNS17801.1,
RC ECO:0000313|Proteomes:UP000243797};
RA Cheng Q.;
RT "Draft genome sequence of a variant of Elsinoe murrayae.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:PNS17801.1}.
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; NKHZ01000049; PNS17801.1; -; Genomic_DNA.
DR STRING; 2082308.A0A2K1QRX9; -.
DR InParanoid; A0A2K1QRX9; -.
DR OrthoDB; 116867at2759; -.
DR Proteomes; UP000243797; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005839; C:proteasome core complex; IEA:InterPro.
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 GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:UniProt.
DR CDD; cd03760; proteasome_beta_type_4; 1.
DR CDD; cd06141; WRN_exo; 1.
DR Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR InterPro; IPR002562; 3'-5'_exonuclease_dom.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR016295; Proteasome_beta4.
DR InterPro; IPR016050; Proteasome_bsu_CS.
DR InterPro; IPR001353; Proteasome_sua/b.
DR InterPro; IPR023333; Proteasome_suB-type.
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 Pfam; PF00227; Proteasome; 2.
DR SMART; SM00474; 35EXOc; 1.
DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR PROSITE; PS00854; PROTEASOME_BETA_1; 1.
DR PROSITE; PS51476; PROTEASOME_BETA_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Proteasome {ECO:0000256|ARBA:ARBA00022942};
KW Reference proteome {ECO:0000313|Proteomes:UP000243797}.
FT DOMAIN 1329..1520
FT /note="3'-5' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00474"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 144..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 510..549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 588..849
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 888..914
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1073..1137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1151..1176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1193..1261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1543..1567
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1811..1847
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 277..304
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 514..533
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 608..630
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 662..676
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 677..709
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 751..774
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 789..803
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 831..849
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1074..1104
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1193..1208
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1997 AA; 220562 MW; 0E5AC0D41EFE0CA5 CRC64;
MARRWAAIKE SGEDPETAKK YQERMRAQED LMRSKENEHR SLFSKLLQEK RKSDEALALL
EQQDRDVNKE LARGIEAGLK PLRRVESDLR TREKAIISLG NERAALERSL KEAQETVMAI
EARTSAATAA LQEDLQIQRS REQRLKRELD STKGSLSSQT RQNSQWKPIV DRHLEQIREA
AKAQNEQVAR AAAREDYASF RAHFQRVQQS AFDYRDALQG VHHIAVAAEQ YWWGATIAFE
KFQRDLERGQ ALADHKSIIV AIRAKLLEMR HDRRRTCSNL RCQISQFNQR LSEYSNEAHA
LRRLSRVLRY RLAQEHPYPM FVVMHEAPRT LQAADLALLN RFAHPDQESF ARGDDRYKVL
SNALRPILIP NLKTTEDLLR LRTKYMQIAW TESAPPAEQI SYHLSAAVSG KFLRLVSQLR
KDDVRLGRVD VDARRMLSRD YKVKAKLDYA NQVVLARRMY ESLVWMRRYA EEALGQQRDE
EAEQAHVRLQ GARPNILASI AECAARASGQ AKPAVKETTP TSSPSSIKSP SPEEKISQVP
KAKRSKRSQR LLRIANLSLA RLEKRIKAEP ERSEELTAKI AKMRELIRRH SASDVPSTEP
ATNDKESGQK VSGDKVSSNR DLDGKGSDNK DLNGALKANT TSTRTAARRR RRAERLRSRT
GSDVPSTEPA TDDKGSNQKV SGDKVSDNKA SDDKVSSNKD SDSKGSDNKD LNGALKANTT
STRTAARRRR RAERLRSRTE SLVSSIEPVA DDKVSDTKDS EDTISSDKVS NDKVSNDKVS
NVKTSNDRVS DDNALDKKGS KSALKADTTP SHPAARLGRR AERLRRRTTS DVPSTEPITD
DKVSKSALKG GNTLSRVAAR LKRRAGELAA KLTGTHGPAV EDVQAAPVAD ADDSAVKPTD
SNRSVVGDVQ SPSVPVADGK DVKLIISDEP VVETPSTAAD DTAAKVIGSN GPVVGDAQTT
SVAVSDADDK ANKLTKSDAS VIGDVQATSI STTDNTAATL TDSNVPAISD VQETSMNSTD
DTTATLIKPN GPIVRYVDTF IMSDVNDLTR ADKNLDSPVT KMGKNIDDAR VASHMPSHSS
SVYETSTPQN QESGTDSTGS IGDAGRSAGT ELSKASRLRN PMQARLRDGP ELEKGPLPIR
KVVGQDPLSR LGKEVAARSA RRSVRAKGRR DRTPVKRMPT GVWADLCEVA RSTFSPTSSS
ASSDKATTES ENGKTEPKAD MGSSELSSEK TLARKIDSGG NPNGLADPRP EDKDPTSAVR
QAGRLVKSMF KPTDPKNMSL GRSSWRTGEA AFRIRQEALA LASAKARTEH GIHWSHHLYR
SPSNEPVKVF YCTNKDWAET VAQMFLGERV VGFDLEWEPN RPLYNDVSDM KNYLSLIQIA
AEDKIALFHI SMFPGGSPDE LMPRSLKVLL ESESTLKVGV HVGGDSTRLL KCFGFSGKGY
IELSHCYKLV KYHDDQPESI NRLLVKLETQ VQEILGYPLL KDAVRTSAWS TRLSKEQQDY
AATDAYAGYQ LFRELEALRQ AMDPTPPRPA FYELRQPILL ADGQRPPKAP GQTQVEDSQI
PGDTKADAEP YATASSWLHP DCENVGLEEQ PPAAGSNGQP INEHLAAAEA WCISYKVRRD
QTGLAAAKRS SLTAYALWHH HEQEPAQIAE IMRSPALKIN TVNSYIVDAV SFDRSLPYDS
LRLKQIITSM PPNLFKVRQL AYPIGMNHFP QSWGRPRDDV YGSYDHTHFG HGQPVSHTQS
PIVTGTSVLG IKYKDGVVLA ADNLASYGSL ARFTDVKRLR KFNANSVIGF GGDVSDMQYL
DRLLSSLRRE QEYQQPSATL STPTPGAADA PAPSTAPTTE AERQAKTQLS AKNLHTYISK
VMYKRRSDFN PLWNAVLVGG LDDAGNPFLA SADLLGTTFS APTLATGFGA HLAQPIMRRH
VPTEEAAKDL TREQAVEIVR ECMKVLFYRD ARSLDNYSIA VVGKGEKDGV TLLENEKLEG
QSWAFAERVR GYGTQVV
//
