ID A0A2R5GPB9_9STRA Unreviewed; 1174 AA.
AC A0A2R5GPB9;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=5'-3' exoribonuclease {ECO:0000256|PIRNR:PIRNR037239};
DE EC=3.1.13.- {ECO:0000256|PIRNR:PIRNR037239};
GN ORFNames=FCC1311_083742 {ECO:0000313|EMBL:GBG32149.1};
OS Hondaea fermentalgiana.
OC Eukaryota; Sar; Stramenopiles; Bigyra; Labyrinthulomycetes;
OC Thraustochytrida; Thraustochytriaceae; Hondaea.
OX NCBI_TaxID=2315210 {ECO:0000313|EMBL:GBG32149.1, ECO:0000313|Proteomes:UP000241890};
RN [1] {ECO:0000313|EMBL:GBG32149.1, ECO:0000313|Proteomes:UP000241890}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Sedici K., Godart F., Aiese Cigliano R., Sanseverino W., Barakat M.,
RA Ortet P., Marechal E., Cagnac O., Amato A.;
RT "Sequencing, de novo assembly and annotation of complete genome of a new
RT Thraustochytrid species, strain FCC1311.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Possesses 5'->3' exoribonuclease activity. May promote
CC termination of transcription by RNA polymerase II.
CC {ECO:0000256|PIRNR:PIRNR037239}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the 5'-3' exonuclease family. XRN2/RAT1
CC subfamily. {ECO:0000256|ARBA:ARBA00006994,
CC ECO:0000256|PIRNR:PIRNR037239}.
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:GBG32149.1}.
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DR EMBL; BEYU01000115; GBG32149.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2R5GPB9; -.
DR EnsemblProtists; GBG32149; GBG32149; FCC1311_083742.
DR InParanoid; A0A2R5GPB9; -.
DR Proteomes; UP000241890; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0004534; F:5'-3' RNA exonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-UniRule.
DR CDD; cd18673; PIN_XRN1-2-like; 1.
DR Gene3D; 1.25.40.1050; -; 1.
DR Gene3D; 3.40.50.12390; -; 2.
DR InterPro; IPR027073; 5_3_exoribonuclease.
DR InterPro; IPR041412; Xrn1_helical.
DR InterPro; IPR004859; Xrn1_N.
DR InterPro; IPR017151; Xrn2/3/4.
DR PANTHER; PTHR12341:SF41; 5'-3' EXORIBONUCLEASE 1; 1.
DR PANTHER; PTHR12341; 5'->3' EXORIBONUCLEASE; 1.
DR Pfam; PF17846; XRN_M; 2.
DR Pfam; PF03159; XRN_N; 1.
DR PIRSF; PIRSF037239; Exonuclease_Xrn2; 1.
PE 3: Inferred from homology;
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|PIRNR:PIRNR037239};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR037239};
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664,
KW ECO:0000256|PIRNR:PIRNR037239};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|PIRNR:PIRNR037239};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000241890};
KW rRNA processing {ECO:0000256|ARBA:ARBA00022552}.
FT DOMAIN 1..250
FT /note="Xrn1 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03159"
FT DOMAIN 326..431
FT /note="Xrn1 helical"
FT /evidence="ECO:0000259|Pfam:PF17846"
FT DOMAIN 560..941
FT /note="Xrn1 helical"
FT /evidence="ECO:0000259|Pfam:PF17846"
FT REGION 412..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 492..586
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 965..1174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 515..534
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 535..553
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 559..586
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 986..1014
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1042..1109
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1174 AA; 132440 MW; 097C390B17ABC2C8 CRC64;
MGVPAFFRWI SEKYPKIMTR CIEEHRSSGQ APVDASQPNP NGYEFDNLYL DMNGLIHPCT
HPEGEPAPET EEEMYLVIFR YLDRLLNMVR PRKLIYMAID GVAPRAKMNQ QRSRRFRAAQ
EAAEAAEDAD RIRKEMISQG HRPPPKKPPA WDSNVITPGT EFMAKLSDYL RWYIAERLNH
NAAFKNVRIV LSDAQSPGEG EHKIMQFIRR QRAEPGYDPN TTHILYGLDA DLIMLGLASH
EIHFTILREE VLFGKQKRKQ GFQRDAVLNN SSAGSTDGDM SPDDSDMGLI GTNKKPFDLV
RLWILREYLA HEFRPEAFYQ PLPFAYNFEA CIDDFVFICF FVGNDFLPHL PSLSIREGGL
ELLLDLYKRV LPTVGGYLTK DGQVNLSRVD VYMGVLGTVE DEIFRRRRAS EVWDQQRRKN
NQRTRREGGK TRAEGALALA AASGSGPEVQ GRTKRGKFNV QDFSGADGKN LVPLGQGVSG
AKAAALVPLG KKSGASAAPP AKPVPPPDSN ANKSAAAELR DKLKRGKKRP ADSDRAGPSS
SSSSSSSPSS SAAPEEGRKA KQQATEERKK ERKEARDIRR AQERARDAVD KIKLDSYDAD
DSKAAHDAFE ARIKEKEKQR NVHEDVEDEV RFGEPGWKNR YYASKFGPEY EDPKSEKRRE
VVRSYVTGLC WVMEYYYRGC QSWTWFYEYH YAPFASDLVN IDDINIEFPP SMPFKPFEQL
MGVFPPASAH ALPEPCRWYM TDIDSPIADF YPTQFEYDAN GKAVRWLWVA LLPFIDESRL
LAVTADLEKE FKPHEKERNE YNPDLVFARV DAVGTDKMMV AADEAERAMP SKTQAIKDED
GKQITPTTAG DVRASGKGGK PHARLLLASA TNGLSGYFTH PPDKFKFEPG KTIPPAGRRV
DPLPDNKTVA FEFRLPKMRP HLSMLLPDVR VPRPVLSADD LIIKIPKLGR GANVANLLVE
TTRQAHPSSF QQPSHGGGLG QRQAAHFQRS YGSMEPSMNL NRNSRGGRQP YPPPSQHQHQ
QPPPWQRQQQ GYPPQRGGGY PYGQHQQHQQ QHYPNQQQHG RGYPPQQAHH YQQHRQAYGQ
YPPHQQQHQQ HQQQGYQYNR QQQAPSGPPG RGGSNPFLPN QPPPAGNSRP SSSKSALMDR
LSSALQARGA PGAPPLYPGH GHQQHHHQQN QWRR
//
