ID A0A0V0ULQ4_9BILA Unreviewed; 1177 AA.
AC A0A0V0ULQ4;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=RNA exonuclease 1-like protein {ECO:0000313|EMBL:KRX52233.1};
GN ORFNames=T09_10391 {ECO:0000313|EMBL:KRX52233.1};
OS Trichinella sp. T9.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=181606 {ECO:0000313|EMBL:KRX52233.1, ECO:0000313|Proteomes:UP000054681};
RN [1] {ECO:0000313|EMBL:KRX52233.1, ECO:0000313|Proteomes:UP000054681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS409 {ECO:0000313|EMBL:KRX52233.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) 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:KRX52233.1}.
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DR EMBL; JYDN01000263; KRX52233.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0ULQ4; -.
DR STRING; 181606.A0A0V0ULQ4; -.
DR Proteomes; UP000054681; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR CDD; cd06145; REX1_like; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR InterPro; IPR013520; Exonuclease_RNaseT/DNA_pol3.
DR InterPro; IPR034922; REX1-like_exo.
DR InterPro; IPR031736; REXO1-like_dom.
DR InterPro; IPR047021; REXO1/3/4-like.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR000571; Znf_CCCH.
DR PANTHER; PTHR12801:SF115; RNA EXONUCLEASE 5; 1.
DR PANTHER; PTHR12801; RNA EXONUCLEASE REXO1 / RECO3 FAMILY MEMBER-RELATED; 1.
DR Pfam; PF15870; EloA-BP1; 1.
DR SMART; SM00479; EXOIII; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 2.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS50103; ZF_C3H1; 1.
PE 4: Predicted;
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000313|EMBL:KRX52233.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022839, ECO:0000313|EMBL:KRX52233.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00723};
KW Nuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000313|EMBL:KRX52233.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054681};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00723};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00723}.
FT TRANSMEM 828..850
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1134..1157
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 7..33
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT ZN_FING 7..33
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 37..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 85..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 120..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..62
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..101
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1177 AA; 132545 MW; A6C0FE871385C88A CRC64;
MFPSNNRFGQ FSCPFFSTGA CNRPYCFFSH QESSKAVHKK TNSSDVNNKS TTAYSNDNNC
SSSPSSAAPA AAVAVAYTPT PIAELKKRKE DREKRRKARQ LENAQSCPTP CSVDIIDLTK
SEPTSSPVSS SSAAEQETSP PVTRELEKCP SSTPNLLIVE EQPISQLKRQ KPEEVVEILD
NAGSLSTSTP KKIRKVDLFG EDSDDDRLIA FCAVDEDEVE KPSVDETTDQ LFQSLLVEKA
KSYANVPSVD EDTVLESASV AYEKRKVDLE KEASMIQQKY NTSSNIRWSA YKTGQLASTS
HQPEAVEKAN IVQNDPGAMF STLPADIKPE KTTTLENNSI NAELAIKQLR SAKKENNQKV
LVDFSSSCAH KLLIKRPVIV PGSHLKIPFT VRQTILNYFI DAFLQQGATE EQALEKAQKE
EEFLCRSCQH KMTYNVAAIH RLKRIKDGEL SIRSVSSCGA VDSQVLLDLF YNKLERFVLS
LDDLQAHGFP LPDPTNFTRA YFSKKEVAKT YLPVDDKKRQ CDRCGKSFYL TPDWMYPDRQ
DRCVYHFGKA FNVRSSGSTD LQHTCCKGDL QSDGCCMANC HVTRVSPESE LNNYIHTAGF
KQKKKSVFAL DCEMVYTTIG SMLARVTVVD WNLETVYERL VKPPGALLDC NTRFSGITEQ
ELAKAEWTLE DVQKDLSEIF SPDSILIGHS LDCDLRALKL IHMKVVDTSV VFPHRRGLPY
KRALKSLAME YLKKIIQENV GGHDSKEDAS ACMELMNDTS SLVKKETMCL RSVVALNTGE
NGLSFCLTLM NSGKCLTEYT FSRCATAENC RRVVEAMAAA ILRRQNGMLF RAKLSAILIF
FTIFTLVNAL DSRDAVELLD KCRELLNEKQ ANWKVKIFRR QLFRLCSLAE RYVDDSLIVL
FCGNAKRYPI CQQVDLQLKA ELKKRPAPLR PAYIMTDNFA FADDLHVRHF PALTYTVAGR
MFHYTGKWNK EEISRWIRQM GAGVARSVDY SNFNQLLNKN VAVMILLYKQ ENAKCARFAG
RWWDRLAKSA SDYKQTEFVK LECSGVNGFF AAERLQMTIT DDNCPTLLML YNDKLKLFSA
DLSEPGVATS VRHFLLNQRH LADGWRPLGD EPTDLEYIEF DMQRRLDSRM NRPVHIVTGF
TGGFGVIVLA VSIFWGLKGS AFISELKALR TATVDSR
//
