ID A0A0V1LGE2_9BILA Unreviewed; 1089 AA.
AC A0A0V1LGE2;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 22-FEB-2023, entry version 21.
DE SubName: Full=Cleavage stimulation factor subunit 3 {ECO:0000313|EMBL:KRZ58515.1};
GN Name=CSTF3 {ECO:0000313|EMBL:KRZ58515.1};
GN ORFNames=T02_3317 {ECO:0000313|EMBL:KRZ58515.1};
OS Trichinella nativa.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6335 {ECO:0000313|EMBL:KRZ58515.1, ECO:0000313|Proteomes:UP000054721};
RN [1] {ECO:0000313|EMBL:KRZ58515.1, ECO:0000313|Proteomes:UP000054721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS10 {ECO:0000313|EMBL:KRZ58515.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the actin family.
CC {ECO:0000256|RuleBase:RU000487}.
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:KRZ58515.1}.
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DR EMBL; JYDW01000056; KRZ58515.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1LGE2; -.
DR STRING; 6335.A0A0V1LGE2; -.
DR Proteomes; UP000054721; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0031124; P:mRNA 3'-end processing; IEA:InterPro.
DR CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1.
DR Gene3D; 1.25.40.1040; -; 1.
DR Gene3D; 3.30.420.40; -; 2.
DR InterPro; IPR004000; Actin.
DR InterPro; IPR004001; Actin_CS.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR003107; HAT.
DR InterPro; IPR045243; Rna14-like.
DR InterPro; IPR008847; Suf.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR19980:SF0; CLEAVAGE STIMULATION FACTOR SUBUNIT 3; 1.
DR PANTHER; PTHR19980; RNA CLEAVAGE STIMULATION FACTOR; 1.
DR Pfam; PF00022; Actin; 1.
DR Pfam; PF05843; Suf; 1.
DR PRINTS; PR00190; ACTIN.
DR SMART; SM00268; ACTIN; 1.
DR SMART; SM00386; HAT; 9.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS00432; ACTINS_2; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000054721}.
FT DOMAIN 370..546
FT /note="Suppressor of forked"
FT /evidence="ECO:0000259|Pfam:PF05843"
SQ SEQUENCE 1089 AA; 123933 MW; 9FC38113E8DC660F CRC64;
MAAISVNDIK EKILTNPLNV EAWSDFLESV DEIPIEEARL MYNKLIETFP SSPQYWTSFI
RFELSNSAFV QVEALFRRCL LKVLHIDVWK IYLAYVRDTK SCVTGFKKSI KEAYEFSLDK
IGLDFYSYSV YHEFIKWLLQ MLPESESGAR KESEGADTNV DEIRRVFLRG ISCPIENIAA
LWNEYEQFEK KYGGLTAQNR IDTARKVYLK TSEVAKCLEK LLVGINTKRI SVPLQNTVSE
KNQLSRWYAY IDYEKSNPLA TQCFDLLVRR VIYAYEQVLM CFSDCLALWC DLISFMVQSI
ETANSRNEVD LSEKLSEEVS RTFERAMDAG MKDEYLIYFV YSQFLENQKR YSEVKEVLQS
FIQIPNVDPT IAYIHFMQFA NRTGSLDSAR TIFKSAREDE RTKCEMYIAA AEMEYRWKKD
PTISVRIYEL GLKRYKNDSK FACSYLKFVM GLNEDSNTRV LFERILSSGM LNEQSAVEVW
NLYVEFESLV GDLATITKIN QRRQHALTKR FQENPTAMLV DRYKFMNLLP CKKQELDLLG
YMESSALKSE TLSLTRTQCS TYPDISGLLP YKPRECPKGF FHYVAGGIFP PPAEVAKVLS
VLPPPGCFHG PFVKVDDLFQ FVEENLKSFK PKNVSSRECP KEFPKYKFAF VAASTMTGFN
SADDLGALVL DPGHHSFRIG YAGDDNPKLD LPGVYGYIDD TLVSGDDTAD GDLLQGGGFA
SNNKFRKYFI GTNAIHVPRA EVEYGSFLQD GLINDWDMFE NVLMHTFNIF FMENTCNYPI
LFSEASWNTR TKRERLTEVM FEKFGIPAFY VAKNSVLAAF ANGRQTAIVL DSGATHTTAS
PVYDGFCMTN AIVKTSLGGI ALNNHIKKLF QEIGIEVVPK YMVKSKQPVS EGHPPRWKKK
KNLPEVTSSF HDFGIKEVLE DFKASVCQVS DSALDPIIVD KFPRVNFEFP NGFSVDFGRE
RFEVGEALFD LSYLKGENIH PALSVSSAVH TSVNICDSDY RTALYNSVVV TGGNSLLSGF
VDRFIHEVNT RSSSNAKVKI HSAVTASERR FGAWIGGSIL ASLANFQQMW ISKQEYEETG
RGIVEKKCP
//
