ID A0A0V1NXK6_9BILA Unreviewed; 1055 AA.
AC A0A0V1NXK6;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 22-FEB-2023, entry version 22.
DE SubName: Full=Actin-like protein 6A {ECO:0000313|EMBL:KRZ88752.1};
GN Name=CSTF3 {ECO:0000313|EMBL:KRZ88752.1};
GN ORFNames=T08_11254 {ECO:0000313|EMBL:KRZ88752.1};
OS Trichinella sp. T8.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92180 {ECO:0000313|EMBL:KRZ88752.1, ECO:0000313|Proteomes:UP000054924};
RN [1] {ECO:0000313|EMBL:KRZ88752.1, ECO:0000313|Proteomes:UP000054924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS272 {ECO:0000313|EMBL:KRZ88752.1};
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 -!- 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:KRZ88752.1}.
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DR EMBL; JYDM01000080; KRZ88752.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1NXK6; -.
DR Proteomes; UP000054924; 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; 3.30.420.40; -; 2.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 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; 8.
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:UP000054924}.
FT DOMAIN 336..512
FT /note="Suppressor of forked"
FT /evidence="ECO:0000259|Pfam:PF05843"
SQ SEQUENCE 1055 AA; 119814 MW; 6383883E568E1B1D CRC64;
MAAISVNDIK EKILTNPLNV EAWSDFLESV DEIPIEEARF MYNKLIETFP SSPQYWTSFI
RFELSNSAFV QVEALFRRCL LKVLHIDVWK IYLAYVRDTK SCVTGFKLPE SESGARKESE
GADTNVDEIR RVFLRGISCP IENIAALWND YEQFEKKYGG LTAQNRIDTA RKVYLKTSEV
AKCLEKLLVG INTKRISVPL QNTVSERNQL SRWYAYIDYE KSNPLATQCF DLLVRRVIYA
YEQVLMCFSD CLALWCDLIS FMVQSIETAN SRNEVDLSEK LSEEVSRTFE RAMDAGMKDE
YLIYFVYSQF LENQKRYSEV KEVLQSFIQI PNVDPTLAYI HFMQFANRTG SLDSARTIFK
SAREDERTKC EMYIAAAEME YRWKKDPTIS VRIYELGLKR YKNDSKFACS YLKFVMGLNE
DSNTRVLFER ILSSGMLNEQ SAVEVWNLYV EFESLVGDLA TITKINQRRQ HALTKRFQEN
PTAMLVDRYK FMNLLPCKKQ ELDLLGYMES SALKSETLSL TRTQCSTYPD ISGLLPYKPR
ECPKGFFHYV AGGIFPPPAE VAKVLSVLPP PGCFHGPFVK VDDLFQFVEE NLKSFKPKNV
SSRECPKEFP KYKFAFVAAS TMTGFNSADD LGALVLDPGH HSFRIGYAGD DNPKLDLPGV
YGYIDDTLVS GDDTADGDLL QGGGYASNNK FRKYFIGTNA IHVPRAEVEY GSFLQDGLIN
DWDMFENVLM HTFNIFFMEN TCNYPILFSE ASWNTRTKRE RLTEVMFEKF GIPAFYVAKN
SVLAAFANGR QTAIVLDSGA THTTASPVYD GFCMTNAIVK TSLGGIALNN HIKKLFQEIG
IEVVPKYMVK SKQPVSEGHP PRWKKKKNLP EVTSSFHDFG IKEVLEDFKA SVCQVSDSAL
DPIIVDKFPR VNFEFPNGFS VDFGRERFEV GEALFDLSYL KGENIQPALS VSSAVHTSVN
ICDSDYRTAL YNSVVVTGGN SLLSGFVDRF IHEVNTRSSS NAKVKIHSAV TASERRFGAW
IGGSILASLA NFQQMWISKQ EYEETGRGIV EKKCP
//
