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Database: UniProt
Entry: A0A0V0S4I5_9BILA
LinkDB: A0A0V0S4I5_9BILA
Original site: A0A0V0S4I5_9BILA 
ID   A0A0V0S4I5_9BILA        Unreviewed;      1069 AA.
AC   A0A0V0S4I5;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Actin-related protein 2 {ECO:0000313|EMBL:KRX21677.1};
DE   Flags: Fragment;
GN   Name=arx-2 {ECO:0000313|EMBL:KRX21677.1};
GN   ORFNames=T07_6216 {ECO:0000313|EMBL:KRX21677.1};
OS   Trichinella nelsoni.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=6336 {ECO:0000313|EMBL:KRX21677.1, ECO:0000313|Proteomes:UP000054630};
RN   [1] {ECO:0000313|EMBL:KRX21677.1, ECO:0000313|Proteomes:UP000054630}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS37 {ECO:0000313|EMBL:KRX21677.1};
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   -!- SIMILARITY: Belongs to the KIN17 family.
CC       {ECO:0000256|ARBA:ARBA00008517}.
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:KRX21677.1}.
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DR   EMBL; JYDL01000037; KRX21677.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V0S4I5; -.
DR   Proteomes; UP000054630; Unassembled WGS sequence.
DR   GO; GO:0070569; F:uridylyltransferase activity; IEA:InterPro.
DR   CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1.
DR   Gene3D; 2.30.30.140; -; 1.
DR   Gene3D; 2.30.30.30; -; 1.
DR   Gene3D; 3.30.420.40; -; 2.
DR   Gene3D; 1.10.10.2030; DNA/RNA-binding protein Kin17, conserved domain; 1.
DR   Gene3D; 2.160.10.10; Hexapeptide repeat proteins; 2.
DR   InterPro; IPR004000; Actin.
DR   InterPro; IPR020902; Actin/actin-like_CS.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR019447; DNA/RNA-bd_Kin17_WH-like_dom.
DR   InterPro; IPR037321; KIN17-like.
DR   InterPro; IPR038254; KIN17_WH-like_sf.
DR   InterPro; IPR041330; KN17_SH3.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   InterPro; IPR014722; Rib_uL2_dom2.
DR   InterPro; IPR002618; UDPGP_fam.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   PANTHER; PTHR12805:SF0; DNA_RNA-BINDING PROTEIN KIN17; 1.
DR   PANTHER; PTHR12805; KIN17 KIN, ANTIGENIC DETERMINANT OF RECA PROTEIN HOMOLOG; 1.
DR   Pfam; PF00022; Actin; 1.
DR   Pfam; PF10357; Kin17_mid; 1.
DR   Pfam; PF18131; KN17_SH3; 1.
DR   Pfam; PF01704; UDPGP; 2.
DR   PRINTS; PR00190; ACTIN.
DR   SMART; SM00268; ACTIN; 1.
DR   SMART; SM01253; Kin17_mid; 1.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR   PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054630};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          461..585
FT                   /note="DNA/RNA-binding protein Kin17 WH-like"
FT                   /evidence="ECO:0000259|SMART:SM01253"
FT   REGION          639..659
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          570..601
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        639..658
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KRX21677.1"
SQ   SEQUENCE   1069 AA;  121822 MW;  FE4F7E9BF37D3A57 CRC64;
     LLAIGYKEMV DSAGRKLIVL DNGTGFVKCG YAGTNFPEHV FPSVVGRPTI RSKIKVNDVE
     LQDVMIGSKC AAVRHMLDLS YPMDNGIVRN WDDMDLVWDY TFGPECLNLQ PSECKLLLTE
     APLNPIKNRE KMFEVMFEKF GFHSVYVAVQ AVLTLYAQGL ETGVVVDSGD GVTHICPVYQ
     GFALNHLTKR LDIAGRNITS YLVSLLKLRG YAFNHSADFE TVRQIKEKLC YTAYDIEQEV
     KLALETVILV KPYTLPDGRV IRVGSERFQA PEVLFQPNLI DVECCGISEL LFNVIQSADI
     DTRAEFYKHI VLSGGSTMFA GLPSRFEREI KQLYLERVLK GNKEAFQKFK IRVEASPGRK
     YVVFEGGSLL AKLMRDREDF WVSRMDFKEH GINCVRKKFG LYLGSTLLSM PKHEPFTPKA
     ISNRIKAKGL QKLRWFCQMC QKQCRDQNGF KCHLTSESHQ RQLLLFAESP GRFLGQYSGE
     FKKGFLDILT RQFGTKRVKA NTVYQEYIKD RNHVHMNSTC WFTLTGFVNY LGRTGICKVD
     QTEKGWFIQY IDRSLEERRE KMAKKVKMDM DDEERMRDII MKQAERARER LKESGELEEE
     APYSELKKSD DQKIEFKLPK MVPVKDKLKP LEILSNAARS STDGKFDKPS TSKSVTRPKS
     ALDEIKEAEE MYKEKKNRTR CWLHPGIVVK IISKRYGERL NNEKGVVTNV KEERFACLQL
     LSDEDTTVTV EQKHLETVIP ALNRTVLIVN GAYRGQKATL ESTFFGVAAL VMKVERKSED
     WKDATKRETM DSMSFELDRL LETSLPADLE IKPYSDLTEP SMDKVRSMLS KMVIVKLNGG
     LGTTMGCKGP KSLIPVRHDL TFLDLTMQQI EHLNLTHDVD IPLVLMNSFN TDQDTKRALR
     KYRNVKVCVY SFNQKTLMPI SSSLRNMDGE SWYPPGHGDF YQAFYNSGLL DKFVQSGKEY
     CFVSNIDNLG ATLDLIFNQG FVVPRSRFLP VKKTQDLLLV KSNLYDLANG CLILSNKRTF
     SPVPLVKLGS SFEKGTVIII ANHGDRIDIP PGALLANKIV SGNLRIMDH
//
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