ID A0A0V0XW22_TRIPS Unreviewed; 435 AA.
AC A0A0V0XW22;
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=Cytidine deaminase {ECO:0000313|EMBL:KRX92308.1};
GN Name=cdd {ECO:0000313|EMBL:KRX92308.1};
GN ORFNames=T4E_7371 {ECO:0000313|EMBL:KRX92308.1};
OS Trichinella pseudospiralis (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6337 {ECO:0000313|EMBL:KRX92308.1, ECO:0000313|Proteomes:UP000054815};
RN [1] {ECO:0000313|EMBL:KRX92308.1, ECO:0000313|Proteomes:UP000054815}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS141 {ECO:0000313|EMBL:KRX92308.1};
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 cytidine and deoxycytidylate deaminase
CC family. {ECO:0000256|ARBA:ARBA00006576}.
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:KRX92308.1}.
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DR EMBL; JYDU01000115; KRX92308.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0XW22; -.
DR STRING; 6337.A0A0V0XW22; -.
DR Proteomes; UP000054815; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR CDD; cd01283; cytidine_deaminase; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR Gene3D; 3.40.140.10; Cytidine Deaminase, domain 2; 1.
DR Gene3D; 1.10.750.20; SOCS box; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR002125; CMP_dCMP_dom.
DR InterPro; IPR016193; Cytidine_deaminase-like.
DR InterPro; IPR001496; SOCS_box.
DR InterPro; IPR036036; SOCS_box-like_dom_sf.
DR PANTHER; PTHR11644; CYTIDINE DEAMINASE; 1.
DR PANTHER; PTHR11644:SF2; CYTIDINE DEAMINASE; 1.
DR Pfam; PF00023; Ank; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF00383; dCMP_cyt_deam_1; 1.
DR Pfam; PF07525; SOCS_box; 1.
DR SMART; SM00248; ANK; 5.
DR SMART; SM00969; SOCS_box; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF53927; Cytidine deaminase-like; 1.
DR SUPFAM; SSF158235; SOCS box-like; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 3.
DR PROSITE; PS50088; ANK_REPEAT; 4.
DR PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 1.
DR PROSITE; PS50225; SOCS; 1.
PE 3: Inferred from homology;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW Reference proteome {ECO:0000313|Proteomes:UP000054815}.
FT DOMAIN 3..126
FT /note="CMP/dCMP-type deaminase"
FT /evidence="ECO:0000259|PROSITE:PS51747"
FT REPEAT 175..207
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 208..240
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 241..277
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 278..310
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 380..435
FT /note="SOCS box"
FT /evidence="ECO:0000259|PROSITE:PS50225"
SQ SEQUENCE 435 AA; 48850 MW; 2D5904A0AB38FAF9 CRC64;
MESSISQLIL DSISAKEFSY SPYSKFRVGA ALLCRDGTVY KGCNIENCSY GLTVCAERTA
LLKAISEGQK QFKAIAINTD IDQFPTPCGA CRQFLCEATM GEQQSQLWRR REIDVPVLLR
MPSSVRDLHI AVMRNDMNLL MRVIEAGNEW KYPFLDVCVD VNYPWWDHEN PSAKNGLTAL
EEAIALNHLS IAKALIEAGA NVLFVNVNGS STLHKAAYHG RQAMIELLAS SGAQVNHCDY
NGNTPLHILC LNALIHNNVK CVSTMLQYGG KVNTRNLECA TPLHYAAACG AAKIAELLIK
WKADPDMMDR KSFTPFYYCV LPVINRGFQG TTADIREMLR RQLSCIKVLL NAGCDSLGFA
TWMLSYQKSI PEDGEFKCWL AKSSPESLKH LCRVFIQNRL RCNKTRQQNL CTNKTVNQFD
IPNTLKAYLR RRVID
//
