ID A0A1Z4VMA2_9GAMM Unreviewed; 544 AA.
AC A0A1Z4VMA2;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=CMP/dCMP deaminase zinc-binding protein {ECO:0000313|EMBL:BAZ92615.1};
GN ORFNames=FOKN1_0211 {ECO:0000313|EMBL:BAZ92615.1};
OS Thiohalobacter thiocyanaticus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiohalobacterales;
OC Thiohalobacteraceae; Thiohalobacter.
OX NCBI_TaxID=585455 {ECO:0000313|EMBL:BAZ92615.1, ECO:0000313|Proteomes:UP000218765};
RN [1] {ECO:0000313|EMBL:BAZ92615.1, ECO:0000313|Proteomes:UP000218765}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FOKN1 {ECO:0000313|EMBL:BAZ92615.1,
RC ECO:0000313|Proteomes:UP000218765};
RA Oshiki M., Fukushima T., Kawano S., Nakagawa J.;
RT "Thiocyanate degradation by Thiohalobacter thiocyanaticus FOKN1.";
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC family. {ECO:0000256|ARBA:ARBA00006576}.
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DR EMBL; AP018052; BAZ92615.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z4VMA2; -.
DR KEGG; ttc:FOKN1_0211; -.
DR Proteomes; UP000218765; Chromosome.
DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR Gene3D; 3.40.140.10; Cytidine Deaminase, domain 2; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd.
DR InterPro; IPR002125; CMP_dCMP_dom.
DR InterPro; IPR016193; Cytidine_deaminase-like.
DR InterPro; IPR015517; dCMP_deaminase-rel.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; NF041025; antiphage_deaminase; 1.
DR PANTHER; PTHR11086:SF18; CYTIDINE AND DCMP DEAMINASE DOMAIN-CONTAINING PROTEIN 1-RELATED; 1.
DR PANTHER; PTHR11086; DEOXYCYTIDYLATE DEAMINASE-RELATED; 1.
DR Pfam; PF00383; dCMP_cyt_deam_1; 1.
DR SUPFAM; SSF53927; Cytidine deaminase-like; 1.
DR PROSITE; PS00903; CYT_DCMP_DEAMINASES_1; 1.
DR PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000218765};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 267..465
FT /note="CMP/dCMP-type deaminase"
FT /evidence="ECO:0000259|PROSITE:PS51747"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 544 AA; 61335 MW; 3EDBA218AE44B368 CRC64;
MCAAVTKKRS VKKKAGSTRG VADPKRTAKK KSRSKENEVG PAPELFIGLV GAVGSDLETV
NRQIRSYLKA ANYKTVDIRL SRLITDCKDY AHLEKLKNGP ENERIDKLMD AGDDLRRNLK
RGDAVSLLGI LAVRAHRKTR KGDSKEPVSR TAYIFNSLKH PDEIESLRNI YGESFFVVST
YAPKRERIES LAKRIARSKG KFRADDYENE AESLVEKDEK EVGEDYGQNV RDAFPLADVF
ISQRKNVDSQ IKRFIELIFG HPFITPTVDE YGMFHAKAAA LRSADLSRQV GAVITTDDGE
MISAGCNEVP KAGGGSVWED KVESKQDYRD FKIGQDASAV MKREIITEIF EKLKTAGWLS
QAKRRKRPDK LAEDALYSKT DAPLKDTRAA SIIEFGRIVH AEMSAITDAA RRGLSVKDAN
LYCTTFPCHM CARHIVAAGM QRVVYVEPYP KSMAKDLYKR SIQVDGDEAD EDAVVFEPFV
GIAPIRYISL FEMPPRKDKR GYPLDWELAT ANPQIQETYP RYIDLEEGYI EPLFKRYEQY
AATD
//
