ID A0A0W8CC11_PHYNI Unreviewed; 1221 AA.
AC A0A0W8CC11;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE SubName: Full=Cytidine deaminase {ECO:0000313|EMBL:KUF81612.1};
GN ORFNames=AM587_10011139 {ECO:0000313|EMBL:KUF81612.1};
OS Phytophthora nicotianae (Buckeye rot agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=4790 {ECO:0000313|EMBL:KUF81612.1, ECO:0000313|Proteomes:UP000052943};
RN [1] {ECO:0000313|EMBL:KUF81612.1, ECO:0000313|Proteomes:UP000052943}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=race 0 {ECO:0000313|Proteomes:UP000052943};
RA Liu H., Ma X., Yu H., Fang D., Li Y., Wang X., Wang W., Dong Y., Xiao B.;
RT "Genomes and virulence difference between two physiological races of
RT Phytophthora nicotianae.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
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:KUF81612.1}.
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DR EMBL; LNFO01004094; KUF81612.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0W8CC11; -.
DR STRING; 4790.A0A0W8CC11; -.
DR EnsemblProtists; KUF81612; KUF81612; AM587_10011139.
DR OMA; CRWLDAQ; -.
DR Proteomes; UP000052943; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005246; F:calcium channel regulator activity; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR CDD; cd01283; cytidine_deaminase; 1.
DR CDD; cd04508; Tudor_SF; 1.
DR Gene3D; 2.30.30.140; -; 1.
DR Gene3D; 3.40.140.10; Cytidine Deaminase, domain 2; 1.
DR Gene3D; 1.10.238.10; EF-hand; 1.
DR Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1.
DR InterPro; IPR002125; CMP_dCMP_dom.
DR InterPro; IPR016193; Cytidine_deaminase-like.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR037608; STIM.
DR InterPro; IPR002999; Tudor.
DR PANTHER; PTHR15136; STROMAL INTERACTION MOLECULE HOMOLOG; 1.
DR PANTHER; PTHR15136:SF5; STROMAL INTERACTION MOLECULE HOMOLOG; 1.
DR Pfam; PF00536; SAM_1; 1.
DR SMART; SM00454; SAM; 1.
DR SMART; SM00333; TUDOR; 2.
DR SUPFAM; SSF53927; Cytidine deaminase-like; 1.
DR SUPFAM; SSF47473; EF-hand; 1.
DR SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000052943};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 126..246
FT /note="CMP/dCMP-type deaminase"
FT /evidence="ECO:0000259|PROSITE:PS51747"
FT DOMAIN 282..347
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT DOMAIN 372..407
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT REGION 674..770
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 881..982
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1102..1146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1192..1221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 684..762
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 881..896
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 897..915
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 916..934
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 951..967
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1120..1146
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1221 AA; 138790 MW; F89A0375525C6160 CRC64;
MSNQLEDDLH RVLRLARAEA RASKQKKNIN YKKPRQVEQR HRHDQYLTGS KERQTLLTAK
MQGLAAVYGL DSSSRHLGNC SSKSVLYHNK ETLEDDQVLQ QRLDARRTLY KRHFSGVMTD
SSGRKRDIEN VLEAAAREAR SSRSKGVGIG AALLTESQTI YSAGAIENGA LVRCAEHAAV
MKMLTSYANS SPIIVAMAIC SEQRDLLPFP CGSCRELLAD CGDFPVYLVN ALGETEETRS
SALFPRARHS EFTQILTKSV SKRSPVRTPT PSDQTPVEVK DWTTDHVLKW LEHDVELPQY
REVFERNNID GCTLVLLEGS DLQLLLGITH PLHRSKLLTY LDRLRDRELL ARGLDFTQLE
DYLAVLDIDR VSAVAQLKTT FDRLDADKDG FLDFNQVKQA LSRLRCTIPT ANKDGVVEAS
PQEVERLLYS EELFGKEASS TGKVSFPAFT RAFSKLATQP ADTSTVTQGS FAVHAFGPRL
PVLDLKNLRE CFEQQVQGNS LDEAGLVRLL IELGQSDTQS KELACRWLDA QDDIEESGDT
MSFAQLVARY AQLVDSNETS GVSRLQQLFT SYEPVHSTRL KPRTVVQRAL STLFPAVPSD
EVNVWCASFW PAKVSRANAD TKPKITTLAF PEFTLACLEF AAEVYAREQE AASIKRSLRN
DALVHRSRVV HLHSSGHVRM CPQPPDELKS DKKDRKAVPK LKEDSKSDED EGKCAEREGK
AQDSDDEKSQ RRSRREQQVN EAFDRFVRRH STQVRSSSDD GKQNSEDEDE SCMLNAVEAA
QAALELGAVL SREQVLRYLE REGLGRIRRR DISRTAFHRL MKRLDANQSY PRDLLLDIND
RTQKREVFVR TASKSPRHRA YKNMPDYDEF LRRKLAESNG SQWKKEVDEL RRKQQRREER
RTSKKLKKRS SRHRKHDSDG KHDSDSDSTA SERRQSRSKH KRKSHHHRPS SSDTSTATET
SSNESTRSSH RPTRRGFEPG ARVASMVHGR GTIERIYRDY FVADVHFDST KTRRQGKIIL
CRTDGTFDVL VNEFGLAQTL KRMPRSALTL ANVKPRIYRD GDRVMVRQRT EYLRGKVCNC
RTEGTYDVKL IRSPQKILER LAPELLAPDN DEDGYTDDEI EVDKTPKSKP KKDSDDEFEP
EFSRGDRVEA RFGGKETYYP GTIERVHPNG CCDISYDDGD EEERVKPSLI RALLKKTGPR
KPTPARKTSD DGYESDLFES D
//
