GenomeNet

Database: UniProt
Entry: A0A1A0H625_9ASCO
LinkDB: A0A1A0H625_9ASCO
Original site: A0A1A0H625_9ASCO 
ID   A0A1A0H625_9ASCO        Unreviewed;       452 AA.
AC   A0A1A0H625;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=choline-phosphate cytidylyltransferase {ECO:0000256|ARBA:ARBA00026101};
DE            EC=2.7.7.15 {ECO:0000256|ARBA:ARBA00026101};
GN   ORFNames=METBIDRAFT_222149 {ECO:0000313|EMBL:OBA19368.1};
OS   Metschnikowia bicuspidata var. bicuspidata NRRL YB-4993.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Metschnikowiaceae; Metschnikowia.
OX   NCBI_TaxID=869754 {ECO:0000313|EMBL:OBA19368.1, ECO:0000313|Proteomes:UP000092555};
RN   [1] {ECO:0000313|EMBL:OBA19368.1, ECO:0000313|Proteomes:UP000092555}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL YB-4993 {ECO:0000313|EMBL:OBA19368.1,
RC   ECO:0000313|Proteomes:UP000092555};
RG   DOE Joint Genome Institute;
RA   Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goker M.,
RA   Salamov A., Wisecaver J., Long T.M., Aerts A.L., Barry K., Choi C.,
RA   Clum A., Coughlan A.Y., Deshpande S., Douglass A.P., Hanson S.J.,
RA   Klenk H.-P., LaButti K., Lapidus A., Lindquist E., Lipzen A.,
RA   Meier-kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J., Peng Y.,
RA   Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C., Stielow J.B.,
RA   Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V., Jeffries T.W.;
RT   "Comparative genomics of biotechnologically important yeasts.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the cytidylyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00010101}.
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:OBA19368.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LXTC01000007; OBA19368.1; -; Genomic_DNA.
DR   RefSeq; XP_018709900.1; XM_018855149.1.
DR   AlphaFoldDB; A0A1A0H625; -.
DR   STRING; 869754.A0A1A0H625; -.
DR   GeneID; 30028125; -.
DR   OrthoDB; 5474784at2759; -.
DR   Proteomes; UP000092555; Unassembled WGS sequence.
DR   GO; GO:0004105; F:choline-phosphate cytidylyltransferase activity; IEA:InterPro.
DR   CDD; cd02174; CCT; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   InterPro; IPR041723; CCT.
DR   InterPro; IPR004821; Cyt_trans-like.
DR   InterPro; IPR045049; Pcy1-like.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   NCBIfam; TIGR00125; cyt_tran_rel; 1.
DR   PANTHER; PTHR10739:SF13; CHOLINE-PHOSPHATE CYTIDYLYLTRANSFERASE; 1.
DR   PANTHER; PTHR10739; CYTIDYLYLTRANSFERASE; 1.
DR   Pfam; PF01467; CTP_transf_like; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
PE   3: Inferred from homology;
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209};
KW   Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264};
KW   Reference proteome {ECO:0000313|Proteomes:UP000092555}.
FT   DOMAIN          146..273
FT                   /note="Cytidyltransferase-like"
FT                   /evidence="ECO:0000259|Pfam:PF01467"
FT   REGION          63..116
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          348..370
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          402..452
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        79..116
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        402..419
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   452 AA;  52174 MW;  23F903F83872B79B CRC64;
     MCTHVTPGLF PQKYHRLFPQ HISDCPNIMA KQADAEASDI NSPLTRTLSV DLIAPKLTSL
     FRKRKRSHSN ISSPNRSAEN SEDESHDNSG TEEGSHKRRK VKTKEEEELE AREKELDAEL
     PEEYRKFRPL GHKFNLPPTD RPIRIYADGV FDLFHLGHMR QLEQAKKSFE NVELVCGVPS
     DKETQKRKGL TVLSDKHRVE TLKHCKWVDE VIADAPWCVT PSFLIKNRID YVAHDDLPYA
     SADSDDIYKP IKERGMFLTT QRTEGISTSD IITKIIRDYD KYLMRNFARG ATRKELNVSW
     FKKNELDFKK HISDFRTYWM RNRNSFNNVS KDLYVEVREY LRGRKSENLH SGNSSLTLAS
     DTDDASRPSS PLTEFASKYI GNKNDKPLRS ILGNFKDWIG RDDSHDEDSA GDEPKRITRS
     RSAPGTPKNG MKEDDLKSTH KANKKPKKRK EY
//
DBGET integrated database retrieval system