ID   CAPTB_DICDI             Reviewed;         409 AA.
AC   Q54XM0;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=Uncharacterized CDP-alcohol phosphatidyltransferase class-I family protein 2;
GN   Name=captB; ORFNames=DDB_G0278947;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-I
CC       family. {ECO:0000305}.
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; AAFI02000024; EAL68075.1; -; Genomic_DNA.
DR   RefSeq; XP_647783.1; XM_642691.1.
DR   AlphaFoldDB; Q54XM0; -.
DR   STRING; 44689.DDB0266710; -.
DR   PaxDb; Q54XM0; -.
DR   EnsemblProtists; EAL68075; EAL68075; DDB_G0278947.
DR   GeneID; 8621742; -.
DR   KEGG; ddi:DDB_G0278947; -.
DR   dictyBase; DDB_G0278947; captB.
DR   eggNOG; KOG2877; Eukaryota.
DR   HOGENOM; CLU_035066_0_1_1; -.
DR   InParanoid; Q54XM0; -.
DR   OMA; FPYQNVL; -.
DR   PhylomeDB; Q54XM0; -.
DR   Reactome; R-DDI-1483191; Synthesis of PC.
DR   Reactome; R-DDI-1483213; Synthesis of PE.
DR   PRO; PR:Q54XM0; -.
DR   Proteomes; UP000002195; Chromosome 3.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016780; F:phosphotransferase activity, for other substituted phosphate groups; IEA:InterPro.
DR   GO; GO:0008654; P:phospholipid biosynthetic process; IEA:InterPro.
DR   Gene3D; 1.20.120.1760; -; 1.
DR   InterPro; IPR000462; CDP-OH_P_trans.
DR   InterPro; IPR043130; CDP-OH_PTrfase_TM_dom.
DR   InterPro; IPR014472; CHOPT.
DR   PANTHER; PTHR10414; PTHR10414; 1.
DR   Pfam; PF01066; CDP-OH_P_transf; 1.
DR   PIRSF; PIRSF015665; CHOPT; 1.
DR   PROSITE; PS00379; CDP_ALCOHOL_P_TRANSF; 1.
PE   3: Inferred from homology;
KW   Membrane; Reference proteome; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..409
FT                   /note="Uncharacterized CDP-alcohol phosphatidyltransferase
FT                   class-I family protein 2"
FT                   /id="PRO_0000328508"
FT   TRANSMEM        53..73
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        83..103
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        115..135
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        141..161
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        183..203
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        205..225
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        243..263
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        265..285
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        299..319
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        329..349
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          388..409
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        388..402
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   409 AA;  46188 MW;  86828AA39389E356 CRC64;
     MSKYFKYISE KGITNLANYH YSGVDNSFCG NKFLKHWWNY CVNFTPLWLA PNIITLVGLL
     CNIGMYLIMY VHCPTLTEEA PRWCYFAVAF LIFAYQTLDN VDGKQARKTK SSSPLGELFD
     HVCDALSVAM FAIVMSATLR IGPYWTFFSF IVGMWPFYLA HWEEYHAGIL VMGEFNGPTE
     AQVLFMIIEI ITGIFGSDIW TYGTSTTVGK IATVFVSIGA VVTCLQNFTN TYKLENRMTF
     GKCLLQLTPI CLFTALIVIW ASVSNLITEQ PHLFIMTLGI LFGYIQSRYI TQRVCHDDCS
     LFYPIFVPII IVVLNSILAS SDVHLVSETV ALWILFSIAC AQFLLFSYFT TQQLCDHLKI
     KVFTIPYPSN SGIGPSQEYE NSLLSQMEEG SSSIGNSTDD INPSEIEEI