ID   F2UA35_SALR5            Unreviewed;      1135 AA.
AC   F2UA35;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   RecName: Full=PA14 domain-containing protein {ECO:0000259|PROSITE:PS51820};
GN   ORFNames=PTSG_05319 {ECO:0000313|EMBL:EGD73610.1};
OS   Salpingoeca rosetta (strain ATCC 50818 / BSB-021).
OC   Eukaryota; Choanoflagellata; Craspedida; Salpingoecidae; Salpingoeca.
OX   NCBI_TaxID=946362 {ECO:0000313|Proteomes:UP000007799};
RN   [1] {ECO:0000313|Proteomes:UP000007799}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 50818 {ECO:0000313|Proteomes:UP000007799};
RA   Russ C., Cuomo C., Burger G., Gray M.W., Holland P.W.H., King N.,
RA   Lang F.B.F., Roger A.J., Ruiz-Trillo I., Young S.K., Zeng Q., Gargeya S.,
RA   Alvarado L., Berlin A., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA   Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C.,
RA   Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., White J., Yandava C., Haas B., Nusbaum C.,
RA   Birren B.;
RT   "Annotation of Salpingoeca rosetta.";
RL   Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-
CC       pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}.
CC   -!- SIMILARITY: Belongs to the chondroitin N-
CC       acetylgalactosaminyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00009239}.
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DR   EMBL; GL832966; EGD73610.1; -; Genomic_DNA.
DR   RefSeq; XP_004993891.1; XM_004993834.1.
DR   AlphaFoldDB; F2UA35; -.
DR   STRING; 946362.F2UA35; -.
DR   EnsemblProtists; EGD73610; EGD73610; PTSG_05319.
DR   GeneID; 16074470; -.
DR   KEGG; sre:PTSG_05319; -.
DR   eggNOG; KOG3588; Eukaryota.
DR   eggNOG; KOG4599; Eukaryota.
DR   InParanoid; F2UA35; -.
DR   OrthoDB; 2907318at2759; -.
DR   Proteomes; UP000007799; Unassembled WGS sequence.
DR   GO; GO:0032580; C:Golgi cisterna membrane; IEA:InterPro.
DR   GO; GO:0008376; F:acetylgalactosaminyltransferase activity; IEA:InterPro.
DR   CDD; cd00761; Glyco_tranf_GTA_type; 1.
DR   Gene3D; 3.10.450.240; -; 1.
DR   InterPro; IPR008428; Chond_GalNAc.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   InterPro; IPR037524; PA14/GLEYA.
DR   InterPro; IPR011658; PA14_dom.
DR   InterPro; IPR007379; Tim44-like_dom.
DR   PANTHER; PTHR12369; CHONDROITIN SYNTHASE; 1.
DR   PANTHER; PTHR12369:SF5; HEXOSYLTRANSFERASE; 1.
DR   Pfam; PF05679; CHGN; 1.
DR   Pfam; PF07691; PA14; 1.
DR   SMART; SM00978; Tim44; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR   PROSITE; PS51820; PA14; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007799};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        7..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          167..323
FT                   /note="PA14"
FT                   /evidence="ECO:0000259|PROSITE:PS51820"
FT   REGION          49..156
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1109..1135
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        66..84
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        98..112
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        138..156
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1135 AA;  127825 MW;  44962A137DF6DF72 CRC64;
     MVERGRLSFL VGIVVGLVLS SAISYMYPGS STTSTSTLST KCTCPTTGHV IDLPTQAPSF
     PSTPPPEQQQ QQQQQQQQQQ QQQQQEENRE EEVPEKRSTT AQQTNTNAST AGGGGGGDAA
     GGKDAGGADD DDAEREDSPM EPVTPEPEKQ ELPEDAVKKQ DVANAGDLRN KVNAHYWLNM
     CGKSLRILKN HPHFPGKPHF VSFLEDLQIR YHTVNYAQRL LGFIHPPSDG SYRFALSSRG
     CSEMHMSTDT FPANAQLIVS LCKGREEKFT EPNDFSHVSK PLKLHAGKKY YFDVLHKAGD
     GSEHLQVAWS RDDGPFTIIK GDHLSAYEDT TVSSILSRDA SEGEWEVEQV FTQEQYTDKH
     LPSFTVPMYY PDAELKSVLP ACSWSPSYAR PHRVSQYQAA NSYVCKMSAV YPDDHTTLLG
     SHQARGPNKS MQKSFAERIA KAYVQKINAK RQQDGKSAVA LKKIVHMESK EHAGQTRVLA
     ELDVERDGRV LRVSRYIVSK GNGELCDANN FQWRKQAMVH IIVPVLNQGA WVRHLIENLG
     HVYETTKDER FNLILVDFGS DDIDIQAALE NSPLKRYQVV SLDGPFSRSL GVQRGADAVD
     SDEDIIFTCD LHLEMPPILI EDIRKHCVYG KAGYNPVVAR LGCGNFQNEP KGFWEMLGYG
     LFAMYKKDFD AIGGMNVQKY KYQWGGEDWD MLDRFDAKGF ECERLKVYGF YHFHHSRTTM
     WGGSNPIADR LDVPFDFAVT ENTNVIVGSC DGALAMWMRG AVGAIRPQTS KDFVLEPKNG
     VIRLTKHPNA PSVGQKFDLA PNTKAVKVMQ SGLCLLAEKE GKPATVGSCT SKPGDVPATP
     SSLMSMLLVS MWRSSRVTMQ APLLRTQVRA MSYQKRKKKM MKQMMSRAPK RESAAKTSAM
     NKEIQETQHL QLDSLGIVVD HWVPIPASHK ASIFSLEGLK QRWEHVKKRF RSTLSVGVIR
     RYDKSWKPVP FAQQVQDMLV EVQTAFSEAS RQHSPLRLQD KLTAQALSAM KKQAQTPHVW
     EFVEQVERPR VVNAFTFPVE DKNNLYGQVT VRLHMKQRYA PLGHPLEERD VVDYVVLEKR
     VVSPSAPWRI CSKIVPMFLL PPEEKAKLKA RHEDMERRMK ERKEKEKQQQ NANKN
//