ID A0A059LS92_9CHLO Unreviewed; 1023 AA.
AC A0A059LS92;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=Glycosyltransferase {ECO:0000256|RuleBase:RU363055};
DE EC=2.4.2.- {ECO:0000256|RuleBase:RU363055};
GN ORFNames=H632_c49p1 {ECO:0000313|EMBL:KDD76980.1};
OS Helicosporidium sp. ATCC 50920.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC Chlorellales; Chlorellaceae; Helicosporidium.
OX NCBI_TaxID=1291522 {ECO:0000313|EMBL:KDD76980.1, ECO:0000313|Proteomes:UP000026042};
RN [1] {ECO:0000313|EMBL:KDD76980.1, ECO:0000313|Proteomes:UP000026042}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50920 {ECO:0000313|EMBL:KDD76980.1,
RC ECO:0000313|Proteomes:UP000026042};
RX PubMed=24809511;
RA Pombert J.F., Blouin N.A., Lane C., Boucias D., Keeling P.J.;
RT "A lack of parasitic reduction in the obligate parasitic green alga
RT helicosporidium.";
RL PLoS Genet. 10:E1004355-E1004355(2014).
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000256|RuleBase:RU363055}; Single-pass type II membrane protein
CC {ECO:0000256|RuleBase:RU363055}.
CC -!- SIMILARITY: Belongs to the PDK/BCKDK protein kinase family.
CC {ECO:0000256|ARBA:ARBA00006155}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 77 family.
CC {ECO:0000256|ARBA:ARBA00007033, ECO:0000256|RuleBase:RU363055}.
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:KDD76980.1}.
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DR EMBL; AYPS01000049; KDD76980.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A059LS92; -.
DR STRING; 1291522.A0A059LS92; -.
DR OrthoDB; 311766at2759; -.
DR UniPathway; UPA00251; UER00320.
DR Proteomes; UP000026042; Unassembled WGS sequence.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0004852; F:uroporphyrinogen-III synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0080147; P:root hair cell development; IEA:InterPro.
DR CDD; cd06578; HemD; 1.
DR Gene3D; 3.40.50.10090; -; 2.
DR Gene3D; 1.20.140.20; Alpha-ketoacid/pyruvate dehydrogenase kinase, N-terminal domain; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR036108; 4pyrrol_syn_uPrphyn_synt_sf.
DR InterPro; IPR003754; 4pyrrol_synth_uPrphyn_synth.
DR InterPro; IPR036784; AK/P_DHK_N_sf.
DR InterPro; IPR018955; BCDHK/PDK_N.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005069; Nucl-diP-sugar_transferase.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR044290; RRA1/2/3.
DR PANTHER; PTHR46581; ARABINOSYLTRANSFERASE RRA3; 1.
DR PANTHER; PTHR46581:SF3; ARABINOSYLTRANSFERASE RRA3; 1.
DR Pfam; PF10436; BCDHK_Adom3; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF02602; HEM4; 1.
DR Pfam; PF03407; Nucleotid_trans; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF69012; alpha-ketoacid dehydrogenase kinase, N-terminal domain; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF69618; HemD-like; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE 3: Inferred from homology;
KW Cell wall biogenesis/degradation {ECO:0000256|RuleBase:RU363055};
KW Glycosyltransferase {ECO:0000256|RuleBase:RU363055};
KW Golgi apparatus {ECO:0000256|RuleBase:RU363055};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Reference proteome {ECO:0000313|Proteomes:UP000026042};
KW Signal-anchor {ECO:0000256|RuleBase:RU363055};
KW Transferase {ECO:0000256|RuleBase:RU363055, ECO:0000313|EMBL:KDD76980.1};
KW Transmembrane {ECO:0000256|RuleBase:RU363055}.
FT DOMAIN 559..706
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
SQ SEQUENCE 1023 AA; 112735 MW; 72EB6FE9113EF8ED CRC64;
MCGGTSYEDY KALTAADRHK PWTPSIERDA KHPELASVLR KVAINNEVMI AVSNINYAAK
GGMLDMWIDG LKKSGVTNFL VVALDDKTKE VVEEQGVAAV RMDLEIPDSQ KNAGSNHAVS
ALKFRILRGF LELGYSVFLS DVDIVTFQNP FNFLERDSDV ESLSDGWDHG TAYGYNDVLD
DESMGWSRYQ HSMRVFVFNS GLFYIRPTRA AMDLIDLVIH RVETENGWDQ ALFNECIFFP
SRPGYKDPSI TRRVLDYTKF MNTKYLFKYL RHDEAQYKAS NPVMVHVNYH PNKFERMRAI
VKRYRDKNMT ALDKFPDGSQ IGCGARRGVW SDSLSELDTS RRVSFYDNTI EEYAGQPLER
LTLRKLMQFG RDAWYDKSRI VASANFVQEE LPKRLARRLL DLQLLPHLVV SNPHISVVYD
AYYSALCELR RAPRVSNLQD NAAFCALLKR LVDEHTPMLD CLATGLREVR SKPLVGSALQ
LDAFLDGMLR SRISRRVLAE QHLQLESARP GYVGIIATEL GLADSVELAA ARCRSVCAET
YGAAPQIVVI GPRDKTIPYI PAHLDYMLYE LFKNSTRAVM ERRAHVGKHL PPIHVRICDG
DDKVTLRVSD QGGGVPVGVE SKIWQFGFST AQEGRKPEST DKAPSFGAAM AAVEATGGGV
GRFKMGGLGF GLPLSRLYAR YFGGDLTLVN LPGYGADAYL ALRRLGDEWE ETLHEDGGVD
NHSEAQSLPL CAASTSGHSN LPRASLPGCV LLTREVGKNA ELEELLTARR ICFRTLPLVE
TAAGPDRGQL ASVLQSSKFD WVCITSPTAA RELSEAWRGA GRPVLSLAVV GEGTAAALER
FSDGSLTAHF IASQADAVHL GYELPWPARR ASAGSSPPKV LYPTSARAGP GLLQQLSSRG
FEVTRLDVYD TVGALQPSER ERADFHRQAQ KNARQLARLP PHVSEILRDV TAVVVASPSA
VVAWEALARA AGEAREKELL ALRLVCIGPT TGTAARTRGF ACIVAGAPTP AGLADAVEEA
MRL
//
