ID A0A1D6LPP2_MAIZE Unreviewed; 714 AA.
AC A0A1D6LPP2;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Geranylgeranyl transferase type-2 subunit alpha {ECO:0000256|RuleBase:RU367120};
DE EC=2.5.1.60 {ECO:0000256|RuleBase:RU367120};
DE AltName: Full=Geranylgeranyl transferase type II subunit alpha {ECO:0000256|RuleBase:RU367120};
GN ORFNames=ZEAMMB73_Zm00001d036598 {ECO:0000313|EMBL:AQK81466.1};
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577 {ECO:0000313|EMBL:AQK81466.1};
RN [1] {ECO:0000313|EMBL:AQK81466.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Seedling {ECO:0000313|EMBL:AQK81466.1};
RG Maize Genome Sequencing Project;
RA Ware D.;
RT "Update maize B73 reference genome by single molecule sequencing
RT technologies.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the transfer of a geranyl-geranyl moiety from
CC geranyl-geranyl pyrophosphate to cysteines occuring in specific C-
CC terminal amino acid sequences. {ECO:0000256|RuleBase:RU367120}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=geranylgeranyl diphosphate + L-cysteinyl-[protein] =
CC diphosphate + S-geranylgeranyl-L-cysteinyl-[protein];
CC Xref=Rhea:RHEA:21240, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11537,
CC ChEBI:CHEBI:29950, ChEBI:CHEBI:33019, ChEBI:CHEBI:57533,
CC ChEBI:CHEBI:86021; EC=2.5.1.60;
CC Evidence={ECO:0000256|ARBA:ARBA00001577,
CC ECO:0000256|RuleBase:RU367120};
CC -!- SIMILARITY: Belongs to the protein prenyltransferase subunit alpha
CC family. {ECO:0000256|ARBA:ARBA00006734, ECO:0000256|RuleBase:RU367120}.
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DR EMBL; CM000782; AQK81466.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1D6LPP2; -.
DR ExpressionAtlas; A0A1D6LPP2; baseline and differential.
DR GO; GO:0004663; F:Rab geranylgeranyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0097354; P:prenylation; IEA:UniProtKB-UniRule.
DR Gene3D; 1.25.40.120; Protein prenylyltransferase; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR025875; Leu-rich_rpt_4.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR002088; Prenyl_trans_a.
DR PANTHER; PTHR11129:SF2; GERANYLGERANYL TRANSFERASE TYPE-2 SUBUNIT ALPHA; 1.
DR PANTHER; PTHR11129; PROTEIN FARNESYLTRANSFERASE ALPHA SUBUNIT/RAB GERANYLGERANYL TRANSFERASE ALPHA SUBUNIT; 1.
DR Pfam; PF12799; LRR_4; 1.
DR Pfam; PF01239; PPTA; 5.
DR SMART; SM00365; LRR_SD22; 2.
DR SUPFAM; SSF52058; L domain-like; 1.
DR SUPFAM; SSF48439; Protein prenylyltransferase; 1.
DR PROSITE; PS51450; LRR; 2.
DR PROSITE; PS51147; PFTA; 5.
PE 3: Inferred from homology;
KW Prenyltransferase {ECO:0000256|ARBA:ARBA00022602,
KW ECO:0000256|RuleBase:RU367120}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|RuleBase:RU367120, ECO:0000313|EMBL:AQK81466.1}.
SQ SEQUENCE 714 AA; 81837 MW; 72193BAF6C3B14E7 CRC64;
MHGRPRRPAK PEDDEAASAK AAKLRDLQAQ VLHNHHARTY TKESIGLSFK LLETNPEAYT
AWNYRKLALQ HNVKELSDPQ AIKSAIDDEL RVAEVALRQN PKSYGAWYHR KWLLNQKLAP
VDFKYELGLL DKLLKVDARN FHGWNYRRFL ARFMGLPDDE ELKYTMDKIS DNFSNYSAWH
NRSILLSNLL IQQSKGFESK QKIFSEEFEL VTQALFTDPS DQSGWFYHLW LLAQTSSPDN
PQLIASWPSN AAKLSFSFIK EKAEQHTLSS VWSRTVPIVL YFNEPVKGLN HSSVNLKSDL
EFGKDIQWRP LTMADSGYSK CWATYLQITN ECSSLQEYSV EMSIPCSDDI VSRSGSNYNC
PVHFTFYIEL ISNNAAQGLD TFDKPVAWNC SDSFQSHGNR DPIPLDLLNI TSALVEHDSD
WHFERLSEEI DLFRELADDN SKFGKLTLAR LLLACAAIKS RGRSLIERKG YCEEALGLFT
DLIHLDPSHK QYYEDERSLA LMDKVKNVLN RLTCDMETFT KHCSVQVQPN SAPLHHVQFR
RLSVTRIGFA ERLLWVQMLD LSHNSLRSVE GLEALQRLVF LNISNNQISS FTALEPLTKI
ISLKVLDLSF NEIGAHSIDT ARYICPSPFS HKTEASEAFE EYQEVNNINV TEYWDAILFF
RSLKLAQLDI RGNAVASKDG FRTLVVTLIP CLKWFDGEVP LRSWAILVVS RLTM
//