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Database: UniProt
Entry: Q1K4W9_NEUCR
LinkDB: Q1K4W9_NEUCR
Original site: Q1K4W9_NEUCR 
ID   Q1K4W9_NEUCR            Unreviewed;       419 AA.
AC   Q1K4W9;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 60.
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=NCU01571 {ECO:0000313|EMBL:EAA26972.1};
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110 {ECO:0000313|EMBL:EAA26972.1, ECO:0000313|Proteomes:UP000001805};
RN   [1] {ECO:0000313|EMBL:EAA26972.1, ECO:0000313|Proteomes:UP000001805}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987
RC   {ECO:0000313|Proteomes:UP000001805};
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., Jaffe D.,
RA   FitzHugh W., Ma L.J., Smirnov S., Purcell S., Rehman B., Elkins T.,
RA   Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., Qui D.,
RA   Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P., Glass L., Orbach M.J., Berglund J.A., Voelker R., Yarden O.,
RA   Plamann M., Seiler S., Dunlap J., Radford A., Aramayo R., Natvig D.O.,
RA   Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I., Sachs M.S.,
RA   Lander E.S., Nusbaum C., Birren B.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
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; CM002237; EAA26972.1; -; Genomic_DNA.
DR   PIR; T49344; T49344.
DR   RefSeq; XP_956208.1; XM_951115.2.
DR   AlphaFoldDB; Q1K4W9; -.
DR   STRING; 367110.Q1K4W9; -.
DR   PaxDb; 5141-EFNCRP00000001663; -.
DR   EnsemblFungi; EAA26972; EAA26972; NCU01571.
DR   GeneID; 3872346; -.
DR   KEGG; ncr:NCU01571; -.
DR   VEuPathDB; FungiDB:NCU01571; -.
DR   HOGENOM; CLU_031996_2_0_1; -.
DR   InParanoid; Q1K4W9; -.
DR   OrthoDB; 5489560at2759; -.
DR   Proteomes; UP000001805; Chromosome 6, Linkage Group II.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005968; C:Rab-protein geranylgeranyltransferase complex; IBA:GO_Central.
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; 2.
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; PF01239; PPTA; 5.
DR   SUPFAM; SSF48439; Protein prenylyltransferase; 1.
DR   PROSITE; PS51147; PFTA; 5.
PE   3: Inferred from homology;
KW   Prenyltransferase {ECO:0000256|ARBA:ARBA00022602,
KW   ECO:0000256|RuleBase:RU367120};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001805};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|RuleBase:RU367120}.
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          84..154
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        84..133
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   419 AA;  48609 MW;  7619A32BC6067957 CRC64;
     MADQGGSNHG IARTSRTRTE EQRQKDLERI KDYRALEDQV RHHAAKNDYS SDVFALTSKL
     LRLNPEYYTV WNVRRRCLIS GLLSKPSPGS SPSKALPTSS PTATTTTSSA DFSSSLSTET
     PPAPESQTTG KSGITAEDDE EQKQQTRQQD QQNDQQILQK ELHFTIPLLL ESPKCYWIWS
     YRLWILKQVI ERLPVPVARN IWEEELGLTS KMLLRDQRNF HAWGYRRHVV EQLESPELEG
     KSLVESEFEF TTKKISQNLS NFSAWHSRSK LIPRLLDERN ANDEARKAFF EEELNKIGEA
     INVGPDDQSL WYYHQFLMLN LVNSAEHPTI APAFTQEERV TYLRREIESI QELLEDYDDA
     KLIYEALFDY TLYLCQLQGR KPNEQEEKDL KGWLGNLKKL DPMRSGRWAD LERDLGLKE
//
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