ID A0A151NPP2_ALLMI Unreviewed; 657 AA.
AC A0A151NPP2;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Rab proteins geranylgeranyltransferase component A {ECO:0000256|PIRNR:PIRNR016550};
GN Name=CHM {ECO:0000313|EMBL:KYO38455.1};
GN ORFNames=Y1Q_0015689 {ECO:0000313|EMBL:KYO38455.1};
OS Alligator mississippiensis (American alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=8496 {ECO:0000313|EMBL:KYO38455.1};
RN [1] {ECO:0000313|EMBL:KYO38455.1, ECO:0000313|Proteomes:UP000050525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSC_2009_1 {ECO:0000313|EMBL:KYO38455.1};
RX PubMed=22293439; DOI=10.1186/gb-2012-13-1-415;
RA St John J.A., Braun E.L., Isberg S.R., Miles L.G., Chong A.Y., Gongora J.,
RA Dalzell P., Moran C., Bed'hom B., Abzhanov A., Burgess S.C., Cooksey A.M.,
RA Castoe T.A., Crawford N.G., Densmore L.D., Drew J.C., Edwards S.V.,
RA Faircloth B.C., Fujita M.K., Greenwold M.J., Hoffmann F.G., Howard J.M.,
RA Iguchi T., Janes D.E., Khan S.Y., Kohno S., de Koning A.J., Lance S.L.,
RA McCarthy F.M., McCormack J.E., Merchant M.E., Peterson D.G., Pollock D.D.,
RA Pourmand N., Raney B.J., Roessler K.A., Sanford J.R., Sawyer R.H.,
RA Schmidt C.J., Triplett E.W., Tuberville T.D., Venegas-Anaya M.,
RA Howard J.T., Jarvis E.D., Guillette L.J.Jr., Glenn T.C., Green R.E.,
RA Ray D.A.;
RT "Sequencing three crocodilian genomes to illuminate the evolution of
RT archosaurs and amniotes.";
RL Genome Biol. 13:415-415(2012).
CC -!- FUNCTION: Substrate-binding subunit (component A) of the Rab
CC geranylgeranyltransferase (GGTase) complex. Binds unprenylated Rab
CC proteins and presents the substrate peptide to the catalytic component
CC B. The component A is thought to be regenerated by transferring its
CC prenylated Rab back to the donor membrane.
CC {ECO:0000256|PIRNR:PIRNR016550}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR016550}.
CC -!- SIMILARITY: Belongs to the Rab GDI family.
CC {ECO:0000256|ARBA:ARBA00005593, ECO:0000256|PIRNR:PIRNR016550}.
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:KYO38455.1}.
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DR EMBL; AKHW03002524; KYO38455.1; -; Genomic_DNA.
DR RefSeq; XP_014462753.1; XM_014607267.2.
DR AlphaFoldDB; A0A151NPP2; -.
DR STRING; 8496.A0A151NPP2; -.
DR GeneID; 102574278; -.
DR KEGG; amj:102574278; -.
DR CTD; 1121; -.
DR eggNOG; KOG4405; Eukaryota.
DR OrthoDB; 197300at2759; -.
DR Proteomes; UP000050525; Unassembled WGS sequence.
DR GO; GO:0005968; C:Rab-protein geranylgeranyltransferase complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005092; F:GDP-dissociation inhibitor activity; IEA:InterPro.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:UniProtKB-UniRule.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR Gene3D; 1.10.405.10; Guanine Nucleotide Dissociation Inhibitor, domain 1; 1.
DR Gene3D; 3.30.519.10; Guanine Nucleotide Dissociation Inhibitor, domain 2; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR018203; GDP_dissociation_inhibitor.
DR InterPro; IPR001738; Rab_escort.
DR PANTHER; PTHR11787; RAB GDP-DISSOCIATION INHIBITOR; 1.
DR PANTHER; PTHR11787:SF4; RAB PROTEINS GERANYLGERANYLTRANSFERASE COMPONENT A; 1.
DR Pfam; PF00996; GDI; 2.
DR PIRSF; PIRSF016550; Rab_ger_ger_transf_A_euk; 1.
DR PRINTS; PR00893; RABESCORT.
DR PRINTS; PR00891; RABGDIREP.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|PIRNR:PIRNR016550};
KW GTPase activation {ECO:0000256|PIRNR:PIRNR016550};
KW Reference proteome {ECO:0000313|Proteomes:UP000050525};
KW Transferase {ECO:0000313|EMBL:KYO38455.1}.
FT REGION 152..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 605..657
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..179
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..204
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 641..657
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 657 AA; 73278 MW; A59D5E39BBFD6437 CRC64;
MADNLPSEFD VAVIGTGLPE SIIAAACSRS GQRVLHVDSR SYYGGNWASF SFSGLLSWIK
EKQEKTEVSE ESEDWRKLIL ETEEAISLSK KDTTIQHVED VCYISQDSAE DIEEAGALSK
LPDLGGSDTN ETAQQSGKGC LALDKQLGTK GCEMSPETIA SNDRECTPEG EDTEVISERE
SSYDATSGHS TLETEKTENA STAEVSNLEP KKITYSQIVK EGRRFNIDLV SKVLYSQGLL
IDLLIKSNVS RYAEFKNATR ILVFREGKVE QVPCSRADVF NSKQLTMIEK RMLMKFLTFC
LEYEQHPDEY QDYKDCTFSK YLKSQKLTPN LQHFILHSIA MVSESDSSTT DGLKATKKFL
HCLGRYGNTP FLFPLYGQGE ISQCFCRMCA VFGGTYCLRH SIQCLVVDKE SGRCKAIIDH
FGQRISANYF VVEDSYLSEE TCTNVCYRQI SRAVLITDQS VLKTQSDQQI SVLTVPPVEP
GQPVVCVIEL CSSTMTCMKG TYLVHLTCSS TKTAKEDLEP VIQKLFILND EKETESENGG
GLEKPRVLWA VYFNMRDSAG IDRNSYDSLP PNVYICSGPD CALGNDYAVK QAETIFQEMF
PKEEFCPPPP NPEDIVYDGD GTQPEDPGFS ISPEPKAEPL PEESSNIENK VTEEHNE
//
