GNL1_MACFA
ID GNL1_MACFA Reviewed; 607 AA.
AC Q4R8D2; Q4R939;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Guanine nucleotide-binding protein-like 1;
GN Name=GNL1; ORFNames=QtsA-10775, QtsA-12735;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Possible regulatory or functional link with the
CC histocompatibility cluster. {ECO:0000250}.
CC -!- DOMAIN: In contrast to other GTP-binding proteins, this family is
CC characterized by a circular permutation of the GTPase motifs described
CC by a G4-G1-G3 pattern.
CC -!- SIMILARITY: Belongs to the TRAFAC class YlqF/YawG GTPase family.
CC {ECO:0000255|PROSITE-ProRule:PRU01058}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB168258; BAE00382.1; -; mRNA.
DR EMBL; AB168522; BAE00640.1; -; mRNA.
DR RefSeq; XP_005553701.1; XM_005553644.2.
DR AlphaFoldDB; Q4R8D2; -.
DR STRING; 9541.XP_005553701.1; -.
DR Ensembl; ENSMFAT00000098093; ENSMFAP00000051961; ENSMFAG00000001167.
DR GeneID; 101926006; -.
DR KEGG; mcf:101926006; -.
DR CTD; 2794; -.
DR VEuPathDB; HostDB:ENSMFAG00000001167; -.
DR eggNOG; KOG1424; Eukaryota.
DR GeneTree; ENSGT00940000158047; -.
DR OrthoDB; 839833at2759; -.
DR Proteomes; UP000233100; Chromosome 4.
DR Bgee; ENSMFAG00000001167; Expressed in temporal lobe and 13 other tissues.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR030378; G_CP_dom.
DR InterPro; IPR043358; GNL1-like.
DR InterPro; IPR006073; GTP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR45709; PTHR45709; 1.
DR Pfam; PF01926; MMR_HSR1; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51721; G_CP; 1.
PE 2: Evidence at transcript level;
KW GTP-binding; Nucleotide-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..607
FT /note="Guanine nucleotide-binding protein-like 1"
FT /id="PRO_0000295688"
FT DOMAIN 178..418
FT /note="CP-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01058"
FT REGION 1..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 547..607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..28
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..59
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..583
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 225..228
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 367..374
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 411..415
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT MOD_RES 32
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P36915"
FT MOD_RES 33
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P36915"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P36915"
FT MOD_RES 48
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P36915"
FT MOD_RES 50
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P36915"
FT MOD_RES 51
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P36915"
FT MOD_RES 68
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P36915"
FT MOD_RES 324
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P36915"
FT MOD_RES 561
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P36915"
FT MOD_RES 562
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P36915"
FT MOD_RES 563
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P36915"
FT CONFLICT 10
FT /note="K -> E (in Ref. 1; BAE00382)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 607 AA; 68661 MW; 03FC159423FD6FCA CRC64;
MPRKKPFSVK QKKKQLQDKR ERKRGLQDGL RSSSNSRSGS RERREEQTDT SDGESVTHHI
RRLNQQPSQG LGPRGYDPNR YRLHFERDSR EEVERRKRAA REQVLQPVSA EVLELDIREV
YQPGSVLDFP RRPPWSYEMS KEQLMSQEER SFQEYLGKIH GAYSSEKLSY FEHNLETWRQ
LWRVLEMSDI VLLITDIRHP VVNFPPALYE YVTGELGLAL VLVLNKVDLA PPALVVAWKH
YFHQHYPQLH VVLFTSFPRD PRTPQDPSSV LKKSRRRGRG WTRALGPEQL LRACEAITVG
KVDLSSWREK IARDVAGATW GNGSGEEEEE DDGPAVLVEQ QTDSAMEPTG PTRERYKDGV
VTIGCVGFPN VGKSSLINGL VGRKVVSVSR TPGHTRYFQT YFLTPSVKLC DCPGLIFPSL
LPRQLQVLAG IYPIAQIQEP YTAVGYLASR IPVQALLHLR HPEAEDPSAE HPWCAWDICE
AWAEKRGYKT AKAARNDVYR AANSLLRLAV DGRLSLCFHP PGYSEQKGTW ESHPETTELV
VLQGRVGPAG DEEEEEEEEL SSSCEEEGEE DRDADEEGEG DEDTPTSAPG SSLAGRNPYA
LLGEDEC
