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GNL1_PONAB
ID   GNL1_PONAB              Reviewed;         607 AA.
AC   Q5RA07;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Guanine nucleotide-binding protein-like 1;
GN   Name=GNL1;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) 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}.
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DR   EMBL; CR859219; CAH91403.1; -; mRNA.
DR   RefSeq; NP_001125827.1; NM_001132355.1.
DR   AlphaFoldDB; Q5RA07; -.
DR   STRING; 9601.ENSPPYP00000018342; -.
DR   Ensembl; ENSPPYT00000019076; ENSPPYP00000018342; ENSPPYG00000016408.
DR   GeneID; 100172755; -.
DR   KEGG; pon:100172755; -.
DR   CTD; 2794; -.
DR   eggNOG; KOG1424; Eukaryota.
DR   GeneTree; ENSGT00940000158047; -.
DR   HOGENOM; CLU_013649_1_1_1; -.
DR   InParanoid; Q5RA07; -.
DR   OMA; CDFPVRP; -.
DR   OrthoDB; 839833at2759; -.
DR   TreeFam; TF324569; -.
DR   Proteomes; UP000001595; Chromosome 6.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0006974; P:cellular response to DNA damage stimulus; IEA:Ensembl.
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_0000295690"
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"
SQ   SEQUENCE   607 AA;  68675 MW;  03471E24238D057A 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 EDGPAVLVEQ 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
 
 
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