GNL1_MACMU
ID GNL1_MACMU Reviewed; 607 AA.
AC Q5TM59;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Guanine nucleotide-binding protein-like 1;
GN Name=GNL1;
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15269276; DOI=10.1093/molbev/msh216;
RA Kulski J.K., Anzai T., Shiina T., Inoko H.;
RT "Rhesus macaque class I duplicon structures, organization, and evolution
RT within the alpha block of the major histocompatibility complex.";
RL Mol. Biol. Evol. 21:2079-2091(2004).
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; AB128049; BAD69767.1; -; Genomic_DNA.
DR RefSeq; NP_001040604.1; NM_001047139.1.
DR AlphaFoldDB; Q5TM59; -.
DR STRING; 9544.ENSMMUP00000034184; -.
DR Ensembl; ENSMMUT00000032630; ENSMMUP00000030533; ENSMMUG00000020077.
DR GeneID; 713303; -.
DR KEGG; mcc:713303; -.
DR CTD; 2794; -.
DR VEuPathDB; HostDB:ENSMMUG00000020077; -.
DR VGNC; VGNC:104402; GNL1.
DR eggNOG; KOG1424; Eukaryota.
DR GeneTree; ENSGT00940000158047; -.
DR HOGENOM; CLU_013649_1_1_1; -.
DR InParanoid; Q5TM59; -.
DR OMA; CDFPVRP; -.
DR OrthoDB; 839833at2759; -.
DR TreeFam; TF324569; -.
DR Proteomes; UP000006718; Chromosome 4.
DR Bgee; ENSMMUG00000020077; Expressed in primary visual cortex and 21 other tissues.
DR ExpressionAtlas; Q5TM59; baseline.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
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 3: Inferred from homology;
KW GTP-binding; Nucleotide-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..607
FT /note="Guanine nucleotide-binding protein-like 1"
FT /id="PRO_0000295689"
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; 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
