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Database: UniProt
Entry: A0A3B4UY65_SERDU
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Original site: A0A3B4UY65_SERDU 
ID   A0A3B4UY65_SERDU        Unreviewed;       323 AA.
AC   A0A3B4UY65;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=GPN-loop GTPase 2 {ECO:0000256|ARBA:ARBA00014588, ECO:0000256|RuleBase:RU365059};
OS   Seriola dumerili (Greater amberjack) (Caranx dumerili).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Carangiformes; Carangidae; Seriola.
OX   NCBI_TaxID=41447 {ECO:0000313|Ensembl:ENSSDUP00000023483.1, ECO:0000313|Proteomes:UP000261420};
RN   [1] {ECO:0000313|Ensembl:ENSSDUP00000023483.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- FUNCTION: Small GTPase required for proper localization of RNA
CC       polymerase II and III (RNAPII and RNAPIII). May act at an RNAP assembly
CC       step prior to nuclear import. {ECO:0000256|ARBA:ARBA00003181,
CC       ECO:0000256|RuleBase:RU365059}.
CC   -!- SUBUNIT: Binds to RNA polymerase II (RNAPII).
CC       {ECO:0000256|RuleBase:RU365059}.
CC   -!- SIMILARITY: Belongs to the GPN-loop GTPase family.
CC       {ECO:0000256|ARBA:ARBA00005290, ECO:0000256|RuleBase:RU365059}.
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DR   AlphaFoldDB; A0A3B4UY65; -.
DR   STRING; 41447.ENSSDUP00000023483; -.
DR   Ensembl; ENSSDUT00000023918.1; ENSSDUP00000023483.1; ENSSDUG00000017084.1.
DR   GeneTree; ENSGT00950000183172; -.
DR   OMA; ATHNYFL; -.
DR   Proteomes; UP000261420; Unplaced.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   CDD; cd17871; GPN2; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR004130; Gpn.
DR   InterPro; IPR030231; Gpn2.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR21231:SF3; GPN-LOOP GTPASE 2; 1.
DR   PANTHER; PTHR21231; XPA-BINDING PROTEIN 1-RELATED; 1.
DR   Pfam; PF03029; ATP_bind_1; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   GTP-binding {ECO:0000256|RuleBase:RU365059};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU365059};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU365059}.
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..20
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   323 AA;  36252 MW;  305D672C6FEDCEF4 CRC64;
     MPPSLLGTET MSSQTGATPP LRFGQVVIGP PGSGKTTYCQ GMQEFLTHLG RKVVVVNMDP
     ANEGLPYSCD INISELVTLD DVMEGLKLGP NGGLLYCMEY VEANLDWLQN KLKQHSDCYF
     LFDCPGQVEL YTHQNSVKNI FSQLAKWNFR LTAVHLVDSH YCADPAKFIS VLCTSLSTML
     HVELPHVNIL SKMDLIEQYG KLAFNLDFYT EVMDLTYLLD HLAADPFFKK FHHLNEKLAE
     VIQDYGLVSF VPLNVQDKES MIQVLRAVDK ANGYCFGDLE ERNLQAMMSA AVGADFQFDS
     TLGVQERYVE TSGKTVEEEM MDL
//
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