ID A0A2K6FT77_PROCO Unreviewed; 611 AA.
AC A0A2K6FT77;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=HBS1-like protein {ECO:0000256|ARBA:ARBA00015186};
OS Propithecus coquereli (Coquerel's sifaka) (Propithecus verreauxi
OS coquereli).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lemuriformes;
OC Indriidae; Propithecus.
OX NCBI_TaxID=379532 {ECO:0000313|Ensembl:ENSPCOP00000017189.1, ECO:0000313|Proteomes:UP000233160};
RN [1] {ECO:0000313|Ensembl:ENSPCOP00000017189.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
CC Evidence={ECO:0000256|ARBA:ARBA00001702};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000256|ARBA:ARBA00001702};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A
CC subfamily. {ECO:0000256|ARBA:ARBA00007249}.
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DR AlphaFoldDB; A0A2K6FT77; -.
DR Ensembl; ENSPCOT00000027824.1; ENSPCOP00000017189.1; ENSPCOG00000020390.1.
DR GeneTree; ENSGT00650000094590; -.
DR Proteomes; UP000233160; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-KW.
DR CDD; cd16267; HBS1-like_II; 1.
DR CDD; cd04093; HBS1_C_III; 1.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 2.40.30.10; Translation factors; 2.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR015033; HBS1-like_N.
DR InterPro; IPR037189; HBS1-like_N_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR InterPro; IPR004160; Transl_elong_EFTu/EF1A_C.
DR PANTHER; PTHR23115:SF188; HBS1-LIKE PROTEIN; 1.
DR PANTHER; PTHR23115; TRANSLATION FACTOR; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF03143; GTP_EFTU_D3; 1.
DR Pfam; PF08938; HBS1_N; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF50465; EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain; 1.
DR SUPFAM; SSF109732; HBS1-like domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50447; Translation proteins; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000233160};
KW Translation regulation {ECO:0000256|ARBA:ARBA00022845}.
FT DOMAIN 259..367
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 139..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 181..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 220..242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..239
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 611 AA; 67625 MW; C93784E064B4A8CD CRC64;
MARHRNVRGY NYDEDFEDDD LYGQSVEDDY CISPSTAAQF IYSRRDKPSV EPVEEYDYED
LKESSNSLSN HQLSGIDQAR LYSCLDHMRE VLGDAVPDEI LVEAVLKNKF DVQKALSVVL
EQDNMQNFKD KSEGTIFTGR TEKGKSVGSQ SSRNESEMVP KVAKMTVSGK KQTMGFEVPG
VTSEENDHSF HTPQKGLPSE DASIATSDVL EMMSKSAIPP HTIQASEEQG STPTPVKKSG
KLRQQIDVKA ELEKRQGGKQ LLNLVVIGHV DAGKSTLMGH MLYLLGNVNK RTMHKYEQES
KKAGKASFAY AWVLDETGEE RERGVTMDVG MTKFETTTKV ITLMDAPGHK DFIPNMITGA
AQESDVAFIP TSGLSGDNLI TRSQSSELTK WYKGVCLLEQ IDSFKPPQRS IDKPFRLCVS
DVFKDQGSGF CVTGKIEAGY IQTGDRLLAM PPNETCTAKG ITLHDEPVDW AAAGDHVSLT
LVGMDIIKIN VGCVFCGPKE PIKACTRFRA RILIFNIEIP VTKGFPVLLH FQTVSEPAVI
KRLISVLNKS TGEVTKKKPK LLTKGQNALV ELQTQRPVAL ELYKDFKELG RFMLRYGGST
IAAGVVTEIK E
//