ID A0A251UV43_HELAN Unreviewed; 552 AA.
AC A0A251UV43;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase {ECO:0000256|RuleBase:RU365081};
DE Short=PPIase {ECO:0000256|RuleBase:RU365081};
DE EC=5.2.1.8 {ECO:0000256|RuleBase:RU365081};
GN Name=ATCYP59 {ECO:0000313|EMBL:OTG26642.1};
GN ORFNames=HannXRQ_Chr05g0160881 {ECO:0000313|EMBL:OTG26642.1},
GN HanXRQr2_Chr13g0595381 {ECO:0000313|EMBL:KAF5774016.1};
OS Helianthus annuus (Common sunflower).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Asteroideae;
OC Heliantheae alliance; Heliantheae; Helianthus.
OX NCBI_TaxID=4232 {ECO:0000313|EMBL:OTG26642.1, ECO:0000313|Proteomes:UP000215914};
RN [1] {ECO:0000313|EMBL:KAF5774016.1, ECO:0000313|Proteomes:UP000215914}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. SF193 {ECO:0000313|Proteomes:UP000215914};
RC TISSUE=Leaves {ECO:0000313|EMBL:KAF5774016.1};
RX PubMed=28538728; DOI=10.1038/nature22380;
RA Badouin H., Gouzy J., Grassa C.J., Murat F., Staton S.E., Cottret L.,
RA Lelandais-Briere C., Owens G.L., Carrere S., Mayjonade B., Legrand L.,
RA Gill N., Kane N.C., Bowers J.E., Hubner S., Bellec A., Berard A.,
RA Berges H., Blanchet N., Boniface M.C., Brunel D., Catrice O., Chaidir N.,
RA Claudel C., Donnadieu C., Faraut T., Fievet G., Helmstetter N., King M.,
RA Knapp S.J., Lai Z., Le Paslier M.C., Lippi Y., Lorenzon L., Mandel J.R.,
RA Marage G., Marchand G., Marquand E., Bret-Mestries E., Morien E.,
RA Nambeesan S., Nguyen T., Pegot-Espagnet P., Pouilly N., Raftis F.,
RA Sallet E., Schiex T., Thomas J., Vandecasteele C., Vares D., Vear F.,
RA Vautrin S., Crespi M., Mangin B., Burke J.M., Salse J., Munos S.,
RA Vincourt P., Rieseberg L.H., Langlade N.B.;
RT "The sunflower genome provides insights into oil metabolism, flowering and
RT Asterid evolution.";
RL Nature 546:148-152(2017).
RN [2] {ECO:0000313|EMBL:OTG26642.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Leaves {ECO:0000313|EMBL:OTG26642.1};
RA Langlade N., Munos S.;
RT "Sunflower complete genome.";
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KAF5774016.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaves {ECO:0000313|EMBL:KAF5774016.1};
RA Gouzy J., Langlade N., Munos S.;
RT "Helianthus annuus Genome sequencing and assembly Release 2.";
RL Submitted (JUN-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC cis-trans isomerization of proline imidic peptide bonds in
CC oligopeptides. {ECO:0000256|RuleBase:RU365081}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-peptidylproline (omega=180) = [protein]-
CC peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-
CC COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833,
CC ChEBI:CHEBI:83834; EC=5.2.1.8;
CC Evidence={ECO:0000256|ARBA:ARBA00000971,
CC ECO:0000256|RuleBase:RU365081};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU365081}.
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIL4
CC subfamily. {ECO:0000256|RuleBase:RU365081}.
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DR EMBL; MNCJ02000328; KAF5774016.1; -; Genomic_DNA.
DR EMBL; CM007894; OTG26642.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A251UV43; -.
DR STRING; 4232.A0A251UV43; -.
DR EnsemblPlants; mRNA:HanXRQr2_Chr13g0595381; mRNA:HanXRQr2_Chr13g0595381; HanXRQr2_Chr13g0595381.
DR Gramene; mRNA:HanXRQr2_Chr13g0595381; mRNA:HanXRQr2_Chr13g0595381; HanXRQr2_Chr13g0595381.
DR InParanoid; A0A251UV43; -.
DR OMA; KMRHTRM; -.
DR OrthoDB; 169228at2759; -.
DR Proteomes; UP000215914; Chromosome 5.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd01921; cyclophilin_RRM; 1.
DR CDD; cd12235; RRM_PPIL4; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR Gene3D; 2.40.100.10; Cyclophilin-like; 1.
DR InterPro; IPR035542; CRIP.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR InterPro; IPR035538; Cyclophilin_PPIL4.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR PANTHER; PTHR45843; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE-LIKE 4; 1.
DR PANTHER; PTHR45843:SF1; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE-LIKE 4; 1.
DR Pfam; PF00160; Pro_isomerase; 1.
DR Pfam; PF00076; RRM_1; 1.
DR Pfam; PF00098; zf-CCHC; 1.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SMART; SM00360; RRM; 1.
DR SMART; SM00343; ZnF_C2HC; 1.
DR SUPFAM; SSF50891; Cyclophilin-like; 1.
DR SUPFAM; SSF57756; Retrovirus zinc finger-like domains; 1.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
DR PROSITE; PS50102; RRM; 1.
DR PROSITE; PS50158; ZF_CCHC; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU365081};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Nucleus {ECO:0000256|RuleBase:RU365081};
KW Reference proteome {ECO:0000313|Proteomes:UP000215914};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00176,
KW ECO:0000256|RuleBase:RU365081};
KW Rotamase {ECO:0000256|ARBA:ARBA00023110, ECO:0000256|RuleBase:RU365081};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00047}.
FT DOMAIN 7..161
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
FT DOMAIN 243..321
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 343..356
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT REGION 355..552
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..552
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 552 AA; 64230 MW; 00A8FB5EFE7341D5 CRC64;
MSVLIVTSLG DIVVDLHSDR CPLTCKNFLK LCKIKYYNGC LFHTVQKDFT AQTGDPTGTG
SGGDSIYKFM YGDQARFFQD EIHLDLKHAK KGTIAMASAG ENLNASQFYI TLRDDLDYLD
GKKTVFGEVA EGFETLDRIN EAYVDDKNRP YKNIRIKHTY VLDDPFEDPE QLTELVPDAS
PEGKPKDEVD DEVRLEDDWV PMDEKLGTAE LEEVIRAKEA HSRAVVLESI GDIPDAEVKP
PDNVLFVCKL NPVTEDEDLN TIFSRFGTVT SADIIRDYKT GDSLCYAFVE FEDREACEQA
YFKMDNVLID DRRIHVDFSQ SVSRMWNQYR RKGNRSGIAG KGCFKCGSLD HIAKDCTGGP
DTKEPPKYVL KDDDIARKGG NDSSRYDMVF DDDTHGSPQR KKPPRHNEGG TRHEHRKPSH
RDMEDTKKND YKHKDEVDER RKEYMRDDRH HTSGGRRDYK RDELDHRTPR NYDDRDRSRS
DDRRRDSRDD RKRYSEDEYD RKKDSRRDES YSRRSTHEDD AGHKRSKGED RNRDRDRVKT
STRYDDRDRR RD
//
