ID A0A812JM93_9DINO Unreviewed; 1712 AA.
AC A0A812JM93;
DT 29-SEP-2021, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 1.
DT 08-OCT-2025, entry version 15.
DE RecName: Full=peptidylprolyl isomerase {ECO:0000256|ARBA:ARBA00013194, ECO:0000256|PROSITE-ProRule:PRU00277};
DE EC=5.2.1.8 {ECO:0000256|ARBA:ARBA00013194, ECO:0000256|PROSITE-ProRule:PRU00277};
GN Name=PRPF4B {ECO:0000313|EMBL:CAE7211558.1};
GN ORFNames=SNAT2548_LOCUS7117 {ECO:0000313|EMBL:CAE7211558.1};
OS Symbiodinium natans.
OC Eukaryota; Sar; Alveolata; Dinophyceae; Suessiales; Symbiodiniaceae;
OC Symbiodinium.
OX NCBI_TaxID=878477 {ECO:0000313|EMBL:CAE7211558.1, ECO:0000313|Proteomes:UP000604046};
RN [1] {ECO:0000313|EMBL:CAE7211558.1}
RP NUCLEOTIDE SEQUENCE.
RA Dougan E. K., Rhodes N., Thang M., Chan C.;
RL Submitted (FEB-2021) to the EMBL/GenBank/DDBJ databases.
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, ECO:0000256|PROSITE-
CC ProRule:PRU00277};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CAE7211558.1}.
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DR EMBL; CAJNDS010000491; CAE7211558.1; -; Genomic_DNA.
DR OrthoDB; 9332038at2759; -.
DR Proteomes; UP000604046; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR FunFam; 3.10.50.40:FF:000006; Peptidyl-prolyl cis-trans isomerase; 1.
DR Gene3D; 3.10.50.40; -; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 3.30.200.20; Phosphorylase Kinase, domain 1; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR029058; AB_hydrolase_fold.
DR InterPro; IPR049492; BD-FAE-like_dom.
DR InterPro; IPR014955; DUF1826.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR001179; PPIase_FKBP_dom.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR050494; Ser_Thr_dual-spec_kinase.
DR PANTHER; PTHR24058; DUAL SPECIFICITY PROTEIN KINASE; 1.
DR PANTHER; PTHR24058:SF103; SERINE_THREONINE-PROTEIN KINASE PRP4 HOMOLOG; 1.
DR Pfam; PF20434; BD-FAE; 1.
DR Pfam; PF08856; DUF1826; 1.
DR Pfam; PF00254; FKBP_C; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF54534; FKBP-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50059; FKBP_PPIASE; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|PROSITE-
KW ProRule:PRU00277}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000604046};
KW Rotamase {ECO:0000256|ARBA:ARBA00023110, ECO:0000256|PROSITE-
KW ProRule:PRU00277};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..1712
FT /note="peptidylprolyl isomerase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5032984657"
FT DOMAIN 743..830
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
FT DOMAIN 1010..1341
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 872..891
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1040
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1712 AA; 186674 MW; EC955A4F2D8E0F74 CRC64;
MARHVESRLA RLLCICASLL FASWSQDFTV HTAQYGKGRQ QVGDFVKPDK DKCKGIVMLV
HGGFWRAGFD RSLMIDISDD LLASGLCVWN VDYRSVGSGG GYPETLEDMA SAWNWLTTDD
AASLGVRPDL PLGIVGHSAG GHLATWLAIQ GLLDHSDFGV SGKIRPRIAV SQAGVLDLKG
AYEANLGRSA VRDFIGSPPE STTSRMLAAS NGAVLDVVAG PAADADTRYL GADPTALLSR
VPAARLSGSD APVFALVHGQ NDDIVPPAQS TAFQSVFSRR GASDKCIYKL IPGEGHFEHL
RRDSAAWAST ADLLNVGKPL ANVVLKALAP EVQDLLSKWS AWWRLRMLAW IRSRGDSPLS
DIMPDILRSI SSEAGSAWHR HEGGCGSVVS WAVPRLARLR GIEPSASRQA FPFNRGGTLD
YNCFRPPISL GIQLTKKKNV RPNTPSYVFE QIDEMLCQEK VSWSCKERQI MLADYMASTL
DVASRGSHSA AKLNQPAPEV EIVVPTAASE VFESLDSFAP DSVPRKLAEQ LNDCSLEMAN
LLDEVAKTDT GLQRDLESES WRQVDEKVVE ETPAEAVARD PGPALLAARE VPTLFRDIDA
HLPRSKRKAY ETLRSAGAVD IHRFVEENFE GAFGRRDDGV QWVHKVMHRK DRHPGQSAWT
RKALQLLDAE RLDRRLDLGL GDLRQEKREV TRQGQAPRLS PEALSAGQGV QTCVDTGLFT
AGLAKQPPQL FKVIGEGEAP VKGQTVKVHY TGKLENGQVF DSSIPRGESL DFSVGTGQVI
AGWDEGILTM RVGGKRELKI PPKLGYGSRG IGPIPGNATL FFECELVRLK ALHVQRNGQA
GVVEDYVRTK QRWRVRLLVS GKSHDFKAEN LEIEEPADRP PPADWVGPES DRDEAYAQPK
VAYKEVAEEP LKLTALAAGC QVILHSLKGA AELNGQRGEV ESFVSESSRW RVKLLSGSMK
DLKPENLRPL SASEMDASTT ALSELDALEA DLGIDFAAAP GDTCGPENRF VIEEKLGEGT
FSTVFRCHDT CAENAKYAVK FTRSNAQTRR ALEREIKIMG QLIAKVGERD AEGMGAILTL
AFFEGFQHKG RLAAVFELMK CNLRTALTKY GAGKGLPLLP TVRDFGRQLF LALRVLRRAG
LIHCDVKPEN LLLGGDNATI KLSDFGSCQG LPERLKSDQL MPRNYRAPEI IVGLDYDYSV
DVWSAAATLF ELATDSVLFQ GDTNNDMLHA MFKVCGSCTK SFVLSGTFTQ NHFSASGEFL
NAKGDLAINS ANPRVIPLEA FDPPSRPLQF LLENVRKRPP KGVAASRHEG LVSHFSDLLG
QCLRLALERP TPETALGHKF FQKGASLSAY DHSSQAPQAY PCTCGMRSPP CRGGAYVQVG
SALTTWYAST GLFAWAWPSW ELGAGNDAPG RLREVTATTG GCGIAGDVDE AAGLLQDPEV
LACFLDLRSG ELLREWEAAL PQLSAFDGKA IVMPDEKSLD ATISRTWPLE LQAGGRLEHL
GAETLAQAKR LVKLFWRAGS VSCPRQHLAL QVRLASFDYV QCSRLHWDDV PLRLVCTLAG
AGTQVLPESS ADRTAFRALE SMPIERQGSM STEDWNNRIV SSSARSWLSG GWKRALVQVP
TGWAVLLKGS TWGTDAKEGY KPTSPGALHR SPEEASQRVC CLRKTHPPRL NSCTAKKRAH
LGVFLSCWSF KIGPVQVLLQ VDFADSVAGS GQ
//
