ID A0A498MB07_LABRO Unreviewed; 1201 AA.
AC A0A498MB07;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE RecName: Full=peptidylprolyl isomerase {ECO:0000256|PROSITE-ProRule:PRU00277};
DE EC=5.2.1.8 {ECO:0000256|PROSITE-ProRule:PRU00277};
GN ORFNames=ROHU_027157 {ECO:0000313|EMBL:RXN17033.1};
OS Labeo rohita (Indian major carp) (Cyprinus rohita).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Labeoninae; Labeonini; Labeo.
OX NCBI_TaxID=84645 {ECO:0000313|EMBL:RXN17033.1, ECO:0000313|Proteomes:UP000290572};
RN [1] {ECO:0000313|EMBL:RXN17033.1, ECO:0000313|Proteomes:UP000290572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DASCIFA01 {ECO:0000313|EMBL:RXN17033.1};
RC TISSUE=Testis {ECO:0000313|EMBL:RXN17033.1};
RA Das P., Kushwaha B., Joshi C.G., Kumar D., Nagpure N.S., Sahoo L.,
RA Das S.P., Bit A., Patnaik S., Meher P.K., Jayasankar P., Koringa P.G.,
RA Patel N.V., Hinsu A.T., Kumar R., Pandey M., Agarwal S., Srivastava S.,
RA Singh M., Iquebal M.A., Jaiswal S., Angadi U.B., Kumar N., Raza M.,
RA Shah T.M., Rai A., Jena J.K.;
RT "Draft genome sequence of Rohu Carp (Labeo rohita).";
RL Submitted (MAR-2018) 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; Evidence={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:RXN17033.1}.
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DR EMBL; QBIY01012766; RXN17033.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A498MB07; -.
DR STRING; 84645.A0A498MB07; -.
DR Proteomes; UP000290572; Unassembled WGS sequence.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProt.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.10.50.40; -; 3.
DR Gene3D; 1.10.238.10; EF-hand; 1.
DR Gene3D; 3.30.70.1820; L1 transposable element, RRM domain; 1.
DR InterPro; IPR040676; DUF5641.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR001179; PPIase_FKBP_dom.
DR PANTHER; PTHR46046; -; 1.
DR PANTHER; PTHR46046:SF3; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE FKBP10; 1.
DR Pfam; PF18701; DUF5641; 1.
DR Pfam; PF00254; FKBP_C; 3.
DR SUPFAM; SSF47473; EF-hand; 1.
DR SUPFAM; SSF54534; FKBP-like; 3.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
DR PROSITE; PS50059; FKBP_PPIASE; 3.
PE 1: Evidence at protein level;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Isomerase {ECO:0000256|PROSITE-ProRule:PRU00277,
KW ECO:0000313|EMBL:RXN17033.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Proteomics identification {ECO:0007829|PeptideAtlas:A0A498MB07};
KW Reference proteome {ECO:0000313|Proteomes:UP000290572};
KW Rotamase {ECO:0000256|PROSITE-ProRule:PRU00277}.
FT DOMAIN 539..627
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
FT DOMAIN 651..739
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
FT DOMAIN 763..833
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
FT DOMAIN 1160..1195
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 140..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 197..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 821..891
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 54..81
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 929..984
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..27
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 840..884
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1201 AA; 135630 MW; 5E37015F5D5CA87D CRC64;
MDKSQPSKNV EEADQALEIE SRSGRSHRST RSSASAAATT ARAKAAACKV KASYAEKEAI
MMRERAQLEE HQQKILAETA RRKAEVEAEL YVLKLQKEAV AASKEADVYD AAVLREDELG
EDLEKLSCIS NKTERTREYV QTHSQLPNVP NLTSNSQHES ENSQYVTRSY VEGSLSSHSP
TKKEESKAEI VPMEQEHTVQ HSFQCSPSKV KSDPFEGDDE VRHQSYPVRI QCESDPLSRE
PAGCSTPAPH VNDFTTYLLR KEMVSSGLFQ FDDCPENYWA WKTSFQAVTS ELNLTSREEI
DLLIRWLGPD SSNHAKRIKS VYVSNPTSGV GVIWRRLEDC YGCPEVIEQA MLKRLDAFPR
ITNKDIHRLR DLGDLLLELQ SAKESGRLPG LAYLDTARGV NPIVEKLPFG LQDKWITQGS
RCKYASSAPT PPGNFELGHL HKSQWRQVQM LADSFWKRWK QEYLSTLQSR RKWTEERDNI
QEGDVVLLKD GEAKRSSVIP PDTTLVFDVL LLDLWNKEDK VQIRTLHKRR NCKRTVMPSD
YVRYHYNGSL LVGSLFDSSH LRNSTYNTYV GQGSLIKGME EGLLGMCVGE RRSIIIPPFL
AYDDKGYGTK VPPYATLIFD VLLVDVFNVK DDVRVEVQKI PQPCRRRAVA GDFIRYHYNG
TFQDGTVFDS SYSRNSTYNT FIGMGYVIAG IDKALQGVCV GEWRRVTVPP HLAYGETGSG
ELIPGSAVLI FDLHIIDFHN PKDQVDIKLI YKPADCNLTS AANDLIMYRY NCSLLDGTRL
YSSDDYPEPP RVTLGQGKLI TGLDEGLQGM CVLERREITV PPHLAHGTNG EMPGTGRGSR
DKPKSTTQSK LTSFGAHGAE QPTSREANTT KDANAASTEA NGGDVNNEAL IPPSKDQQLL
NMAKDEILGE IRNLKSEFTG RFVRVLKAIE ETRKEVTECT ERMAGAEVRL SNVVDEQVDL
KAVVESSQTR NKHLEDKVVD METRSRLNNL RLVGLPENSE GFDMCGFLES WLPDALELNP
MRHPLVLERA HRIGPKRDTN TSPRTVIMRF LNYKQKEIVL RTAKTKKDIF YKNQRVKLFA
DVATEVHRQP LGVPSSAVLL FELELLQLQK GVPEGFLFIW LQDSPEQLFP AMDMNQDQEF
SAFIKLQVAE GRGRLHPGID RDIVLRDMFK KQDRNADGKI TEDELNVIVN EEEEVPKHEE
L
//