ID A0A3N0XJW0_ANAGA Unreviewed; 503 AA.
AC A0A3N0XJW0;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 08-NOV-2023, entry version 15.
DE SubName: Full=Peptidyl-prolyl cis-trans isomerase-like 2 {ECO:0000313|EMBL:ROI26639.1};
GN ORFNames=DPX16_21582 {ECO:0000313|EMBL:ROI26639.1};
OS Anabarilius grahami (Kanglang fish) (Barilius grahami).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Xenocyprididae; Xenocypridinae; Xenocypridinae incertae sedis; Anabarilius.
OX NCBI_TaxID=495550 {ECO:0000313|EMBL:ROI26639.1, ECO:0000313|Proteomes:UP000281406};
RN [1] {ECO:0000313|EMBL:ROI26639.1, ECO:0000313|Proteomes:UP000281406}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AG-KIZ {ECO:0000313|EMBL:ROI26639.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:ROI26639.1};
RA Jiang W.;
RT "Genome assembly for a Yunnan-Guizhou Plateau 3E fish, Anabarilius grahami
RT (Regan), and its evolutionary and genetic applications.";
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
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:ROI26639.1}.
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DR EMBL; RJVU01073134; ROI26639.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N0XJW0; -.
DR Proteomes; UP000281406; Unassembled WGS sequence.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:InterPro.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR CDD; cd01923; cyclophilin_RING; 1.
DR Gene3D; 2.40.100.10; Cyclophilin-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR InterPro; IPR044666; Cyclophilin_A-like.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45625; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE-RELATED; 1.
DR PANTHER; PTHR45625:SF1; RING-TYPE E3 UBIQUITIN-PROTEIN LIGASE PPIL2; 1.
DR Pfam; PF00160; Pro_isomerase; 1.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SUPFAM; SSF50891; Cyclophilin-like; 1.
DR PROSITE; PS00170; CSA_PPIASE_1; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
PE 4: Predicted;
KW Isomerase {ECO:0000313|EMBL:ROI26639.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000281406}.
FT DOMAIN 264..412
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
FT REGION 427..503
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..459
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..487
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 503 AA; 56809 MW; 5120596F0BAE97BD CRC64;
MGKRQHQKDK MYITCAEYTQ FYGGKKSEIP RDNFRRLPFD HCRSIVPWIK KFGTNPITGE
KLEAKSLIKL NFCKNNEGKY HCPVLYTVFT NNSHIVANKV TGNVFSHEAV DQLNIKTKSY
KDLLTDEPFT RQDLITLQDP TNLDKFNVSN FFHVKNNMKV LDPDEEKAKQ DPAYHLKSTN
LETRETLAEL YRDYKGDELL ASTMKEPETK KTDKFNAAHY STGRVSASFT STAMAPATTH
EADAIADDAV RYQYVKKKGY VRLHTNKGDL NVELHCDKVP KAGENFIKLC KKGYYDGTIF
HRSIRNFMIQ GGDPTGTGTG GESFWRKPFK DEFRPNLSHT GRGILSMANS GPNTNKSQFF
ITFRSCAYLD RKHTVFGRVV GGLEALTAME NVESDPKTDK PKSEIKLLSA TVFVDPYEEA
DAQIAAEREK EAQKQEEERA QTSASVNKAK TEDKPKIFKP GVGKYINMVA AKHSHPDSDK
PSTSEAPAKK PKGRTGFGDF SSW
//
