ID A0A1I7VC64_LOALO Unreviewed; 489 AA.
AC A0A1I7VC64;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Spliceosome-associated protein CWC27 homolog {ECO:0000256|ARBA:ARBA00040027};
DE AltName: Full=Probable inactive peptidyl-prolyl cis-trans isomerase CWC27 homolog {ECO:0000256|ARBA:ARBA00042090};
GN Name=LOAG_11869 {ECO:0000313|WBParaSite:EN70_12144};
OS Loa loa (Eye worm) (Filaria loa).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Loa.
OX NCBI_TaxID=7209 {ECO:0000313|Proteomes:UP000095285, ECO:0000313|WBParaSite:EN70_12144};
RN [1] {ECO:0000313|Proteomes:UP000095285}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Genome Sequencing Center for Infectious Disease;
RA Nutman T.B., Fink D.L., Russ C., Young S., Zeng Q., Gargeya S.,
RA Alvarado L., Berlin A., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heilman E.R., Heiman D., Howarth C.,
RA Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., White J., Yandava C., Haas B., Henn M.R.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Loa loa.";
RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|WBParaSite:EN70_12144}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2016) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR AlphaFoldDB; A0A1I7VC64; -.
DR STRING; 7209.A0A1I7VC64; -.
DR WBParaSite; EN70_12144; EN70_12144; EN70_12144.
DR eggNOG; KOG0885; Eukaryota.
DR InParanoid; A0A1I7VC64; -.
DR Proteomes; UP000095285; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:InterPro.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR CDD; cd01925; cyclophilin_CeCYP16-like; 1.
DR Gene3D; 2.40.100.10; Cyclophilin-like; 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 PANTHER; PTHR45625; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE-RELATED; 1.
DR PANTHER; PTHR45625:SF6; SPLICEOSOME-ASSOCIATED PROTEIN CWC27 HOMOLOG; 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 Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000095285}.
FT DOMAIN 26..173
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
FT REGION 256..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 396..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 450..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..282
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..483
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 489 AA; 56471 MW; 212147FF053596F1 CRC64;
MDFQAISMSN IYVNEPATNG KVCMKTTVGD IDIELWSKEC PLACRNFIQL CMEGYYNGTI
FHRVIRDFIV QGGDPTGTGE GGESIYTASF KNEFHQRLKF NRRGLVGMAS GNDGMNGSQF
FFTLNATPDL DKKHTLFGKV VGNTLFNMLR LGECEIGDDD KPLTKQKILQ VKILSNPFND
IIPREKKKDK KKKEKIRDKK DAKKNLTLLS FGDEAEEDEI ELQEANEKFK CKSKSAHDIL
TDETLSKELA VPMEELIEPI EPSSSSNIED TGEREARMER IKEKLRKRKR KASDSDRNDE
EDEDFEAMIK QEMSDRQKQE LEKITAEVKL VQKDLKAMLK PKKEEEEIEE EKLLTEATKR
HLEMKQMFRE SAKVKLKSKD PRRQDETMSM LEKILAEHEG MKSFNPVRER NPEKEKKKEE
EHEVSAGKLN YDNEEDLDTA EILAHKFVAP EEDGKVSKAK DANLREESED WYDITDPRNK
INQRRRGVV
//