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Database: UniProt
Entry: C5LAN4_PERM5
LinkDB: C5LAN4_PERM5
Original site: C5LAN4_PERM5 
ID   C5LAN4_PERM5            Unreviewed;       945 AA.
AC   C5LAN4;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 86.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EER06490.1};
GN   ORFNames=Pmar_PMAR006302 {ECO:0000313|EMBL:EER06490.1};
OS   Perkinsus marinus (strain ATCC 50983 / TXsc).
OC   Eukaryota; Sar; Alveolata; Perkinsozoa; Perkinsea; Perkinsida; Perkinsidae;
OC   Perkinsus.
OX   NCBI_TaxID=423536 {ECO:0000313|Proteomes:UP000007800};
RN   [1] {ECO:0000313|EMBL:EER06490.1, ECO:0000313|Proteomes:UP000007800}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 50983 / TXsc {ECO:0000313|Proteomes:UP000007800};
RA   El-Sayed N., Caler E., Inman J., Amedeo P., Hass B., Wortman J.;
RL   Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; GG680729; EER06490.1; -; Genomic_DNA.
DR   RefSeq; XP_002774674.1; XM_002774628.1.
DR   AlphaFoldDB; C5LAN4; -.
DR   EnsemblProtists; EER06490; EER06490; Pmar_PMAR006302.
DR   GeneID; 9065678; -.
DR   InParanoid; C5LAN4; -.
DR   OrthoDB; 5474929at2759; -.
DR   Proteomes; UP000007800; Unassembled WGS sequence.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:InterPro.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   CDD; cd16669; RING-H2_RNF181; 1.
DR   CDD; cd02249; ZZ; 1.
DR   Gene3D; 3.30.60.90; -; 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; IPR039525; RNF126-like_zinc-ribbon.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR000433; Znf_ZZ.
DR   InterPro; IPR043145; Znf_ZZ_sf.
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   Pfam; PF13639; zf-RING_2; 1.
DR   Pfam; PF14369; zinc_ribbon_9; 1.
DR   Pfam; PF00569; ZZ; 1.
DR   PRINTS; PR00153; CSAPPISMRASE.
DR   SMART; SM00184; RING; 1.
DR   SMART; SM00291; ZnF_ZZ; 1.
DR   SUPFAM; SSF50891; Cyclophilin-like; 1.
DR   SUPFAM; SSF57850; RING/U-box; 2.
DR   PROSITE; PS00170; CSA_PPIASE_1; 1.
DR   PROSITE; PS50072; CSA_PPIASE_2; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
DR   PROSITE; PS50135; ZF_ZZ_2; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007800};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00228}.
FT   DOMAIN          139..284
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50072"
FT   DOMAIN          753..798
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          846..917
FT                   /note="ZZ-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50135"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          337..356
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          815..845
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          914..937
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   945 AA;  106763 MW;  B56E5516263CAED6 CRC64;
     MSQNAESKEI AETGGNEGIR SSDALRRIFS ERDQRKKLRE QGVKVMGDFP VSEDQRKSIY
     SEAREAAIKA ARPDPSASIK HDLYTTGAAA SSFTSTRMNL AYDNEYREMT DLEKRTILYD
     KVRKAHKKGY VAITLDHGGT LNLELHCDIA PQTCDNFIRL CKSGYYNGVK FHRVIRNFMM
     QGGDPEGTGR AGKSAFEGGA PFRDEFDSRL THSGAGVVSM ANSGRDTNRS QFFITFKSCE
     HLNNKHTIFG RVVGGGAALD VLNETETDRK ERPIDPIKIV KTQVFVNPFE TILDDEAAQK
     KEEEDKLKEA QLLRDRMDVM KDHPKRESTG IGKYLSATHK RKSHSGTSIE ESSGPVLGQM
     GKSKRHKAFG FQDCFFSFRS SPLTIPESAE PGFAESYPNN ENFYMDRSRA RTEERAAYDN
     MSNSDKVKAY LCSVWKKTKL EWEVLKVAWP WIILGIIFQI LHDWAHNWVY YLSGKYDVYG
     GPENALVDFG HMAFPDIDTL TVSPEPENPV LYTCMILAVA FAVIGPIFGG RDDFTLIGVF
     SGFDVQNGCG DLVFSSHMMY CLLATLVVTH YSRSLIFMTN SGSKGRASEN EFRIAHGNYL
     ARNRPEYDQR MKIIMHLDTR VDRNMDKSCF SSVYGGHTPT CCVRATTMEW YYCHECRKSI
     PRLTDENRCP ECNGGFVEAA RVPADDMMQA LMMLAGAERS QTEESSNVLN RRQQDEANPC
     TCKAFIERLP VAPRRVKTEM KADDLIESSV AECSICTMEF EKEDSEDAHC TSLPCEHFFH
     RDCLVPWLKR SDSCPVCRLS EVLREIGENV EADKLESERR RRNPLHEFMS RRSMMGRGPE
     SGGPRHPNVR CDCCEMFPIV GRNRWKCVQC QDYDLCDGCY HAFMDGQRDI PEHASRRTQL
     PGGQEHHTFR LMRSPVPRTT GSRGEQVGGG EGGSAWVGMA KHDLG
//
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