ID   A0A2K5KGW1_COLAP        Unreviewed;       534 AA.
AC   A0A2K5KGW1;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=PCI domain-containing protein {ECO:0000259|PROSITE:PS50250};
OS   Colobus angolensis palliatus (Peters' Angolan colobus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Colobinae; Colobus.
OX   NCBI_TaxID=336983 {ECO:0000313|Ensembl:ENSCANP00000040332.1, ECO:0000313|Proteomes:UP000233080};
RN   [1] {ECO:0000313|Ensembl:ENSCANP00000040332.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the proteasome subunit S3 family.
CC       {ECO:0000256|ARBA:ARBA00007912}.
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DR   RefSeq; XP_011785253.1; XM_011929863.1.
DR   AlphaFoldDB; A0A2K5KGW1; -.
DR   STRING; 336983.ENSCANP00000040332; -.
DR   Ensembl; ENSCANT00000063597.1; ENSCANP00000040332.1; ENSCANG00000043854.1.
DR   GeneID; 105503108; -.
DR   KEGG; cang:105503108; -.
DR   CTD; 5709; -.
DR   OMA; AKVYFYF; -.
DR   OrthoDB; 514836at2759; -.
DR   Proteomes; UP000233080; Unplaced.
DR   GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
DR   GO; GO:0030234; F:enzyme regulator activity; IEA:InterPro.
DR   GO; GO:0042176; P:regulation of protein catabolic process; IEA:InterPro.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR   InterPro; IPR013586; 26S_Psome_reg_C.
DR   InterPro; IPR000717; PCI_dom.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR10758:SF2; 26S PROTEASOME NON-ATPASE REGULATORY SUBUNIT 3; 1.
DR   PANTHER; PTHR10758; 26S PROTEASOME NON-ATPASE REGULATORY SUBUNIT 3/COP9 SIGNALOSOME COMPLEX SUBUNIT 3; 1.
DR   Pfam; PF01399; PCI; 1.
DR   Pfam; PF08375; Rpn3_C; 1.
DR   SMART; SM00753; PAM; 1.
DR   SMART; SM00088; PINT; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS50250; PCI; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000233080}.
FT   DOMAIN          286..465
FT                   /note="PCI"
FT                   /evidence="ECO:0000259|PROSITE:PS50250"
FT   REGION          1..70
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          500..534
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        502..521
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   534 AA;  60970 MW;  9B82906435FDACC5 CRC64;
     MKQEGSARRR GADKAKPPPG GGEQEPALPP APQDVEMKEE AATGGGSTGE ADGKTAAAAA
     EHSQRELDTV TLEDIKEHVK QLEKAVSGKE PRFVLRALRM LPSTSRRLNH YVLYKAVQGF
     FTSNNATRDF LLPFLEEPMD TEADLQFRPR TGKAASAPLL PEVEAYLQLL MVIFMMNSKR
     YKEAQKISDD LMQKISTQNR RALDLVAAKC YYYHARVYEF LDKLDVVRSF LHARLRTATL
     RHDADGQATL LNLLLRNYLH YSLYDQAEKL VSKSVFPEQA NNNEWARYLY YTGRIKAIQL
     EYSEARRTMT NALRKAPQHT AVGFKQTVHK LLIVVELLLG EIPDRLQFRQ PSLKRSLMPY
     FLLTQAVRTG NLAKFNQVLD QFGEKFQADG TYTLIIRLRH NVIKTGVRMI SLSYSRISLA
     DIAQKLQLDS PEDAEFIVAK AIRDGVIEAS INHEKGYVQS KEMIDIYSTR EPQLAFHQRI
     SFCLDIHNMS VKAMRFPPKS YNKDLESAEE RREREQQDLE FAKEMAEDDD DSFP
//