ID A0A166FIN6_9AGAM Unreviewed; 1309 AA.
AC A0A166FIN6;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KZP16841.1};
GN ORFNames=FIBSPDRAFT_912172 {ECO:0000313|EMBL:KZP16841.1};
OS Fibularhizoctonia sp. CBS 109695.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Atheliales; Atheliaceae; Fibularhizoctonia.
OX NCBI_TaxID=436010 {ECO:0000313|EMBL:KZP16841.1, ECO:0000313|Proteomes:UP000076532};
RN [1] {ECO:0000313|EMBL:KZP16841.1, ECO:0000313|Proteomes:UP000076532}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 109695 {ECO:0000313|EMBL:KZP16841.1,
RC ECO:0000313|Proteomes:UP000076532};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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DR EMBL; KV417589; KZP16841.1; -; Genomic_DNA.
DR STRING; 436010.A0A166FIN6; -.
DR OrthoDB; 151732at2759; -.
DR Proteomes; UP000076532; Unassembled WGS sequence.
DR GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR CDD; cd12169; PGDH_like_1; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR InterPro; IPR029753; D-isomer_DH_CS.
DR InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002015; Proteasome/cyclosome_rpt.
DR InterPro; IPR048570; PSMD1_RPN2_N.
DR InterPro; IPR040623; RPN2_C.
DR PANTHER; PTHR10943; 26S PROTEASOME NON-ATPASE REGULATORY SUBUNIT; 1.
DR PANTHER; PTHR10943:SF2; 26S PROTEASOME NON-ATPASE REGULATORY SUBUNIT 1; 1.
DR Pfam; PF00389; 2-Hacid_dh; 1.
DR Pfam; PF02826; 2-Hacid_dh_C; 1.
DR Pfam; PF13646; HEAT_2; 1.
DR Pfam; PF01851; PC_rep; 2.
DR Pfam; PF18004; RPN2_C; 1.
DR Pfam; PF21505; RPN2_N; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Proteasome {ECO:0000256|ARBA:ARBA00022942};
KW Reference proteome {ECO:0000313|Proteomes:UP000076532};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 7..311
FT /note="26S proteasome non-ATPase regulatory subunit 1/RPN2
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF21505"
FT DOMAIN 757..912
FT /note="26S proteasome regulatory subunit RPN2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF18004"
FT DOMAIN 1007..1291
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 1089..1264
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
FT REGION 814..886
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 814..848
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 854..885
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1309 AA; 141474 MW; 3C0C821D125794FF CRC64;
MVARYQTSAV GVLALLSEPE PEFKEHALKA LIPLVPQFWA EISEHIALIE ALYESNEIKK
DARASAALLA SKVYYFLGEY DEALSFALGA GHAFEAESRA PGSEEYVETV VSKAIDRYIE
FETEEAVGKG KIDPRLQSII EGIFRRCIAD GEYKQAIGIA LESRRFDIIE QIYNHTKDTA
LLSYAMEAVL DTGFSLQYRD DVLHKLLPLF PPPTIESQSP HIHALTRLLV TLSDASLTVP
LFTSLVPNEK LLAYQFAFDL VEGGAQDFLE SVRSGLPEGD EKTKDIFENL RNILGGQESV
KLYLEFLRRN NKVDLLILKN TKEALEPRNS IYHTALTLQN AFMHSGTTSD VFLRENLEWL
GLASNWSKFS ATAALGVIHK GYIEEGMTIL GPYLPQAGVD NTMHGAQYSE GGALYALGLI
NAGSGKNVES FLRESLKSAQ GEVVQHGAAL GLGVAGMGGK NAEAFDDLKQ TLFTDSAIAG
EGAGYAMGLI MLGTADASSA EEMLTYARET QHEKIIRGLA VGVGFIYYSR QEEADETIKI
LLAEKDPILR YGGVYTLALA YAGTSNNNAV RRLLHIAVSD TSDDVRRAAV TSLAFLLFKN
PSQVPRIVQL LSESYNPHVR CGATLALGIA CAGTGLQDAV DILEPMTKDS VDFVRQGAFV
ALGMVLVQQS DASSPSLAAT RALYTKVVSD KHEDPMARFG AALGQGFIDA GGRNVTISLQ
SRAGSRNTSA IVGMVMFCQF WYWYPLAHCA CLAFEPTAII GLNGDLKAPV FDFVSNAKPS
LFAYPLPTTP PKKEAATKVA TAVLSTTARV KAREKRKAAA EDAMDTDDKA PSEVKKDVDV
EMNSEEPKHG DVSPINGSIS NLAEDSRPST SKSGARKNEP SSENLPNFAR VMPAQLSHIA
FPLDSRYQPV RAVSAKAASN KGIKVGVAPA GSKSATAAIG LSSEKYAGGG GILILTDRFP
DQEAEFIEIN PPAATEVQAN PTNDTASLEP HIALDPNEPE VDPPEAFEVN TLSTEDDLVA
RLKPYAIICA MRERTKFRAS LLDKLPNLKL IATTGPRNAA IDISYAASKG IVVSGTGGSG
NSTLEHIWAL ILGTARHLAT EDRNVKAGKE QWQSTLPIGL AGRTLGLIGV GHLGSQTAKI
ARAFDMRVVG WSPNLTSERA AEAGVEFAKT KEELLKQSDI VSLHMVLSDR SKGILAAGDF
SKMKPSAILI NTSRGPLVDE AALIKALQQK TIAGAGLDVY DVEPLPLDHD LRKLDNVTLS
PHIGYVSEEN YEVFWTQTVE NISGFLDGEP KRVFGVNEDN YYKARVEAR
//
