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Database: UniProt
Entry: A0A165RYR8_9APHY
LinkDB: A0A165RYR8_9APHY
Original site: A0A165RYR8_9APHY 
ID   A0A165RYR8_9APHY        Unreviewed;      1237 AA.
AC   A0A165RYR8;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=RRN6 beta-propeller domain-containing protein {ECO:0000259|Pfam:PF10214};
GN   ORFNames=DAEQUDRAFT_666367 {ECO:0000313|EMBL:KZT71316.1};
OS   Daedalea quercina L-15889.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Daedalea.
OX   NCBI_TaxID=1314783 {ECO:0000313|EMBL:KZT71316.1, ECO:0000313|Proteomes:UP000076727};
RN   [1] {ECO:0000313|EMBL:KZT71316.1, ECO:0000313|Proteomes:UP000076727}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L-15889 {ECO:0000313|EMBL:KZT71316.1,
RC   ECO:0000313|Proteomes:UP000076727};
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).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC       {ECO:0000256|ARBA:ARBA00006375}.
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DR   EMBL; KV429046; KZT71316.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A165RYR8; -.
DR   STRING; 1314783.A0A165RYR8; -.
DR   OrthoDB; 1704154at2759; -.
DR   Proteomes; UP000076727; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   Gene3D; 1.50.40.10; Mitochondrial carrier domain; 1.
DR   InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR   InterPro; IPR023395; Mt_carrier_dom_sf.
DR   InterPro; IPR048535; RRN6_beta-prop.
DR   PANTHER; PTHR45624:SF9; CARRIER PROTEIN, PUTATIVE (AFU_ORTHOLOGUE AFUA_4G06390)-RELATED; 1.
DR   PANTHER; PTHR45624; MITOCHONDRIAL BASIC AMINO ACIDS TRANSPORTER-RELATED; 1.
DR   Pfam; PF00153; Mito_carr; 3.
DR   Pfam; PF10214; Rrn6_beta-prop; 1.
DR   SUPFAM; SSF103506; Mitochondrial carrier; 1.
DR   PROSITE; PS50920; SOLCAR; 3.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PROSITE-
KW   ProRule:PRU00282}; Reference proteome {ECO:0000313|Proteomes:UP000076727};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|PROSITE-
KW   ProRule:PRU00282}; Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          306..433
FT                   /note="RRN6 beta-propeller"
FT                   /evidence="ECO:0000259|Pfam:PF10214"
FT   REPEAT          918..1001
FT                   /note="Solcar"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT   REPEAT          1015..1109
FT                   /note="Solcar"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT   REPEAT          1128..1225
FT                   /note="Solcar"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          794..813
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..23
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        794..809
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1237 AA;  137660 MW;  7F2BB7EFA9858ED5 CRC64;
     MDCWPTDDRD TAKASDTSKG RKSRKPLPNW TYPVVEHGSL GAAALHRNQQ RLEWSFVVQD
     SSKRRVVSTR NPVQVFPETF GRPARHDMSV LQRADQGVQF LRTYYPDFEM SAELVREEIA
     ADARASQALQ EFDPYLGSTL ETFTCTRKAG RSLTCLAFPM GDSYFDLNIS PLTYSRKRGV
     MVNAIAKPIH TFQTPIQQLT ASVPQSTEDE EHVLATLLGV RTRGSTALFD IEPVNAQAST
     VEASQLVNVT RSDVGNRPIV DMFLPATERT LAILVSDAGA IYRCAAPGGT KQLLHSAAND
     SGDSGRDVVW KVAIWDGEDN CLAMSGRNAY CIDFRAPNSV VDLYTSNQPS ALLTSIETHR
     KDRLIRLVTT SELLWFDVRS ANKPLFGVKH FRDFDRTLRS DTKILAKAPI TFLTSQRNGL
     VSVYDVSQSG STIRMASPEY CLPRLRIPDG RNLGHVFVQH PHSSNSAELS ALQLSEFGAV
     HIMHLAMSDD IQVPIEGGLA NRDWSDEVEE LDERVKASGL DVGPLGARTL SEANLRQAYQ
     RLFMDLPEND HPDAVYDLLE KIPMFWQEVD PPIEHALTTF DIAYRCGPEL PNASRNDLFT
     ESVLNSKRGS RALMQGRIPI HQLARRTPWH LNITSFVQLH VPDLREDSAG TFEQLSRYDL
     ASDGRRPAGS LRRETEAREQ LTLDLHLSSD VFSPSRCRKP AELDIDAAME TMSRATEAMS
     LGDMEPSDVL FGFLHPVHEE ATEYYSKAAD TPKDTSGKHL APLGVRLLLK DWDVGVDPST
     YRYEDPYDVS NNRATVPRFT RNPPSRNKEP AAQWQRPPLI VPTLNLAPPH VAQSGSQPMD
     SWNMQSSSQI PFASTQIVPG PYGGRPGPPK KPAKKRVVPS CRRATLAYIA SVCYCGEYAP
     SYRSSGYLFD SAALNESLRY NKAVVCAISA SYISTFAGYP LDSIKSRLQT TRERTTVPKL
     ALQVYKEEGV IGFYRGLWIP LITISFVRAA SFTIYTSTKE YFHERHWLAY NTVWSVASTG
     GIGGALSGSL ISFGSAPFEL VKVRRQLEYS IAASKGVRIV KAPGTLDAVR DIFQLHGLRG
     LYLGFRLHFV RDTLGTGLYF FEYDAMRHLM GRLPSGEQGP TPYWMPIPAS TVPFMCGSLA
     GVTSWALIYP LDVVKTKVQQ RALAGERSRT VWETLYRLIR GPDPASPKPI LMGLARLYRG
     LGVSALRSIT THGLLWTFFD LTASYIDNLP RAPDDNT
//
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