ID A0A060SI51_PYCCI Unreviewed; 1963 AA.
AC A0A060SI51;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=Glycosyltransferase Family 2 protein {ECO:0000313|EMBL:CDO74187.1};
GN ORFNames=BN946_scf185043.g239 {ECO:0000313|EMBL:CDO74187.1};
OS Pycnoporus cinnabarinus (Cinnabar-red polypore) (Trametes cinnabarina).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Polyporaceae; Trametes.
OX NCBI_TaxID=5643 {ECO:0000313|EMBL:CDO74187.1, ECO:0000313|Proteomes:UP000029665};
RN [1] {ECO:0000313|EMBL:CDO74187.1, ECO:0000313|Proteomes:UP000029665}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRFM137 {ECO:0000313|EMBL:CDO74187.1,
RC ECO:0000313|Proteomes:UP000029665};
RA Levasseur A., Lomascolo A., Ruiz-Duenas F.J., Uzan E., Piumi F., Kues U.,
RA Ram A.F.J., Murat C., Haon M., Benoit I., Arfi Y., Chevret D., Drula E.,
RA Kwon M.J., Gouret P., Lesage-Meessen L., Lombard V., Mariette J.,
RA Noirot C., Park J., Patyshakuliyeva A., Wieneger R.A.B., Wosten H.A.B.,
RA Martin F., Coutinho P.M., de Vries R., Martinez A.T., Klopp C.,
RA Pontarotti P., Henrissat B., Record E.;
RT "The genome of the white-rot fungus Pycnoporus cinnabarinus: a
RT basidiomycete model with a versatile arsenal for lignocellulosic biomass
RT breakdown.";
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC {ECO:0000256|ARBA:ARBA00007025}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CDO74187.1}.
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DR EMBL; CCBP010000125; CDO74187.1; -; Genomic_DNA.
DR STRING; 5643.A0A060SI51; -.
DR HOGENOM; CLU_234563_0_0_1; -.
DR OrthoDB; 5491077at2759; -.
DR Proteomes; UP000029665; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR CDD; cd18008; DEXDc_SHPRH-like; 1.
DR CDD; cd00761; Glyco_tranf_GTA_type; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR Gene3D; 3.90.25.10; UDP-galactose 4-epimerase, domain 1; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001509; Epimerase_deHydtase.
DR InterPro; IPR001173; Glyco_trans_2-like.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45626:SF12; DNA REPAIR PROTEIN RAD16; 1.
DR PANTHER; PTHR45626; TRANSCRIPTION TERMINATION FACTOR 2-RELATED; 1.
DR Pfam; PF01370; Epimerase; 1.
DR Pfam; PF00535; Glycos_transf_2; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000029665};
KW Transferase {ECO:0000313|EMBL:CDO74187.1};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT DOMAIN 1396..1563
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1713..1755
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 1793..1946
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1038..1071
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1083..1111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1161..1189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1206..1236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1263..1291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1038..1069
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1091..1110
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1270..1291
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1963 AA; 219511 MW; 736C88C86CE3536A CRC64;
MLKETDLILI TGAYGFIVSM SVPILDIPDS DLEQGGHVAR KLHSLGYRLR VTDVAHKASN
GQLADSGGEI VTGNLCDPSF CARIVVGVDY VLHFAATMGG MGTIHEANDF VIYQENHSMT
SNLVSACVAA GVRGFFYASS ACVYPESLQA PGRDVSLAES DVWKNPPPHP QGLYGLEKLV
SELVLYQQQG GMEVKIARFH NVYGPFGTWV GGREKVPAAF LRKALAAKLA SDAPVAFEIW
GDGRQRRSFC FIEDAVEAVL RLLGSDCSEP VNVGSDQAVS IQRLAELSLA ASGVDLADVV
FEYKTDRPVG VGSRNSDNTF VHERLGWEPA YSLEEGMRIT GKWICSQILE NIASMSQSER
KEYLHLLQTS EMVDLRRDAN TFAILLPITS RGLNSPHDCL ANLGRFARSL AASTADDVAR
LGERYAVRVY LAIDNDDDFL WQVDGGDLAT PILRDQGFRD ITTLRCDRPR GHVCALWRDC
ARRAYEDGCD YYILMGDDVV LEEPDWMSSM HQTFARLAAT EHVPHGIGCV AFTDTSFPGM
PTFPAVHRTH MDIFGGDVIP DCFTNQDGDP FLFQLYRRWG CSKMIHSRVR NELGGSEAAR
YEKIPAAGWT FGTLDDATVA VDTWLRHHSP VSKRKLTLDV IIPCYRVDMQ YIDAFLRLRQ
SSTIEVMFII IVDDPLSPRV KDLMQKHGHR PDVRIRINKQ NLGASASRNR GLQESAAEWV
HFLDDDVTPD EDLLVEAEKA IRAHPKAAGF VGGAQFPSAD KVFTTAIHLA GVTYFWNIAE
KIEFDVPWGV TANLIARRNV LDNVQFDLQF PKTGGGEDID FCRKKREFSI AHGGEPFWAA
PTVRVTHPWW YCGRRSYWRF YMWSKGDGGL VKLYPKHCYR DAFPNGAECL LLSVVVFLSG
TILGLTDLGQ GRRAALFGIA WAASTMLSNV VFDLFRHLVL HPGRVRDMKT TVAGIWWICA
IVEGAFLRVF SEWGRVVGIL DRDATINKVQ ARLVASPAFA SADLATYNYN SFPSTTILFC
FDSHFASMVS TRRRALTAQS ASTTPSTTVS PVFSAGASPP STPQTSNMGE NEDELDHYAQ
KRGMRGATAA TKKRALEEDG NEEMAAERAP KRRVMQQAAY VEIASTKTAK TRTFESNETL
RVTTRGKPAA AILAVNFESE EEILESDDSG SDFNPEEESV SDLEDDLDED DEEVMVDAAV
RESLQTARQD AEHAAGLSSA GAGSSKARPP TNKAAALRAA AAERRLARAS EVDVIDLTSD
FEALSSESDS EEEPLSKGKE KQAAKAKAAK SMTLTELRKA RREERKEARL RRNATATEEA
KLREELGRRL TYAEKATIAL RRHHPELLDV WGDVERRIEI IEPKKSEQPP NLKVRLLPFQ
LESLSWFKEQ EKGVWRGGML ADEMGMGKTI QMIALMVSDY GAKPNLVVAP TVAIMQWRNE
IEMHTDNMLK TLVWHGASRE SSISELKKYD VVLTSYAVLE SCFRKQHSGF KRKGKIVKEK
SPLHAIEWNR VILDEAHNIK ERSTNTAKAT FELNARYRWC LSGTPLQNRV GELYSLVRFL
GGDPFSYYFY CGHSPMKHTC FWNNEILTPI QKNGMLGPGQ IAFKKLKILL DRMMLRRTKI
QRADDLGLPP RTVIIRRDYF SPEEKELYLS LFSDAKRQFN TYVDEGTVLN NYSNIFSLLT
RMRQMACHPD LVLRSKNNAG MFIQDDTGEG TVCRLCNEYA EDAIQAKCRH IFDRECIKQY
VEASIEQTPA CPVCHVALTI DLEAPALELE ETAKVRQGIL GRLDLNKWRS STKIEALVEE
LSNLRQQDAT TKSIVFSQFV NFLDLIAFRL QRAGFNVCRL EGTMSPQARD ATIKYFMNNV
HVTVFLVSLK AGGVALNLTE ASRVYLMDSW WNPAVEYQAM DRIHRLGQHR PVQAIKLVVE
DSIESRIIQL QEKKAAMVDA TLSADDSAMG RLTPEDLGFL FRL
//
