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Database: UniProt
Entry: A0A166RX67_9PEZI
LinkDB: A0A166RX67_9PEZI
Original site: A0A166RX67_9PEZI 
ID   A0A166RX67_9PEZI        Unreviewed;       764 AA.
AC   A0A166RX67;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Alpha-mannosyltransferase {ECO:0000313|EMBL:KZL69890.1};
GN   ORFNames=CT0861_04552 {ECO:0000313|EMBL:KZL69890.1};
OS   Colletotrichum tofieldiae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum spaethianum species complex.
OX   NCBI_TaxID=708197 {ECO:0000313|EMBL:KZL69890.1, ECO:0000313|Proteomes:UP000076552};
RN   [1] {ECO:0000313|EMBL:KZL69890.1, ECO:0000313|Proteomes:UP000076552}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0861 {ECO:0000313|EMBL:KZL69890.1,
RC   ECO:0000313|Proteomes:UP000076552};
RA   Hacquard S., Kracher B., Hiruma K., Weinman A., Muench P., Garrido Oter R.,
RA   Ver Loren van Themaat E., Dallerey J.-F., Damm U., Henrissat B.,
RA   Lespinet O., Thon M., Kemen E., McHardy A.C., Schulze-Lefert P.,
RA   O'Connell R.J.;
RT   "Survival trade-offs in plant roots during colonization by closely related
RT   pathogenic and mutualistic fungi.";
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:KZL69890.1}.
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DR   EMBL; LFIV01000099; KZL69890.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A166RX67; -.
DR   STRING; 708197.A0A166RX67; -.
DR   OrthoDB; 200191at2759; -.
DR   Proteomes; UP000076552; 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:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   CDD; cd18008; DEXDc_SHPRH-like; 1.
DR   CDD; cd18793; SF2_C_SNF; 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   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
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   PANTHER; PTHR45626:SF51; SINGLE-STRANDED DNA-DEPENDENT ATPASE (EUROFUNG); 1.
DR   PANTHER; PTHR45626; TRANSCRIPTION TERMINATION FACTOR 2-RELATED; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Glycosyltransferase {ECO:0000313|EMBL:KZL69890.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076552};
KW   Transferase {ECO:0000313|EMBL:KZL69890.1}.
FT   DOMAIN          187..356
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          596..748
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   764 AA;  86080 MW;  56C001BBA6615E48 CRC64;
     MIQEMLDDDT LRLYAVCNVS ELPSVRLSGK KFDQASCNLN ITVYGPAEEF EEIGKWFQEY
     NVYLQDPLMC HVDARYCNPH KLASNDVGTC PMLSDVVFQG SEQITFQDIT EPMDMLDMLN
     SRCDLKEAKQ PAVITAELKR HQKQALTFML RRERGWGFLD GQSDIWRVID TAQRRSFVNM
     ISESHQHEEP PQFYGGIIAD PMGLGKTLTM IALVATDLEE EKHESEVRTS SDEYGGRHTG
     ATLIVIPPPL IGSWEEQLSE LIMNEVNRDG VNIVLTTYHT VSTEWRAGDG MQTSPLFAVR
     WRRIILDEAH YIRNENSRMA RAVCALDSIS RWAVTGTPIQ NRLSDLATIV KFIRAHPYTD
     TRQFDADLSQ LWKSGEDEKA VQRLKNLSAC LILRRAKGTI SLPPRHDKLC HVDFTREERL
     VYDEMRQRAI ARIEEALLQD SGLETSNVSM YHNALQQIES LRLFCNLGLG YHSRHEKVTH
     YSTENYQDWT LHAQQLFNLQ WQKGPIVCLG CSSTLDMDET MTDQSEAAQA GPRYSRCLQF
     SCSDCVKRSS RAGRTLACGH KPPCPVAPVS TSHSALEELP TSTPPDAMSG VGLPSKVKAL
     VADLDRQPPG VKSIVFSTWK MTLDVVERAL NKAGKASVRF DGNVPQKDRQ PLVEKFRNDP
     GVSVMLLTLS CGAVGLTLTV ASRVYLMEPH WNPNLEEQAL ARVHRIGQTR EVTTVRLYVR
     DSFEEQVMEV QKSKKQLAGL LLSPHDGGQS DDSLSGLQKL RSLL
//
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