ID A0A1Y1WFM3_9FUNG Unreviewed; 1245 AA.
AC A0A1Y1WFM3;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ORX72118.1};
GN ORFNames=DL89DRAFT_274270 {ECO:0000313|EMBL:ORX72118.1};
OS Linderina pennispora.
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC Kickxellomycetes; Kickxellales; Kickxellaceae; Linderina.
OX NCBI_TaxID=61395 {ECO:0000313|EMBL:ORX72118.1, ECO:0000313|Proteomes:UP000193922};
RN [1] {ECO:0000313|EMBL:ORX72118.1, ECO:0000313|Proteomes:UP000193922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12442 {ECO:0000313|EMBL:ORX72118.1,
RC ECO:0000313|Proteomes:UP000193922};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
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:ORX72118.1}.
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DR EMBL; MCFD01000003; ORX72118.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y1WFM3; -.
DR STRING; 61395.A0A1Y1WFM3; -.
DR OrthoDB; 5482994at2759; -.
DR Proteomes; UP000193922; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR CDD; cd18660; CD1_tandem; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 2.40.50.40; -; 1.
DR Gene3D; 6.10.140.1440; -; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 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; IPR025260; CHD1-like_C.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR023780; Chromo_domain.
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; PTHR45623:SF14; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 1; 1.
DR PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR Pfam; PF13907; CHD1-like_C; 1.
DR Pfam; PF00385; Chromo; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00298; CHROMO; 2.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM01176; DUF4208; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF54160; Chromo domain-like; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS50013; CHROMO_2; 1.
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 Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000193922};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 1..58
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 189..362
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 495..659
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 655..676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 763..816
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 863..895
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1002..1070
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1155..1245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 779..793
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 801..816
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1041..1055
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1169..1183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1197..1220
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1245 AA; 140787 MW; E684C7EFCEF81FB2 CRC64;
MVRDFRLREG AAGQHCNEIG NLEFYIKWKG WSYRHATWDT AEFLKDFKGY KKVENYFKAT
VLLDYAIRND PEVSREDIEQ LDINREMERD TLRDYTNIER VVASRQSTAG RRRLPYSSCS
WVTADEIKPE EQVELDAFLD REQSICLAHR SAPTAKAKRP KFQRMTKQPE YLVGGELRDY
QLTSLNWMAH LWCNDENGIL ADEMGLGKTI QTISFLSYLF HTQEIYGPFL VVVPLSTIGA
WQREFARWAP DLNTLCYIDD NRSRAIMREY EFYKNGSGNP PRVKLNVLLT TYELVLKDRD
LLGSIKWNFL AVDEAHRLKN SESQLHEALS SFHTTNRLLV TGTPLQNTVK ELVTLCRFLN
PERFADLDDD FDIRVTAGDT EQEGKIAELH RRLKPYMLRR LKKDVEKSLP NRTERILRVE
LSGMQVHYYK NILTRNYAAL NRGATGSVQM SLLNIMAELK KASNHPYLFP NAESQAEAKD
EVLRGLITHS GKMVLLDKLL AKLKAGGHRV LIFSQMVRML DILADYMAMR GYAYQRLDGS
VPSEVRKRSI EHYNAPGSPD FVFLLSTRAG GLGINLETAD TVVLYDSDFN PQADMQAMAR
AHRIGQKKQV SVYRFVSKNT IEEEILERAK RKMVLEYCII KGMDTSGLHV TDTERKQIEK
SKQGKSGGLV GNSSGASSFS REELAAILKF GASSMFADDS VTMQQHKLDD MDLDKMLEDA
EQAETSEAGV ADDFLSQFKV ADYGGSGMSW DEIIPEDERK RVEFEEQQKQ EEELLVADGN
SSDGSTASSM RGRRKGGSSR RRNEGRTNDP KAFGEKEVRA LIRGVQKFGS PENRQELEGK
DAESVKAMGL ELIKSCEDAL RSHLHGTNGD TNDSAAGGGE DEDLGGRRLQ QPGQRDELTS
FRIGVPLKPV HHWSCLWGQR EDAMLLVGIY RHGFGNWDRI QADPDLGPAE EAKAASVQSI
GGTVRGASGA AAGKRIVAPK ATHLVRRGEY LLKVLREGDE RRTPAPLNLT PRRSAPARKR
RVFTEDSDAN STGINNDEQA PESEMDARPP GDVEDGELSE PESMDERACK DLMRPVKRYL
QRLRDEAEHT KSSQSKVKLI SDCLLPIGRH IRSVIERKRS RAASDPVEDV DRLYRHLPVN
YKKLVHLFER LEESSLSAPP PPALSPTAKH QDSAASPTSS RHRSHGRSWS RSRSRSVSPS
RSREDTERYR KRSLSRGDED EGDFADGDGR CQCQWRGASP QQRLA
//
