ID A0A2T9ZKV1_9FUNG Unreviewed; 2288 AA.
AC A0A2T9ZKV1;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:PVV05224.1};
GN ORFNames=BB560_000273 {ECO:0000313|EMBL:PVV05224.1};
OS Smittium megazygosporum.
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC Harpellomycetes; Harpellales; Legeriomycetaceae; Smittium.
OX NCBI_TaxID=133381 {ECO:0000313|EMBL:PVV05224.1, ECO:0000313|Proteomes:UP000245609};
RN [1] {ECO:0000313|EMBL:PVV05224.1, ECO:0000313|Proteomes:UP000245609}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC-DP-2 {ECO:0000313|EMBL:PVV05224.1,
RC ECO:0000313|Proteomes:UP000245609};
RX PubMed=29764946;
RA Wang Y., Stata M., Wang W., Stajich J.E., White M.M., Moncalvo J.M.;
RT "Comparative Genomics Reveals the Core Gene Toolbox for the Fungus-Insect
RT Symbiosis.";
RL MBio 9:e00636-e00618(2018).
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:PVV05224.1}.
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DR EMBL; MBFS01000026; PVV05224.1; -; Genomic_DNA.
DR STRING; 133381.A0A2T9ZKV1; -.
DR Proteomes; UP000245609; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR CDD; cd18007; DEXHc_ATRX-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 Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1.
DR InterPro; IPR044574; ARIP4-like.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR45797:SF1; HELICASE ARIP4; 1.
DR PANTHER; PTHR45797; RAD54-LIKE; 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 SUPFAM; SSF47769; SAM/Pointed domain; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000245609}.
FT DOMAIN 1411..1659
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1852..2046
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 164..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 223..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 581..678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 706..753
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1057..1078
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1100..1119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1135..1178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2099..2121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2185..2288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 581..636
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 643..678
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 732..753
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1152..1178
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2185..2215
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2223..2270
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2288 AA; 260401 MW; 314D17A0AFA99576 CRC64;
MDPVTKSDLD RVSPLYWTIH QVSAWIESKF HDKELASTFQ ENCIDGGILV KFLTYNMLRV
DMKVVIGKAA RVIEELVNLL EQWELPSSRL RDKHYGVNLE TSGRAEINTA NQNPNRDGFG
LATERIPTKR ALVAPEPEYI DIIPKKPKDS SKVSIFGSSS LFLANDSPEH PPAHMSRSSS
RSERIKLEDS QSPPGSFETL SYHKPAVPYS CYNETVERNL FGSTKSANQY PPDAHTEKRN
SKNISPDNVI LQNKKRLYSD NKNSSHSKLA ALSKSVARID AILQSNKTNT QSPVEFSGQR
TKPNTDNKNT ILGQIKSKYN GSKIHRHSPK PTRLNHFENI PSLHESCWKK LNDTSLTSPF
WFRRLLGRGY SNSSTLNDKI LYSNIWLKRL LIKEDSEKYR FDNSTIAHKT GNFGYKTIAK
ASRKAPLGVP KLLSYQERIE KKYKDVWESN YYPKLLRNKE AFIEQRKDDL KNILDDYKMI
KNSIDSFFLK SNNVEELGQE VVLKYMHYFT AMWLIGVLKA RAASTSVSQS TEGHLKTDSQ
SSISDIEQYR LDETETQPSA NTSPERPQKA ISLVEISRVS NAQSGKQISP SKGSDLLENN
SSVPIHNTRS RPNDFTSARI RPGVTSNSIL SSKNDKHESV SISDSDGSSF SIEMSDSKSV
DSFDSLQNSS KESTPSKENV YLKPSILASA KENDSEMARI ETDYSRYSSD MEISDSDEQT
DQADQVEQNK EIKKGTSSIG SESRPNNTHN EVTNFASVPH RNDAQLVPPM TDSLDDFVSD
DSEPEWNLDR VIDLNEDEII EIQQSDFQLL QQKRQKYLEM QKQKYFYQLQ SDEQLRQDKL
LIENVNENPQ KLTRLRRVFS CPSIYALNSD RSHSKRFEDK LLSQNPSFHC STKKLVKLGV
YTMPFDQFFE KMNDFLRLHS HDSPLSQLSP SDCYHIRTHF PKAIDTDSPT FNKTGAILFW
HSFHSWLKDR SSDELQSLAF ESSEGLLDKL PIDKGGDITP IKEALRRYWD YHMEILENSY
DLISENQKIS SLADSGQINY FEPDPYELRK HLSAKDRRRL KNNSGSGDQV VNPSDDSDDD
IFGFRAAGAF GEYNDIISSD GGYTVDSSDS DGNRSAGESD EIKLAQFIQR LENRATGNKV
TIPERKRQAQ STRKQAGSNT QDKSSNSSQS RKGNTQSLTD KIVSYMERQQ KYLKDRTEDY
TKKIEQIKKD NENQVKMLDK GLSVRTIDTS FQTSSLNNNH NLGYSVSGYD TDSSNSIFRE
ATNNNQLQPD TANSSSRLYQ IPGYPNLPPN ANGGIIPPLN PQMFRPQHDI QVGVRQLLPP
ALQTKLTHQR ADALLKLNKT GNSANQARED ALSKQKVADT TRVYEPIMIN PGHSEAYRDV
FIPEFLGRWL KPHQIEGVQF MWKNLIMFRD GAEGVQQHGC VIAHSMGLGK TLQVIAFVYT
LLEAIQIDKK MKLGMKSRNI DARSKEFKLS GVPDDLFGSQ ILVLCPPTLQ TNWQREFIKW
LESDGKDRSL YNRPLTRAEI VNKEKHSRRI REVIKMILVF DKVEGSLDHK ASILEEWHRT
GGVLILGYAA FRDMIKSPKE SGKSLSSTKK YIKRIFKCLQ NPGPAVVIAD EGHSIKNMKS
QLSISAENIN TKARICLTGY PLQNNLDEYW TMVNFVYPNI LGDFADFHTS YSVPISEGLF
TDSTPLARKL SQIKLKALSD HLEPLVLRRD AGILELEIPP KTEYFIMCNL SPLQQNLYTA
FLNSFQQKIG VTNKGVIARY ATFSAICNHP GAVKVLFMER RNRFREKINK LNNSLYTGID
EEDEQEVLER RVTESQEMMN ETVDDSWSKP VFGSVAPSSV VKPSQSSKLM ILLSIIYNSI
ISNEKVLVFS HFISTLDFIW WVLKNTKVTE SAERERKRRA REKILPHEVL GLEPIGLSSA
RNAATIEQLV LRIDGRTKMS DRTMFIDQFN DAKNPSKVFL ISTGTGSLGV NLVGATRVVL
YDVGWNPLYD EQAVARAYRY NQTKPVYVYR LISMGTWEQT MFYNNRHKVG LSLRVIDRKK
VDEKVSKDAT KRYYAPLPPL NTVHPLTNEV ARNLIMKYSQ DFVFLSALKR NKNKITDIRG
HTTTSNYTPA EDNPIEDDHT SNKYEYENFS QNVFDELVAE ERHKLNTYVA KGRVLNRFPH
SDNEDSDIEI DTIELNSPYM DLHSTVEKSS GKQNIQSGRS LHPSQDNTAG NYSERRSFFE
KNVPRLSNKN VNMDSENTDS DAPSASSKSS ILHLSKDYIR NNQGSLKPKL KSRFSDNKSK
QVGRYNNY
//
