ID A0A137P2I6_CONC2 Unreviewed; 2179 AA.
AC A0A137P2I6;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=U5 small nuclear ribonucleo protein 200 kDa helicase {ECO:0000313|EMBL:KXN69250.1};
GN ORFNames=CONCODRAFT_8360 {ECO:0000313|EMBL:KXN69250.1};
OS Conidiobolus coronatus (strain ATCC 28846 / CBS 209.66 / NRRL 28638)
OS (Delacroixia coronata).
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota;
OC Entomophthoromycotina; Entomophthoromycetes; Entomophthorales;
OC Ancylistaceae; Conidiobolus.
OX NCBI_TaxID=796925 {ECO:0000313|EMBL:KXN69250.1, ECO:0000313|Proteomes:UP000070444};
RN [1] {ECO:0000313|EMBL:KXN69250.1, ECO:0000313|Proteomes:UP000070444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 28638 {ECO:0000313|EMBL:KXN69250.1,
RC ECO:0000313|Proteomes:UP000070444};
RX PubMed=25977457; DOI=10.1093/gbe/evv090;
RA Chang Y., Wang S., Sekimoto S., Aerts A.L., Choi C., Clum A., LaButti K.M.,
RA Lindquist E.A., Yee Ngan C., Ohm R.A., Salamov A.A., Grigoriev I.V.,
RA Spatafora J.W., Berbee M.L.;
RT "Phylogenomic Analyses Indicate that Early Fungi Evolved Digesting Cell
RT Walls of Algal Ancestors of Land Plants.";
RL Genome Biol. Evol. 7:1590-1601(2015).
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DR EMBL; KQ964542; KXN69250.1; -; Genomic_DNA.
DR STRING; 796925.A0A137P2I6; -.
DR EnsemblFungi; KXN69250; KXN69250; CONCODRAFT_8360.
DR OMA; QTEIQYY; -.
DR OrthoDB; 57056at2759; -.
DR Proteomes; UP000070444; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProt.
DR CDD; cd18019; DEXHc_Brr2_1; 1.
DR CDD; cd18795; SF2_C_Ski2; 1.
DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 2.
DR Gene3D; 2.60.40.150; C2 domain; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 4.
DR Gene3D; 1.10.3380.10; Sec63 N-terminal domain-like domain; 2.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041094; Brr2_helicase_PWI.
DR InterPro; IPR048863; BRR2_plug.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR004179; Sec63-dom.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR47961; DNA POLYMERASE THETA, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G05260)-RELATED; 1.
DR PANTHER; PTHR47961:SF4; U5 SMALL NUCLEAR RIBONUCLEOPROTEIN HELICASE; 1.
DR Pfam; PF21188; BRR2_plug; 1.
DR Pfam; PF00270; DEAD; 2.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF18149; Helicase_PWI; 1.
DR Pfam; PF02889; Sec63; 2.
DR PIRSF; PIRSF039073; BRR2; 1.
DR SMART; SM00382; AAA; 2.
DR SMART; SM00487; DEXDc; 2.
DR SMART; SM00490; HELICc; 2.
DR SMART; SM00973; Sec63; 2.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 3.
DR SUPFAM; SSF158702; Sec63 N-terminal domain-like; 2.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 2.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:KXN69250.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000070444}.
FT DOMAIN 511..695
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 729..939
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1358..1537
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT REGION 16..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 214..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 394..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..88
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..243
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 257..276
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..418
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2179 AA; 248777 MW; ED0C540068D3D7C8 CRC64;
MAEEYAKNAQ YQYVANSNLV TQADRSQITR RDNDPTGEPE TLAGRISISD FGSRAVRDKV
SGQEIKKHKS SHKSGDRSRR KEEDSRRNVV TNSVLNVSED FEGLNYRPKT QETKSLYEML
LTFVSKRLGD QSHDILRSAT DTVLEILKDE NMKDSSRKSE IDSIIGTITV EELNQLLNVS
RKINDYKSSD QKENGETQEE LDDELGVAVV FDDEDEDDDQ VGGQFEVKDS SEDEDEEDQN
QGQNGEADID QAYPSFKSAN GDGNGDLNQS RSSAISKDTV HPHEIHAHWL QKQIKEYFSD
SQEAEGKTLE TKDILFSDID ARECENQLMQ AFDFDQEKFS LINRLIKNRD VIVWCTKLSE
VGGPQSQEYQ NIASEMTELG LDWILKAIRG GQEGSLNSVP ATNGELSTQS KSHPTDLPTL
ATSKFVPKSS IDLDDLIFKE GNHLLSKEKC VLPAGTTKTK KKEYEEIQVP IPNRMPDPPE
SLISTKKLPE WAHESFKGMP NLNRVQSEVF PSAFGQNDNI LLCAPTGAGK TNVAMLTILN
EINKHFDEET KTLNLNNFKI VYIAPMKALV QEMVNTFTRR LSYLDIKVAE LTGDSQLTKQ
QIAETQIIVT TPEKWDVITR KANDRSYTNL VRLIIIDEIH LLHDDRGPIL ENIVVRSLRH
MEQTQTITRL VGLSATLPNY QDVADFLRVP ESNVFFFDSK FRPCPLKQNF IGVSEKKAIK
RFQVMNEVTY EKVMEQAGKN QVLIFVHSRK ETVRTAAFLR DAALDRETIG MFVKPESASR
AQLENEAEQV LDQNLKELLP YGFAVHHAGM KREDRTVVEE LFLEKHIQVL VSTATLAWGV
NLPAHTVIIK GTQIYSPEKG RWVELSPQDV LQMLGRAGRP QFDSFGEGII ITTLNELQYY
LSLLNTQLPI ESQLVSKLTD SLNAEISLGT IRNREDAVQW LGYSYLYIRM LRNPSLYMIS
PSEYKEDPTL VQRRTDLVHA AALLLDQCQL VKYDRKTGRF QGTELGRIAS HYYISHRSMA
TYNQHLKPTM SFIELFRAFS LSDEFKYIPI REEEKLELAK LLERVPIPVK ESVEEPVAKI
NVLLQAYISQ LKLDGFALMA DMVYVTQSAG RILRSIFEMC LKKGWANLAR LALDMCKMVE
KRSWLSMSPL RQFSGLDPKL INRLERKDFS WSRYLDLNPE EIGELIGIPK AGRVIHKFLH
KFPKLELRAY VQSITRSLLK IELTIIPDFQ WDDKIHGNSE GFWILVEDLD GENVLYYDYF
VLKKAYATEE HYNSFTIPLS DPIPPNCFVT LLSDRWLHSE AKLPISFKHL ILPERYPPHT
ELYDMHPLPT SGQEPKGLFE YYANEFSEFN PIQTQTFHAL YKTNDNVFLG APTGSGKTIC
AEFAILKVLS QTKPGERPSP IVYLVPNDDL AKNAFVYFTH RFRNLEELNV VQFTGELSAD
FKQLVEGDII VTTPTQWDGI SRKWKTRERI QRIRLFICDE VHMVGGDVGP TYEAVVSRMR
YMNSQLNNKI RFVALSVPLS NSKDMANWLG VSPQTTFNFS PIDRPIPLEV HIQSFQINHF
ASLMISMSKP AYQAIGQYSP NQPVIIFVPN RKQCRLTASD IITHQYATSE NPHFLHCKAE
EMEAAVEKIS DPYLKESLLS GIGLYHEALS PSDRNIVSKL YLSGWFQVLI ASRDTCWSMN
HLTSHMVIIM GAQYFEGKEH RYVDYPVTDM LQMMGRANRP LIDQTGQCLL MCNSNKKEYY
KKFIEEALPV ESHLDHFLHD FFNAEISVET IENKQDAVDC LTYTFLFRRI SQNPTYYNIQ
GITPTHISNY LSELVEDTLN QLSESGCIQI DEDEVDVHPL NLGMIAAFYN IQYTTLDSFA
LSLTNRTKLR GLLEIISAAS EFETLPIRHH EDNLLKKLYD RLPVKLTEDK LNLNLPNVKT
HILLQSHFSR TQLPPDLQAD QTMVISQIIP LLQGCVDVIS SKGWLNPALA TMELCQMIVQ
AMWDKDSPLR QIPYFDMDRI TKANKMDVES VFDFIDLDDS DRKSLLKDLT NPQLRKVADF
VNTYPSLELN INVLTPKDEL RCGEKVQLHI QIERDGVDED EISGSVNAPY YPKLKDENWW
IVVGSPTENL LLGIKRFNLK QILNLKLEFE APASSSVGPN QFKVYLMSDS YLGCDQELDL
NVDLLEALSE DEDSEDADE
//
