ID A0A098VNE8_9MICR Unreviewed; 2051 AA.
AC A0A098VNE8;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE SubName: Full=Subunit Brr2 of U5 snRNP complex {ECO:0000313|EMBL:KGG50602.1};
GN ORFNames=DI09_62p60 {ECO:0000313|EMBL:KGG50602.1};
OS Mitosporidium daphniae.
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Mitosporidium.
OX NCBI_TaxID=1485682 {ECO:0000313|EMBL:KGG50602.1, ECO:0000313|Proteomes:UP000029725};
RN [1] {ECO:0000313|EMBL:KGG50602.1, ECO:0000313|Proteomes:UP000029725}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UGP3 {ECO:0000313|EMBL:KGG50602.1,
RC ECO:0000313|Proteomes:UP000029725};
RC TISSUE=Spores {ECO:0000313|EMBL:KGG50602.1};
RA Haag K.L., James T.Y., Larsson R., Schaer T.M., Refardt D., Pombert J.-F.,
RA Ebert D.;
RT "A new species of microsporidia sheds light on the evolution of extreme
RT parasitism.";
RL Submitted (APR-2014) 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:KGG50602.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JMKJ01000571; KGG50602.1; -; Genomic_DNA.
DR RefSeq; XP_013237046.1; XM_013381592.1.
DR GeneID; 25260514; -.
DR VEuPathDB; MicrosporidiaDB:DI09_62p60; -.
DR HOGENOM; CLU_000335_1_0_1; -.
DR OrthoDB; 57056at2759; -.
DR Proteomes; UP000029725; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase 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; cd18795; SF2_C_Ski2; 1.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 1.10.3380.10; Sec63 N-terminal domain-like domain; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR041094; Brr2_helicase_PWI.
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 PANTHER; PTHR47961; DNA POLYMERASE THETA, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G05260)-RELATED; 1.
DR PANTHER; PTHR47961:SF4; U5 SMALL NUCLEAR RIBONUCLEOPROTEIN HELICASE; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF18149; Helicase_PWI; 1.
DR Pfam; PF02889; Sec63; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00973; Sec63; 1.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF158702; Sec63 N-terminal domain-like; 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:UP000029725}.
FT DOMAIN 518..719
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 750..953
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 15..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 210..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..68
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..89
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2051 AA; 222154 MW; 03AF527426474A62 CRC64;
MAGDDEHVHR FDYARNANLV LHSDGKKRGE HDVEDGSEIG SLWGRINPLE FGAKAERERP
KLPSTKRKPP SDESTNGGGH MSDALSQSSS LTLSELATLK YRPRTQETRS IYERMLKLVM
DLAEEESGEM GRALLDEALI ILCSSELREL EQRSSLEALL MRPMESLAFS QLLALSKRLV
DWNASASTST EANTAEAEEE SFGLTVVEPD HLLNDDDDDG GGEASQYLPD IKEDPEENIG
QFRGDEETEI DPFYLSHVVP SEEEQGDMHL PKSSIPRIDI RDIDVHYLQR LLSLPGEDAW
VSHSRSKAVL ALLQDRTLEG WILEGRILKE LCKHHSRHEN PFELLSLLVS NRMALVAGIA
LAEADPLGGD GEAKEAILQQ LIAEGPEGAV LAALVDTPRT TSAVAPFEKN STVDASSVIA
STAPSKSSSS SSAETLAAMA RDARDAQTLA ARRLPLPPGS WRRAHAGYEL IHVPAPPAIP
AHVRDAPSLC VVEALPSWTH GAWEGQPTLN RIQSAVLAHA FFSDQNLLVS APTGAGKTGI
AILALLRLFG SACGRKIDFP GCSTIIESSD GETVASKRST IAVYIAPMRA LVSEITATFR
SRFLESGLWD SNELAISELT GESGGGLGAL LAEQGFASCR LIVATPEKWD IVSRKPAALI
PDLLIVDEVH LIGDAPRGTA LEAIVARSLG EARIVALSAT LPNAEQVGSW LRARVHCFGG
EWRPCPLSLS FYGVMERKVS KRMAKMNEIL LEEVIERLPQ GPILVFVHSR RETARTARLL
RDGAATRGLL ALFHRAGGND AEDANDSAFD SAELGELMPA GIGIHHAGLS RQDRGTVERL
FGSGQLSVLV STATLAWGVN LPAHTVIIKG TEIYDPGTES GSGPAWTLLS SQDLLQMWGR
AGRPQFDRHG EALLLTSHEN LSRYVAVTAQ PVLSQMLTTA ATDGEADGIT SSASSFSSSS
CSMMMRILPH LAAEVARSTL IRSMDDACAW ISDRLFLGQM VRDDPAALGI DPQGGDPREW
IVTLASASMA LIRLLGLVEG ATASSSLFHA TPLGEIASFF YIAPATIRTI LHELRPQGER
ASIAAVSAYE RVLSLLSRTM ELAALSRIRE EEQGALDRLA SLLPVPMERT HKAALLLQAV
ISRVGLEDGP MAMDAAHVAA IAPRLLRAIF EIAVMERGNR GGGAGLFAVA RTALLLARSV
ELRCWPTCSP VIQLLDKETT AAADLARLER RELNLAQLRL LTPGELAALI PQKIDLSVLP
SIEITASAIP LTQDILRVDV AIQRTESHSI AFWLFLTDLE DEKILHHQRL LLRETVTTAT
LRVPIGRPVP PAIMIHVLSD RFHHCDVRLP ISFRALQLPA DEEVPLKRIE QLAPVSLEQV
RALYMCQANV TDCMKTDTTS PDHTVMLSAV ERHVLWLLRL ECSPLVVGLP FSLLADAATM
VRLLEFGIGL TIACEQPVEV ALIDDTPKVK RQLVLATSPW RGRRVALGRT LAALFEPGQL
LLDEKHSLPS ALASLFENAD HQKPVVAVGE VTFLFGLLRA VSASSFPFSV RLVMEWGVIS
ESQMLYQELL LTEIHALADA SVSLLVAPAT MPSLRSLGRW VGTSPGRLLR LPHRRPQASV
VRFWRVDQNE EKNSAFLPLL PLIEDNGPQT SRDSVLLCVA DEDAANALAA TLMRHVRCNK
LSLATDADAI AELIGDGADV KCDYLEWLAA GIAYAADPLG WTAFNRGLLP ILITPLSMVG
EVIASTEICR LKQIIAWQTA AVLENACMFG LGLAMGAPAT MGPVLFSCES QGLSTSMMMS
PGESVLMPSL AMALPAALLA SNAGDEATLQ AAMDYICQHS WLLERMRANP NFYHLTERSE
IVLAERLSEA LESALDMDEE AQQKESHADH APATLARVAT HYGLSDELLR TMVWPNILPT
TRAKSLLAIL SQATVTCAAG HIRVPCVDFI NATGPLDVKF GVSLLSAVVD ICLLKSSCGE
DANYLSTALA AMDLVQALRQ GCKPGRADPV DVIRRQLGLT PDQVQSLISA VPLGETPSLY
ELALYVREPE H
//
