ID A0A397HNS9_9EURO Unreviewed; 1420 AA.
AC A0A397HNS9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Pre-mRNA-splicing factor {ECO:0000256|PIRNR:PIRNR038901};
GN ORFNames=CDV55_106901 {ECO:0000313|EMBL:RHZ62120.1}, CFD26_100862
GN {ECO:0000313|EMBL:RLL96404.1};
OS Aspergillus turcosus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1245748 {ECO:0000313|EMBL:RHZ62120.1, ECO:0000313|Proteomes:UP000215394};
RN [1] {ECO:0000313|Proteomes:UP000215289, ECO:0000313|Proteomes:UP000215394}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMR AF 1038 {ECO:0000313|EMBL:RLL96404.1}, and HMR AF 23
RC {ECO:0000313|EMBL:RHZ62120.1};
RA Parent-Michaud M., Dufresne P.J., Fournier E., Martineau C., Moreira S.,
RA Perkins V., De Repentigny L., Dufresne S.F.;
RT "Draft genome sequences of two Aspergillus turcosus clinical strains
RT isolated from bronchoalveolar lavage fluid: one azole-susceptible and the
RT other azole-resistant.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in mRNA splicing where it associates with cdc5 and
CC the other cwf proteins as part of the spliceosome.
CC {ECO:0000256|PIRNR:PIRNR038901}.
CC -!- SUBUNIT: Belongs to the 40S cdc5-associated complex (or cwf complex), a
CC spliceosome sub-complex reminiscent of a late-stage spliceosome.
CC {ECO:0000256|PIRNR:PIRNR038901}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PIRNR:PIRNR038901}.
CC -!- SIMILARITY: Belongs to the CWF11 family.
CC {ECO:0000256|PIRNR:PIRNR038901}.
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:RHZ62120.1}.
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DR EMBL; NKHV02000093; RHZ62120.1; -; Genomic_DNA.
DR EMBL; NIDN02000111; RLL96404.1; -; Genomic_DNA.
DR STRING; 1245748.A0A397HNS9; -.
DR Proteomes; UP000215289; Unassembled WGS sequence.
DR Proteomes; UP000215394; Unassembled WGS sequence.
DR GO; GO:0005684; C:U2-type spliceosomal complex; IEA:UniProtKB-UniRule.
DR GO; GO:0004386; F:helicase activity; IEA:InterPro.
DR GO; GO:0045292; P:mRNA cis splicing, via spliceosome; IEA:UniProtKB-UniRule.
DR CDD; cd17935; EEXXQc_AQR; 1.
DR CDD; cd18808; SF1_C_Upf1; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR048966; Aquarius_b-barrel.
DR InterPro; IPR048967; Aquarius_insert.
DR InterPro; IPR032174; Aquarius_N.
DR InterPro; IPR026300; CWF11_fam.
DR InterPro; IPR045055; DNA2/NAM7-like.
DR InterPro; IPR041679; DNA2/NAM7-like_C.
DR InterPro; IPR041677; DNA2/NAM7_AAA_11.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR047187; SF1_C_Upf1.
DR PANTHER; PTHR10887; DNA2/NAM7 HELICASE FAMILY; 1.
DR PANTHER; PTHR10887:SF5; RNA HELICASE AQUARIUS; 1.
DR Pfam; PF13086; AAA_11; 1.
DR Pfam; PF13087; AAA_12; 1.
DR Pfam; PF16399; Aquarius_N_1st; 1.
DR Pfam; PF21143; Aquarius_N_2nd; 1.
DR Pfam; PF21144; Aquarius_N_3rd; 1.
DR PIRSF; PIRSF038901; AQR_cwf11; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW mRNA processing {ECO:0000256|PIRNR:PIRNR038901};
KW mRNA splicing {ECO:0000256|PIRNR:PIRNR038901};
KW Nucleus {ECO:0000256|PIRNR:PIRNR038901};
KW Reference proteome {ECO:0000313|Proteomes:UP000215289}.
FT DOMAIN 28..412
FT /note="RNA helicase aquarius N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16399"
FT DOMAIN 491..659
FT /note="RNA helicase aquarius beta-barrel"
FT /evidence="ECO:0000259|Pfam:PF21143"
FT DOMAIN 707..798
FT /note="RNA helicase aquarius insertion"
FT /evidence="ECO:0000259|Pfam:PF21144"
FT DOMAIN 810..1106
FT /note="DNA2/NAM7 helicase helicase"
FT /evidence="ECO:0000259|Pfam:PF13086"
FT DOMAIN 1118..1309
FT /note="DNA2/NAM7 helicase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13087"
FT REGION 754..776
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1387..1420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 760..776
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1387..1409
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1420 AA; 161611 MW; 56B4C87FEE77DB0A CRC64;
MGLQTRQAMA HGLDSRPTVE DFREDSSWVQ LAKTHWLGTS KVRKAKQDVI RKDLWEPLEA
ENFRLRSLLT LENLNILEKY LWPTYSEDAS NHHVLLIALI VSIKQRDHLP IWETFSDRPD
DFSNLFHRIL SMSVDNSLST FSRQSILSFI ISAFQSLENV LIRKECAPLV SISIWHNLSS
EEARDRILAK VPSLKKAWRA AGKRYEAGDE AAKAKMRFER SWLFTMLLDF LRRLNGSEQE
LSDNLRYCER FMEYLVDLES QLPTRRYVNT LLKDLNLLPV IRLSQMYRSP ENALFRDFFE
LLKHFSGFAI DDYTGEPLGP QAVYESHSQE LAHLQRTAMK HFKDKLMILA LSNYGSIEQR
SELEGQLSAL NDSELESLCA HLGFRTDYPK QSQVMPTRHL YLEILLSFYE RRVPFQETAS
QLSIVPTEKD LYDPSFLRNE TYDGSRPLAI PKLNLQYLSL GDFLWRSFLL YRSEAFFQIR
KDMEAVIKRM QPRSSRDGKT LTFDGFSRMA IPISKPAIIE VAPPKVGSSN PAFVRAEIAI
EVGRLADHIR KEWDSLRPDD VVFLLAVQPG TANNSIFQDS SVETPSLTYL RTATVVQVLD
EQSRPLREPV AGHTNGYQSR PRLRRLLLNL DPSAFKADKD RTSQGKQDIY PLINVIARRK
GRENNFRSIL ENIQRLIVSD VTLPSWIQDI FLGYGDPAGA RYTELPNRLR SVDFRDTFLD
WQHLVESFPG STIEPSGNEA SSFGPPYVLE YVENSTKAPS TSSKKRRRDA IEKEKSSAAV
IRVSTYKQPN PGPYPVDAPK LNAVRFTPAQ VEAIASGTQP GLTVIVGPPG TGKTDVATQI
INNIYHDFPN ERTLLIAHSN QALNQLFQKI VALDIDERHL LRLGHGEEEL ETETSYSKYG
RVESFLDNRN YFLAEVTRLA ASIGAEGAHG NSCETAGYFN TVYIQPAWAK FFDHARAEST
TPEDIIASFP FHAYFSTAPQ PVLDPAASKE TLLDVAEGCQ RHIDKVFSEL EDIRPFEILR
QSRDKANYLL VKEARIIAMT STHAAMRRQE IADLGFHYDN VVMEEAAQIT EIESFIPSAL
QHMKNGELPL KRVVLCGDHL QNSPIIQNLA FRQYAHFEQS LFLRLVRLGV PVINLDQQGR
ARPSLADLFR WRYKQLGDLP NVHTAQEYKQ ANAGFQYDYQ FINVPDYQGS GEREPTPHFI
QNLGEAEYAV AIYQYMRLLG YPASKISILA TYAGQTALIK DVLAHRCAKN ALFGMPKIVT
TVDKYQGEQN DYVILSLTRT RTVGYLRDVR RLTVALSRSR LGLYILGRRE VFESCYELKP
AFDLLLQRPD KLMLTTGEMF PTTRSLDDEV QGTPMEGVEH LGQYVFEMTQ AKVKALGDQD
IIVDDAMPDG DDGDDGLLDE DEVMLGAGEE PEEDPLHEHS
//