ID A0A139HT71_9PEZI Unreviewed; 1766 AA.
AC A0A139HT71;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KXT05685.1};
GN ORFNames=AC578_5571 {ECO:0000313|EMBL:KXT05685.1};
OS Pseudocercospora eumusae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX NCBI_TaxID=321146 {ECO:0000313|EMBL:KXT05685.1, ECO:0000313|Proteomes:UP000070133};
RN [1] {ECO:0000313|EMBL:KXT05685.1, ECO:0000313|Proteomes:UP000070133}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 114824 {ECO:0000313|EMBL:KXT05685.1,
RC ECO:0000313|Proteomes:UP000070133};
RA Chang T.-C., Salvucci A., Crous P.W., Stergiopoulos I.;
RT "Comparative genomics of the Sigatoka disease complex on banana suggests a
RT link between parallel evolutionary changes in Pseudocercospora fijiensis
RT and Pseudocercospora eumusae and increased virulence on the banana host.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. SWR1 subfamily.
CC {ECO:0000256|ARBA:ARBA00009220}.
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:KXT05685.1}.
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; LFZN01000011; KXT05685.1; -; Genomic_DNA.
DR STRING; 321146.A0A139HT71; -.
DR OrthoDB; 5475375at2759; -.
DR Proteomes; UP000070133; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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 InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
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; PTHR45685:SF1; HELICASE SRCAP; 1.
DR PANTHER; PTHR45685; HELICASE SRCAP-RELATED; 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 PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000070133}.
FT DOMAIN 931..1104
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1486..1637
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 586..912
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1668..1716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..67
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..134
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..156
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..234
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..256
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..294
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..322
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..366
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 595..642
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 643..658
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 659..677
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 678..699
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 706..733
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 734..754
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 762..793
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 816..833
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 848..884
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1678..1698
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1766 AA; 198674 MW; 3C92FC4AA939E846 CRC64;
MTSRPSPPAD TRKPPAADTD TDIIIGTASH DADNHDTTSQ RASSSELDTP PSEGPANPKS
ATTTIKCEHG EQQHDETQVE GGGGDAIVAE TNGKPPTLRP APLPSRKRRE SEAALHTPDA
YEKGNDDAKA FKKRKRGASP PWQFPTVQTS TLRNADGRRV SARVRLGTPG LSESDDQRGR
STSVSTSQPL TATRSRPPSP PWKKVEAEGP TSIIVDGQRK SGRVNKELAH GPKRVSPRTK
KHVNKLAGEK HAETKQSPAA SKSMGGIKRK SDAEAKNQVN GVDRPSTSSD SAARIAELRA
QIAALQPTRS FDTPTTNADH TPKSVKSKSR RDLVKHEPSQ SPPLERNSHR PSEVQHSPDR
AKSSPRIKLK LSASRRVIEA PHPLGRPPSP LHPPRSLQQV IEEYELAELQ QPYTENDRGP
PDAEFFVQRA IKQAEEEGVI RKRLLKEAEP GGALSREKLS LFRDERQAEP PQQYDHHDHL
VAHTLFLRQL QIREKTQHRL LAKKLAHEAL EKWKARHGPT EEDIIAERIR IFDHVRKQVV
ADMKAKWEMV EAHVQELKKR AWEREQERIR SERLQKKLEG AKDLLAKQRG YADSEDIDMD
EDSTGDVHDS NDSEEEDSEE NMSDSDSESG EDEPEEEGEM DKDDLAAYLA QREAEPPDRE
SDADDDDEDD ENDDDHAGSG DESMAGVEEE PKDDALAQSS KADEGLQSEQ PHDVTETGKP
DEMDTDQPPA STRTRDRTSR SPPPDQTQAE VEAHLSSDES TDMDSEDYDS DEDMSSTGDE
ADNDDDDDGA SDASDEPADA RTSLLGFYSK TELMQDRNGG LPTPNTSVEN DGDDQPRPQS
EPRSEGQADA GAAEKVDSQE HSAAMEHIDV DRTIEVQPRA EEDEGTEQDN AEAESTADHE
EHSASKSMVP QPTLLRGTLR SYQQAGLDWL ASLYRNGTNG ILADEMGLGK TIQTISLLAH
LAEVHEVWET HLVIVPTSVI LNWVTEFQKF LPGFRVLGYY GTAEERAFKR KGWTNDAHHD
DKTKRGYNVV ITSYNVAMQD INAIRNVQWH YLILDEAHNI RNFNSQRWQV LIRLRTRARL
LLTGTPLQND LAEVWSLLTF LTAGNDDQSQ GELEEFLAHW KDPVKEIFDQ GVEKISENAQ
KVVEQLHISL RPFLLRRKKI EVEKDLPKKT ESVVVCKLSK RQRQLYQDYM GLAETKATLA
KGSGVQAGAV LLSLRRVCNH PDLFDPRPIQ TSFAMEYSPL ETYGIQEQLI RRMLGAKDQF
PDCLMIAARE SQNRSKLRRA KQLSGTDHLR RQLDKLVAVQ VDAKPDPATV AGSIALQRLH
RRERKLAQLR ACIQVTESGF DNQPLYGSDL KELVTIHKDQ PYQFDRRRVP AYKALHAWLP
TSRRPLLLEH PSNWHILKST RLQEDIATLD SYAERLQETI QRFAFVPPAV TVPILEFAIP
RPVQEAIRSS SLYPTDEDYA HEARVRTSIA FPDKRLLIYD SGKLQRLTYL LRELQSKGSR
SLIFTQMTGT LNVLEQFLSL MNLPYLRLDG STPVERRQLY SAEFNRPDSK YQCMILSSRA
GGVGLNLTGA SSVIFYDLDW NPQMDRQCMD RAHRIGQVRD VEVYKMVSEK TVEENILRRA
NQKSLLDQTV IQEGHFTTEY QHKEDKEDDV AQAIDRFLGG EEKTTQALAS VEDKEDTQAA
QQAAKEDRQD DVDFADRSSK GPSKANTPGP GATEVDEIDD ERKGHVDLYM IKHMQLLMKD
WVYVPAPVRK LDKHGRDPSH RPKKRR
//
