ID A0AAE0WFK3_9PEZI Unreviewed; 1841 AA.
AC A0AAE0WFK3;
DT 29-MAY-2024, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2024, sequence version 1.
DT 08-OCT-2025, entry version 7.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KAK3671242.1};
GN ORFNames=LTR78_008877 {ECO:0000313|EMBL:KAK3671242.1};
OS Recurvomyces mirabilis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Recurvomyces.
OX NCBI_TaxID=574656 {ECO:0000313|EMBL:KAK3671242.1, ECO:0000313|Proteomes:UP001274830};
RN [1] {ECO:0000313|EMBL:KAK3671242.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCFEE 5485 {ECO:0000313|EMBL:KAK3671242.1};
RA Coleine C., Stajich J.E., Selbmann L.;
RT "Black Yeasts Isolated from many extreme environments.";
RL Submitted (JUL-2023) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00089}.
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:KAK3671242.1}.
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DR EMBL; JAUTXT010000045; KAK3671242.1; -; Genomic_DNA.
DR Proteomes; UP001274830; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:TreeGrafter.
DR GO; GO:0042393; F:histone binding; IEA:InterPro.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IEA:TreeGrafter.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR CDD; cd00167; SANT; 4.
DR CDD; cd00202; ZnF_GATA; 1.
DR Gene3D; 3.30.50.10; Erythroid Transcription Factor GATA-1, subunit A; 1.
DR Gene3D; 1.10.20.10; Histone, subunit A; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 2.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR001766; Fork_head_dom.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR009057; Homeodomain-like_sf.
DR InterPro; IPR017930; Myb_dom.
DR InterPro; IPR050560; MYB_TF.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR018465; Scm3/HJURP.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR InterPro; IPR000679; Znf_GATA.
DR InterPro; IPR013088; Znf_NHR/GATA.
DR PANTHER; PTHR45614:SF25; MYB PROTEIN; 1.
DR PANTHER; PTHR45614; MYB PROTEIN-RELATED; 1.
DR Pfam; PF00250; Forkhead; 1.
DR Pfam; PF00320; GATA; 1.
DR Pfam; PF00249; Myb_DNA-binding; 1.
DR Pfam; PF10384; Scm3; 1.
DR PRINTS; PR00053; FORKHEAD.
DR SMART; SM00339; FH; 1.
DR SMART; SM00717; SANT; 5.
DR SMART; SM00401; ZnF_GATA; 1.
DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR SUPFAM; SSF46689; Homeodomain-like; 2.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS50039; FORK_HEAD_3; 1.
DR PROSITE; PS50114; GATA_ZN_FINGER_2; 1.
DR PROSITE; PS51294; HTH_MYB; 1.
DR PROSITE; PS50090; MYB_LIKE; 2.
PE 4: Predicted;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PROSITE-
KW ProRule:PRU00089}; Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00094};
KW Nucleus {ECO:0000256|PROSITE-ProRule:PRU00089};
KW Reference proteome {ECO:0000313|Proteomes:UP001274830};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00094};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00094}.
FT DOMAIN 384..439
FT /note="GATA-type"
FT /evidence="ECO:0000259|PROSITE:PS50114"
FT DOMAIN 541..583
FT /note="Myb-like"
FT /evidence="ECO:0000259|PROSITE:PS50090"
FT DOMAIN 601..651
FT /note="Myb-like"
FT /evidence="ECO:0000259|PROSITE:PS50090"
FT DOMAIN 861..889
FT /note="HTH myb-type"
FT /evidence="ECO:0000259|PROSITE:PS51294"
FT DOMAIN 1293..1363
FT /note="Fork-head"
FT /evidence="ECO:0000259|PROSITE:PS50039"
FT DNA_BIND 1293..1363
FT /note="Fork-head"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00089"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 97..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 202..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 321..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 779..836
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1112..1143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1151..1170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1407..1428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1485..1530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1563..1653
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1684..1841
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..11
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..44
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..56
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..146
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..168
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..223
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 340..353
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 790..814
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 815..836
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1131..1140
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1151..1164
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1516..1525
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1597..1610
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1612..1625
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1635..1652
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1684..1710
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1810..1821
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1841 AA; 202109 MW; B189F2A4DE04A27F CRC64;
MASPSQYSSD TCDAEMEEEV YATPPEGWAE DDGDPDESGP ENDSPELRRD RNANDQRLRG
RFEHIFAKYS RDFTDVGDQI DIETGEIVID NGHLRNMLHE ADPGQGSRSL QLLEHEDDSA
SDDGDVSDDG DDDELESDSS DSDVDELANG YDQDIAQDTE SGPEDESDHD SSVLEASVNV
DLSNVDPELR KLIHATSNTA LPKPLATPAE QDWHVRDSQD PDRTLSSNVI SLPALQESLQ
ELSHATGLGR DIDSNAIEKL GKDIADQLAR YVGQKNKNRT KRKSKVSRGD SSWDYPELPA
FKRRRLADPQ PRPQLVQLSD ILSPPKGRRG PRESIWAPVH HPKQPGVRTR RKDKAVIGNR
TALYTDTAVS GEGLSGAENT PDQTAAIREC AHCLIKVTTA WRLGPDRENL CNACGMYWYR
YDLMRPLLPP TPDPLSEDEA VEDDVVRGDP YPANTSRTVS YPGFRSGAFT TEEDALIIKL
KEIDCLPWER IGRFFPGRSH YGVQCRYSKR LNNQSSEGRS ALVEQGFTFE EPPEADISDI
FTEEQGDLLV QLREDHEFTW GRIAEHFPGK TDESVEFHYN TLIGIVALPA KPRKRRAALK
APGNHQRPYT KEEDELIIKL REIDKLPWEL LAQEFPQRTW LALQKRYVRT LAHRHQAMRD
GEDDPYTYLF LECHPEDEVR LGPAGRNSMG GLLRQRREED LALMRMKDEE GLTFEEIAEA
LPGRTVESLN NRYEHLTEVK NMMNVPVPTS TQDEDHEINI HEALEDDDQA AEDNVCIIDP
ALTGGTGSER TSRTAEQDPD AHGEVSKINS DTEHPTITGS PSGMTTAVTP PSSHQARSMA
IRKYTKSEHA RIAELRNVNL DWKTIAAELP DRTPASIASY WAQYCKHKAT WSSPLSGKKK
RGSKQSRALL RQAMDNGMRR IPNGGKRAIE LPSVVVDGHP GPMNLFTSLL RNAHEKEDGH
NEVDEEVDLD FANVSTDQVR SSPKEPAQDK EISDEEVDFD FAKLGQGPLD RISASTTPVK
DSMMSANAFQ AQMASSPDMI RNSGLVDYGV GTSTLLSSPV KPLSHASDVR PSISRALHSN
IEPAAALLPI IHGLPTHTPV HGELSRRPTL SEIPELLNPP PSAVEAQQTT EEWRPRDPTR
YVKQPGRTFH LSATTPARAS TSRPPATPVE AATPFKTPLP ASSPFMAAPA PAMYSTPARY
SQQKMPYFNM PRSTLMAASP AQVEELLDMP DDMVEDDMTV VSSEDDSKPV IRTVAPTSFA
YPNLTARSLS PPGATIKDRL VSIPSTAGRS AEAPPFSWTD LITMALKSSQ SQHLEVREMQ
AYLKDKFPYF KSRGEGWKRT LRAHLATSSE FQKMPGRRDI WTFRTKEAVM TLKDRTSNSN
EPQTTVNVEL TAPEGGMASE PALLAGTAHD AAEQPGTDRS TSSSAAIDPR LMAADDDTTA
TASNTPDIAT PALEHESARM PNSQLAAVTD TWIPDLLMAQ REISLRRKPG RPPKNGIISQ
ADQRALGPRR PPGRPPGARN KPKGPQGITE YALPSSFLEN NQEIAAPQYE VPSTSGDILQ
RQLMGPKITR PKSRKDPKTV GDTAPPIEAH ASIISDVNRE PESSPARDHG IAQVAEAERA
VAQQQDSSAV HEKAPNQTSV NNSATRSSSP SFMQRIERTP VLGYSRAGTP AQADSAIVEN
AKQKTLATTQ STTPAKINTR AATSAKSVPT ASEKAEQRPL AGKKSARTPP AKPASSVVEK
LKQRDLVVAR PVTPAISLST ASEKPKPRPS AGRRSGTPAK AASSVVEKLK QRSLVGERSA
TPALAGGRGL RSESVKVKAD SSARQSMQKV GGLDGSEDEL A
//
