ID B6QNR3_TALMQ Unreviewed; 1749 AA.
AC B6QNR3;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 24-JAN-2024, entry version 83.
DE SubName: Full=PHD finger and BAH domain protein (Snt2), putative {ECO:0000313|EMBL:EEA21551.1};
GN ORFNames=PMAA_053550 {ECO:0000313|EMBL:EEA21551.1};
OS Talaromyces marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333)
OS (Penicillium marneffei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441960 {ECO:0000313|EMBL:EEA21551.1, ECO:0000313|Proteomes:UP000001294};
RN [1] {ECO:0000313|Proteomes:UP000001294}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18224 / CBS 334.59 / QM 7333
RC {ECO:0000313|Proteomes:UP000001294};
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(2015).
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DR EMBL; DS995903; EEA21551.1; -; Genomic_DNA.
DR RefSeq; XP_002150160.1; XM_002150124.1.
DR STRING; 441960.B6QNR3; -.
DR VEuPathDB; FungiDB:PMAA_053550; -.
DR HOGENOM; CLU_001514_0_0_1; -.
DR OrthoDB; 1409291at2759; -.
DR PhylomeDB; B6QNR3; -.
DR Proteomes; UP000001294; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0003682; F:chromatin binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd04710; BAH_fungalPHD; 1.
DR CDD; cd15571; ePHD; 1.
DR Gene3D; 2.30.30.490; -; 1.
DR Gene3D; 3.30.50.10; Erythroid Transcription Factor GATA-1, subunit A; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 3.
DR InterPro; IPR001025; BAH_dom.
DR InterPro; IPR043151; BAH_sf.
DR InterPro; IPR000949; ELM2_dom.
DR InterPro; IPR034732; EPHD.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017884; SANT_dom.
DR InterPro; IPR029617; Snt2.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013088; Znf_NHR/GATA.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR47672; E3 UBIQUITIN-PROTEIN LIGASE SNT2; 1.
DR PANTHER; PTHR47672:SF1; E3 UBIQUITIN-PROTEIN LIGASE SNT2; 1.
DR Pfam; PF01426; BAH; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF13832; zf-HC5HC2H_2; 1.
DR SMART; SM00439; BAH; 1.
DR SMART; SM00249; PHD; 3.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 2.
DR SUPFAM; SSF46689; Homeodomain-like; 1.
DR PROSITE; PS51038; BAH; 1.
DR PROSITE; PS51156; ELM2; 1.
DR PROSITE; PS51805; EPHD; 1.
DR PROSITE; PS51293; SANT; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000001294};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 286..404
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT DOMAIN 585..758
FT /note="ELM2"
FT /evidence="ECO:0000259|PROSITE:PS51156"
FT DOMAIN 769..814
FT /note="SANT"
FT /evidence="ECO:0000259|PROSITE:PS51293"
FT DOMAIN 1032..1082
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1141..1273
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 1..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 516..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 682..701
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 958..1025
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1106..1127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1344..1373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1451..1749
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..113
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..132
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..258
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 958..981
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1108..1127
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1344..1364
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1503..1517
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1567..1598
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1614..1629
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1712..1749
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1749 AA; 190821 MW; 5387279B9335CC50 CRC64;
MSEDSQSTES MPSSAEQSDS AGPGPANINN NNNNDSSSPA RSKSRNAAPA TKTATITDKP
EKPEDAKTAN AIANNTNANG AVAQSQPMTV SNSASSVMTS ITDAASNAAV PYSTRSRGRR
DGAPRPNYAE DVEMDFELTS PAPNAKSAAN STKRTTATSS VNGSPSAAAD SEKGPSASTR
KSQSTAANAT TNGTQANAAA KEPIPGTSTF SANATNSNTP SSASSASRKR KQPPSGATGA
NPNGSAKRTL TSTSGYKHDI RLSSMMTFEN SGARLRNGKL KADDGTTLEV NDHVYLICEP
PGEPYYLGRI MEFLPSKGNP TGPVEMVRVN WYYRPKDIQR RVPDPRLVFA SMHSDPCPLS
SLRGKCTIKH VSEIENLDEY RKLRDCFWYD KMFDRYMLRY YEVVPTKEVI NVPSHVKRVL
DERWRFVLCE PARKKELTGA VKTCVKCALY AASVDSVDCA VCHNTYHMNC VRPKLTKKPA
RGFAWACALC SRAQERKLEA RNTPLIGETL PDIEEDLPEE EEEEQNNNAA VGTERSSPVV
DDDKKPAPAT AAQIAQAKMW PYRYYGIHCQ LEDALDYDDR IYPRASSRIG TRHQAIVSPW
YGKPVEYIKP VDLKRKAKSS KSGSSKLSKA ALATIEAEKQ ERLKRPWVMD EPPGFVRRGE
DEPVMVNGKE VRTAELLFKL PEPNQIPSGR GEDDHPAPEM SEADCEKFID DYMAKAKDVA
TERGLPRYHT NFLDKALEYI YAEKFNVETA LKRLRKADLY KDLKEPKLSK EQKALFAEGV
SKYGSEWINI RRHIGNIEHR HVVRYYYMWK KTPEGRRVWN AYEGRHGKKE AKRADSTSKL
LDDIADEADD SAFDNEKASD KKRGFQCKFC LTRTSPQWRR APLTLPGATV PAEPSSKKAD
KGGQLAVALC HRCALLWRKY AIEYKDADEL AKKLQASGNK AWRRKLDDEL CAQALVQQET
PQITTTPSTG TSINAPSTTE TAPEPAKKKR PLEKDSASAS ARNSVEPPPK KKAVEKPVEP
PPIVPDPPRA KVLPCAVCRK PDPTGETSVT CRDCRLTVHQ GCYGVGPDSC HAKWLCDMCS
NDRNPMVSTL YECVMCPVTL TEQELMEAPK SSSHKKKTER DREKERMEKE MVVEAIKLYQ
QRQEAVGKPI HPREPLKRTV GNNWVHVNCA IWHPEIKFGK AEELEPAEGF GLIPRERYRE
TCKVCKTTAG ACLSCHYPNC NVKVHVGCAL QAGYTFGFDV TPVKGSRRDS TITMKMGGEN
GSVSPSIWCP NHAVQSIVHD MSEPTDQNNL TALELYVRTY KQADLSMTGT VRKAAHVQQQ
QQHAQSIFQS NGHGTRRASL INNAGSASAS ERRNSSSTIQ DPTEGPTHAE PPRLQSEHKI
CIYCRTSCSP RWWSVQHYPP TSSMVSNGMN HLMNGASPMH SRTISQASNS YGNGQSEQAY
ECHKCHIKKP AAPLQPSPET LPAGPFASQT PRGSLLPAPR QPEYTPYAPH GNPGSLQNVL
TSRPHGPPPP PGPVPSGPEW YSSYDKRLGT HGGPQTNGYG HGQPSPFPSG PLPHLNGYAS
GPAPAPTATS LPGPPPSSTP SHGHPPPSSG PGPSPHMPPV STHHHQTPGH YPGPMSSNLP
PPPPPPSHSY VGSGLGVPSM LSPRAPPARP FGTSMSPPDL HASLHRSPPT HGLPTARPRL
YSIDRFGPGP PLAKSHTDTQ LPGILDEHAS QPPSSGRYSG PGPSGASGTS GTNGSSGASA
SPSLKNLLS
//
