ID A0A1M2VHB2_TRAPU Unreviewed; 1445 AA.
AC A0A1M2VHB2;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=NFX1-type zinc finger-containing protein 1 {ECO:0000313|EMBL:OJT06979.1};
GN ORFNames=TRAPUB_2180 {ECO:0000313|EMBL:OJT06979.1};
OS Trametes pubescens (White-rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Polyporaceae; Trametes.
OX NCBI_TaxID=154538 {ECO:0000313|EMBL:OJT06979.1, ECO:0000313|Proteomes:UP000184267};
RN [1] {ECO:0000313|EMBL:OJT06979.1, ECO:0000313|Proteomes:UP000184267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FBCC735 {ECO:0000313|EMBL:OJT06979.1,
RC ECO:0000313|Proteomes:UP000184267};
RA Makela M.R., Granchi Z., Peng M., De Vries R.P., Grigoriev I., Riley R.,
RA Hilden K.;
RT "Genome sequence of the basidiomycete white-rot fungus Trametes
RT pubescens.";
RL Submitted (OCT-2016) 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:OJT06979.1}.
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DR EMBL; MNAD01001233; OJT06979.1; -; Genomic_DNA.
DR STRING; 154538.A0A1M2VHB2; -.
DR OMA; INKVFHS; -.
DR OrthoDB; 2971338at2759; -.
DR Proteomes; UP000184267; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004386; F:helicase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043170; P:macromolecule metabolic process; IEA:UniProt.
DR CDD; cd18808; SF1_C_Upf1; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR Gene3D; 4.10.1000.10; Zinc finger, CCCH-type; 1.
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 InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR PANTHER; PTHR10887; DNA2/NAM7 HELICASE FAMILY; 1.
DR PANTHER; PTHR10887:SF341; NFX1-TYPE ZINC FINGER-CONTAINING PROTEIN 1; 1.
DR Pfam; PF13086; AAA_11; 2.
DR Pfam; PF13087; AAA_12; 1.
DR Pfam; PF00642; zf-CCCH; 1.
DR SMART; SM00356; ZnF_C3H1; 2.
DR SUPFAM; SSF90229; CCCH zinc finger; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50103; ZF_C3H1; 2.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00723}; Reference proteome {ECO:0000313|Proteomes:UP000184267};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00723};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00723}.
FT DOMAIN 5..33
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 56..84
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT ZN_FING 5..33
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT ZN_FING 56..84
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 31..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 987..1019
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1044..1067
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..53
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1004..1018
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1050..1067
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1445 AA; 161092 MW; 9C58F10D55D82B4A CRC64;
MASGRNHRPP CRFYSKPGGC KNGSSCTFAH IDGANPSPPG QPGPRQPFVP RPPVPNAPPG
VCKFYYDRGF CSRGSDCRFR HEVNAAQRRP SAEGSVSENV AAFLTPAALA RIQGPGTDGF
FDTTAAVMKP SEVRHHLNRF LENGYRFKYA ADVYSFVTLL SNASSGNTSW SAEDGQLFLS
AIGTDNGLLR IGDILSWSEV SVRPTSRTAI SFQRGYVPLL RYLSSEYVVK SITSKVVNSL
YSLVLEHFNH FCEVVQSCME EALNDRKTFK EQSMSLLASS HTELTGSQVL SCIAQVLFEY
ITRFKNAVVT HPSLRPLVQK LRTWTDAWIA AISATPPTFD DPITKAPAQA TRFLVDRLRE
LVERLISIVD RKQRDIERAN QPNHGLLPLH GLTHANEGIL AALHNAYQGP GNLRAEGPRH
DNDFVNISDI QIAPTHGELT SPLQPFLPAN MYGAPHPLPA ESMEQLLDIQ FRLLREELTA
SLRVSAQAIL GDLGEKKKHT QLNALLEKGG GKYRGHAVGQ DTVLFNVYTG AEFTTITPAQ
RGLTVGVAID TPPGRARSGQ ASIRAQFWES MSSKRLMQGG LVALVWQRLD GTTEVHLGTL
ASSVKDLTDS AKQRQDNIKI RVSFFSPEVE LRILQELRTP RHERQGTKLL IEATVMFESV
RPFLEALRVD PENIPFARYL AHHPPEFYRT MQITPPTYAI LPNFAFQLAS LFPSEAGVED
LKLVVNDPES IEGARELLKH SSRLDPSQAD AIVDALTREV SLMQGPPGTG KSYTGVEMLR
VLIENHAGPV LMIAFTNHAL DHMLRSVLEA NITQKIVRLG SRSADERIAE FSLENMENVA
GRSRLSSVFS NYRWALRDVE KEIKDFMESF FREEVDTDDL LRYLTFQAPV LEESITFPPE
WVKALYDLQR TEQDERWHTA GRNKPGRLDP DDDSLYAFWV RGGDVEFLHS THRALHYRPP
PPPQPVLPQQ QARPVNAFEL LAVETADGPA VAPDTGDTGK DAAGPEADDD DSDDGSEVEL
RPEEAWILAD FVDDSEDSDL LVTDSEDEVP EPPAPGPVPP PVAATPPMAP QELASVAAGH
RTPAPIQPDD FTNIREFFVA FGCTDIPAVP ATTRSVAELL EQDDAWSMSV RERELLHRAW
ADEVRITSRE TQMMEFRRLR EKHAQASREY AEGQAEIRKQ LLRNVDIIGC TTTGAAKLTA
LLKGIGPKVV LVEEAGQVLE AHVLGSLVPS IQHLILIGDP LQLRPTLNNY SLSMDHSHGR
LVYKFDMSLM ERLSSSGMPM SQINVQRRMR PEIADLVRMT LYPRLEDHDL VKNYPHVQGM
AKDVFFFNHD HKENGGEDDF VSKYNQFEVD MIKDLVLYLL RQGPYSAEGD IVVLCAYLGQ
LARLREALSS EVAVVIDERD QAELDDRNAE NEESMQNVTA FERVRVSRRV LLRTIDNFQG
EEAKV
//
