ID C1GKW1_PARBD Unreviewed; 2237 AA.
AC C1GKW1;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 2.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=CCHC-type domain-containing protein {ECO:0000259|PROSITE:PS50158};
GN ORFNames=PADG_07968 {ECO:0000313|EMBL:EEH43148.2};
OS Paracoccidioides brasiliensis (strain Pb18).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX NCBI_TaxID=502780 {ECO:0000313|EMBL:EEH43148.2, ECO:0000313|Proteomes:UP000001628};
RN [1] {ECO:0000313|EMBL:EEH43148.2, ECO:0000313|Proteomes:UP000001628}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pb18 {ECO:0000313|EMBL:EEH43148.2,
RC ECO:0000313|Proteomes:UP000001628};
RX PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT "Comparative genomic analysis of human fungal pathogens causing
RT paracoccidioidomycosis.";
RL PLoS Genet. 7:E1002345-E1002345(2011).
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DR EMBL; KN275969; EEH43148.2; -; Genomic_DNA.
DR RefSeq; XP_010763257.1; XM_010764955.1.
DR STRING; 502780.C1GKW1; -.
DR GeneID; 22586352; -.
DR KEGG; pbn:PADG_07968; -.
DR VEuPathDB; FungiDB:PADG_07968; -.
DR eggNOG; KOG1801; Eukaryota.
DR HOGENOM; CLU_000459_2_0_1; -.
DR InParanoid; C1GKW1; -.
DR OMA; PWHQSEL; -.
DR OrthoDB; 170190at2759; -.
DR Proteomes; UP000001628; Unassembled WGS sequence.
DR GO; GO:0004386; F:helicase activity; IEA:InterPro.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd18042; DEXXQc_SETX; 1.
DR CDD; cd18808; SF1_C_Upf1; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 4.10.60.10; Zinc finger, CCHC-type; 1.
DR InterPro; IPR045055; DNA2/NAM7-like.
DR InterPro; IPR041679; DNA2/NAM7-like_C.
DR InterPro; IPR041677; DNA2/NAM7_AAA_11.
DR InterPro; IPR024481; Helicase_Sen1_N.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR047187; SF1_C_Upf1.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR PANTHER; PTHR10887; DNA2/NAM7 HELICASE FAMILY; 1.
DR PANTHER; PTHR10887:SF525; HELICASE SENATAXIN-RELATED; 1.
DR Pfam; PF13086; AAA_11; 1.
DR Pfam; PF13087; AAA_12; 1.
DR Pfam; PF12726; SEN1_N; 1.
DR SMART; SM00343; ZnF_C2HC; 3.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF57756; Retrovirus zinc finger-like domains; 1.
DR PROSITE; PS50158; ZF_CCHC; 2.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Reference proteome {ECO:0000313|Proteomes:UP000001628};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00047}.
FT DOMAIN 1982..1997
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT DOMAIN 1999..2015
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT REGION 942..1077
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1883..1943
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2052..2106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2119..2237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 942..973
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 992..1016
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1020..1036
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1043..1069
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1885..1931
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2083..2103
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2157..2175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2237 AA; 249761 MW; 8C4626FBF6F850C8 CRC64;
MAEWVSIVEE LKTLADQLHM FCPRQNDNDM GQYNDDYIQS LNLTGLDVKP NVENLDRISE
ATVRRQKFLS SMRLLAYNSD EIQIHQQWIW SRLEHDLGKC ELCVKEYYRG KGWLMENLRE
SYDESEVENF SKIIDERDIK RVVKNLDRAT EALKAVPPQQ RSLSVLDRAA MLSIFEAMSS
KAMVNDDELL RAHFDEPFNL IQTNRTLKMT EYIPATTHFL FSDNQERRRW AIMSWGKMKR
PPTTLEFDWA IKEPLVEAIR RASYVPLQPD LVQRLWTGVH AIIDRLGKEQ ITHNLRALET
DPCRLSVDHL AIPTPGLRPL LNTLQIFLEK SPGDFWDAMQ AISPQAIVEQ IFSNPQYDAF
LLETPEDSSL EKPSPLRDML SWVEPFMASL QGAQQPQACR VLAFHLLNRL QASRFPPVSR
FNCFRVGLNI LISTLRTFTD NESTRGSVAR VVLSDILEVI SDNIDHFLEP TEFPIDGSQE
LLAGLCVAVI RNALALECQS LKSDYESILR QKTMAHEVST YSAKIWDAVV RHLNEDNLGL
SSAALMGILP LVGLEKFPTK GENSREKTNF NVIYGHLTHL VSQILERLAD FKPEHLDHLF
KSHDTNGSLI SALFSADLNT YQAAVDLIKT ISGQSGRKEA ISHLLQSFFA TTMYGFSFSF
RRISNMRTFA SAPRMLKTGT DIIDVLCDSE TGILRTRKLV DRVEVLALQK LWEYQWQALT
TIFQQTEAWH MMGNDRMVML EFCRDTIQFA DLVFNQFNIF ASSIAEFNPS ETKSSSENLV
KAPASTMESM VKWLRLKDDF LATTIVGLVA KLLRRMGELE VKLATVSLKY IEDVARFSVI
KTILTAQEKA ELVRALESYY KKSFPSEQLA PTPAPKKQKQ IMITAYAKPV DTISISSSSS
KVSASEGDEF GYLSDDVLVE LSSSVELNKA RIAAQKKSQK LAALSEKSTL KPSLPSDKST
HSSEKSTLSL QRPTLPFPKR APQPLKPAVS VSSFREKRER EKEEKKKRDM AELARVKKKL
SVQTANQGSG VSGIGANSSG DRPVESMMVS DSDSSADSEG GNDSGAYGQQ IKSKPAAVRE
YEESKRHLLN RRGPIRKIKV ARSAKDMRAR LSPDLSGLHK TLLGWDFFAD GDIPPASGRT
DYTLVSNTFS DATDYRKTFQ PLLILEVWQS FQSAKEEGSF RPFEIKVSSR ITVDSFVEVT
TFMRPAEVKD LGLGEADLVL ISKSSDPSSD SKEPHCLARI ISSTKKKGMI EVGYRLNVST
PLNSFIAPGN SLFAVRVMSL TPVEREYGSL LALKYYDLSE EILSARPSPI LKYTPESLQP
IIDTYKVNPA QAKAVRSALD NDAFTLIQGP PGSGKTKTII ALVGALLSPI LREQSISCSS
SSSSTRPALS SSTQSAAKNA PTFKSKKLLV CAPSNAAVDE LVMRFKQGVI STDGHKREIS
VVRLGRSDAI NSNVIDVTLD ELVNEKLSGT ARKSGNEKDL QTFYLEHKDA CTQFNGVRER
IDQCRAKSER VPEELEREFD LLKRKKAQLS QAIDDARDSN LVAARNADLL RRKIQQNILE
DAHVLCATLS GSGHEMFQSL DIEFETVIID EAAQSIELSA LIPLKYGCSK CILVGDPKQL
PPTVLSKVAS RFQYEQSLFV RMQANHPQDV HLLDTQYRMH PEISRFPSAA FYDGRLQDGP
DMDKLRSRIW HKSELLGPYR FFDVQGLHSS APKGHSLVNL AEVRVAMKLY ERLTTDFKIY
DFTNKIGIIT PYKGQLREMK NQFANKYGSS IFTMIEFNTT DAFQGRECEI IIFSCVRASD
RGIGFLADIR RMNVGLTRAK SSLWVLGSSK SLVQGEFWRG LINDAHTRKL VTQGDILGIL
QKPQIIPDIE LNDVEMIDAP RSAICSPSSR PQSTTPNDNG SSRPSSSLST GRLSSIAEAH
NTSSRDTPGH SPKLSPSAVP DGPSGGKFGL NELAMCGYCG SYEHMTPNCD NLAAKMAAQG
SCRRCGDASH SKRDCKEERC LQCGKFGHLA PACKSSVILP KRQKDKIAHS ERIHAEVQKA
NLERQRLRQL GDHVPKVPPI QVPSNISPNR SPPIFRATPP RRDLPNPEQD DSGKRKRMEP
DPPVPLKNVK VRKQNAQFNA QFAPPPTAPI GPRGKKFDPN VIAPPSSDLV IPSKPGNGYQ
PISTKEQQQY RSPSFGPGLT AGPGPILDQH PANTGLPPAA SPHLNTSSPR RNIKVRGPPP
PIRKKKPTSI FIQPKRR
//
