ID M3JZJ3_CANMX Unreviewed; 1684 AA.
AC M3JZJ3;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Protein ECM5 {ECO:0008006|Google:ProtNLM};
GN ORFNames=G210_1683 {ECO:0000313|EMBL:EMG47864.1};
OS Candida maltosa (strain Xu316) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=1245528 {ECO:0000313|EMBL:EMG47864.1, ECO:0000313|Proteomes:UP000011777};
RN [1] {ECO:0000313|EMBL:EMG47864.1, ECO:0000313|Proteomes:UP000011777}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Xu316 {ECO:0000313|Proteomes:UP000011777};
RA Yu J., Wang Q., Geng X., Bao W., He P., Cai J.;
RT "Genome sequence of Candida maltosa Xu316, a potential industrial strain
RT for xylitol and ethanol production.";
RL Submitted (FEB-2013) 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:EMG47864.1}.
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DR EMBL; AOGT01001350; EMG47864.1; -; Genomic_DNA.
DR STRING; 1245528.M3JZJ3; -.
DR eggNOG; KOG1246; Eukaryota.
DR HOGENOM; CLU_240564_0_0_1; -.
DR OMA; GFDQVCK; -.
DR OrthoDB; 2734339at2759; -.
DR Proteomes; UP000011777; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd16100; ARID; 1.
DR CDD; cd15518; PHD_Ecm5p_Lid2p_like; 1.
DR Gene3D; 1.10.150.60; ARID DNA-binding domain; 1.
DR Gene3D; 2.60.120.650; Cupin; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001606; ARID_dom.
DR InterPro; IPR036431; ARID_dom_sf.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR003349; JmjN.
DR InterPro; IPR013637; Lys_sp_deMease-like_dom.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR10694:SF146; LID2 COMPLEX SUBUNIT JMJ3; 1.
DR PANTHER; PTHR10694; LYSINE-SPECIFIC DEMETHYLASE; 1.
DR Pfam; PF01388; ARID; 1.
DR Pfam; PF02373; JmjC; 2.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF08429; PLU-1; 1.
DR SMART; SM01014; ARID; 1.
DR SMART; SM00501; BRIGHT; 1.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF46774; ARID-like; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR PROSITE; PS51011; ARID; 1.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS51183; JMJN; 1.
DR PROSITE; PS01359; ZF_PHD_1; 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:UP000011777};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 108..149
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 202..305
FT /note="ARID"
FT /evidence="ECO:0000259|PROSITE:PS51011"
FT DOMAIN 596..824
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 1384..1431
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 537..573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1557..1684
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1594..1668
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1669..1684
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1684 AA; 193763 MW; DEDFA84F3F2757B9 CRC64;
MSLYSGDFSR NTLQNIFNQQ NPHPTTPRSK FPKTSRFFDT SSLPDLKTLE LTRQNKRVLF
NGQSTNFNYS PFSLPQQKLK ASVPLDYGHL PTKITIAPSI AESSIEQIPC YVLDSNQIKD
PISFIDGLSE VGKKYGAVKV KLPSYDTELF QSTIQINSDL FWFPTNKLLN NPPEDEIYMR
LKFHHDLLQF HQSEDYLKYE DLDGKKSNVS AVASSASSSS SSTAVAAAII AQVNKLPMID
KRPLDLYRLF HSVLIRGGFM EVINKKLWAQ IGRELGYKGK IMTSLSSSLK SSYQKILYPY
ELYLAAQASK SNGVQEEIHA NGKRSLHEDD SSVNKKVKLE DIGAPLIIGS AKDFKRSIKV
KQSKGYLLNT PYAIDVKQPN IFTMKHDDKK RRRQNDKIDL SILPQTELEA ALQYMDNTQD
ESRLKASPKL ASIYTLRQFM EKDIKFQEFL LSANPSFFDS NVAESNVITI DKLEQLYWKY
ISNTNTEASL KCGLELEMGK DIPNFVNGSG FVKMGDDLIN YKNCLNSEHL NLSHSKPVSN
TAQMSASTQS TSTIPPSSSS STGNYNQKSN YFLPHSHNQN ESKKFNSDQF IQMLLQSALH
PWNLHNLPSL PNSLFGAFTE NDINDKDLNE SRLNIGMTFA TENWTCEDHF TNMINYLFFG
SIKKWYFIPE SEFEKFEELV KKVNESDQFR SNMNSRKPVD IEKIMEYLRK SVDEVEYEIV
VKTLDSLINI DGDTKLPLSN EKFEQLVNRN DTFKYNQEFM ITPELLEQHG IKYTTVIQEP
GEFIIKFPKT YSACISFGFN MSEEVNLATN KWLDYSLEGE AWLAKQNIIP CFSTFKLLVN
LALMYDSGTN LLFNSDILSK AGVMYENLYR KEIELRNEVR KFKVKEYIID SDDTDTISDD
NMSNVFPSRI LLVDTKTKES MILSIEKFLQ CQKEDDKLMK QFSVEFQLYY SDEKLKNFSK
ILNSYSVDFE TWMQSYEELM KENSDVSLKT YKSLLSDAER ICSSVESSSA VKHQDIDYAK
FSSFKATLDN LRFFIDNSNQ VVEECQNLLA IKHQQRIRNG NESSREKVYS YNDLLELVAK
IPRLNFTCPE MDQIVEFKNE IENFDKASRS LLLKKNKSLM EFNDLISLGQ SFGLEIPSLT
FITRIRDRMK WLRTYSLIEK GVDPFGDKKE VFTIDDLREF FNEGLQVLSK NDIDTIKEVE
AILNRSISFD GEASKFLKFD YVHDLDLVKL DEIAKKFSTE KLFISMKNYL DLSKLHVNLK
LIRQYKELDN APYPEVKQLY SAIMESGLKF DTTEIVQKLS TTEAWIERIW SRISETKVIT
TLNKDVDLDH LNPKLTMHTK LIEKLLQLLY KSEFSLSDDD KYEESSSFLT AAADSNEDSD
STSKFYCICR EYEYGTMVEC DKCKEWYHVQ CVKSVSNPDD DKYRCPICMI SSSESDTKDS
LLSDQLTFDD LKEIYNEGKS LSVYPVNELT VMKDLIDELT KYHEKYQELI MKVTNESNVE
EKVSIFKFIL RKLYGSGVLL EDLWMHVLNL IREFQEILNN SEVLNNEISS EPTQVQVKQE
PQEPETVVVE DVAEPPTKIK VEPETLDTST PINGGKEESE EPDVKKEVIE NEEVVDDQKV
ADIEETANNE EVAKNEEVAK NEDVAEKVEE TPVKSETHTQ EDSDKQETLD NSTSTSIVKQ
EQVE
//
