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Database: UniProt
Entry: N1QJ36_SPHMS
LinkDB: N1QJ36_SPHMS
Original site: N1QJ36_SPHMS 
ID   N1QJ36_SPHMS            Unreviewed;       530 AA.
AC   N1QJ36;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=C2H2-type domain-containing protein {ECO:0000259|PROSITE:PS00028};
GN   ORFNames=SEPMUDRAFT_145588 {ECO:0000313|EMBL:EMF16302.1};
OS   Sphaerulina musiva (strain SO2202) (Poplar stem canker fungus) (Septoria
OS   musiva).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Sphaerulina.
OX   NCBI_TaxID=692275 {ECO:0000313|EMBL:EMF16302.1, ECO:0000313|Proteomes:UP000016931};
RN   [1] {ECO:0000313|EMBL:EMF16302.1, ECO:0000313|Proteomes:UP000016931}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SO2202 {ECO:0000313|EMBL:EMF16302.1,
RC   ECO:0000313|Proteomes:UP000016931};
RX   PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA   Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA   Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA   LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA   Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA   Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA   Grigoriev I.V.;
RT   "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT   genomes of eighteen Dothideomycetes fungi.";
RL   PLoS Pathog. 8:E1003037-E1003037(2012).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the REI1 family.
CC       {ECO:0000256|ARBA:ARBA00034126}.
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DR   EMBL; KB456260; EMF16302.1; -; Genomic_DNA.
DR   RefSeq; XP_016764423.1; XM_016903146.1.
DR   AlphaFoldDB; N1QJ36; -.
DR   STRING; 692275.N1QJ36; -.
DR   GeneID; 27900283; -.
DR   eggNOG; KOG2785; Eukaryota.
DR   HOGENOM; CLU_018787_1_2_1; -.
DR   OMA; NATHMER; -.
DR   OrthoDB; 180831at2759; -.
DR   Proteomes; UP000016931; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW.
DR   InterPro; IPR003604; Matrin/U1-like-C_Znf_C2H2.
DR   InterPro; IPR041661; ZN622/Rei1/Reh1_Znf-C2H2.
DR   InterPro; IPR040025; Znf622/Rei1/Reh1.
DR   InterPro; IPR022755; Znf_C2H2_jaz.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR13182; ZINC FINGER PROTEIN 622; 1.
DR   PANTHER; PTHR13182:SF8; ZINC FINGER PROTEIN 622; 1.
DR   Pfam; PF12756; zf-C2H2_2; 1.
DR   Pfam; PF12171; zf-C2H2_jaz; 1.
DR   SMART; SM00355; ZnF_C2H2; 4.
DR   SMART; SM00451; ZnF_U1; 2.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 3.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016931};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Ribosome biogenesis {ECO:0000256|ARBA:ARBA00022517};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          15..37
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS00028"
FT   DOMAIN          80..102
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS00028"
FT   DOMAIN          249..271
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS00028"
FT   REGION          165..188
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          323..396
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          429..530
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        166..180
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        357..373
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        380..396
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        430..449
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        486..505
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        516..530
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   530 AA;  59149 MW;  914EB5A780C2F974 CRC64;
     MASVTSTQTA HPFTCNTCQV AFRSSDLQRT HMQSDWHRYN LKRRVASLPP LTSEIFAEKV
     LANKATAAAT AARASFEKRC EPCDKTYFSE GAFVNHLGSQ KHRIHVARYT ARGGGVDGAD
     TDSMADSTFT LGDSIETVST TASTAHGEEE TEDALDQVVG GMSRTNLAEG PQQHTSSQPA
     GADGEDDDYE HQADLKQCLF CNYISPTMDL NINHMSRQHG FFVPEKDYLV DLPGLINYLS
     ETVSVLHQCL LCHKQLHTTS GIQTHMRDRG HCMIAYGTED EQMDVGEFYD FRATYSDEDS
     GTEDEGTGGG VKLGVKRTAK TTIENANGED VEMDDEEGWE SDGSLSSVPT DEITSVPVDQ
     PDKKYERLGA HRHHSHTDPR RHKNSDGFHS HSHGGSHAVY HDDYELHLPS GRTAGHRSLR
     AYYRQNLRNY PSAEEREQQR MIADGRHDSD ADDEDADTET NGRDDRRGRQ VATRANGGTG
     MIGVSEAKKR EVRAVEKRDA KRAQRAQARY QWGNDRRGNM QKHFRDPLLQ
//
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