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Database: UniProt
Entry: C6HCX7_AJECH
LinkDB: C6HCX7_AJECH
Original site: C6HCX7_AJECH 
ID   C6HCX7_AJECH            Unreviewed;       506 AA.
AC   C6HCX7;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=SP-RING-type domain-containing protein {ECO:0000259|PROSITE:PS51044};
GN   ORFNames=HCDG_04058 {ECO:0000313|EMBL:EER41411.1};
OS   Ajellomyces capsulatus (strain H143) (Darling's disease fungus)
OS   (Histoplasma capsulatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX   NCBI_TaxID=544712 {ECO:0000313|EMBL:EER41411.1, ECO:0000313|Proteomes:UP000002624};
RN   [1] {ECO:0000313|Proteomes:UP000002624}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H143 {ECO:0000313|Proteomes:UP000002624};
RA   Champion M., Cuomo C.A., Ma L.-J., Henn M.R., Sil A., Goldman B.,
RA   Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A.M.,
RA   Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA   Griggs A., Gujja S., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA   Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S.,
RA   Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J.,
RA   Yandava C., Klein B., McEwen J.G., Puccia R., Goldman G.H., Felipe M.S.,
RA   Nino-Vega G., San-Blas G., Taylor J.W., Mendoza L., Galagan J.E.,
RA   Nusbaum C., Birren B.W.;
RT   "The genome sequence of Ajellomyces capsulatus strain H143.";
RL   Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Protein modification; protein sumoylation.
CC       {ECO:0000256|ARBA:ARBA00004718}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the NSE2 family.
CC       {ECO:0000256|ARBA:ARBA00008212}.
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DR   EMBL; GG692423; EER41411.1; -; Genomic_DNA.
DR   AlphaFoldDB; C6HCX7; -.
DR   STRING; 544712.C6HCX7; -.
DR   VEuPathDB; FungiDB:HCDG_04058; -.
DR   eggNOG; KOG2979; Eukaryota.
DR   HOGENOM; CLU_028753_1_0_1; -.
DR   OMA; TWFSHLE; -.
DR   UniPathway; UPA00886; -.
DR   Proteomes; UP000002624; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0030915; C:Smc5-Smc6 complex; IEA:InterPro.
DR   GO; GO:0019789; F:SUMO transferase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:InterPro.
DR   GO; GO:0016925; P:protein sumoylation; IEA:UniProtKB-UniPathway.
DR   CDD; cd16651; SPL-RING_NSE2; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR026846; Nse2(Mms21).
DR   InterPro; IPR004181; Znf_MIZ.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR21330:SF1; E3 SUMO-PROTEIN LIGASE NSE2; 1.
DR   PANTHER; PTHR21330; UNCHARACTERIZED; 1.
DR   Pfam; PF11789; zf-Nse; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS51044; ZF_SP_RING; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002624};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00452}.
FT   DOMAIN          329..429
FT                   /note="SP-RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51044"
FT   REGION          1..62
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          115..143
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          194..224
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          429..506
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        115..129
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        470..489
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   506 AA;  55569 MW;  8F79D8BCEB9C5D39 CRC64;
     MSANSTPRSR AALPSRNTPN QQPRSSRSAR LSDAHGGSSR RQDQSTRGTL LQPPPYQPQV
     APFNASALHK LSQLSRFPRL AALQSRLTSA AQALTECAGM INDRLVDAKA RQAKRAGMKR
     KAADAENEEV AERGDGEGDE ASNKLVDLEK RVKTVTDQLE EKMRKIVDAE VRTVSLTDGL
     IQIHRDAAMV VPAAPHAKRR KMRRRPGEEN EEDEDEGEGE GEEKLVVEEP LYIRNGGTCK
     VLRKELKEKK AQWKGTSLTD RYTTNDKYIG FYRIVHESKY PGDEIPPLPH PSTWFADVEQ
     PTTASLSEVT TTNATGGTNG GNAGSTVDDS DDLAIHSERA SLCCPITLLP FTEPVKSKKC
     PHSFERRAIV AMIERSKKRI VIPANGTNGA GPAGKRVGCV DCPVCSVPIS MHDLEVDVVA
     VRRLRRAEER RRMEEEEEGG EDREGEDVYG DDDGKEIAMG SVGRMGKSKG KGKGRAEVKA
     EREQGMQRDG SRELSVVPDT QMVDLA
//
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