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Database: UniProt
Entry: A0A137PEV9_CONC2
LinkDB: A0A137PEV9_CONC2
Original site: A0A137PEV9_CONC2 
ID   A0A137PEV9_CONC2        Unreviewed;       596 AA.
AC   A0A137PEV9;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=C3H1-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=CONCODRAFT_15434 {ECO:0000313|EMBL:KXN73544.1};
OS   Conidiobolus coronatus (strain ATCC 28846 / CBS 209.66 / NRRL 28638)
OS   (Delacroixia coronata).
OC   Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota;
OC   Entomophthoromycotina; Entomophthoromycetes; Entomophthorales;
OC   Ancylistaceae; Conidiobolus.
OX   NCBI_TaxID=796925 {ECO:0000313|EMBL:KXN73544.1, ECO:0000313|Proteomes:UP000070444};
RN   [1] {ECO:0000313|EMBL:KXN73544.1, ECO:0000313|Proteomes:UP000070444}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 28638 {ECO:0000313|EMBL:KXN73544.1,
RC   ECO:0000313|Proteomes:UP000070444};
RX   PubMed=25977457; DOI=10.1093/gbe/evv090;
RA   Chang Y., Wang S., Sekimoto S., Aerts A.L., Choi C., Clum A., LaButti K.M.,
RA   Lindquist E.A., Yee Ngan C., Ohm R.A., Salamov A.A., Grigoriev I.V.,
RA   Spatafora J.W., Berbee M.L.;
RT   "Phylogenomic Analyses Indicate that Early Fungi Evolved Digesting Cell
RT   Walls of Algal Ancestors of Land Plants.";
RL   Genome Biol. Evol. 7:1590-1601(2015).
CC   -!- FUNCTION: May be involved in the turnover of nuclear polyadenylated
CC       (pA+) RNA. {ECO:0000256|ARBA:ARBA00043866}.
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DR   EMBL; KQ964435; KXN73544.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A137PEV9; -.
DR   EnsemblFungi; KXN73544; KXN73544; CONCODRAFT_15434.
DR   OrthoDB; 5406435at2759; -.
DR   Proteomes; UP000070444; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProt.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.70.330; -; 1.
DR   Gene3D; 1.20.1390.10; PWI domain; 1.
DR   Gene3D; 4.10.1000.10; Zinc finger, CCCH-type; 1.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR002483; PWI_dom.
DR   InterPro; IPR036483; PWI_dom_sf.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR045137; RBM26/27.
DR   InterPro; IPR000504; RRM_dom.
DR   InterPro; IPR000571; Znf_CCCH.
DR   PANTHER; PTHR14398; RNA RECOGNITION RRM/RNP DOMAIN; 1.
DR   PANTHER; PTHR14398:SF0; ZINC FINGER PROTEIN SWM; 1.
DR   Pfam; PF01480; PWI; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   SMART; SM00360; RRM; 2.
DR   SMART; SM00356; ZnF_C3H1; 1.
DR   SUPFAM; SSF101233; PWI domain; 1.
DR   SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR   PROSITE; PS50102; RRM; 1.
DR   PROSITE; PS50103; ZF_C3H1; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00723};
KW   mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070444};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW   ProRule:PRU00176}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00723};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00723}.
FT   DOMAIN          119..146
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50103"
FT   DOMAIN          209..281
FT                   /note="RRM"
FT                   /evidence="ECO:0000259|PROSITE:PS50102"
FT   ZN_FING         119..146
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT   REGION          375..424
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          556..596
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        382..424
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   596 AA;  68124 MW;  D0AFE59C6F9A15F6 CRC64;
     MTLSLENTEK LKDFISETLT KSFDLEPETL TEYIIALLSE DAPIYKLKDS CIVQLQDFLH
     DGTSAFVQEL FNYIREHKVI SNKDAQIHHN DPYGYRPMVQ QHMPYIPYDP NTLMYGQPPR
     SMPTCKYYLK FGQCTNPNCQ FYHPLNTHEP QGYHPYDPSY AQPAYVPEYP RPPRRSNSFR
     NVFIPPTFQS NTFIPQNSQL PKTVKEPYKT IFVTKIPLNF IEEEHVRETF QEFGQIENIV
     LHREFRQAKV TFQDLASAKK AHDSQVRFFN SVATSVEYDS ETDPIEFKYI PENGTNPNAS
     SEIEKKNQAL LARLSLKRSK EKLLEKLVEQ KKIITEALEK PDITEESKTE LTSFLEKVNS
     NITETEEFMK KMFPQKSAQA GKSEGDEGTS NSSTLNNGQS TVAENARNGN PSAKTSTVPD
     NSKLTPSQIQ DLYILDNRPG KFVLKGFSEE NKPSIEEHFS KAISFISITF DYDDQNGALI
     RFRTRPSAET AIRAFSKKEI GNLEGTWILE HDQEIQSEIQ PEVQLDTETD INLVGEPEAQ
     ADIDLTIEPE IQLDTQSAVQ VEAEPSSDLK RTISEVEDEE LLDNDINPEK LTKSEV
//
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