ID A0A0F4Z606_TALEM Unreviewed; 841 AA.
AC A0A0F4Z606;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Spindle poison sensitivity protein Scp3 {ECO:0000313|EMBL:KKA25750.1};
GN ORFNames=T310_0228 {ECO:0000313|EMBL:KKA25750.1};
OS Rasamsonia emersonii CBS 393.64.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Rasamsonia.
OX NCBI_TaxID=1408163 {ECO:0000313|EMBL:KKA25750.1, ECO:0000313|Proteomes:UP000053958};
RN [1] {ECO:0000313|EMBL:KKA25750.1, ECO:0000313|Proteomes:UP000053958}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 393.64 {ECO:0000313|EMBL:KKA25750.1,
RC ECO:0000313|Proteomes:UP000053958};
RA Heijne W.H., Fedorova N.D., Nierman W.C., Vollebregt A.W., Zhao Z., Wu L.,
RA Kumar M., Stam H., van den Berg M.A., Pel H.J.;
RL Submitted (APR-2015) 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:KKA25750.1}.
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DR EMBL; LASV01000013; KKA25750.1; -; Genomic_DNA.
DR RefSeq; XP_013332362.1; XM_013476908.1.
DR AlphaFoldDB; A0A0F4Z606; -.
DR STRING; 1408163.A0A0F4Z606; -.
DR GeneID; 25312283; -.
DR OrthoDB; 2906101at2759; -.
DR Proteomes; UP000053958; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0016043; P:cellular component organization; IEA:UniProt.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0000209; P:protein polyubiquitination; IEA:InterPro.
DR Gene3D; 4.10.1000.10; Zinc finger, CCCH-type; 1.
DR InterPro; IPR045072; MKRN-like.
DR InterPro; IPR041367; Znf-CCCH_4.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR PANTHER; PTHR11224; MAKORIN-RELATED; 1.
DR PANTHER; PTHR11224:SF10; RING-TYPE E3 UBIQUITIN TRANSFERASE; 1.
DR Pfam; PF00642; zf-CCCH; 1.
DR Pfam; PF18044; zf-CCCH_4; 1.
DR SMART; SM00356; ZnF_C3H1; 2.
DR SUPFAM; SSF90229; CCCH zinc finger; 1.
DR PROSITE; PS50103; ZF_C3H1; 2.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00723}; mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW Reference proteome {ECO:0000313|Proteomes:UP000053958};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00723};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00723}.
FT DOMAIN 320..347
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 349..376
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT ZN_FING 320..347
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT ZN_FING 349..376
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 242..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 446..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 638..660
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 683..841
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 85..142
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 446..460
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 697..724
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 732..791
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 811..841
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 841 AA; 91428 MW; 6BAB8973F0C3AB0E CRC64;
MGSRITSISR SSRPYSVRYN PQLGPPSSHR VSFFNAFQQA IDISTNLHNK VTKVWYSGKQ
LVYHALQDLS EVDTPETIAA IDEEIQQVQN GLSTLKIREK ELREKLAAVC AIVPMPELRD
SVSKLEEEKA SALNRLLKLQ GEETVCISAE EMTRVEKEWK TWQGHVQTRR RIFSELWAKC
TEVLPEDTTE EDLKLSLRSL SVAGDAGCCD NNLSSLPLPL LHDSEPPPSC NTPPIPVVAA
RPSPAMQHAH QHQPQLPAQQ RNPPVPLANG LRSHPNRLSS EMRTRGPVPG HPPNGHARNI
SGAAPFEMVA RSPPNPSPKN TKHVPCKFFR QGACQAGPAC PFLHSTDASV DNAPCKYFTK
GNCKFGAKCA LAHILPDGRR VNRPNFGLGM GGGSGGHLNL GGRVNPQAYH NQDSALTNSV
LSQQRMNGHD VRHTYPFPGQ DDFAALQAQQ QQQQQQQQQQ PPPPEGIPMI DTGFVSDAGS
KYGSPVDDVR QPTSPKRHLT ALDAPLPASF DSQGISHAAR YGPVAASMPS KFGLELSSLS
SPPSQRTPSD TLKSLRDAAF GSDLRKPSSN FGSSPAAEDS LGPRFLHSQR MASRSKFLSA
SVPRPTVLDD WDDGNFPMEE DFLPVNLHDD VLTPQEKMRR LSRTEQELSS SNREFGSLGI
GTGSLKVGSP LASSPSRFGA LFAKQRQKKE EEAHGASSSS FNHIGSPLRE SSLQLSSSPN
PRPIGSRPVS GDVSPFVSSP ARQSSMSMIS QQLSSLSLHP NSARQSSTSA APTSSSRLDR
TVSSPVTTSK IDEEQGDLVF SMEEEESNKR SSVGWNSSDK SSTSNNKEEP SSSSQDLEFQ
S
//
