ID Q9P5M4_NEUCS Unreviewed; 1283 AA.
AC Q9P5M4;
DT 01-OCT-2000, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2000, sequence version 1.
DT 27-MAR-2024, entry version 115.
DE SubName: Full=Related to SCP160 protein {ECO:0000313|EMBL:CAB91673.1};
GN Name=B23L21.050 {ECO:0000313|EMBL:CAB91673.1};
GN ORFNames=GE21DRAFT_9118 {ECO:0000313|EMBL:KHE78963.1};
OS Neurospora crassa.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=5141 {ECO:0000313|EMBL:CAB91673.1};
RN [1] {ECO:0000313|EMBL:CAB91673.1}
RP NUCLEOTIDE SEQUENCE.
RA Schulte U., Aign V., Hoheisel J., Brandt P., Fartmann B., Holland R.,
RA Nyakatura G., Mewes H.W., Mannhaupt G.;
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CAB91673.1}
RP NUCLEOTIDE SEQUENCE.
RA German Neurospora genome project;
RL Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KHE78963.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=73 {ECO:0000313|EMBL:KHE78963.1};
RG DOE Joint Genome Institute;
RA Baker S.E., Grigoriev I., Haridas S., LaButti K., McCluskey K.;
RT "Draft genome sequence of Neurospora crassa strain FGSC 73.";
RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; AL356172; CAB91673.1; -; Genomic_DNA.
DR EMBL; KN389818; KHE78963.1; -; Genomic_DNA.
DR PIR; T49692; T49692.
DR VEuPathDB; FungiDB:NCU03897; -.
DR eggNOG; KOG2208; Eukaryota.
DR HOGENOM; CLU_003293_0_0_1; -.
DR OMA; DHAGQQV; -.
DR OrthoDB; 5489311at2759; -.
DR Proteomes; UP000053122; Unassembled WGS sequence.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR CDD; cd00105; KH-I; 1.
DR CDD; cd22447; KH-I_ScSCP160_rpt2; 1.
DR CDD; cd22448; KH-I_ScSCP160_rpt3; 1.
DR CDD; cd22449; KH-I_ScSCP160_rpt4; 1.
DR CDD; cd22450; KH-I_ScSCP160_rpt5; 1.
DR CDD; cd22407; KH-I_Vigilin_rpt3; 1.
DR CDD; cd22408; KH-I_Vigilin_rpt4; 1.
DR Gene3D; 3.30.1370.10; K Homology domain, type 1; 9.
DR InterPro; IPR004087; KH_dom.
DR InterPro; IPR004088; KH_dom_type_1.
DR InterPro; IPR036612; KH_dom_type_1_sf.
DR PANTHER; PTHR10627:SF31; DODECA-SATELLITE-BINDING PROTEIN 1, ISOFORM A; 1.
DR PANTHER; PTHR10627; SCP160; 1.
DR Pfam; PF00013; KH_1; 8.
DR SMART; SM00322; KH; 10.
DR SUPFAM; SSF54791; Eukaryotic type KH-domain (KH-domain type I); 8.
DR PROSITE; PS50084; KH_TYPE_1; 9.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00117}.
FT DOMAIN 206..284
FT /note="K Homology"
FT /evidence="ECO:0000259|SMART:SM00322"
FT DOMAIN 288..378
FT /note="K Homology"
FT /evidence="ECO:0000259|SMART:SM00322"
FT DOMAIN 383..450
FT /note="K Homology"
FT /evidence="ECO:0000259|SMART:SM00322"
FT DOMAIN 702..765
FT /note="K Homology"
FT /evidence="ECO:0000259|SMART:SM00322"
FT DOMAIN 769..858
FT /note="K Homology"
FT /evidence="ECO:0000259|SMART:SM00322"
FT DOMAIN 863..934
FT /note="K Homology"
FT /evidence="ECO:0000259|SMART:SM00322"
FT DOMAIN 938..1015
FT /note="K Homology"
FT /evidence="ECO:0000259|SMART:SM00322"
FT DOMAIN 1019..1087
FT /note="K Homology"
FT /evidence="ECO:0000259|SMART:SM00322"
FT DOMAIN 1088..1198
FT /note="K Homology"
FT /evidence="ECO:0000259|SMART:SM00322"
FT DOMAIN 1203..1272
FT /note="K Homology"
FT /evidence="ECO:0000259|SMART:SM00322"
FT REGION 1..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 815..834
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 363..390
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..44
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..119
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1283 AA; 140356 MW; 63FF6D5E285B0F48 CRC64;
MADSTEQSAA AQLLQQHLET ASNAGSSHRV LVEEVEDEDL HKPVSSSETP AAPKPKPKTL
DTQSRELFPE LGGPKPKASV VAPIWGAKSN TNGSSNGAAP ANGTPQTSAP PSGVSTPIGS
GRQGPGPHPL SIPGRNVETM LLDPPHILPR TQLKRPLPDI LKDLNRKARA NVTMHALGNG
QLRFDAVGPQ EHATQALKDL VNQIGTKQNI TVQIPSSARA HIIGKGGSTI KAIQEKTGAR
IQLPKADESQ PPADEDDDTM INVHIEGNAF SAAAAQQEID RIAGERAANV QTKLRNIPAE
FYPFIAGPKN NLVHKLEEDM GVQIRVPPLQ GRSLQPPSIP APGQRPIFAP APQDYNIQLA
GERTAVQNAR AAIERRAEEL RRQLALEQLS IQRGRHQFII GDRGVPVDQF FEDTGCAIIL
PNDEDDDMVT IIGPQDHVQA GLERAMDLAM NMQCSNIDIS RFHRQAPGGA AAHARNVTRY
LRQRKAIEQL ERQHNVQVNT PFSNEGALPW ELYARDGKNA IRAQSEIKGL VDSHPPARIQ
AVQVDPFFHT YIRKDITPRV RQDYRVQLVV PEATEANAPV LLVYEGPSSP TSYEIPRGQP
SQSEVSEMQK WLQDARQHIL GLVSQQEEII HASLDVPQKY HDKLRKFIRK EQDERRSQEK
IPARVSNIGT TVNIKGPRSA VENLASKCEA FIEQEKADEK ERGFTLEFEF PQKFANHLIG
KGGSNIRELR EKFDVDIQVQ DGKVELKGPK AKAEAAKTHI LALGRQLQDE ATHILKIDPQ
FHRALIGAQG AQINRLQTRY KVLIFFPRTQ KASNDDESVA EASDAGKPRR QQAADEVIVR
GPKRGADEAR DELLSLLQYL KDTSYTATVT VQQKQIPSLI GSGGAALDAL RNETKAVIDI
PSARDTADGL VEIQIKGTKE AVAAAKKALE AKKAVFEDTV VKTIEVDRKY HRSLIGAGGS
TIRDIVVKAG GSDDRREIAR AVQFPKQDNS DNTIKIEGRT SVVDNIIQQI EAIVAERQNQ
VTEVIEVPVE KHRSLIGRGG DVKRGLESQF KVSIDVPRQG SGQTGIKIVG QSADVEKAKA
HIQSLTKDQP GETLQVPRAL HHSVSNNGQI FRRLKSDHHV TVDHAGHSIP TKPAAPASIR
ANGGSLPLIT DDEESTADAH SWTVVDQTST EEGDIPWVIR GSPENIEKAK KVIETAIEQA
KKEDAIGYLI LPDPRTYRYV IGQGGAKVNQ IRKQSGCKIT VPRDQAKGEA IEVVGNKEGV
EKAKDLILAA VKEGQNASRS PRE
//
