ID W9RPR0_9ROSA Unreviewed; 2245 AA.
AC W9RPR0;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Protein tas {ECO:0000313|EMBL:EXC01805.1};
GN ORFNames=L484_021444 {ECO:0000313|EMBL:EXC01805.1};
OS Morus notabilis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Moraceae; Moreae; Morus.
OX NCBI_TaxID=981085 {ECO:0000313|EMBL:EXC01805.1, ECO:0000313|Proteomes:UP000030645};
RN [1] {ECO:0000313|Proteomes:UP000030645}
RP NUCLEOTIDE SEQUENCE.
RA He N., Zhao S.;
RT "Draft Genome Sequence of a Mulberry Tree, Morus notabilis C.K. Schneid.";
RL Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KE345336; EXC01805.1; -; Genomic_DNA.
DR RefSeq; XP_010104755.1; XM_010106453.1.
DR STRING; 981085.W9RPR0; -.
DR eggNOG; KOG1575; Eukaryota.
DR Proteomes; UP000030645; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd19094; AKR_Tas-like; 1.
DR CDD; cd00065; FYVE_like_SF; 2.
DR Gene3D; 3.20.20.100; NADP-dependent oxidoreductase domain; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 2.130.10.30; Regulator of chromosome condensation 1/beta-lactamase-inhibitor protein II; 5.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR013591; Brevis_radix_dom.
DR InterPro; IPR027988; BRX_N.
DR InterPro; IPR023210; NADP_OxRdtase_dom.
DR InterPro; IPR036812; NADP_OxRdtase_dom_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR009091; RCC1/BLIP-II.
DR InterPro; IPR000408; Reg_chr_condens.
DR InterPro; IPR000306; Znf_FYVE.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR22870; REGULATOR OF CHROMOSOME CONDENSATION; 1.
DR PANTHER; PTHR22870:SF352; REGULATOR OF CHROMOSOME CONDENSATION (RCC1) FAMILY WITH FYVE ZINC FINGER DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00248; Aldo_ket_red; 1.
DR Pfam; PF08381; BRX; 2.
DR Pfam; PF13713; BRX_N; 2.
DR Pfam; PF01363; FYVE; 2.
DR Pfam; PF00415; RCC1; 11.
DR PRINTS; PR00633; RCCNDNSATION.
DR SMART; SM00064; FYVE; 2.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 2.
DR SUPFAM; SSF51430; NAD(P)-linked oxidoreductase; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF50985; RCC1/BLIP-II; 2.
DR PROSITE; PS51514; BRX; 2.
DR PROSITE; PS00626; RCC1_2; 2.
DR PROSITE; PS50012; RCC1_3; 13.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000030645};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00091}.
FT REPEAT 645..703
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 704..755
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 756..806
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 807..858
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 869..920
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 921..972
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 973..1024
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT DOMAIN 1029..1083
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT DOMAIN 1354..1409
FT /note="BRX"
FT /evidence="ECO:0000259|PROSITE:PS51514"
FT REPEAT 1454..1514
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 1515..1569
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 1570..1621
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 1632..1683
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 1684..1735
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 1736..1787
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT DOMAIN 2120..2175
FT /note="BRX"
FT /evidence="ECO:0000259|PROSITE:PS51514"
FT REGION 1148..1175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1281..1350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1914..1941
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2049..2115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1189..1223
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1955..1989
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1295..1350
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2061..2115
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2245 AA; 248186 MW; F4FFE67B740CA884 CRC64;
METFGVGTYS KTIYNANVNA NLIFSIKKKS VSEHSSVTYW PQVVPLAKAH STTISKPETS
LFTSLKTVVP TRQIAVIHDI LGHVLTGHLP RITLFSPLQW PKLHAPPFAR LFTRRNSSPL
PQKLRHCRRK LGDSDLVISE ITLGTMTFGE QNTEKESHEI LSYAFEHGIN ALDTAEAYPI
PMKKETQGRT DLYISSWLNS QPRDKIIVAT KVCGYSERMS YIRENAKVLR VDSANIKESV
EKSLKRLNTD YIDLLQIHWP DRYVALFGEF FYNPTKWRPS VPFVEQLRAF QELIDEGKVR
YIGVSNETSY GVMEFVRAAK VEGLPKIVSI QNSYSLLVRC AFEVDLVEVC HPKNCNVGLL
AYSPLAGGAL TGKYLDSDSE AARKGRLNLF PGYMERYNKS VAKEATIKYI ELAKKHGVSP
VQLALGFARD RPFMTSTIIG ATSVEQLKED IDAFLTTERP LPAEAIVALK KGTQLIKYCR
KRKPKLYPFR ISPAVFRRYL RPEKDYLSFS LLYNNGERSL DLICKDKAEI ELWFVGLKEL
IPSGQQRTRR SKSDYFDQQD GSDIIQNGSP LRVSFDFTCI AHGRVSIDLN SSRESPLNLV
GSDLASECAS MQLRTNPGDG FRISVSSTPS CSSGGSGPDD IESLGDVYLW GEVSLDGTLP
DGSMSPVPIK TDVLTPRPLE LNVVLDVHQI SCGVRHVALV TRQGKVFTWG EESGGRLGHG
IDKDFSRPRL VEFLAINNVG FVACGEYHSC VVSTTGDFFT WGDGAHNAGL LGHGTDIPKR
VNGPLEGLQV LSVACGTWHS ALSTSNGKLF PFCDGTFSVL GHGDRQSVSY PREVQLLSGL
KTIKVACGVW HTAAIVEVAG QAGSSISSRK LFTWGNGDKN RLGHGNKETY LLPTCVSSLI
DYNFQQLGCG RTMTVALTTS GHVFTMGGTS YGQLGNPSSD GKTPCLVQDK LVGEFVEEIS
CGANHVDVLT SRSEVFTWGK GANGRLGHGD IEDQKTPTLV EALKDRHVKN ISCGSNFTTS
ICIHKWVSGA DQSVCSGCRQ AFGFTRKRHN CYNCGLVHCH ACSSRKAFRA ALAPTPGKPH
RVRSSRVLLY PTTEPVKYLE VRFGRSGTKS DYSSMVRASQ VPSLLQLKHI AFPSSLSAIQ
NALKPVMTTS PHTSVNSRTS SPYARKPSPP RSATPVFSKS VIDNIKKSNE LLTQEVTKLH
GQVKSLKQKC DVQDAEMQQL RRDAKAATSF AEGQSSKCKV AKELVKSFTE QLKAITEKLP
TEDSENEIMK SLHVRAEDFL NMTNETTSET SSSLRTSLER EHRHTNHLSH EGGDTSPHSD
KPSISRTRED ETQPSSEDGS KSHRSLAMKA EKGKEVIEQF EPGVYVTLIQ LQNGTRIFRR
VKFSKRRFSE QQAEEWWNNN KDRLLKTYNV PQKCFGHGID KDFSRPRLVE FLAINNVGFV
ACGEYHSCVV STTGDFFTWG DGAHNAGLLG HGTDCFGHGI DKDFSRPRLV EFLAINNVGF
VACGEYHSCV VSTTGDFFTW GDGAHNAGLL GHGTDVSHWI PKRVNGPLEG LQVLSVACGT
WHSALSTSNG KLFTFGDGTF GVLGHGDRQS VSYPREVQLL SGLKTIKVAC GVWHTAAIVE
VAGQAGSSIS SRKLFTWGNG DKNRLGHGNK ETYLLPTCVS SLIDYNFQQL GCGRTMTVAL
TTSGHVFTMG GTSYGQLGNP SSDGKTPCLV QDKLVGEFVE EISCGANHVD VLTSRSEVFT
WGKGANGRLG HGDIEDQKTP TLVEALKDRH VKNISCGSNF TTSICIHKWV SGADQSVCSG
CRQAFGFTRK RHNCYNCGLV HCHACSSRKA FRAALAPTPG KPHRVVEVRS SRVLLYPTTE
PVKYLEVRFG RSGTKSDYSS MVRASQVPSL LQLKHIAFPS SLSAIQNALK PVMTTSPHTS
VNSRTSSPYA RKPSPPRSAT PVFSKSVIDN IKKSNELLTQ EVTKLHGQVK SLKQKCDVQD
AEMQQLRRDA KAATSFVEGQ SSKCKVAKEL VKSFTEQLKA ITEKLPTEDS ENEIMKSLHA
RAEDFLNMTN ETTSETSSSL RTSLEREHQH TNHLSHEGGD TSPHSDRPSV FRTREDETQP
SSEDGSKSHR SLAMKAEKGK EVIEQFEPGV YVTLIQLQNG TRIFRRVKFS KRRFSEQQAE
EWWNNNKDRL LKTYNVPQKV NPAQTRSSST PAPRLFLRLL RKAPTLSHLP RHREEKGVNC
NTIVFIYLPH VSLLNCPWLH SNGFV
//
