ID A0A2G9HCH9_9LAMI Unreviewed; 1066 AA.
AC A0A2G9HCH9;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:PIN15245.1};
GN ORFNames=CDL12_12121 {ECO:0000313|EMBL:PIN15245.1};
OS Handroanthus impetiginosus.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Bignoniaceae; Crescentiina; Tabebuia alliance;
OC Handroanthus.
OX NCBI_TaxID=429701 {ECO:0000313|EMBL:PIN15245.1, ECO:0000313|Proteomes:UP000231279};
RN [1] {ECO:0000313|Proteomes:UP000231279}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. UFG-1 {ECO:0000313|Proteomes:UP000231279};
RX PubMed=29253216; DOI=10.1093/gigascience/gix125;
RA Silva-Junior O.B., Grattapaglia D., Novaes E., Collevatti R.G.;
RT "Genome assembly of the Pink Ipe (Handroanthus impetiginosus,
RT Bignoniaceae), a highly valued, ecologically keystone Neotropical timber
RT forest tree.";
RL Gigascience 7:1-16(2018).
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:PIN15245.1}.
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DR EMBL; NKXS01002117; PIN15245.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G9HCH9; -.
DR STRING; 429701.A0A2G9HCH9; -.
DR OrthoDB; 551430at2759; -.
DR Proteomes; UP000231279; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd00065; FYVE_like_SF; 1.
DR CDD; cd13365; PH_PLC_plant-like; 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; 3.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR013591; Brevis_radix_dom.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
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; PF08381; BRX; 1.
DR Pfam; PF01363; FYVE; 1.
DR Pfam; PF16457; PH_12; 1.
DR Pfam; PF00415; RCC1; 6.
DR PRINTS; PR00633; RCCNDNSATION.
DR SMART; SM00064; FYVE; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF50985; RCC1/BLIP-II; 1.
DR PROSITE; PS51514; BRX; 1.
DR PROSITE; PS00626; RCC1_2; 2.
DR PROSITE; PS50012; RCC1_3; 7.
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:UP000231279};
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 227..284
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 285..336
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 337..391
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 392..443
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 454..505
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 506..557
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 558..609
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT DOMAIN 614..676
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT DOMAIN 983..1038
FT /note="BRX"
FT /evidence="ECO:0000259|PROSITE:PS51514"
FT REGION 774..815
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 928..979
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 817..858
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 775..790
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 939..959
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1066 AA; 116260 MW; 9B81D414CC50B1A2 CRC64;
MADPPSYGNP DRDIEQALIA LKKGTQLIKY CRKGKPKFRT FRLSTDETTL IWYSHGSERH
LKLSSVSRII PGQRTPVFKR FLRPDKEYLS FSLIYNDGER SLDLICKDKI ETEVWISGLK
SLISTGQANS RLTKSEISDF HGCGDIYQEN RTFGAKLEYS ASISQGRVST DSNSRDNYLN
RSSSHVGSEC ASMQIRTSGA DGFRVSVSST PSWSSQGSGP DDIESLGDVY VWGEIWSDGT
TDGTGNPFTV KTDVLTPKLL ESNVVLDVQQ IACGVRHIAL VTRQGEVFIW GEESGGRLGH
GVEKDVSGPR LVESLSITNV DFAACGEFHT CALSTSGDFY TWGDGTHNAG LLGHGNDYSH
WIPKRVSGSL ECLHVLSVAC GTWHSAIVTS TGHLFTFGDG TFGALGHGDR ESIPYPKEVQ
SLSGLRTFAV SCGVWHTAAI VEVIHHSGAN VSSRNLFTWG DGDKNRLGHG DKETYLLPTC
VSALIEYNIH QVACGHNITV ALTLSGHVFT MGSNVYGQLG NPLSDGKLPG LVQDRLVGEF
VEQITCGAHH VALLTSRSEV FTWGRGANGR LGHGDVEDHN VPTLVEALRD RNVRSITCGS
NFTASICIHK WVSGADQSVC TACRQAFGFT RKRHNCYNCG LVHCHACSSK KALRAALAPT
PGKPHRVCDS CYLKLKRAAE VGNAATLIRR SSGPRRSMDF SIKTDRGDRR TSRVLLSPTV
EPVKYLEVKS AMAGARSDNY SIVRASQVPS LLQLRDIAFP TSLSALQLAL KPVITSAPSP
PPPPQPQSQS NSRPASPYAR RPSPPRSGTP GFSRGVIDSL KKANDLLNQE VSKLHGQIKN
LKQRSEAQDA EIQKLKRAAE DAASLADDRS SKYIRTTQAV KTIADQLKEI TEFLPLEISE
SESFKALQTQ VESLLDAIGA EASEDRSAFP PELTNEQQNH SAEGHRTEDH VDESSVSDRK
EVNQSSTGGG TGAPQAAQKV GQKEVIEQFE PGVYVTLVQL VNGTKFFKRV RFSKRKFNEQ
QAEEWWKENK DRFVKAYSPA KTTNGAVEVT AAQPPAEEVK AAAQSS
//