ID A0A2U1Q576_ARTAN Unreviewed; 1392 AA.
AC A0A2U1Q576;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Zinc finger, RING-CH-type {ECO:0000313|EMBL:PWA93137.1};
GN ORFNames=CTI12_AA074180 {ECO:0000313|EMBL:PWA93137.1};
OS Artemisia annua (Sweet wormwood).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Asteroideae; Anthemideae;
OC Artemisiinae; Artemisia.
OX NCBI_TaxID=35608 {ECO:0000313|EMBL:PWA93137.1, ECO:0000313|Proteomes:UP000245207};
RN [1] {ECO:0000313|EMBL:PWA93137.1, ECO:0000313|Proteomes:UP000245207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Huhao1 {ECO:0000313|Proteomes:UP000245207};
RC TISSUE=Leaf {ECO:0000313|EMBL:PWA93137.1};
RX PubMed=29703587; DOI=10.1016/j.molp.2018.03.015;
RA Shen Q., Zhang L., Liao Z., Wang S., Yan T., Shi P., Liu M., Fu X., Pan Q.,
RA Wang Y., Lv Z., Lu X., Zhang F., Jiang W., Ma Y., Chen M., Hao X., Li L.,
RA Tang Y., Lv G., Zhou Y., Sun X., Brodelius P.E., Rose J.K.C., Tang K.;
RT "The genome of Artemisia annua provides insight into the evolution of
RT Asteraceae family and artemisinin biosynthesis.";
RL Mol. Plant 11:776-788(2018).
CC -!- SIMILARITY: Belongs to the cyclin family.
CC {ECO:0000256|RuleBase:RU000383}.
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:PWA93137.1}.
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DR EMBL; PKPP01000408; PWA93137.1; -; Genomic_DNA.
DR Proteomes; UP000245207; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR CDD; cd20506; CYCLIN_AtCycA-like_rpt2; 1.
DR CDD; cd16461; RING-H2_EL5-like; 1.
DR Gene3D; 1.10.472.10; Cyclin-like; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR013763; Cyclin-like_dom.
DR InterPro; IPR036915; Cyclin-like_sf.
DR InterPro; IPR004367; Cyclin_C-dom.
DR InterPro; IPR006671; Cyclin_N.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR011016; Znf_RING-CH.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR46225; C3H4 TYPE ZINC FINGER PROTEIN; 1.
DR PANTHER; PTHR46225:SF29; ZINC FINGER, RING_FYVE_PHD-TYPE-RELATED; 1.
DR Pfam; PF02984; Cyclin_C; 1.
DR Pfam; PF00134; Cyclin_N; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00385; CYCLIN; 2.
DR SMART; SM01332; Cyclin_C; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00744; RINGv; 1.
DR SUPFAM; SSF47954; Cyclin-like; 2.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Cyclin {ECO:0000256|ARBA:ARBA00023127, ECO:0000256|RuleBase:RU000383};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Reference proteome {ECO:0000313|Proteomes:UP000245207};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT TRANSMEM 923..943
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1074..1094
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1106..1126
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1199..1217
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1229..1262
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1330..1371
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 347..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..379
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1392 AA; 155387 MW; A9EDB94B0FF6A3E8 CRC64;
MSLYYMPAAI RSKLESLRQN FFIGSELGDR KMAWVSWNTC LASKELGGLG IGSIHALNVG
LLFKWIWRFL HNQSDLWISV IKGIYGCSGG IFGENFARSC HSPWSGILSM IKKLKHKGID
LMAFCKRKLG NGESILFWED VWWGNQTLKS LYPRIHMLDS HKDCCVAHRL PPHEWNTVLR
CDPRGGIEAS QFNELRLHIE SVVLNSNPDS WSWTPNIHKG FTVASVRLLV DSHLLPVGPH
ATRWNRNIPI KVNVFVWRAL LNKLPSRVNL DQFVSDIVAA IGRYWIESIV IVVFLASSWK
ANQSNICRHS SSRQRDMNKE NVSVANIQGP NGRVTRARAK ALGVSGGLPP LHPVLKQDQK
QALQPKTKRA SSDSKSATDV APAVQVKRRA VLKDISNNSF NGSSVKVLNG FKAQTSKQIK
KCTAKKNERV APSIRVDPRI QKRTTKATEN KTKPITKELQ EATLHPNSEN DRAIQPYISL
DEGNTITSEV EASKVHSIID IDAMHTGPQM CSLYAADVYG NLRTAEKTPE PHQGSKTFAE
HFFLFFAYCK VPPFTQLKLR HSVDYMKTVQ QEITQEMRGI LIDWLVEVCE EYGLAMETFY
LTVALLDLYL SKKCIGKRRL QLLGITCMLL ASKYEEICAP RVEEFCFITD KTYTRGEVLE
MEYQILDVLS FQMSVPTTKK FLRRFLLAAQ SSYKAPVIEL EFLANYLAEL TLVEYSFRKF
LPSLVAASAV FLAKWTIDQD EDPWNATLEH YTRYKASELK ATVLALQDLQ LNDATPLRTI
RQKYKQQKVG FECVAGKDKR YHLNVLKQFF AISIPCVHYF TILVEDLDGH QDRPVNGLNS
QQVENLPSTS VTDRVFQHAF STTNGTNARN IPITRRGNSN APRRSPLNSG YWISIELVIT
VSQLIAAVIV LSLSRHEQPH APLFTWVIGY ASGCVATLPL LFWRFYFRNH ATDQDPALPR
QSSAPSSISA IATSFTSSSN GTSSLAADTQ NTTARTRPIA ALLYASAHVI DIDQDRPVNG
LNSQQVENLP STSVTDRVFQ HAFSTTNGTN ARNIPITRRG NSNAPRRSPL NSGYWISIEL
VITVSQLIAA VIVLSLSRHE QPHAPLFTWV IGYASGCVAT LPLLFWRFYF RNHATDQDPA
LPRQSSAPSS ISAIATSFTS SSNGTSSLAA DTQNTTARTR PIAALLYARL KVPVEYFKMG
LDCFFAVWFV VGNVWIFGGH TSASDAPNLY RLCLVFLTFC CIGYAMPFIL CATICCCLPC
IISVLGFRED MSQNRGATTE SINSLPTYKF KIKKHKRGNS KESQAGASEG GIVAAGTEKE
RVVSGEDAVC CICLAKYANN DELRELPCTH FFHKDCVDKW LKINASCPLC KSEVGESVLG
SITEPTAAGV QS
//
