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Database: UniProt
Entry: A0A2T7PNL8_POMCA
LinkDB: A0A2T7PNL8_POMCA
Original site: A0A2T7PNL8_POMCA 
ID   A0A2T7PNL8_POMCA        Unreviewed;      1266 AA.
AC   A0A2T7PNL8;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:PVD35023.1};
GN   ORFNames=C0Q70_06304 {ECO:0000313|EMBL:PVD35023.1};
OS   Pomacea canaliculata (Golden apple snail).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Architaenioglossa; Ampullarioidea; Ampullariidae; Pomacea.
OX   NCBI_TaxID=400727 {ECO:0000313|EMBL:PVD35023.1, ECO:0000313|Proteomes:UP000245119};
RN   [1] {ECO:0000313|EMBL:PVD35023.1, ECO:0000313|Proteomes:UP000245119}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SZHN2017 {ECO:0000313|EMBL:PVD35023.1};
RC   TISSUE=Muscle {ECO:0000313|EMBL:PVD35023.1};
RA   Liu C., Liu B., Ren Y., Zhang Y., Wang H., Li S., Jiang F., Yin L.,
RA   Zhang G., Qian W., Fan W.;
RT   "The genome of golden apple snail Pomacea canaliculata provides insight
RT   into stress tolerance and invasive adaptation.";
RL   Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the SPT20 family.
CC       {ECO:0000256|ARBA:ARBA00009112}.
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:PVD35023.1}.
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DR   EMBL; PZQS01000003; PVD35023.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T7PNL8; -.
DR   STRING; 400727.A0A2T7PNL8; -.
DR   EnsemblMetazoa; XM_025231133.1; XP_025086918.1; LOC112559751.
DR   EnsemblMetazoa; XM_025232381.1; XP_025088166.1; LOC112560487.
DR   Proteomes; UP000245119; Miscellaneous, Linkage group lg3.
DR   GO; GO:0000124; C:SAGA complex; IEA:InterPro.
DR   GO; GO:0003712; F:transcription coregulator activity; IEA:InterPro.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   CDD; cd20504; CYCLIN_CCNA_rpt1; 1.
DR   Gene3D; 1.10.472.10; Cyclin-like; 2.
DR   InterPro; IPR032447; Cyclin-A_N.
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; IPR048258; Cyclins_cyclin-box.
DR   InterPro; IPR021950; Spt20.
DR   InterPro; IPR046468; Spt20-like_SEP.
DR   PANTHER; PTHR13526; TRANSCRIPTION FACTOR SPT20 HOMOLOG; 1.
DR   PANTHER; PTHR13526:SF8; TRANSCRIPTION FACTOR SPT20 HOMOLOG; 1.
DR   Pfam; PF02984; Cyclin_C; 1.
DR   Pfam; PF00134; Cyclin_N; 1.
DR   Pfam; PF16500; Cyclin_N2; 1.
DR   Pfam; PF12090; Spt20_SEP; 1.
DR   SMART; SM00385; CYCLIN; 2.
DR   SMART; SM01332; Cyclin_C; 1.
DR   SUPFAM; SSF47954; Cyclin-like; 2.
DR   PROSITE; PS00292; CYCLINS; 1.
PE   3: Inferred from homology;
KW   Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW   Cell division {ECO:0000256|ARBA:ARBA00022618};
KW   Cyclin {ECO:0000256|ARBA:ARBA00023127, ECO:0000256|RuleBase:RU000383};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245119}.
FT   DOMAIN          214..298
FT                   /note="Cyclin-like"
FT                   /evidence="ECO:0000259|SMART:SM00385"
FT   DOMAIN          307..425
FT                   /note="Cyclin C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01332"
FT   DOMAIN          310..394
FT                   /note="Cyclin-like"
FT                   /evidence="ECO:0000259|SMART:SM00385"
FT   REGION          1..64
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          947..1007
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..46
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        955..976
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        977..1007
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1266 AA;  138297 MW;  C055F2245659FBF0 CRC64;
     MSTMPNRIRP SQKENVQRPK QGLTSRSQVP RRAALGNISN QVRVQPSRAV KGPHETKTGQ
     DENAFVQQKV FGKTKAQPFT IFVDEPQPQQ PSAQSEATSS SRFDLEDIEN RLPSIDDVAP
     LPELCPAAAH DDSKSCASPM LLDTSVMDTI EDENLVDDAQ TGAVARAAYI QDVPEYAEDI
     YDYMLSTENK LKPRPGFMRR QVDVTSTMRA ILVDWLVEVA EEYKLHRETL FLAVNYIDRF
     LSVMSVARPK LQLVGTAAMF LASKYEEIYP PDVSEFVYIT DDTYTKKQVL RMEHLLLKVL
     QFDVSVPTVS WFCDRILRDT GADEQTQYLT MYLTELVLVE MDTFLKYPSS LVAAAALCLA
     NITLDVENPW PESHKKSSRY SLEELAACLN EMHTLHRQAE DHPQQSVREK YKLTKFMQVA
     FMPPPAALSL VGVKSLDQKL LELYVEECGK QPDDKSLNYA SHLLGKLLKR ERLNCLVLSL
     YPGTEGYSLM LRARSGVESE TIKLPYEETE VLEYIDAAEL PPFLLDLLEK AQVNVFYSGC
     VIVEVRDYRR SASGCYDAHY VLLRPSAQSL LCDTLSLAAE YGNSSWTQDD FQQLESEMLL
     ATSEPLCLDP SPAVAMVATE LTRQQKMFND PSLKRSIKRY TQVAQNRKKK LAQGPAPREL
     RLLDFLHKKR DKSKIGHAAN KSIKCSIDTW KQRSVQLNTP ENLEVEKFFK VPDRPASPGE
     NLILVEEHKL ERDPNQEHRM LACITIYRQR LADGFIGRLY LDHDYSGEES SQKGCSCQFP
     LGTRQNVDRY LEQFKELFTE EGRRLVKITT QRAGQAPEVV LTQVSQTPTA ATSITITSSQ
     ALLKQATPVG QGDSTNNSLA TKRNIPIQLS LSITPVGTVS TTASITSQGT VVTSAGMTGQ
     ATQLQASSQR FKQLNLHSRA NSSPLASPAS TPTSAPQQIA AALVSQQSVL QKAPTPTPAP
     TPPPISRTPT PTQPPTPTSS TSRRGSLQAG DGQLSQQATA QPGQQQTSNI SFVQQESLGG
     VSLSQPSTQG TQLSNINIAS ISSLPPNINL QGLTGLQGVS LGLQHMQVSL SMPGIAVPVP
     ITMINTNPSI LQNQTSILLP GGQQSIPLLS LQQQQQQRGG QLKTGTLTAT IATTTAGGAS
     RQGSTTTTTV PLSGVLTSQQ MSALTSLTVG KGGGTTATPL SAHQFIHLTG GTQGTSSTVS
     TAQGGSQTIH TQIALQKPAG SSGQTFQFHP LHLKQGAVAT SALAGTGIST TKPKIKKRGG
     TTPPKS
//
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