ID F2UJW4_SALR5 Unreviewed; 1679 AA.
AC F2UJW4;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 55.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
DE AltName: Full=Checkpoint with forkhead and RING finger domains protein {ECO:0000256|ARBA:ARBA00031332};
DE AltName: Full=RING-type E3 ubiquitin transferase CHFR {ECO:0000256|ARBA:ARBA00029800};
GN ORFNames=PTSG_12744 {ECO:0000313|EMBL:EGD77413.1};
OS Salpingoeca rosetta (strain ATCC 50818 / BSB-021).
OC Eukaryota; Choanoflagellata; Craspedida; Salpingoecidae; Salpingoeca.
OX NCBI_TaxID=946362 {ECO:0000313|Proteomes:UP000007799};
RN [1] {ECO:0000313|Proteomes:UP000007799}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50818 {ECO:0000313|Proteomes:UP000007799};
RA Russ C., Cuomo C., Burger G., Gray M.W., Holland P.W.H., King N.,
RA Lang F.B.F., Roger A.J., Ruiz-Trillo I., Young S.K., Zeng Q., Gargeya S.,
RA Alvarado L., Berlin A., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C.,
RA Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., White J., Yandava C., Haas B., Nusbaum C.,
RA Birren B.;
RT "Annotation of Salpingoeca rosetta.";
RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SUBCELLULAR LOCATION: Nucleus, PML body
CC {ECO:0000256|ARBA:ARBA00004322}.
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DR EMBL; GL832977; EGD77413.1; -; Genomic_DNA.
DR RefSeq; XP_004990757.1; XM_004990700.1.
DR STRING; 946362.F2UJW4; -.
DR EnsemblProtists; EGD77413; EGD77413; PTSG_12744.
DR GeneID; 16071315; -.
DR KEGG; sre:PTSG_12744; -.
DR eggNOG; KOG0802; Eukaryota.
DR InParanoid; F2UJW4; -.
DR OrthoDB; 450556at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000007799; Unassembled WGS sequence.
DR GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd00060; FHA; 1.
DR Gene3D; 2.60.200.20; -; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR040909; CHFR_Znf-CRD.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR16079:SF4; E3 UBIQUITIN-PROTEIN LIGASE CHFR; 1.
DR PANTHER; PTHR16079; UBIQUITIN LIGASE PROTEIN CHFR; 1.
DR Pfam; PF00023; Ank; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF00498; FHA; 1.
DR Pfam; PF13923; zf-C3HC4_2; 1.
DR Pfam; PF17979; zf-CRD; 1.
DR SMART; SM00248; ANK; 6.
DR SMART; SM00240; FHA; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 2.
DR PROSITE; PS50088; ANK_REPEAT; 2.
DR PROSITE; PS50006; FHA_DOMAIN; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Reference proteome {ECO:0000313|Proteomes:UP000007799};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT DOMAIN 61..109
FT /note="FHA"
FT /evidence="ECO:0000259|PROSITE:PS50006"
FT DOMAIN 345..384
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REPEAT 1342..1374
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1442..1469
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REGION 144..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 313..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 445..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 552..628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 788..833
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 866..913
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1041..1132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1210..1242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1518..1556
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..183
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..221
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..273
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 313..328
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..466
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 552..578
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 586..600
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 810..824
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 875..894
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 895..911
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1060..1132
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1527..1545
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1679 AA; 177366 MW; 7889948864B2D163 CRC64;
MSSGKSSLGG GAMRATLRRK NTEMVAPHAA ASGSAQAEVE LVPTSPSLPR VRVRGGPADP
ICIGRSEACD TTIENPYLSG THCHLKLSDG KLFLKDTSSN GTQVEGKLVQ RDAWTEVKRG
DEITLVTETP TTAAVSFLAR YRRTPQATAP QQADGNTEEE EVEELERRAP AADVEDAPPA
KKSKTEHPSS VQGGDGGGGG DDEAPSGATT ATTTASTAPA TAEERGGSGD AMVTTADGDG
DDADDEEGHI GAGGHENDQA ASTATATATT APATTATATA GTIGTSSTLT AGASDSDTTT
TATAGTTAAT AGTTAATAGT ATTAVSSNGG EEEEEEDDME ENLLCSICRD VLHDAASLLP
CLHTFCAGCC SQWLTSNSTC PDCRVNVRKM RRNHLVNNLV GVYLKSHPDK KRDAADIATL
DAANQLKVRG KDELRFSARR RGWRDDDDYD DDDDDDDSND DDDDGDFDGG RGGRVGRYGV
RIGGFGMSFS FAPAPVALPP PRCAACDDAS TNVMNFRCSG TGAAHMQCTC CRTYFPHRDL
IAPSTTTTTA AATTTSTAAT TTTPAATTAT TPGATTPPVP ASTGDDGDGD TTSSTTTGPA
DGDGDGDGDG GASSSSPPPS STTAAAVSTP PPPVHCALCS RPFCNLFWTR GCRGPCTALG
GCLRPLQDLT LVSSDLTAFI NRNTYESQVM RDYLREKGMT PRDLLLTCID RAASGALTAA
AIGPVSRSTP TCRQCGLRVF NALAYEYRKA LPASDLPRSA QVTPSGETRA NCWYGYQCRT
QHNRPHHAVR FNHPTHRPLG PYGPSNSSSP SAPRAPPYPG TGHAPPSDPS SVRYPNQEAW
QRYYQHFNWT KWWEMQHKSN LAWHGHGRHP YPSHPGQYPV KPQSPQPTPP PPTSTAAATY
TAASTTDGNN GHHRTRWQDW RWLTGFFISV GCIFALTVGI FVFVFRRLPS SSTPANRSNN
EHMQLLAEIA QYDDPVFMPA TKTAASGPAA PVNPAPPYDV NTAAGTTHTI SISISNGNSN
SNSTDSDSEA CFQGLVTADH RHHDHHQQRD HHHHGHDSAS SSEVGCSSSP WSSSIAHSDP
ATAASNSSAD HSSPGQHSHS HSTGSVVIAM DDTPYNSSSS QQQQQQQQQQ QHASLLPLLP
LDQTTREQKQ TNSQAMALPT YFRTDDADIP TISTSSCSGA ANPSSPSPIS PAAVWSRLYS
LMTALWPAAA TTSSSSPTHQ HQHQHQRQRQ HHSHISGGGR GGGAITADVA QYRRLLQHLY
PRHLLDRAHA HRVLPLRTAV LLGDVDQLSA LLEDTPPSLL AATDAAGRTL LHEAVLSRSG
LDVALIAMLL RHRCPTEVPD LHGRTPLLCA CELSKPAAVR AMAAGGADVN ARDAMQQTGL
MIACARNDAD VASALLTAGA DSALADGRGY TAMHWCCATG AVEAMTRLSA FTSRLVEVKT
GAGDTCLHLA AREANEAVIK VLMGERASVR AVLLTSVNAF GQRAEDAAAA ANHHAIARHL
QQHRVALEQD VLCGRMSLKD RAPRRRRHAS TPAGDGEDDG DAGRHLSTTR PGSKVGRAMY
MRKHRHRHKV ISQLRETRVR HLEGEGAAIA AAVAALKADR HSLMQALAAV SPEHLQRLKG
RKARPAKRRA LALVKTNGSA APLSPPLAPP LAASVAAAAH GNRATKANRR RSLSGAAFV
//
