ID A0A2Y9QKT4_TRIMA Unreviewed; 3748 AA.
AC A0A2Y9QKT4;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=RCR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012249};
DE EC=2.3.2.33 {ECO:0000256|ARBA:ARBA00012249};
GN Name=LOC101355836 {ECO:0000313|RefSeq:XP_023582482.1,
GN ECO:0000313|RefSeq:XP_023582483.1};
OS Trichechus manatus latirostris (Florida manatee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Sirenia; Trichechidae; Trichechus.
OX NCBI_TaxID=127582 {ECO:0000313|Proteomes:UP000248480, ECO:0000313|RefSeq:XP_023582482.1};
RN [1] {ECO:0000313|RefSeq:XP_023582482.1, ECO:0000313|RefSeq:XP_023582483.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine +
CC [acceptor protein]-L-threonine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + [acceptor protein]-3-O-ubiquitinyl-L-threonine.;
CC EC=2.3.2.33; Evidence={ECO:0000256|ARBA:ARBA00000333};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SUBCELLULAR LOCATION: Cell projection, axon
CC {ECO:0000256|ARBA:ARBA00004489}.
CC -!- SIMILARITY: Belongs to the RING-Cys relay (RCR) family.
CC {ECO:0000256|ARBA:ARBA00005415}.
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DR RefSeq; XP_023582482.1; XM_023726714.1.
DR RefSeq; XP_023582483.1; XM_023726715.1.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000248480; Unplaced.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd19799; Bbox2_MYCBP2; 1.
DR CDD; cd16463; RING-H2_PHR; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 2.60.120.820; PHR domain; 2.
DR Gene3D; 2.130.10.30; Regulator of chromosome condensation 1/beta-lactamase-inhibitor protein II; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR004939; APC_su10/DOC_dom.
DR InterPro; IPR017868; Filamin/ABP280_repeat-like.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR012983; PHR.
DR InterPro; IPR038648; PHR_sf.
DR InterPro; IPR009091; RCC1/BLIP-II.
DR InterPro; IPR000408; Reg_chr_condens.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45943; E3 UBIQUITIN-PROTEIN LIGASE MYCBP2; 1.
DR PANTHER; PTHR45943:SF1; E3 UBIQUITIN-PROTEIN LIGASE MYCBP2; 1.
DR Pfam; PF03256; ANAPC10; 1.
DR Pfam; PF08005; PHR; 2.
DR Pfam; PF00415; RCC1; 1.
DR SMART; SM01337; APC10; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF50985; RCC1/BLIP-II; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51284; DOC; 1.
DR PROSITE; PS50194; FILAMIN_REPEAT; 1.
DR PROSITE; PS00626; RCC1_2; 1.
DR PROSITE; PS50012; RCC1_3; 2.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000248480};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT REPEAT 4..54
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 55..112
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 1386..1479
FT /note="Filamin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00087"
FT DOMAIN 2788..2966
FT /note="DOC"
FT /evidence="ECO:0000259|PROSITE:PS51284"
FT DOMAIN 3498..3549
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1779..1999
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2136..2155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2675..2699
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2985..3006
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1784..1805
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1806..1827
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1853..1920
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1930..1960
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1971..1993
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2989..3003
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3748 AA; 412357 MW; 26E055216940AC7D CRC64;
MENGDVYTFG YGQHGQLGHG DVNSRGCPTL VQALPGPSTQ VTAGSNHTAV LLMDGQVFTF
GSFSKGQLGR PILDVPYWNA KPAPMPNIGS KYGRKATWIG ASGDQTFLRI DEALINSHVL
ATSEIFASKH IIGLVPASIS EPPPFKCLLI NKVDGSCKTF NDSEQEDLQG FGVCLDPVYD
VIWRFRPNTR ELWCYNAVVA DARLPSAADM QSRCSILSPE LALPTGSRAL TTRSHAALHI
LGCLDTLAAM QDLKMGVAST EEETQAVMKV YSKEDYSVVN RFESHGGGWG YSAHSVEAIR
FSSDTDILLG GLGLFGGRGE YTAKIKLFEL GPDGGDHETD GDLLAETDVL AYDCAAREKY
AMMFDEPVLL QAGWWYVAWA RVSGPSSDCG SHGQASITTD DGVVFQFKSS KKSNNGTDVN
AGQIPQLLYR LPTSDGSASK GKQQTSEPVH ILKRSFARTV SVECFESLLS ILHWSWTTLV
LGVEELRGLK GFQFTATLLD LERLRFVGTC CLRLLRVYTC EIYPVSATGK AVVEETSKLA
ECIGKTRTLL RKILSEGVDH CMVKLDNDPQ GYLSQPLSLL EAVLQECHNT FTACFHSFYP
TPALQWACLC DLLNCLDQDI QEANFKTSSS RLLAAVMSAL CHTSVKLTSI FPIAYDGEVL
LRSIVKQVST ENDSTLVHRF PLLVAHMEKL SQSEENISGM TSFREVLEKM LVIVVLPVRN
SLRRENELFS SLLVSNTCGL LASIVSELTA SALGSEVDAL NSLHSVKASA NRFTKTSQGR
SWNTGNGSPD AICFSVDKPG IVVVGFSVYG GGGIHEYELE VLVDDSEHVG DSTHSHRWTS
LELVKGTYTT DDSPSDIAEI RLDKVVPLKE NVKYAVRLRN YGSRTANGDG GMTTVQCPDG
VTFTFSTCSL SSNGTNQTRG QIPQILYYRS EFDGDLQSQL LSKANEEDKN CSRALSVVST
VVRAAKDLLH RALAVDADDI PELLSSSSLF SMLLPLIIAY IGPVAAAIPK VAVEVFGLVQ
QLLPSVAILN QKYAPPAFNP NQSTDSTTGN QPEQGLSACT TSNHYAVIES EHPYKPACVM
HYKVTFPECV RWMTIEFDPQ CGTAQSEDVL RLLIPVRTVQ NSGYGPKLTS VHENLNSWIE
LKKFAGSSGW PSMVLVLPGN EALFSLETAS DYVKDDKASF YGFKCFAIGY EFSPGPDEGV
IQLEKELANL GGVCAAALMK KDLALPIGNE LEEDLEILEE AALQVCKTHS GILGKGLALS
HSPTILEALE GNLPLQIQSN EQSFLDDFIA CVPGSSGGRL ARWLQPDSYA DPQKTSLILN
KDDIRCGWPT TITVQTKDQY GDVVHVPNMK VEVKAVPVSQ KKTSLQQEQV KKSQRIPGSP
AVTAASSNTD MTFGGLASPK LDVSYEPMIV KEARYIAITM MKVYENYSFE ELRFASPTPK
RPSENMLIRV NNDGSYCANW TPGAIGLYTI HVTIDGIEID AGLEVKVKDP PKGMVPPGTQ
LVKPKAEPQP NKVRKFVAKD SAGLRIRSHP SLQSEQIGIV KVNGTITFID EIHNDDGVWL
RLNDETIKKY VPNMNGYTEA WCLSFNQHLG KSLLVPVDNI FNASQGVRDL DVFSWTSKAF
FPQEPKTNTD DFFKDINSCC SQEATMQEQD MPFLRGGPGM YKVVKTGPSG HNIRSCPNLR
GIPIGMLVLG NKVKAVGEVT NSEGTWVQLD KNSMVEFCES DEGEAWSLAR DRGGNQYLRH
EDEQVLLDQN SQTPPPSPFS VQAFNKGASC SAQGFDYGLG NNKGDRGNVS TSSRPVSTSG
KSELSSKHSR SLKPDGRMSR TATDQKKPRG TEGLSASESL MLKSDAAKLR SDSHSRSLSP
NHNTLQTLKS EGRMSSSLRA ESPGPGSRSS SPKPKTLPAS RSSPPGAGSP RSSSPHDKNL
PQKSAAPVKT KLDPPRERSK SDSYTLDPDT LRKKKMPLTE PLRGRSTSPK PKSVPKDSKG
SPGSENRAPS PHVVQENLHS EVVEVCTSST LKTNSLTDST CDESSEFKSV DEGSNKVHFS
IGKAPLKDEQ EMRASPKISR KCANRHTRLK KEKSSFLFKG DGSKPLEPAK QAMSPSVAEC
ARAVFASFLW HEGIVHDAMA CSSFLKFNPE LSKEHAPIRS SLNSQQPTEE KETKLKNRHS
LEISSALNMF NIAPHGPDIS KMGSINKNKV LSMLKEPPLH EKCEDGKAET TFEMSMHHTM
KSKSPLPLTL QHLVAFWEDI SLATIKAASQ NMIFPSPGSC AVLKKKECEK ENKKAKKEKK
KKEKAEVRPR GNLFGEMAQL AVGGPEKDTV CELCGESHPY PVTYHMRQAH PGCGRYAGGQ
GYNSIGHFCG GWAGNCGDGG IGGSTWYLVC DRCREKYLRE KQAAAREKVK QSRRKPMQVK
TPRALPTMEA HQVIKANALF LLSLSSAAEP SILCYHPTKP FPSQLPSVKE GISEDLPVKM
PCLYLQTLAR HHHENLVGYQ DDNLFQDEMR YLRSTSVPAP YISVTPDASP NVFEEPESNM
KSMPPSLETS PITDTDLAKR TVFQRSYSVV ASEYDKQHSI LPARVKAIPR RRVNSGDTEV
GSSLLRHPSP ELSRLISAHS SLSKGERNFQ WPVLAFVIQH HDLEGLEIAM KQALRKSACR
VFAMEAFNWL LCNVIQTTSL HDILWHFVAS LTPAPVEPEE EEDEENKTNK ENTEQEKDTR
VCEHPLSDIV IAGEAAHPLP HTFHRLLQTI SDLMMSLPGG SSLQQMALRC WSLKFKQSDH
QFLHQSNVFH HINNILSKSD DGDSEESFSI SIQSGFEAMS QELCIVMCLK DLTSIVDIKT
SSRPAMIGSL TDGSTETFWE SGDEDKNKTK NITINCVKGI NARYVSVHVD NSRDLGNKVT
SMTFLTGKAV EDLCRIKQVD LDSRHIGWVT SELPGGDNHI IKIELKGPEN TLRVRQVKVL
GWKDGESTKI AGQISASVAQ QRNCEAETLR VFRLITSQVF GKLISGDAEP TPEQEEKALL
SSPEGEEKVY NATSDADLKE HMVGIIFSRS KLTNLQKQVC AHIVQAIRME ATRVREEWEH
AISSKENANS QPNDEDASSD AYCFELLSMV LALSGSNVGR QYLAQQLTLL QDLFSLLHTA
SPRVQRQVTS LLRRVLPEVT PSRLASIIGV KSLPPADISD IIHSTEKGDW NKLGILDMFL
GCIAKALTVQ LKAKGTTITG TAGTTAGKGV TTVTLPMIFN SSYIRRGESH WWLKGSTPTQ
ISEIIIKLIK DMAAGHLSEA WSRVTKNAIA ETIIALTKME EEFRSPVRCI ATTRLWLALA
SLCVLDQDHV DRLSSGRWMG KDGQQKQMPM CDNHDDGETA AIILCNICGN LCTDCDRFLH
LHRRTKTHHR QVFKEEEEAI KVDLHEGCGR TKLFWLMALA DSKTMKAMVE FREHTGKPTT
SSSEACRFCG SRSGTELSAV GSVCSDADCQ EYAKIACSKT HPCGHPCGGV KNEEHCLPCL
HGCDKHATTL KQDADDMCMI CFTEALSAAP AIQLDCSHIF HLQCCRRVLE NRWLGPRITF
GFISCPICKN KINHIVLKDL LDPIKELYED VRRKALMRLE YEGLHKSEAI TTPGVRFYND
PAGYAMNRYA YYVCYKCRKA YFGGEARCDA EAGQGDDYDP RELICGACSD VSRAQMCPKH
GTDFLEYKCR YCCSVAVFFC FGTTHFCNAC HDDFQRMTSI PKEELPHCPA GPKGKQLEGT
ECPLHVVHPP TGEEFALGCG VCRNAHTF
//
