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Database: UniProt
Entry: A0A2Y9QGJ7_TRIMA
LinkDB: A0A2Y9QGJ7_TRIMA
Original site: A0A2Y9QGJ7_TRIMA 
ID   A0A2Y9QGJ7_TRIMA        Unreviewed;      4603 AA.
AC   A0A2Y9QGJ7;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
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_023582480.1};
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_023582480.1};
RN   [1] {ECO:0000313|RefSeq:XP_023582480.1}
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_023582480.1; XM_023726712.1.
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; 2.
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   Pfam; PF13540; RCC1_2; 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; 2.
DR   PROSITE; PS50012; RCC1_3; 3.
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          601..656
FT                   /note="RCC1"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT   REPEAT          959..1009
FT                   /note="RCC1"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT   REPEAT          1010..1067
FT                   /note="RCC1"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT   REPEAT          2341..2434
FT                   /note="Filamin"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00087"
FT   DOMAIN          3643..3821
FT                   /note="DOC"
FT                   /evidence="ECO:0000259|PROSITE:PS51284"
FT   DOMAIN          4353..4404
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          87..127
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          170..192
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          898..928
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2634..2854
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2991..3010
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3530..3554
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3841..3861
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        102..121
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        908..924
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2639..2660
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2661..2682
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2708..2775
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2785..2815
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2826..2848
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        3844..3858
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   4603 AA;  505260 MW;  8FC83ED1F0714748 CRC64;
     MMMCSATASP AVVSSGPGGD GFFPAATISS SPAPGAPFMP VSEGSGAAAG LGLGLPAADS
     RGNYQLLLSG RALADRYRRI YTAALSDRDQ GGSSAGHPAS RNKKILNKKK LKRKQKSKSK
     VKTRSKSENL ENTVIIPDIK LHSNPSAFNI YCNVRHCVLE WQKKETSLAA ASKNSVQSGE
     SDSDEEEESK EPPIKLPKII EVGLCEVFEL IKETRFSHPS LCLRSLQALL NVLQGQQPEG
     LQSEPPEVLE SLFQLLLEIT VRSTGMNDST GQSLTALSCA CLFSLVASWG ETGRTLQAIS
     AILTNNGSHA CQTIQVPTIL NSLQRSVQAV LVGKVQIQDW FSNGIKKAAL MHKWPLKEIS
     VDEDDQCLLQ NDGFFLYLLC KDGLYKIGSG YSGTVRGHIY NSTSRIRNRK EKKSWLGYAQ
     GYLLYRDVSN HSMTAIRISP ETLEQDGTVM LPDCHTEGQN ILFTDGEYIN QIAASRDDGF
     VVRIFATSTE PVLQQELQLK LARKCLHACG ISLFDLEKDL HIISTGFDEE SAILGAGREF
     ALMKTASGKI YYTGKYQSLG IKQGGPSAGK WVELPITKSP KIVHFSVGHD GSHALLVAED
     GSIFFTGSAS KGEDGESTKS RRQSKPYKPK KIIKMEGKIV VYTACNNGSS SVISKDGELY
     MFGKDAIYSD SSSLVTDLKG HFVIQVAMGK AHTCVLMKNG EVWTFGVNNK GQCGRDTGAM
     NQGGKGFGVE NMATAMDEDL EEELDEKDEK SMMCPPGMHK WKLEQCMVCT VCGDCTGYGA
     SCVSSGRPDR VPGGICGCGS GESGCAVCGC CKACARELDG QEARQRGILD AVKEMIPLDL
     LLAVPVPGVN IEEHLQLRQE EKRQRVIRRH RLEEGRGPLV FAGPIFMNHR EQALARLRSH
     PAQLKHKRDK HKDGSGERGE KDASKITTYP PGSVRFDCEL RAVQVSCGFH HSVVLMENGD
     VYTFGYGQHG QLGHGDVNSR GCPTLVQALP GPSTQVTAGS NHTAVLLMDG QVFTFGSFSK
     GQLGRPILDV PYWNAKPAPM PNIGSKYGRK ATWIGASGDQ TFLRIDEALI NSHVLATSEI
     FASKHIIGLV PASISEPPPF KCLLINKVDG SCKTFNDSEQ EDLQGFGVCL DPVYDVIWRF
     RPNTRELWCY NAVVADARLP SAADMQSRCS ILSPELALPT GSRALTTRSH AALHILGCLD
     TLAAMQDLKM GVASTEEETQ AVMKVYSKED YSVVNRFESH GGGWGYSAHS VEAIRFSSDT
     DILLGGLGLF GGRGEYTAKI KLFELGPDGG DHETDGDLLA ETDVLAYDCA AREKYAMMFD
     EPVLLQAGWW YVAWARVSGP SSDCGSHGQA SITTDDGVVF QFKSSKKSNN GTDVNAGQIP
     QLLYRLPTSD GSASKGKQQT SEPVHILKRS FARTVSVECF ESLLSILHWS WTTLVLGVEE
     LRGLKGFQFT ATLLDLERLR FVGTCCLRLL RVYTCEIYPV SATGKAVVEE TSKLAECIGK
     TRTLLRKILS EGVDHCMVKL DNDPQGYLSQ PLSLLEAVLQ ECHNTFTACF HSFYPTPALQ
     WACLCDLLNC LDQDIQEANF KTSSSRLLAA VMSALCHTSV KLTSIFPIAY DGEVLLRSIV
     KQVSTENDST LVHRFPLLVA HMEKLSQSEE NISGMTSFRE VLEKMLVIVV LPVRNSLRRE
     NELFSSLLVS NTCGLLASIV SELTASALGS EVDALNSLHS VKASANRFTK TSQGRSWNTG
     NGSPDAICFS VDKPGIVVVG FSVYGGGGIH EYELEVLVDD SEHVGDSTHS HRWTSLELVK
     GTYTTDDSPS DIAEIRLDKV VPLKENVKYA VRLRNYGSRT ANGDGGMTTV QCPDGVTFTF
     STCSLSSNGT NQTRGQIPQI LYYRSEFDGD LQSQLLSKAN EEDKNCSRAL SVVSTVVRAA
     KDLLHRALAV DADDIPELLS SSSLFSMLLP LIIAYIGPVA AAIPKVAVEV FGLVQQLLPS
     VAILNQKYAP PAFNPNQSTD STTGNQPEQG LSACTTSNHY AVIESEHPYK PACVMHYKVT
     FPECVRWMTI EFDPQCGTAQ SEDVLRLLIP VRTVQNSGYG PKLTSVHENL NSWIELKKFA
     GSSGWPSMVL VLPGNEALFS LETASDYVKD DKASFYGFKC FAIGYEFSPG PDEGVIQLEK
     ELANLGGVCA AALMKKDLAL PIGNELEEDL EILEEAALQV CKTHSGILGK GLALSHSPTI
     LEALEGNLPL QIQSNEQSFL DDFIACVPGS SGGRLARWLQ PDSYADPQKT SLILNKDDIR
     CGWPTTITVQ TKDQYGDVVH VPNMKVEVKA VPVSQKKTSL QQEQVKKSQR IPGSPAVTAA
     SSNTDMTFGG LASPKLDVSY EPMIVKEARY IAITMMKVYE NYSFEELRFA SPTPKRPSEN
     MLIRVNNDGS YCANWTPGAI GLYTIHVTID GIEIDAGLEV KVKDPPKGMV PPGTQLVKPK
     AEPQPNKVRK FVAKDSAGLR IRSHPSLQSE QIGIVKVNGT ITFIDEIHND DGVWLRLNDE
     TIKKYVPNMN GYTEAWCLSF NQHLGKSLLV PVDVTNSEGT WVQLDKNSMV EFCESDEGEA
     WSLARDRGGN QYLRHEDEQV LLDQNSQTPP PSPFSVQAFN KGASCSAQGF DYGLGNNKGD
     RGNVSTSSRP VSTSGKSELS SKHSRSLKPD GRMSRTATDQ KKPRGTEGLS ASESLMLKSD
     AAKLRSDSHS RSLSPNHNTL QTLKSEGRMS SSLRAESPGP GSRSSSPKPK TLPASRSSPP
     GAGSPRSSSP HDKNLPQKSA APVKTKLDPP RERSKSDSYT LDPDTLRKKK MPLTEPLRGR
     STSPKPKSVP KDSKGSPGSE NRAPSPHVVQ ENLHSEVVEV CTSSTLKTNS LTDSTCDESS
     EFKSVDEGSN KVHFSIGKAP LKDEQEMRAS PKISRKCANR HTRLKKEKSS FLFKGDGSKP
     LEPAKQAMSP SVAECARAVF ASFLWHEGIV HDAMACSSFL KFNPELSKEH APIRSSLNSQ
     QPTEEKETKL KNRHSLEISS ALNMFNIAPH GPDISKMGSI NKNKVLSMLK EPPLHEKCED
     GKAETTFEMS MHHTMKSKSP LPLTLQHLVA FWEDISLATI KAASQNMIFP SPGSCAVLKK
     KECEKENKKA KKEKKKKEKA EVRPRGNLFG EMAQLAVGGP EKDTVCELCG ESHPYPVTYH
     MRQAHPGCGR YAGGQGYNSI GHFCGGWAGN CGDGGIGGST WYLVCDRCRE KYLREKQAAA
     REKVKQSRRK PMQVKTPRAL PTMEAHQVIK ANALFLLSLS SAAEPSILCY HPTKPFPSQL
     PSVKEGISED LPVKMPCLYL QTLARHHHEN LVGYQDDNLF QDEMRYLRST SVPAPYISVT
     PDASPNVFEE PESNMKSMPP SLETSPITDT DLAKRTVFQR SYSVVASEYD KQHSILPARV
     KAIPRRRVNS GDTEVGSSLL RHPSPELSRL ISAHSSLSKG ERNFQWPVLA FVIQHHDLEG
     LEIAMKQALR KSACRVFAME AFNWLLCNVI QTTSLHDILW HFVASLTPAP VEPEEEEDEE
     NKTNKENTEQ EKDTRVCEHP LSDIVIAGEA AHPLPHTFHR LLQTISDLMM SLPGGSSLQQ
     MALRCWSLKF KQSDHQFLHQ SNVFHHINNI LSKSDDGDSE ESFSISIQSG FEAMSQELCI
     VMCLKDLTSI VDIKTSSRPA MIGSLTDGST ETFWESGDED KNKTKNITIN CVKGINARYV
     SVHVDNSRDL GNKVTSMTFL TGKAVEDLCR IKQVDLDSRH IGWVTSELPG GDNHIIKIEL
     KGPENTLRVR QVKVLGWKDG ESTKIAGQIS ASVAQQRNCE AETLRVFRLI TSQVFGKLIS
     GDAEPTPEQE EKALLSSPEG EEKVYNATSD ADLKEHMVGI IFSRSKLTNL QKQVCAHIVQ
     AIRMEATRVR EEWEHAISSK ENANSQPNDE DASSDAYCFE LLSMVLALSG SNVGRQYLAQ
     QLTLLQDLFS LLHTASPRVQ RQVTSLLRRV LPEVTPSRLA SIIGVKSLPP ADISDIIHST
     EKGDWNKLGI LDMFLGCIAK ALTVQLKAKG TTITGTAGTT AGKGVTTVTL PMIFNSSYIR
     RGESHWWLKG STPTQISEII IKLIKDMAAG HLSEAWSRVT KNAIAETIIA LTKMEEEFRS
     PVRCIATTRL WLALASLCVL DQDHVDRLSS GRWMGKDGQQ KQMPMCDNHD DGETAAIILC
     NICGNLCTDC DRFLHLHRRT KTHHRQVFKE EEEAIKVDLH EGCGRTKLFW LMALADSKTM
     KAMVEFREHT GKPTTSSSEA CRFCGSRSGT ELSAVGSVCS DADCQEYAKI ACSKTHPCGH
     PCGGVKNEEH CLPCLHGCDK HATTLKQDAD DMCMICFTEA LSAAPAIQLD CSHIFHLQCC
     RRVLENRWLG PRITFGFISC PICKNKINHI VLKDLLDPIK ELYEDVRRKA LMRLEYEGLH
     KSEAITTPGV RFYNDPAGYA MNRYAYYVCY KCRKAYFGGE ARCDAEAGQG DDYDPRELIC
     GACSDVSRAQ MCPKHGTDFL EYKCRYCCSV AVFFCFGTTH FCNACHDDFQ RMTSIPKEEL
     PHCPAGPKGK QLEGTECPLH VVHPPTGEEF ALGCGVCRNA HTF
//
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