ID A0A087RCK5_APTFO Unreviewed; 1568 AA.
AC A0A087RCK5;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
DE Flags: Fragment;
GN ORFNames=AS27_04100 {ECO:0000313|EMBL:KFM11209.1};
OS Aptenodytes forsteri (Emperor penguin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Sphenisciformes; Spheniscidae;
OC Aptenodytes.
OX NCBI_TaxID=9233 {ECO:0000313|EMBL:KFM11209.1, ECO:0000313|Proteomes:UP000053286};
RN [1] {ECO:0000313|EMBL:KFM11209.1, ECO:0000313|Proteomes:UP000053286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_AS27 {ECO:0000313|EMBL:KFM11209.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) 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=2.3.2.26; Evidence={ECO:0000256|ARBA:ARBA00000885};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KL226294; KFM11209.1; -; Genomic_DNA.
DR STRING; 9233.A0A087RCK5; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000053286; Unassembled WGS sequence.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd08691; C2_NEDL1-like; 1.
DR CDD; cd00078; HECTc; 1.
DR CDD; cd00201; WW; 2.
DR Gene3D; 2.20.70.10; -; 2.
DR Gene3D; 2.60.40.2840; -; 1.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR Gene3D; 3.30.2160.10; Hect, E3 ligase catalytic domain; 1.
DR Gene3D; 3.30.2410.10; Hect, E3 ligase catalytic domain; 1.
DR Gene3D; 3.90.1750.10; Hect, E3 ligase catalytic domains; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR037795; C2_HECW.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR040524; HECW1_helix.
DR InterPro; IPR032348; HECW_N.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR PANTHER; PTHR11254:SF127; E3 UBIQUITIN-PROTEIN LIGASE HECW2; 1.
DR PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF18436; HECW1_helix; 1.
DR Pfam; PF16562; HECW_N; 1.
DR Pfam; PF00397; WW; 1.
DR SMART; SM00239; C2; 1.
DR SMART; SM00119; HECTc; 1.
DR SMART; SM00456; WW; 2.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR SUPFAM; SSF51045; WW domain; 2.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS50237; HECT; 1.
DR PROSITE; PS01159; WW_DOMAIN_1; 2.
DR PROSITE; PS50020; WW_DOMAIN_2; 2.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000053286};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 169..300
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 803..836
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 981..1014
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 1233..1568
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 338..456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 508..763
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1020..1061
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1157..1183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..416
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..542
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..563
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 603..629
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 643..659
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 670..684
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 698..712
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 742..757
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1159..1177
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1536
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFM11209.1"
FT NON_TER 1568
FT /evidence="ECO:0000313|EMBL:KFM11209.1"
SQ SEQUENCE 1568 AA; 176224 MW; DF4616B703406A65 CRC64;
EMASSAREHL LFVRRRNPQL RYTLSPENLQ SLASQGTMAE NMNLQRANSD TDLVTSDSRS
SLTASMYEYT LGQSQNLIIF WDIKEEVDPT DWIGLYHIDE NSPANFWDSK NRGVTGTQKG
QIVWRIEPGP YFMESEIKIC FKYYHGVSGA LRATTPCITV KNPAVMMGVE GTDEGASGAQ
HSRKLVSFTL SDIRAVGLKK GMFFNPDPYL KMSIQPGKKS TFPTFAHHGQ ERRSTIISNT
TNPVWHREKH SFVALLTDVL EIEVKDKFAK SRPIIKRFLG KLTIPVQRLL ERHAIGDQVL
SYNLGRRLPA DHVSGYLQFK VEITSSVHED ASPETVGTLL GVNSVNGDLG SPSDDEDMPA
GHHDTSTVCS NGPVLEESSG EAILRHPLRT STTLETDQDE LTSGASRSSP TRGRQDSLND
YLDAIEHNNH PRPGTSACGE RPRGASPKLR SSFPTDTRLN AMLHIDSDEE EHELHQDLGF
PSSLEDDGGL VMFNGATRNV ERNGLSYSSD QVMQGPSENE NVSASEAPFP STDDQQETLP
ELPPSQLEGG ESLQGSQSEA PADQAGRESC AAQEAEQPPT SADAGAADAA AGSRRGVSEM
ESIDQGSEPS QMSSETEQSD PARTESVSEA STRPEGESDV EGADSSCNES ATVRRSSVEM
RCSFESARFP ETPAFSSQEE EEGASATSAA RIEPDAEAQD SASTSGSLPA VQLPQEEVQE
AEAGELQDQE EAEEIWQRRS SLQVAAADSQ SQDEETEGAQ AACEGATAQV EGATGGSQPN
GHQPLRSLPS VRQDVSRYQR VDEALPPNWE ARIDSHGRIF YVDHVNRTTT WQRPTAPPAP
QILQRSNSIQ QMEQLNRRYQ SIRRTMTNDR PEEHTNAVDG AGEETDFHHS NADFRRENVL
PHSTSRSRLT LLLQSPPVKF LISPEFFTVL HSNPSAYRMF TNNTCLKHMI TKVRRDTHHF
ERYQHNRDLV GFLNMFANKQ LELPRGWEMK HDHQGKAFFV DHNSRTTTFI DPRLPLQSSR
PTSALVHRQH LTRQRSHSAG EVGEDSRHSG PPVLPRPSST FNTVSRAQYQ DVVPVAYNDK
IVAFLRQPNI FEILQERQPD LTRNHSLREK IQFIRTEGTP GLVRLSSDAD LVMLLSLFEE
EIMSYVPPHA LLHPSYCQSP RGSPVSSPQN SPGTQRANAR APAPYKRDFE AKLRNFYRKL
ETKGYGQGPG KLKLIIRRDH LLEDAFNQIM GYSRKDLQRN KLYVTFVGEE GLDYSGPSRE
FFFLVSRELF NPYYGLFEYS ANDTYTVQIS PMSAFVDNHH EWFRFSGRIL GLALIHQYLL
DAFFTRPFYK ALLRILCDLS DLEYLDEEFH QSLQWMKDND IHDILDLTFT VNEEVFGQIT
ERELKPGGAN IPVTEKNKKE YIERMVKWRI ERGVVQQTES LVRGFYEVVD ARLVSVFDAR
ELELVIAGTA EIDLSDWRNN TEYRGGYHDN HIVIRWFWAA VERFNNEQRL RLLQFVTGTS
SIPYEGFASL RGSNGPRRFC VEKWGKITAL PRAHTCFNRL DLPPYPSFSM LYEKLLTAVE
ETSTFGLE
//
