ID A0A1D2NCR1_ORCCI Unreviewed; 1058 AA.
AC A0A1D2NCR1;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Putative E3 ubiquitin-protein ligase HERC4 {ECO:0000313|EMBL:ODN02865.1};
GN ORFNames=Ocin01_03807 {ECO:0000313|EMBL:ODN02865.1};
OS Orchesella cincta (Springtail) (Podura cincta).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Collembola;
OC Entomobryomorpha; Entomobryoidea; Orchesellidae; Orchesellinae; Orchesella.
OX NCBI_TaxID=48709 {ECO:0000313|EMBL:ODN02865.1, ECO:0000313|Proteomes:UP000094527};
RN [1] {ECO:0000313|EMBL:ODN02865.1, ECO:0000313|Proteomes:UP000094527}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Mixed pool {ECO:0000313|EMBL:ODN02865.1};
RX PubMed=27289101; DOI=10.1093/gbe/evw134;
RA Faddeeva-Vakhrusheva A., Derks M.F., Anvar S.Y., Agamennone V., Suring W.,
RA Smit S., van Straalen N.M., Roelofs D.;
RT "Gene Family Evolution Reflects Adaptation to Soil Environmental Stressors
RT in the Genome of the Collembolan Orchesella cincta.";
RL Genome Biol. Evol. 8:2106-2117(2016).
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:ODN02865.1}.
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DR EMBL; LJIJ01000093; ODN02865.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1D2NCR1; -.
DR STRING; 48709.A0A1D2NCR1; -.
DR OMA; FKSQACW; -.
DR OrthoDB; 5475808at2759; -.
DR Proteomes; UP000094527; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0000209; P:protein polyubiquitination; IEA:InterPro.
DR GO; GO:0009966; P:regulation of signal transduction; IEA:UniProt.
DR CDD; cd00078; HECTc; 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 Gene3D; 2.130.10.30; Regulator of chromosome condensation 1/beta-lactamase-inhibitor protein II; 2.
DR InterPro; IPR044611; E3A/B/C-like.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR009091; RCC1/BLIP-II.
DR InterPro; IPR000408; Reg_chr_condens.
DR PANTHER; PTHR45700:SF8; HECT DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR45700; UBIQUITIN-PROTEIN LIGASE E3C; 1.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF00415; RCC1; 5.
DR Pfam; PF13540; RCC1_2; 1.
DR PRINTS; PR00633; RCCNDNSATION.
DR SMART; SM00119; HECTc; 1.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR SUPFAM; SSF50985; RCC1/BLIP-II; 1.
DR PROSITE; PS50237; HECT; 1.
DR PROSITE; PS00626; RCC1_2; 4.
DR PROSITE; PS50012; RCC1_3; 7.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000094527};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT TRANSMEM 795..818
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REPEAT 41..92
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 93..142
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 143..198
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 199..252
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 253..304
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 305..355
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 355..404
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT DOMAIN 732..1058
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1026
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 1058 AA; 118663 MW; 9009D8BC11CD2310 CRC64;
MESQEMMDTS ENHILKNSQS ELEQHQQSDT DSDETNSSTR KCILGWGSTV NGELGLGGIE
EDSVDTPTKI KFTRKIKSVA CGESHTVFIL EDGTLWSCGC NDHGQLGHDK CRTRPEQVEE
FSGRQIVSVS AGYAHNLAID SWGTLFSWGS NSHGQLGQQL ETTDDKLVNR PKIVKSMATK
TVVQVAAGFF HSVVLTNSGE IYTCGSNSHG QLGLGYANGP NQTKFCLVEL LVGLPTIMVT
AGGFHSFALS VSGSVFGWGK NNSGQLGVGD TDDKCQPTQL ATLRSLGVTY ITAGADHTAF
LTQDGGLFSA GHGTYGQLGH GSSSNEVLPR KILEFGRVVT QVACGRCHTL CWTNDKLYTF
GLNSSGQLGI SGGNRNTPFH VKTLSCVVNS IYAGGDHSIV LVDPVEVNAF ETSVPNAQPA
LSVDYRESAT EKAILTITED FVTQMCSSSE PVDQDIMTLT EILFAAPACW NASFLLPDRE
HAPCTWKNMG VNLDLAESVL SKLASIKAEG LKELIEQQLY MEMLPKLPHQ LKHVEILRVY
VLLPLIPNFY SGGSTMLPII YADRLQSLAP QLVSVVTRWI YHSPMEHLLR IIAVYKKTRD
NGLRICLNFL SLLNSMNKSR MRISYHTFTI PQLASKVDIR MDYYNWLQRK TQSRAVFLCD
FPFVFDAQAK TLLLQTDQLL QMQSAMSKAQ TQLMSFFIFP QMVDPNEVQY LTLTVSRDSI
VQDVMNQIYQ LNTHDLKKPL KVKFIDEEAE DAGGVKKEFF LLLIREILDP KYGMFKHYEE
SRLIWFNEAS FEDDVMYFLI GLLCGLAIYN LIIINIPFPL PLYKKLLNEK IELTDLKELS
PREGKSLEQI MEYSEPDFEE VFQLNFELTR EEFGAVKVVP LKPDGSNLPV TLENKSEFVD
LYVSYVFNVS VNKQFDAFKK GFERVCGSTV LQLFHAQELQ AMVTGNEDYD WGELERNCSY
KGGYNVNEST IKIFWDVFHS LSLAEKKQFL LFLTGSDRIP ILGMKTLKMC IQPTADERYL
PVAHTCFNLL DLPRYQTRER LKYKLLQAIQ QNQGFSLV
//
