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Database: UniProt
Entry: A0A2G8KLL2_STIJA
LinkDB: A0A2G8KLL2_STIJA
Original site: A0A2G8KLL2_STIJA 
ID   A0A2G8KLL2_STIJA        Unreviewed;      1420 AA.
AC   A0A2G8KLL2;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN   ORFNames=BSL78_14324 {ECO:0000313|EMBL:PIK48828.1};
OS   Stichopus japonicus (Sea cucumber).
OC   Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Holothuroidea;
OC   Aspidochirotacea; Aspidochirotida; Stichopodidae; Apostichopus.
OX   NCBI_TaxID=307972 {ECO:0000313|EMBL:PIK48828.1, ECO:0000313|Proteomes:UP000230750};
RN   [1] {ECO:0000313|EMBL:PIK48828.1, ECO:0000313|Proteomes:UP000230750}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Shaxun {ECO:0000313|EMBL:PIK48828.1};
RC   TISSUE=Muscle {ECO:0000313|EMBL:PIK48828.1};
RX   PubMed=29023486;
RA   Zhang X., Sun L., Yuan J., Sun Y., Gao Y., Zhang L., Li S., Dai H.,
RA   Hamel J.F., Liu C., Yu Y., Liu S., Lin W., Guo K., Jin S., Xu P.,
RA   Storey K.B., Huan P., Zhang T., Zhou Y., Zhang J., Lin C., Li X., Xing L.,
RA   Huo D., Sun M., Wang L., Mercier A., Li F., Yang H., Xiang J.;
RT   "The sea cucumber genome provides insights into morphological evolution and
RT   visceral regeneration.";
RL   PLoS Biol. 15:E2003790-E2003790(2017).
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   -!- 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:PIK48828.1}.
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DR   EMBL; MRZV01000500; PIK48828.1; -; Genomic_DNA.
DR   STRING; 307972.A0A2G8KLL2; -.
DR   Proteomes; UP000230750; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR   CDD; cd11709; SPRY; 1.
DR   Gene3D; 2.60.120.920; -; 2.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR043136; B30.2/SPRY_sf.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR045129; RNF123/RSPRY1-like.
DR   InterPro; IPR003877; SPRY_dom.
DR   PANTHER; PTHR13363:SF5; E3 UBIQUITIN-PROTEIN LIGASE RNF123; 1.
DR   PANTHER; PTHR13363; RING FINGER AND SRY DOMAIN-CONTAINING; 1.
DR   Pfam; PF00622; SPRY; 1.
DR   SUPFAM; SSF48371; ARM repeat; 2.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000230750};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1040..1063
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1002..1168
FT                   /note="SPRY"
FT                   /evidence="ECO:0000259|Pfam:PF00622"
FT   REGION          768..813
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1195..1239
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1400..1420
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        790..810
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1209..1236
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1406..1420
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1420 AA;  157281 MW;  CF1D76CEC4E262B8 CRC64;
     MAPSPGRNNA AIAFAALSAS GGALFAFYIY KRVRELRSQQ FPNRIATAIS NEQLAVLAKS
     SNVSLRQSAE QMLLDRILES EAFAEVVQGC YSKDENKLYQ ACSVFCVVLK SVNFSVPLSL
     SQIVKLLTSC LQRSLDRESD SEAKSRDSIF SVKIQRMTLA TICDFLSDSI NRKDVLVSSC
     PDIIPVCIRL VKEGKNKEVL RYSVLLLFQI AGLGTTQEVR EAGAIPVLAS RIITFHGDQI
     MQRITLQTIV VLIGSVDDSK SLCAEIAKPM VLMPVVSSCI SDDVELSFWS LALIQDFVNN
     ASFLKDLTEN TALLQTVSES LKNRNDLVVN YCIRFFKILM QGGHSVIEKL LNISDYSILK
     GLLHVAKEGQ IENKVLMTEL LTEFVMSEKF VSRIVQNGGL DIVKVLAKPN NEDNLSFFSS
     AMLIDMAMIS DEVKGQLAKM YVLPTIYDWI KNAKNEKVAV FATKTLVMLH LIEDLVKISI
     NADGKTTQID VGDVHFTDTQ HSSLRIFHWD SLFVNEITIV PIKKKALAST KDQISIQVSR
     FDSLSAKNSG EVVFVTLCGT EGSKYVQGLL KYMQMKKDDQ DRCLNLAEDD IAVLIAEVDN
     DGCLNLKKMS IASSETEASH SIRYKELFQR RTFSQILPLI MDPLNQKYSQ DGCPLKKKAL
     EVLNVLLCLE DYLNMFISSP TAVSNLLMAL QDSSSNGLTV LQSIIGVLVT LATFESGRSH
     LISLGAPLVL VNFINHQRDR LVTDLSGSPK GDVFDIDVAP VPPSVAAIIN SLPPRPQSRA
     EPRPLRTDDG SVNATDNRSQ ASSSSTNGPL PVIPEDGYIA PEAGETAEAV RLNSLSGLIE
     EAVSSAVEVL KNENRKGDNS NTTGPTTSVI IQNAVSCLAK ILSGKMNHSE NDGKYKEFAT
     SLRTSGTVYT LWSYLLTSKD DLKALQVPVT NSITILSETI ATDDTAFDAK VRFDRKDVTR
     TMFMSTDDLE VLNYNWTFES VRANVGVSQP SNPSPSDHPK GWYYQMELFS DGLIQVGWCS
     EQCQYSPQKG NFDENNFLKI SFSVLTIIYL FVYICYTWVH LVFQIQIYRK TVICLWHRHR
     DDYHSTPLMA SGKKWHGPVA EQTEENAYGE LWKSGDIVTC LLDCYGNISY HHNGKNLGVA
     FAAINMQVCW YPACSVCTDQ WARFNFGDDP VRFPESIPEG FVPISYYKHP PQDAVSNTNQ
     PLIDSGDEPA TSNEKEETAE SFDEENTKEV KEGAVKGQPE AGDSAANIVL PLEGARSISA
     DYLPSLYFEI KLDSNDARPV SLGFNTLNFT DQVTAVIKDS EIVLPDLSIK QVSVERSVVI
     GCGYVASTNH VFFTIDGQAI EVFFEFAGGH VTIPVMPCLS SSRYYVNFGQ RDFQFKIPNT
     EEYFKGAIST CVKFLSSCLS PDSEESEPNG NKKELNPLEY
//
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