ID A0A183LFS1_9TREM Unreviewed; 1601 AA.
AC A0A183LFS1;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=SMRZ_LOCUS2646 {ECO:0000313|EMBL:VDO55599.1};
OS Schistosoma margrebowiei.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=48269 {ECO:0000313|WBParaSite:SMRZ_0000264501-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:SMRZ_0000264501-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDO55599.1, ECO:0000313|Proteomes:UP000277204}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Zambia {ECO:0000313|EMBL:VDO55599.1,
RC ECO:0000313|Proteomes:UP000277204};
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the BRE1 family.
CC {ECO:0000256|ARBA:ARBA00005555}.
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DR EMBL; UZAI01000684; VDO55599.1; -; Genomic_DNA.
DR STRING; 48269.A0A183LFS1; -.
DR WBParaSite; SMRZ_0000264501-mRNA-1; SMRZ_0000264501-mRNA-1; SMRZ_0000264501.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000277204; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR013956; E3_ubiquit_lig_Bre1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR23163:SF0; E3 UBIQUITIN-PROTEIN LIGASE BRE1; 1.
DR PANTHER; PTHR23163; RING FINGER PROTEIN-RELATED; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000277204};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 1..223
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 1548..1587
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 697..733
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1067..1164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1237..1298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 549..576
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 798..832
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 859..893
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 919..960
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1007..1048
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1400..1434
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1470..1525
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1067..1093
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1116..1164
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1601 AA; 181287 MW; D49C894B79153271 CRC64;
MQSRGVLFNY VPYFIERSVC NWSGRNADCQ KMTSTGVFHL DMPEAPSYDD SEENSHDYCS
TNGGVESLLL KVIEIALLIS SIRLCDLMLA SSVIKQQFSS FFSRKSREKL LHSSQGGIWV
SARHKFLAPE ILLRQGHGRA VDWWSLGTLM YDMLSGSPPF TGDDRRQTID LVSNILRGDF
IPVPYLSREA VSLISKFRCF LEYGRFTYVD PQIHIDMARD PWVSTWQTSS RSRRRSGISS
SSSPGFVGHT IMANPNTLMQ GTDILHVGTP HPEQLQSTLV AHLPNTIQTS IPTQSQPFVF
AEDFEDMDVA STNLTYSNNP LDSHSTVINT VNISTSNSVR PTYALPLGSH RLENSRVMET
GICDPYSSRS GEHVNGIIPK PLDTRLVNPS SSAAAQVSAL AAAALATSSR LVGSSVHIPS
IASHNSPNRP FMNEHMMFDP QNIRLMNLGK SQPQTPLAAV EIKPTNDQLF DFYNHVFIHM
LMKRSFSEDT NPDHDLLHGS TSQLDSTPPI SKRLISAASE PISFIRISSL EELDKRALQL
QNKKLWEALM ERRAAIAELK ERIEHLENRQ TKDDALLCVV NRYWNQLDED SLIILQRFDS
DAEEEISTST ESFLKQLASW DKEEVPEKLQ ERVHFSKRII ARLLSAYEKQ VLLISLCLNF
HVSMVTHQFR LRQLLGNTTE TASVSVGSEI SDNILPIHSS SSAPYGTQNS NSEGNNQSTS
SSQEPASTTC SRSGAVDLHE EITLLNKENL RLQSLCTNLH SKHRQSSLRL RELQDLAQTN
SDASAEWQAK FEDLDYKLAE AMKQVTRLDH RLYEAQEKNK KMEVELSALK CSDSPGREDP
SSVDGSITRN KYNDLACELE EYRELANNRI NELERLQRHL EDKVAECASL NMQLRDIPEH
IITESPQYLS LKTQFNILYN EAIQLRSQLE EARSTIQNNR HNHLKQIEEM EANEAAIQNQ
MRSEMLLIEG QYSQLRHKYE TMELDFKQAL THNEQAGPIS CEMRSLISTL QTQNKQLKAE
VTRYRRKCEE TVQEREMIRA DLKCTEDELV RVRTALSEAT AAVIAACEKS DQSTPSTPQS
SNLPQTSVTM PDVASPTADP ELKAKNSIPI KVEENVKYSS PSSSTARSGT VTTSASSHVN
GSVPEKVLKT ESTSDFRSNV SCSSPSNEII RDLKEQLKRS QESQKEMSVL LNMYKVIPKD
QRDKAALLQC EAKLRGELAD ARNEIDKLHA TIKDLQSQQT KMQQQRKSTL TSPIEPNLKM
SPAERSLTSH GNIPLSPSKT CKTGLVSPEE KSSSISGSLP ITSCGKSKIS ASDWQISELQ
MELYIVRRKS QSVEEQLKLH QQRLVAAKQQ EDVLLKEMEI TVQAFEDAQE QNVRLVKTLR
EKDDAHLKLM AERMKTAQLA RLLKEDKQLL EEQIRLMQAK IEALNRAVLK QEEKERLLLT
NLATLEKEAS ARQKSQEAYK RKALESQQVS EDLKVTVQKY QSQLKDAQTT VQEKASAFER
VSFGHQRLQE ELVTVRRKYE RLRKIEQSHN ADEFLLAEIQ DYKEQLTCPT CKINRKDAIL
TKCFHVFCLN CLKVRYETRN RKCPKCNATF GANDYHRIYL T
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