ID A0A158RE05_HYDTA Unreviewed; 670 AA.
AC A0A158RE05;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=DUF1767 domain-containing protein {ECO:0000313|WBParaSite:TTAC_0000642001-mRNA-1};
GN ORFNames=TTAC_LOCUS6405 {ECO:0000313|EMBL:VDM30610.1};
OS Hydatigena taeniaeformis (Feline tapeworm) (Taenia taeniaeformis).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC Eucestoda; Cyclophyllidea; Taeniidae; Hydatigera.
OX NCBI_TaxID=6205 {ECO:0000313|Proteomes:UP000046396, ECO:0000313|WBParaSite:TTAC_0000642001-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:TTAC_0000642001-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (APR-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDM30610.1, ECO:0000313|Proteomes:UP000274429}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Essential component of the RMI complex, a complex that plays
CC an important role in the processing of homologous recombination
CC intermediates to limit DNA crossover formation in cells. Promotes TOP3A
CC binding to double Holliday junctions (DHJ) and hence stimulates TOP3A-
CC mediated dissolution. Required for BLM phosphorylation during mitosis.
CC Within the BLM complex, required for BLM and TOP3A stability.
CC {ECO:0000256|ARBA:ARBA00024977}.
CC -!- SIMILARITY: Belongs to the ATG8 family. {ECO:0000256|ARBA:ARBA00007293,
CC ECO:0000256|RuleBase:RU004384}.
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DR EMBL; UYWX01020302; VDM30610.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A158RE05; -.
DR STRING; 6205.A0A158RE05; -.
DR WBParaSite; TTAC_0000642001-mRNA-1; TTAC_0000642001-mRNA-1; TTAC_0000642001.
DR Proteomes; UP000046396; Unplaced.
DR Proteomes; UP000274429; Unassembled WGS sequence.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR Gene3D; 2.40.50.510; -; 1.
DR Gene3D; 1.10.8.1020; RecQ-mediated genome instability protein 1, N-terminal domain; 1.
DR Gene3D; 2.40.50.770; RecQ-mediated genome instability protein Rmi1, C-terminal domain; 1.
DR InterPro; IPR004241; Atg8-like.
DR InterPro; IPR032199; RMI1_C.
DR InterPro; IPR049363; RMI1_N.
DR InterPro; IPR042470; RMI1_N_C_sf.
DR InterPro; IPR044881; RMI1_N_N_sf.
DR InterPro; IPR013894; RMI1_OB.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR10969:SF33; GAMMA-AMINOBUTYRIC ACID RECEPTOR-ASSOCIATED PROTEIN; 1.
DR PANTHER; PTHR10969; MICROTUBULE-ASSOCIATED PROTEINS 1A/1B LIGHT CHAIN 3-RELATED; 1.
DR Pfam; PF02991; ATG8; 1.
DR Pfam; PF16099; RMI1_C; 1.
DR Pfam; PF08585; RMI1_N_C; 1.
DR Pfam; PF21000; RMI1_N_N; 1.
DR SMART; SM01161; DUF1767; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
PE 3: Inferred from homology;
KW Autophagy {ECO:0000256|RuleBase:RU004384};
KW Lipoprotein {ECO:0000256|PIRSR:PIRSR604241-50};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000274429}.
FT DOMAIN 137..177
FT /note="RMI1 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF21000"
FT DOMAIN 192..336
FT /note="RecQ mediated genome instability protein 1 OB-fold"
FT /evidence="ECO:0000259|Pfam:PF08585"
FT DOMAIN 574..663
FT /note="RecQ-mediated genome instability protein 1 C-
FT terminal OB-fold"
FT /evidence="ECO:0000259|Pfam:PF16099"
FT REGION 396..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 463..483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 498..546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..418
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..439
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 116
FT /note="Phosphatidylserine amidated glycine; alternate"
FT /evidence="ECO:0000256|PIRSR:PIRSR604241-50"
SQ SEQUENCE 670 AA; 75139 MW; F9D26BCB201FB723 CRC64;
MRFAYKQERT FEQRLQEGKK ISERYPSCVP VIVEKSPRAN VPNLDKNKFL VPIDLTVGQF
YYLIRKRIEL KPEQALFFFV DNSIPPTSAT MGALYEEYRD SDKFLYIAYS DESVYGVPAS
SEIESLRSWM ESEALIVPEG WLEACLEWLS DQSDVMMTFQ QLKEGVYQQW LHSDFNQLEC
PILPDQESVM KETLLLEGEL CLQISALIKI GESYYGQIRR LEGNLGNDVP DLETDKELID
DVEATSIDPS FQLSNIATQS SFPSSNRSTH LQNTNISTYA LHLTDGVRTI KAIEVGSAYS
ATRPSPEEWF RIGSKVKLKG PLKLRKGVLL LPNGTISNPA VTAQLPNSQC CFLGGEVQFE
EAGERRMEAF LQRELLLKLN LSPDNPPEWF PGQRHLSTST TKATASNATD NIAGSTTDVV
PQPPARPVED KRREEGDLYD EDDLLLTSAV EDFESLVAAA VGDETTNGTT AGQKEESEAG
ADVHEGEVDA ALEEINFSPQ SDTGSATLQT SFPPKTSLER SYLPPSDSAI HQPQPSSSNS
RRSTQCLQSD IRRFLTTTSA LQPQRQQHSS RMPQFAYLQD IYYDRQQRPG GGSEVHLIRG
MLISIQSQLE HHEGQRWSLT VRLTDGTAVL DADMEDELLH RLIGLSALEV EAMKQMGRRN
DQVSDFFKKI
//
