ID A0A1V9YT40_9STRA Unreviewed; 1699 AA.
AC A0A1V9YT40;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=THO complex subunit 2 {ECO:0000256|ARBA:ARBA00019596};
DE Flags: Fragment;
GN ORFNames=THRCLA_10108 {ECO:0000313|EMBL:OQR88780.1};
OS Thraustotheca clavata.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Thraustotheca.
OX NCBI_TaxID=74557 {ECO:0000313|EMBL:OQR88780.1, ECO:0000313|Proteomes:UP000243217};
RN [1] {ECO:0000313|EMBL:OQR88780.1, ECO:0000313|Proteomes:UP000243217}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 34112 {ECO:0000313|EMBL:OQR88780.1,
RC ECO:0000313|Proteomes:UP000243217};
RX PubMed=25527045; DOI=10.1093/gbe/evu276;
RA Misner I., Blouin N., Leonard G., Richards T.A., Lane C.E.;
RT "The secreted proteins of Achlya hypogyna and Thraustotheca clavata
RT identify the ancestral oomycete secretome and reveal gene acquisitions by
RT horizontal gene transfer.";
RL Genome Biol. Evol. 7:120-135(2014).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the THOC2 family.
CC {ECO:0000256|ARBA:ARBA00007857}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Adenosine and AMP deaminases family. {ECO:0000256|ARBA:ARBA00006676}.
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:OQR88780.1}.
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DR EMBL; JNBS01003017; OQR88780.1; -; Genomic_DNA.
DR STRING; 74557.A0A1V9YT40; -.
DR OrthoDB; 179356at2759; -.
DR Proteomes; UP000243217; Unassembled WGS sequence.
DR GO; GO:0000347; C:THO complex; IEA:InterPro.
DR GO; GO:0003876; F:AMP deaminase activity; IEA:InterPro.
DR GO; GO:0032264; P:IMP salvage; IEA:InterPro.
DR GO; GO:0006406; P:mRNA export from nucleus; IEA:InterPro.
DR GO; GO:0006397; P:mRNA processing; IEA:InterPro.
DR Gene3D; 4.10.800.20; -; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR InterPro; IPR006329; AMPD.
DR InterPro; IPR032466; Metal_Hydrolase.
DR InterPro; IPR040007; Tho2.
DR InterPro; IPR021418; THO_THOC2_C.
DR InterPro; IPR021726; THO_THOC2_N.
DR InterPro; IPR032302; THOC2_N.
DR PANTHER; PTHR21597:SF0; THO COMPLEX SUBUNIT 2; 1.
DR PANTHER; PTHR21597; THO2 PROTEIN; 1.
DR Pfam; PF19326; AMP_deaminase; 1.
DR Pfam; PF11262; Tho2; 1.
DR Pfam; PF11732; Thoc2; 1.
DR Pfam; PF16134; THOC2_N; 2.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE 3: Inferred from homology;
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000243217}.
FT DOMAIN 1..244
FT /note="THO complex subunit 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16134"
FT DOMAIN 269..399
FT /note="THO complex subunit 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16134"
FT DOMAIN 401..475
FT /note="THO complex subunitTHOC2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF11732"
FT DOMAIN 708..996
FT /note="THO complex subunitTHOC2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11262"
FT REGION 1017..1249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1017..1031
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1043..1197
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1198..1213
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1215..1249
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:OQR88780.1"
SQ SEQUENCE 1699 AA; 196221 MW; 81FB90766EC2320B CRC64;
TRNLYTQNKF NLLREESEGF AKVLSLLHAG VNTDNVDAVQ RDLLALIGFF DLDPNRVLDL
LLDVYETDHL NECFLQLISQ FKQEYIVHVV GFKFQYYTRP EALETECFAP RSLYRIAAIL
IDKNYFTLND LYPHLSPKKE VIIENDLQRI QDIKTAARAY GRVNLNAKKD DDKAENTESE
SDANDANQIY GIIIGLLEIG AYKSAVDIIR QFLAKANPVA YPPLARQLCI TIHDLLADLY
APLSLKSMKL VSPTDKFKEP KRFVVSALGT LQEMVDVVFP LLHLLGPFLF HDQFLWTKLQ
RILLHSLPGN DFLIEHLAGL FTHCLFPTLS LHQCCPNLVY QMWDLLKIFS CEKRYALYQT
WQEKYANIPE MMLAHAQTVH MTRKVMRRLT ADKTKPTGRV LTHVAHANPL VAFRTILQQL
QAYENLIQPV VESLKYISPL GMDVLSFVLI TEFSRPRESF KADGTNVSLW LSSLASFSGS
FYRKYPMVEL SALLSYLFQR LSNWESVELI VLSELLTKMG SCLALEDISN TQLEALAGGP
TLGYEAPDPK VMNKRAIPRL RDTLVKQNLA WPLSIAIGQV RSQIEHNDDT SAAHLKLLGG
TYDMCQRTLN QLLAFLHSAA DPATYVTSLP PLPSLVKEYH LPEDVAMALV RPAIRADDPL
LRKVTRSVHS GASTNTSDEP GKNYMYSESF LNSIQEAFVN EELNPFEGIT KELFATFWGL
TLYDIYVPHA QYEREISKVR LELSSLPVGT SKDSKDSKEK SKLKDKLMAN VDKLMTEQKD
QVAHRKLVFE RLEKHKSQFF TSEPTTSVAE LLQRCIIPRA LHSPEDALYC AKFMHHLHSI
DTPNLSTLQY YHKVTLNLSG LVLCTTEREA SNFGIFLKET HALLSRWFES SEEFDTEGAK
TGFSISLNDP SMRMQHRTFK KTYLKWQAHM EKVYAGALAS EDYMPTRNTL VLLTKMIDVF
PISGANGQCL LTLVEKLTKD KREDLKIMAK RYSALLKLRL TGFSDVVVEE KVEEKKKEVV
TLRDKAKERP KSGSSTPLPL NDKRGRSRSR DKKDNTAWKR SRDSLRKDEP KNRRDEPLNR
HDDSYNRRDD SNSRPIHLSA RRDDTSSRAS SREDSFRRGK SKERSIREIA NKRDYERKEH
EKKNDDYKAD DDKNEGTPES TEAALRRQLT EKKERDAGRK IVSLTRKRDD AGTMDEPNTK
RRQSSSPSAS IVEANERRLQ EEKKKRLAER KRSEPRVSRD DKRSMDRGAR GVKVRRYNYE
VRRHCEATND SPSFVILNGR EKMASLSDEE DVDYGDNDDM NTDLEDHQKL TYLQSIYNTA
KQRKLSLVED IEQDEQEKDN NTELSTLFER IPEPYEDNSF FQRIHVTSSE DEHDVETADV
CQNILKCIAL RKKWIEANTM DLKQEQDTIP EPPLTPGGSR AQFRHRDDLP YNIFDIATPT
GSNHRIVVQC GVMMVYDESN EVLYKPHSVE SFYEDWFEIK RIVNSGPVKT YSYKRLQLLE
ARFNLHTLLN ADRELASQKA VPHRDFYNIR KVDTHIHHSA CMNQKHLLRF IKSRLKNSPG
EIVIFRDGRF MTLQEVFHSL NLTAYDLNVD TLDMHASNTF HRFDRFNLKY NPAGQSRLRE
IFLKTDNLIA GRYLADITKE VISDLHASKY QLVEWRLSIY GRKHSEWDKL AKWFYVNRLA
SPHVRWMIQI PRLYFLYKK
//
