ID A0A2A2J3H7_9BILA Unreviewed; 1075 AA.
AC A0A2A2J3H7;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=DM2 domain-containing protein {ECO:0000259|PROSITE:PS51925};
DE Flags: Fragment;
GN ORFNames=WR25_15476 {ECO:0000313|EMBL:PAV56360.1};
OS Diploscapter pachys.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Diploscapter.
OX NCBI_TaxID=2018661 {ECO:0000313|EMBL:PAV56360.1, ECO:0000313|Proteomes:UP000218231};
RN [1] {ECO:0000313|EMBL:PAV56360.1, ECO:0000313|Proteomes:UP000218231}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PF1309 {ECO:0000313|EMBL:PAV56360.1};
RA Fradin H., Zegar C., Gutwein M., Lucas J., Kovtun M., Corcoran D.,
RA Baugh L.R., Kiontke K., Gunsalus K., Fitch D.H., Piano F.;
RT "Genome architecture and evolution of a unichromosomal asexual nematode.";
RL Curr. Biol. 0:0-0(2017).
CC -!- SIMILARITY: Belongs to the tubulin--tyrosine ligase family.
CC {ECO:0000256|ARBA:ARBA00006820}.
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:PAV56360.1}.
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DR EMBL; LIAE01010705; PAV56360.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A2J3H7; -.
DR STRING; 2018661.A0A2A2J3H7; -.
DR Proteomes; UP000218231; Unassembled WGS sequence.
DR GO; GO:0036211; P:protein modification process; IEA:InterPro.
DR GO; GO:0019098; P:reproductive behavior; IEA:UniProt.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR Gene3D; 1.10.245.10; SWIB/MDM2 domain; 1.
DR InterPro; IPR019835; SWIB_domain.
DR InterPro; IPR036885; SWIB_MDM2_dom_sf.
DR InterPro; IPR003121; SWIB_MDM2_domain.
DR InterPro; IPR004344; TTL/TTLL_fam.
DR PANTHER; PTHR12241:SF162; TUBULIN MONOGLUTAMYLASE TTLL4; 1.
DR PANTHER; PTHR12241; TUBULIN POLYGLUTAMYLASE; 1.
DR Pfam; PF02201; SWIB; 1.
DR Pfam; PF03133; TTL; 1.
DR SMART; SM00151; SWIB; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF47592; SWIB/MDM2 domain; 1.
DR PROSITE; PS51925; SWIB_MDM2; 1.
DR PROSITE; PS51221; TTL; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000218231}.
FT DOMAIN 254..331
FT /note="DM2"
FT /evidence="ECO:0000259|PROSITE:PS51925"
FT REGION 22..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 492..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..521
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1075
FT /evidence="ECO:0000313|EMBL:PAV56360.1"
SQ SEQUENCE 1075 AA; 122984 MW; 11D5D1DCF50BC189 CRC64;
MQHQPRGSAA PAVSLTPMAN RYQQQQPQGM PQSSQPHAVR RPMPGQMIPN LAMQQPGRMQ
ANKKKRRYID KLIAPKVREL VPESQAYMDL LAYEQKLDAT ISRKKLDIQE TLKRPQKIKR
RLRIYISHTF LPGREPEREG DEGTTPMWEL RVEGRLLDDI PQNGNGAGNA NGGSGSAVTA
AAAAAAAASR PISKKKFSSF FKSLVIELDK DIYGPDNHLV EWHRTPTTNE TDGFQVKRPG
DRPVKCTILL LLDYQPMKFK LHPRLAKVLG VAAETRPKII EALWQYIKTH KLQDPNDRDT
IMCDVFLEQC FGVKKIRFME VPQRLHQLLS QPDPLVLNHV IQHNEGGAEK NTACYDIDVE
VEDPMKQHMA SFIHSQQNQQ EIASLDQKIF DIVEQINEWK IRRDFYIRFA DNPHQFIDNW
VMSQSQDLQV MAEFQGETEA ERRVEAYFAP DIEEGVFRFH GNLHHSLDRR GTAIFLLELI
CGQSRALVEV ADTDSGRPSS ASSTVNNSEV GSSTPDTPTD NEGMCGLTEL VSSCLAKTRS
APSGPSSRLC SINDGLPSAS SSQNSKDPQP FLHVSLFTGV PPTIKFYTKG TKVTKPNKKI
SSRLTWCYNS LLPIVMRHSL AVSHFTVVDE SLFYVGYWGR HLKSAQYKSL HPYQKVNHYP
GAFHIGRKDR LWMHIKRQID RFGEEEYNII PTTYILPDER EELLEYIRAD PKNHVIMKPP
ASARGTGISV TRKMKEIPTK GQLQQTKTQM IAQHYVSRPL TINSAKFDLR FYIYVPSLEP
LRIYIYEEGL VRFASVPYSK NLSTVSNKYM HLTNYSINKL AEKDGVSESP VPKWTLSYLA
KYFENEGIDW PSIRDRIEDT IVKAFIACEK PIRDHMIKHI RHGFICHELF GVDILLDEDL
KPWLLEVNIS PSLHSGTPLD VSVKAPLAKD VLNMAGIYVP PSSEMLDEAD YSTRPRNWPK
TADQILKERL WIDAYLESQE LDPKILKRLT PEDARMLVEF EDERLRCGDF RLLFPIARSA
HYLRYFEEPV YANLLLQEWQ IEMEADRNAG IDRLEKLCQQ GHMKRRDGKF IGGFW
//