ID A0A026WRU8_OOCBI Unreviewed; 1113 AA.
AC A0A026WRU8;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 28-JUN-2023, entry version 38.
DE SubName: Full=Liprin-alpha-1 {ECO:0000313|EMBL:EZA58775.1};
GN ORFNames=X777_14944 {ECO:0000313|EMBL:EZA58775.1};
OS Ooceraea biroi (Clonal raider ant) (Cerapachys biroi).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Dorylinae; Ooceraea.
OX NCBI_TaxID=2015173 {ECO:0000313|EMBL:EZA58775.1, ECO:0000313|Proteomes:UP000053097};
RN [1] {ECO:0000313|EMBL:EZA58775.1, ECO:0000313|Proteomes:UP000053097}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24508170; DOI=10.1016/j.cub.2014.01.018;
RA Oxley P.R., Ji L., Fetter-Pruneda I., McKenzie S.K., Li C., Hu H.,
RA Zhang G., Kronauer D.J.;
RT "The genome of the clonal raider ant Cerapachys biroi.";
RL Curr. Biol. 24:451-458(2014).
CC -!- SIMILARITY: Belongs to the liprin family. Liprin-alpha subfamily.
CC {ECO:0000256|ARBA:ARBA00007026}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KK107119; EZA58775.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A026WRU8; -.
DR STRING; 2015173.A0A026WRU8; -.
DR OMA; TMCEVMP; -.
DR Proteomes; UP000053097; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR CDD; cd09562; SAM_liprin-alpha1_2_3_4_repeat1; 1.
DR CDD; cd09565; SAM_liprin-alpha1_2_3_4_repeat2; 1.
DR CDD; cd09568; SAM_liprin-alpha1_2_3_4_repeat3; 1.
DR Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 3.
DR InterPro; IPR029515; Liprin.
DR InterPro; IPR037620; Liprin-alpha_SAM_rpt_1.
DR InterPro; IPR037621; Liprin-alpha_SAM_rpt_2.
DR InterPro; IPR037622; Liprin-alpha_SAM_rpt_3.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR PANTHER; PTHR12587; LAR INTERACTING PROTEIN LIP -RELATED PROTEIN; 1.
DR PANTHER; PTHR12587:SF20; LIPRIN-ALPHA, ISOFORM E; 1.
DR Pfam; PF00536; SAM_1; 2.
DR Pfam; PF07647; SAM_2; 1.
DR SMART; SM00454; SAM; 3.
DR SUPFAM; SSF47769; SAM/Pointed domain; 3.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000053097}.
FT DOMAIN 854..923
FT /note="SAM"
FT /evidence="ECO:0000259|SMART:SM00454"
FT DOMAIN 938..1006
FT /note="SAM"
FT /evidence="ECO:0000259|SMART:SM00454"
FT DOMAIN 1027..1099
FT /note="SAM"
FT /evidence="ECO:0000259|SMART:SM00454"
FT REGION 76..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 434..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 582..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 643..675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 694..733
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 35..69
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 168..341
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 367..415
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 536..577
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 86..126
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 434..457
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..475
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 661..675
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 703..733
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1113 AA; 124323 MW; D78E617FC0A76E13 CRC64;
MTVVKRQAAA QSGVSSEVEV LKALKSLFEH HKALDEKVRE RLRVALERNT SLEEELAHTK
EELQQYKITG HPAKAIEDRP KENGQPDEGQ QQNKNETEQA VSQQQLQQQQ HQSQQQQQQL
QPVQKPGTEK SAEVGSRLSN GSLDPAEQDS AIRVIDLQAT LDKQSSELST WQRRVAELGG
RIAELEETLS KTQKDLLKAQ ETGLKLQRDL RENAAQKEDQ EERIATLEKR YLNAQRESTS
LHDLNEKLEQ ELQHKKAQLK LQEEKIAAIQ EKLELAEQKL AQYAKLPEME EQLKQRMEAL
TQAQERHGSA EDRIQRLEAQ LEEKNAEVMR VNQRLKMNEE HNTRLSTTVD KLLSESNERL
QVHLQERMHA LEEKNALTQE LEKTRKVAED LQNEKANIIK DLGKARLEID NIKRQMYQQE
IAFNIQQTDA LTRSLSPNAV DPGSFSRSAS HSSFDTHSLP RRGGKRSIEE DSSKSYARTL
TEQEWEKLQQ AHVLANVQQA FDVSSDAEGD GDNESIFSCA GDVISPTGHT DAQTLAMMLQ
EQLDAINKEI RLIQEEKQTT EARAEELESR VGSLEHMNLL VRGRSLERAS PPLSGRSTPK
SHHSPNRDYL HKYHTAPASM SPAHLHQYAA SLVSPGQLSE SLPASQLQLS GEELHSVSER
DSTGAPGSGS DAASPLTARS LRLERVVQAL AHSQEELRSR HGQHNNGALN SGTPPSPLSS
RHSSQDSLHK NNFSGVGLPI GQLSSSHLHI QATMSPATAA AVAAAQKKKG IKSSLGRFFS
KKEKIKGKDT PMPGDVPGMG GMVCTPADPD YGDSVSVAGT LGSKSDFDRR KKKSMLDSSR
HELLAEAMKA GTPFALWNGP TVVAWLELWV GMPTWYVAAC RANVKSGAIM SALSDTEIQR
EIGISNPLHR LKLRLAIQEM VSLTSPSAPK TSRTTLAFGD MNHEWIGNVW LPSLGLPQYR
STFMECLVDA RMLDHLTKKD LRGQLRMVDS FHRTSLQYGI SCLKRLNYDR QQLEERRRVA
EGANIDVLVW SNDRVIRWVQ SIGLKEYGNN LLESGVHGAL IALDESFDAN SFALTLQIPT
QNTQARQVLE MEFSNLLAVA TERRLDENSS MKS
//
