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Database: UniProt
Entry: F4WUA5_ACREC
LinkDB: F4WUA5_ACREC
Original site: F4WUA5_ACREC 
ID   F4WUA5_ACREC            Unreviewed;      1011 AA.
AC   F4WUA5;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   24-JAN-2024, entry version 53.
DE   SubName: Full=Heterogeneous nuclear ribonucleoprotein U-like protein 1 {ECO:0000313|EMBL:EGI62213.1};
GN   ORFNames=G5I_09463 {ECO:0000313|EMBL:EGI62213.1};
OS   Acromyrmex echinatior (Panamanian leafcutter ant) (Acromyrmex octospinosus
OS   echinatior).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Myrmicinae; Acromyrmex.
OX   NCBI_TaxID=103372 {ECO:0000313|Proteomes:UP000007755};
RN   [1] {ECO:0000313|EMBL:EGI62213.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Nygaard S., Zhang G.;
RT   "The genome of the leaf-cutting ant Acromyrmex echinatior suggests key
RT   adaptations to social evolution and fungus farming.";
RL   Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; GL888355; EGI62213.1; -; Genomic_DNA.
DR   AlphaFoldDB; F4WUA5; -.
DR   STRING; 103372.F4WUA5; -.
DR   EnsemblMetazoa; XM_011061591.1; XP_011059893.1; LOC105149287.
DR   EnsemblMetazoa; XM_011061595.1; XP_011059897.1; LOC105149287.
DR   eggNOG; KOG2242; Eukaryota.
DR   InParanoid; F4WUA5; -.
DR   Proteomes; UP000007755; Unassembled WGS sequence.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR   CDD; cd12884; SPRY_hnRNP; 1.
DR   Gene3D; 2.60.120.920; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 1.10.720.30; SAP domain; 1.
DR   InterPro; IPR001870; B30.2/SPRY.
DR   InterPro; IPR043136; B30.2/SPRY_sf.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR003034; SAP_dom.
DR   InterPro; IPR036361; SAP_dom_sf.
DR   InterPro; IPR003877; SPRY_dom.
DR   InterPro; IPR035778; SPRY_hnRNP_U.
DR   PANTHER; PTHR12381:SF56; B30.2/SPRY DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   PANTHER; PTHR12381; HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN U FAMILY MEMBER; 1.
DR   Pfam; PF13671; AAA_33; 1.
DR   Pfam; PF02037; SAP; 1.
DR   Pfam; PF00622; SPRY; 1.
DR   SMART; SM00513; SAP; 1.
DR   SMART; SM00449; SPRY; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF68906; SAP domain; 1.
DR   PROSITE; PS50188; B302_SPRY; 1.
DR   PROSITE; PS50800; SAP; 1.
PE   4: Predicted;
KW   Methylation {ECO:0000256|ARBA:ARBA00022481};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007755};
KW   Ribonucleoprotein {ECO:0000313|EMBL:EGI62213.1}.
FT   DOMAIN          3..37
FT                   /note="SAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50800"
FT   DOMAIN          354..561
FT                   /note="B30.2/SPRY"
FT                   /evidence="ECO:0000259|PROSITE:PS50188"
FT   REGION          39..169
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          338..380
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          770..932
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        67..141
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        142..157
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        347..361
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        786..814
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        867..881
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        888..932
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1011 AA;  113583 MW;  E06A89A5AAA89BF0 CRC64;
     MDPSKLKVVE LRAALSERGL DTKGNKPVLV ERLRKALEEE AQECGSDSQT ENIDDTALKE
     TQERVVEATR SSQSPRTPNR ASRSSSVTTP TKISTRNASR ASTTPNSSKQ STPNKSQYDE
     KAYETPTTNE EAITQQQEIS KLSPEKYREE QEDDASNILQ NKIHSSDKYE EEEAKCVNIL
     EGNQANIFQV PVTEPSDKPS TIACVDQFSI IQEAHEAGSS IDEVGKVQQL AEETKDITKL
     EEKTEIKDKD KISIEKEHVE RKEDGSNIKD NIDIPEVEQP THIIPDQTDK TCELKHEEET
     IHDDYTVQDK KMDISANVEN LDEKIDTINI LQDKQQKATL DAGESNQMEC NDRKRKRSSS
     PAEVRQLSPV PQKSEDEPDL DESTVILSWY DSDLNLVINK DGFLSGTPMH DGDLCDMWAG
     ARASHGVSNG KVYYEARIVQ HYPTTTKDKK QSHMLRIGWS VPSTSMQLGE EKLSYAYTSA
     GKQGTDKKFT DYGSPFGKDD VVGCYLDMTP ENTIELFYTV NGKNVGSAFS ICKEELGDRP
     LFPHILSKNC TFVCNFGQEE AWCEQIPGYI LVGNAESKNR VAGPRRPNGK ADCEVIMMCG
     LPTAGKTTWA RKHAADHPDK LYNILAVHKL VEKTGDVALL DKEQNICQRE IIIDRCNRAL
     DQLINVASDR RRNYILDQKS NIYSSVQRRK MRNFCGYQRK AIVVIPTDKE YNQRLSMHNT
     IEGNSLVSNL TEMKANFTAP SVGEFFDEVE WAGLGEEEAK KLIEKYNKEG KDAGFSQQPP
     TKQPRLDKTE NIKETRDSRN SRDTRDRRNN YQDRGRNPSW RGSNMGGWRG ERSQRGGYMR
     HTGGYGHPPV PWRLRGRGGP AMARSDRRMG GVDRRSGNDR NRSVAPRQGG WGSMSGNYQG
     SQQSSWGQQD NWSGSQATGN WNQQSGWGQQ QWGGGWKGYS QGTYGQTGYN QHGYGNGNWN
     SWNQQYYNNQ YWGQQQQSGQ TTAASGQAEI TSEMVATTST NTGAGYSYSQ G
//
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