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Database: UniProt
Entry: A0A3L8S3C9_CHLGU
LinkDB: A0A3L8S3C9_CHLGU
Original site: A0A3L8S3C9_CHLGU 
ID   A0A3L8S3C9_CHLGU        Unreviewed;      1271 AA.
AC   A0A3L8S3C9;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=SAM domain-containing protein {ECO:0000259|PROSITE:PS50105};
GN   ORFNames=DV515_00012883 {ECO:0000313|EMBL:RLV95307.1};
OS   Chloebia gouldiae (Gouldian finch) (Erythrura gouldiae).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Passeridae;
OC   Chloebia.
OX   NCBI_TaxID=44316 {ECO:0000313|EMBL:RLV95307.1, ECO:0000313|Proteomes:UP000276834};
RN   [1] {ECO:0000313|EMBL:RLV95307.1, ECO:0000313|Proteomes:UP000276834}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Red01 {ECO:0000313|EMBL:RLV95307.1};
RC   TISSUE=Muscle {ECO:0000313|EMBL:RLV95307.1};
RX   PubMed=30282656;
RA   Toomey M.B., Marques C.I., Andrade P., Araujo P.M., Sabatino S.,
RA   Gazda M.A., Afonso S., Lopes R.J., Corbo J.C., Carneiro M.;
RT   "A non-coding region near Follistatin controls head colour polymorphism in
RT   the Gouldian finch.";
RL   Proc. R. Soc. B 285:0-0(2018).
CC   -!- SIMILARITY: Belongs to the liprin family. Liprin-alpha subfamily.
CC       {ECO:0000256|ARBA:ARBA00007026}.
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:RLV95307.1}.
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DR   EMBL; QUSF01000078; RLV95307.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3L8S3C9; -.
DR   STRING; 44316.ENSEGOP00005018176; -.
DR   Proteomes; UP000276834; 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:SF5; LIPRIN-ALPHA-4; 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.
DR   PROSITE; PS50105; SAM_DOMAIN; 3.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000276834}.
FT   DOMAIN          929..995
FT                   /note="SAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50105"
FT   DOMAIN          1042..1099
FT                   /note="SAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50105"
FT   DOMAIN          1123..1155
FT                   /note="SAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50105"
FT   REGION          221..242
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          750..857
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1242..1271
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          31..72
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          114..148
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          267..399
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          461..576
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          681..722
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        750..770
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        826..843
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1271 AA;  143513 MW;  607F9F39C339480B CRC64;
     MMCEVMPTIS EGDPLGPPQG SEADADFEQL MVNMLDERDK LLDTLRETRE TLAVTQSRLQ
     ETLRERDQLQ RQLNSALPQA SYSSPVYLAD LTAGLARRRA VAIFDEFATL TRELSTCREQ
     LLEREEEISE LKAERNNTRL LLEHLECLVS RHERSLRMTV VKRQAQSPSG VSSEVEVLKA
     LKSLFEHHKA LDEKVRERLR AALERVATLE EQLVDAHRQV AALQQGSSRE PAAGERDERE
     PKEAALKLPW KRLSNGSVHP DDEAGQVVEL QELLEKQNFE VVQAKERISA LAASVAELEE
     DLGTARKDLI KSEEMSSKYQ RDLREALAQK EDMEERITTL EKRYLAAQRE ATSIHDLNDK
     LENELANKES LHRQCEEKAR HLQELLELAE QKLQQTMRKA ETLPEVEAEL AQRIAALTKA
     SGRQWERALH PKKDSDAEMD TRMQQGPHGF GEHHLRRLLF FSQAEERHGS IEEHLRQLET
     QLEEKNQELA RARQREKMNE EHNKRLSDTV DRLLSESNER LQLHLKERMA ALEEKNTLLQ
     ELENTQKQIE EHQHDKRRLS DEIDKLRLEV DQLKTRSGTF VESVHTRSHM GSATDLRFPL
     GAVVHAPAEP FGAAPGLPRA QKGRFSARRE EPAKDWEQAQ AGGVLATGPH AFDSDPDISD
     VDEDDHETLF SSMDVLSPGG HSDAQTLAMM LQEQLDAINE EIRMIQEEKE STELRAEELE
     TRVTSGSMEG LNLTQLCKRA SIPTSLTALS LASSSPPLSG RSTPKLSSRS AAQDLDRMGI
     MTLSPAARDE SREDKTTIKC ETSPPSSPRT LRLEKLGHPA LSQEDGKSSL EDQASNPSSS
     QDSLHKGSKR KGIKSSIGRL FGKKEKGRFN QLSREGATGQ VLLTDVEGGI QDPLGLGKLG
     AQAEKDRRLR KKHELLEEAR RKGLPFAHWD GPTVVSWLEL WVGMPAWYVA ACRANVKSGA
     IMSALSDTEI QREIGISNAL HRLKLRLAIQ EMVSLTSPSA PPTSRTSSGN VWVTHEEMEN
     MATSTKTTLA YGDMNHEWIG NEWLPSLGLP QYRSYFMECL VDARMLDHLT KKDLRVHLKM
     VDSFHRTSLQ YGIMCLKRLN YDRKELERRR EETQHEIKDV LVWTNDQVIH WIQSIGLREY
     GNNLVESGVH GALLALDENF DHNSLALVLQ IPTQNTQAGC KDDMSLLYRL LDRGDDKTFR
     RTPSWRKRFR PRDVHSINLL SGSAETLPAG FRVTSLVPLP PPAAPAKKMP PEVGASGSPR
     LETSTVRTYS C
//
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