ID M7C1E1_CHEMY Unreviewed; 2509 AA.
AC M7C1E1;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=TATA element modulatory factor {ECO:0000313|EMBL:EMP34207.1};
GN ORFNames=UY3_08631 {ECO:0000313|EMBL:EMP34207.1};
OS Chelonia mydas (Green sea-turtle) (Chelonia agassizi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Americhelydia; Chelonioidea; Cheloniidae; Chelonia.
OX NCBI_TaxID=8469 {ECO:0000313|EMBL:EMP34207.1, ECO:0000313|Proteomes:UP000031443};
RN [1] {ECO:0000313|Proteomes:UP000031443}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
CC -!- PATHWAY: Protein modification. {ECO:0000256|ARBA:ARBA00043952}.
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DR EMBL; KB533466; EMP34207.1; -; Genomic_DNA.
DR STRING; 8469.M7C1E1; -.
DR eggNOG; KOG4673; Eukaryota.
DR Proteomes; UP000031443; Unassembled WGS sequence.
DR GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005523; F:tropomyosin binding; IEA:InterPro.
DR GO; GO:0008641; F:ubiquitin-like modifier activating enzyme activity; IEA:InterPro.
DR GO; GO:0090162; P:establishment of epithelial cell polarity; IEA:InterPro.
DR GO; GO:0051694; P:pointed-end actin filament capping; IEA:InterPro.
DR CDD; cd14473; FERM_B-lobe; 1.
DR CDD; cd17200; FERM_F1_FRMD4B; 1.
DR Gene3D; 1.20.80.10; -; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 1.10.10.520; Ubiquitin activating enzymes (Uba3). Chain: B, domain 2; 1.
DR InterPro; IPR019749; Band_41_domain.
DR InterPro; IPR021774; CUPID.
DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR InterPro; IPR035963; FERM_2.
DR InterPro; IPR019748; FERM_central.
DR InterPro; IPR019747; FERM_CS.
DR InterPro; IPR000299; FERM_domain.
DR InterPro; IPR018979; FERM_N.
DR InterPro; IPR018980; FERM_PH-like_C.
DR InterPro; IPR047176; FRMD4A/B.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR022092; TMF_DNA-bd.
DR InterPro; IPR022091; TMF_TATA-bd.
DR InterPro; IPR004934; TMOD.
DR InterPro; IPR023318; Ub_act_enz_dom_a_sf.
DR InterPro; IPR035985; Ubiquitin-activating_enz.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR46079; FERM DOMAIN-CONTAINING PROTEIN 4; 1.
DR PANTHER; PTHR46079:SF1; FERM DOMAIN-CONTAINING PROTEIN 4B; 1.
DR Pfam; PF11819; CUPID; 1.
DR Pfam; PF09380; FERM_C; 1.
DR Pfam; PF00373; FERM_M; 1.
DR Pfam; PF09379; FERM_N; 1.
DR Pfam; PF12329; TMF_DNA_bd; 1.
DR Pfam; PF12325; TMF_TATA_bd; 1.
DR Pfam; PF03250; Tropomodulin; 1.
DR SMART; SM00295; B41; 1.
DR SMART; SM01196; FERM_C; 1.
DR SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF47031; Second domain of FERM; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS00661; FERM_2; 1.
DR PROSITE; PS50057; FERM_3; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW Reference proteome {ECO:0000313|Proteomes:UP000031443}.
FT DOMAIN 5..314
FT /note="FERM"
FT /evidence="ECO:0000259|PROSITE:PS50057"
FT REGION 485..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 523..558
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 606..689
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1197..1224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1257..1291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1300..1319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1330..1357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 331..358
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1546..1865
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1930..2024
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2092..2140
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 485..502
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 523..537
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 606..650
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 662..689
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1257..1290
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1304..1319
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1340..1357
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2509 AA; 284892 MW; A82772D61E2C1C45 CRC64;
MTEGRHCQVQ LLDDRKLELL VQPKLLSREL LDLVASHFNL KEKEYFGITF IDDTGQNIWL
QLDHRVLDHD LPKKPGPAIL YFAVRFYIES ISFLKDRNTV ELFFLNAKSC VHKGQIEVES
ETIFRLAALI LQIYNLFIVQ SVIEHNLFLK SGLTKFSLTN ASEDRVIEHY IKIKGLTRGQ
AIVQYMKVVE ALPTYGVHYY GVKLFQWKQL ENLYFREKKF AVEVHDPHRI SVSRRTFGQS
GLVVQTWYAN TSLIKSIWVM AISQHQFYLD RKQSKAKIPS ARSLDDVAMD LTEMGTPKVS
KLVTSEAKNQ LIMASNGSLI SSGSQDSEVS EEQKKEKITE LKKKEKLLQE KLLQKVEELK
KICLREAELT GKMPQEYPLS VGEKPPQVRR RVGTTFKLDD NLLPSEEDPA LQSLERNFLI
QQKMVEAAKK LASEPDMCKN LKKKRKQDYT AAMKKLQEIE NSINEYRIKC GKKPTQKSTL
ILPANDSLTV PGQGTRSGQL SPRIPPPKSL GVERIHLRKS SINEQLLENR HSRDPLSTHG
SPYRILERQP YGGRSMPTTP VLTRNAYSSS HLQPDISPEH CIQRSGSLES QTPLLSETAG
EKPVFTFSKS QRSSSTEILD DGSSYTSQSS AEYSCVTPNP NPYYTTQTLD NRTRGRRRSK
KQNISAANSG SMPNLAQKDS RTGVYQKSQE QPASSYYVSA YSPYTECDVY YNGGYVYEND
TEGQYSVNPS YRSSVHCGYD RYRELRSYHE GEMERVPHNP YATLRLPRKQ VAKTQHITKN
IHKALVAEHL RGWYQRASGQ KDQGQSLQAG FDSDRGSQRS LGFAGLQVPC SPSSRASSFS
SASSANTSGN WRNQIALGLS DYDTMSHSSY TSCYGNVYGN LPLQSRFKKM SEFSQNSERE
VRIEDIDEDE ILGNLSPEEL RELQCEMEVM APDPRVPVGM IQKDQTEKPP TGNFDHRSLV
DYLYWQKASR RMLEDERVPV NLLPSEGGGR LWRREGDAMW QAPQSGTLNA AFSTRILPPR
ESVRLDGDDP DHIQWIYQQS LERASQFSIK GVTYRLTQGV VKRIIPAVAS TNAVIAGTVM
LKGKALAFIR SAYIPLNNYL VFNDVDGLYT YTFEAERKTV ASIEERTRPN LSKTLKGTNS
LTSGGWDTST WGLNSNIEPQ SPSISSPTAI TKPVRRTVVD ESENFFSAFL STTDIQSIQQ
SPVVSKPPTK SQRPKEEVKS TLKESLCSSQ LETLVETETE AKDSSASVLV DLENLDVPQE
KLEESSALET DAKHEENTNK GTDDKVATPD LKVPEVAVNV KSNAGNDGPG SAPDSPAQSL
TAETKDLGLE SKEQKNEDRQ SNTPSPPIST FSSGTSTTSD IEVLDHESVM SESSVSSRQE
ATESKSSLHL MQTSFQLLST SACAEYNRLD DFQKLTESCS SSDAFERIDS FSVQSLDSRS
VSEINSDDEL SGRGCASASL TVSPLTTKTE MVDPMKNKSK EELNETLVHA EETEMEESGR
SATPVNSEQP DVLIAAVQTD EGQTVKEEVL MHQQGAEKLP KANCEKEELC KMIDLLTEKL
EKRETQLLNV SKEKASLEEA YDNLKDEMFR VKEESSSISS LKEEFTQRIA DAEKKVQLAC
KERDAAKKEV KNVKEELATR LNCNETVELL KEKDEQIKGL MQEGEKLSKQ QLHNSNIIKK
LRMKEKENEN TNTKQSKKIK ELEEELQHLK QVLDGKEEVE KQHRENIKQL NSVVERQEKD
LSRLQVDMEE LEERNRSVQA ALDSAYKELA DLHKANATKD SEAQEAALSR EMKAKEELGL
ALEKAQDEAR QQQEALAIQV ADLRLALQRA EQQAARKEDY LRQEISELQQ RLQEAENRNQ
ELSHSVTSAT RPLLRQIENL QATLGAQTSS WEKLEKNLSD RLGESQALLA AAAERERAAT
EELLSNKIQV SSTESQNSLL RQENSRLQAQ LEAERARLKK LENENNRYEV ELENLKEEYV
KTLDEAKKEK MLLATQLEME KMKVEQEKKR VIFVQETAKE KERKSFTLST METVSSTPTL
SRSSSISGVD MAGLQASFLS QDDPHDHSFG SMSTSGSNLY DAVRMGAGSS IIENLQSQLK
LKEGEISHLQ LEIGNLERTR SIMAEELVKL TNQNDEFEEK VKEIPKLRAQ LRKYLKNLKS
CWGYERSCKP EYRFGYPVCD YVETGWANDI ETAQQIFWKQ ADFGYVKERL AEMKTHCKPI
AKGDSSLACS QYLQHCRATN LYIDLRTIKR NHDRFKEDFL QKGEIGGRCN FDSQAFMAEG
QRKSPLQSWF AELQTYTSLS FRPIEDGKCD IIIEKPTYFM KLDAGVNMYH HFCDFVNLYI
TQHINNSFST DVNIVMWDTV CFKEAVFSLL PRMRYGLFYN TPLDGKIRVT ILARSTDYRK
ILNQNELVNA LKTVSAFEVK VVDYKYKYNC EDERCYLDLA RLRGIRYITW QKKNKVFPQD
QGHHPTLGEH PKFTNYSFDV EEFMYLVLLA ADHVSQHSKW PFRVKHDEF
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