ID M7BSB1_CHEMY Unreviewed; 2094 AA.
AC M7BSB1;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE SubName: Full=PHD finger protein 3 {ECO:0000313|EMBL:EMP34983.1};
GN ORFNames=UY3_07846 {ECO:0000313|EMBL:EMP34983.1};
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:EMP34983.1, 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).
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DR EMBL; KB530466; EMP34983.1; -; Genomic_DNA.
DR STRING; 8469.M7BSB1; -.
DR eggNOG; KOG1634; Eukaryota.
DR Proteomes; UP000031443; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR CDD; cd15638; PHD_PHF3; 1.
DR CDD; cd21548; SPOC_PHF3; 1.
DR Gene3D; 1.10.472.30; Transcription elongation factor S-II, central domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR012921; SPOC_C.
DR InterPro; IPR003618; TFIIS_cen_dom.
DR InterPro; IPR036575; TFIIS_cen_dom_sf.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR11477:SF10; PHD FINGER PROTEIN 3; 1.
DR PANTHER; PTHR11477; TRANSCRIPTION FACTOR S-II ZINC FINGER DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF07744; SPOC; 1.
DR Pfam; PF07500; TFIIS_M; 1.
DR SMART; SM00249; PHD; 1.
DR SMART; SM00510; TFS2M; 1.
DR SUPFAM; SSF46942; Elongation factor TFIIS domain 2; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR PROSITE; PS51321; TFIIS_CENTRAL; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000031443};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 733..788
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 951..1070
FT /note="TFIIS central"
FT /evidence="ECO:0000259|PROSITE:PS51321"
FT REGION 118..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 361..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 681..703
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 818..843
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 926..947
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1387..1421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1609..1735
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1790..1813
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1901..2094
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..152
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..207
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..225
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..247
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..268
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..377
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..419
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 681..696
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 820..837
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1628..1681
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1688..1702
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1713..1735
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1924..2094
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2094 AA; 235471 MW; E91357218F632FDB CRC64;
MDIVDTFNHL IPTEHLDDAL FLGSNLENEV CEDFSTSQNL LEDSLKNMLS DKDPMLGSAS
AQFCLPVLDS NDPNFQMPCS TVIGLDDIMD EEGVKESGND TIDEDDVILP NRNLRDQLDD
TSVKSPRKSP RLMAQEPVRS LRQSTIAKRS NIAPLANTKK AAVKSGCAQK GGPKPQDKGQ
PKQEEVSTPV KLEHLKEVRR SSRLSGQTEE TEEASSPSPS SSKQSACHEK NDEVKSETFK
QGKLDETFSE LRGGSLLTNT CSSTEEAESK TETVMKSGLG FITSANNEAN KVNIDIFKNK
VDETMVGEIG SDASSEEKIE YKIKETEEKP KENDQSKISG MTTISSVTTV CMNSNDIHET
PSVLSRSVEE KTKCRLDPPT AVESAGKNVM SLKDCKTEPL DDSKEADKNV NPSKHLDSTE
FHKTALKSTI SAEAGSNILE SSIIHDSPSQ NVQQQDSYIK MEGCEAAKLQ DDNSISTKSP
KTVKSKHIKS MIQIKQNLTA GAGRKLLTTK QQISHSKKRV GVSVSSFHSA SSISLKRSAD
EQERWQHFHK TVKVRKKQTD KDVKAQSFDM GVTVKKQTHT LVKKVSRVQT PMQVQKTSVQ
NVSDKSLNHQ GCSKEIHHPV SASVHSPSGH LLHQNQKQTQ KHQLAIALKT NSYVKEERET
KDPTGLEHLK EDEKEKLKLK KIEKNLQPRQ RRSSKSLSLD EPPLFIPDNI STVKREGSEH
TSPSESKYVW VPTKQCGFCR KPHGNRFMVG CGRCDDWFHG DCVGLSLSQA QRMGEEDKEY
VCVKCCAEED KKTESCDQNI LDTQLEAYRE DRTMECEKPG MSKQTPTGNP SVTNEKAKQT
DDTMKHKVKI FRRESGDARN LSECRDSDIK KGQVPIRKMG QTVTLPRRCS EEKSEKINKD
SLSVSCSSEK TAKSGVYEKQ EFKKKKTEKV GATGNIPPPA VPASKPSADQ IRQSVRQSLK
EILMKRLTDS SLKIPEERAA KVATRIEKEL FSFFRDTDSK YKNKYRSLMF NLKDPKNNIL
FKRVLKGEVT PDHLIRMSPE ELASKELAAW RQRENRHTIE MIEKEQREVE RRPITKITHK
GEIEIESDAP IKEQEVAMEI QEPTMVKLVE KTEEIEKDKE VDESSFPDTT SQHKNHLFDL
NCKICIGRMA PPTDDLSAKN VKVSVGVARK QSDNEAENIA DALSATSNIL ASELLEDDKQ
ELSKPAFSSI PRSETPGTVE SETLFLARLN FIWKGFINMP SVAKFVIKAY PVSGSFEYLT
EDLPDSIQVG GRISPHTVWE YVEKIKASGT KEICVVRFTP VTEEDQISYA LLFAYFSSRK
RYGVAANNMK QVKDLYLIPL GASDKIPHHL VPFDGPGIEI HRPNLLLGLI IRQKMKRQIS
ASTSLVDEIS ESAPSNLPPE KKSKPSKPDV SSTEVVVEEE EEENDFFNSF TTVLHKQRNK
PQQSNTEEIP AVIEPVVESI KHEPPKPLRF LPGVLVGWEN QSSTLELANK PLPVDDILQS
LLGTTGQIYE HHQSVVDQCA SQEIPLFAEQ TSLKEEKINV AEVTADEAIE TKTRLDDSQE
STDVTVTVDM PVAGTSCSAG TVGTLISLSL KGKPPDVSTE AFLANLSVQS QSKETEECKE
NDPKWQLYDT ENVLQESKRT TDSIFSSSSS NAGKGSGDNN VNIGSAEGMT SNTSKSPQFI
NLKRDPRQAA GRSQQINASD NKEGDTNRNE ERQNIQSDIS GSEQMEMENK QSGEKSLNVY
QSGGQTSEMQ CTSAPTKTDN VCASQMEETK HLQEDTPMKN IETVHSFRRG PATTSSHFEK
ENSSHSEFTS KVPSPVMSGN FSPVRPQQHN FQHLKSNLPG FQFQTLSPPN FPPQNSPMFG
FPPHLPPPLL PPPGFGFAQN PMMPWPPVVH LSGQPPHYVG PIVQGPSLAH KQSRFPGPEN
FYQSKDSKRP ERRHSDPWGR QEQHLERGFS RGKSDQHRQR FYSESHHQKK DRHEKEWNSE
KYWEQDSERN RRKDRNQEKE REKKSREEGH RDKERLRLSH SDRGSDGKSS RESRNPEKKI
DKPKSEEQSH EKDKEREKSR ERHRERESEK NRDRHHKDRD HNDRAKSKRY EAVD
//
