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Database: UniProt
Entry: V9KHH5_CALMI
LinkDB: V9KHH5_CALMI
Original site: V9KHH5_CALMI 
ID   V9KHH5_CALMI            Unreviewed;       756 AA.
AC   V9KHH5;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=PERQ amino acid-rich with GYF domain-containing protein 2-like protein {ECO:0000313|EMBL:AFO97440.1};
DE   Flags: Fragment;
OS   Callorhinchus milii (Ghost shark).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC   Holocephali; Chimaeriformes; Callorhinchidae; Callorhinchus.
OX   NCBI_TaxID=7868 {ECO:0000313|EMBL:AFO97440.1};
RN   [1] {ECO:0000313|EMBL:AFO97440.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Heart {ECO:0000313|EMBL:AFO97440.1};
RX   PubMed=24402279; DOI=10.1038/nature12826;
RG   International Elephant Shark Genome Sequencing Consortium;
RA   Venkatesh B., Lee A.P., Ravi V., Maurya A.K., Lian M.M., Swann J.B.,
RA   Ohta Y., Flajnik M.F., Sutoh Y., Kasahara M., Hoon S., Gangu V., Roy S.W.,
RA   Irimia M., Korzh V., Kondrychyn I., Lim Z.W., Tay B.H., Tohari S.,
RA   Kong K.W., Ho S., Lorente-Galdos B., Quilez J., Marques-Bonet T.,
RA   Raney B.J., Ingham P.W., Tay A., Hillier L.W., Minx P., Boehm T.,
RA   Wilson R.K., Brenner S., Warren W.C.;
RT   "Elephant shark genome provides unique insights into gnathostome
RT   evolution.";
RL   Nature 505:174-179(2014).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the GIGYF family.
CC       {ECO:0000256|ARBA:ARBA00038015}.
CC   -!- SIMILARITY: Belongs to the TFIIA subunit 1 family.
CC       {ECO:0000256|ARBA:ARBA00010059}.
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DR   EMBL; JW864923; AFO97440.1; -; mRNA.
DR   AlphaFoldDB; V9KHH5; -.
DR   GO; GO:0005672; C:transcription factor TFIIA complex; IEA:InterPro.
DR   GO; GO:0006367; P:transcription initiation at RNA polymerase II promoter; IEA:InterPro.
DR   CDD; cd00072; GYF; 1.
DR   CDD; cd07976; TFIIA_alpha_beta_like; 1.
DR   Gene3D; 3.30.1490.40; -; 1.
DR   Gene3D; 2.30.18.10; Transcription factor IIA (TFIIA), beta-barrel domain; 1.
DR   InterPro; IPR003169; GYF.
DR   InterPro; IPR035445; GYF-like_dom_sf.
DR   InterPro; IPR004855; TFIIA_asu/bsu.
DR   InterPro; IPR009088; TFIIA_b-brl.
DR   PANTHER; PTHR14445; GRB10 INTERACTING GYF PROTEIN; 1.
DR   PANTHER; PTHR14445:SF38; GRB10-INTERACTING GYF PROTEIN 2; 1.
DR   Pfam; PF02213; GYF; 1.
DR   Pfam; PF03153; TFIIA; 1.
DR   SMART; SM00444; GYF; 1.
DR   SMART; SM01371; TFIIA; 1.
DR   SUPFAM; SSF55277; GYF domain; 1.
DR   SUPFAM; SSF50784; Transcription factor IIA (TFIIA), beta-barrel domain; 1.
DR   PROSITE; PS50829; GYF; 1.
PE   2: Evidence at transcript level;
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163}.
FT   DOMAIN          510..558
FT                   /note="GYF"
FT                   /evidence="ECO:0000259|PROSITE:PS50829"
FT   REGION          64..162
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          190..238
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          262..448
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          637..708
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        100..136
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        138..159
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        190..217
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        262..281
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        311..362
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        385..408
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        410..426
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        433..448
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        657..681
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        688..708
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AFO97440.1"
SQ   SEQUENCE   756 AA;  85683 MW;  0059E5465D92DC1E CRC64;
     REEMLALYVK DLKIPVDLSD KEFLPILQEE PLPPLALVPF TEEEQRNFSM SVNSLAVLRL
     MGRGGGTVAG APRGRSSSRG RGRGRGEGGF YQRSFDEGEV GFGRGSREMH RSQSWEERGE
     RRFEKPGRKD PGSSHVKDQH PSLCTQNDFL SSTSGFLTKP VRPTFEEVGT STTRKHEFIR
     SESDNWRVCR DEQNGEEDDG GWRLAGPRRE GDRWRTHSPG PFDILTRPEN RYEADAPRSA
     GWREVLERRR RFEFDFRDRD DERGYRRVPS GSGSLEDERD SLPEWCLEDA EEETGTFDSS
     GAFMSLKIKK APKEPIPEEQ ELDFKPVEDG DERSNSENEK EAKEPDKTTK RESFEEPVRT
     EEPKAVPSTA LPPPPSQSHI FVIPSTHNKE ERKPEKNNKI EATEKCRPAA SEEMNTSASS
     PPQKKTPAVS AVPIATVSKS SPSPSSVTTV VTNVSIPQDN DDDGLKHLEQ EAEKMVASLQ
     DNALDDERLS TKIQEKRTKS STLPLSHDAA MKWFYKDPQG EIQGPFSNQE MAEWFQAGYF
     TMSLLVKRGC DEGFQPLGEV IKMWGRVPFA PGPSPPPLLG DLDQERLKRQ QELATLNLFQ
     MQQIQYQQFL QAQLMTRQQY AQAIAHQQKA VVGSITSQQQ QQQQQPPLVM QVDGAGDTSS
     EEDEDDEEDE YDDEEEEKDK EEVGEGGQVE EESLNSEDDV SDEEGQELFD TENVVVCQYD
     KIHRSKNKWK FHLKDGIMNL NGRDFVFSKA IGDAEW
//
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