ID A0A2K1IS78_PHYPA Unreviewed; 1433 AA.
AC A0A2K1IS78;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Transcription initiation factor TFIID subunit 2 {ECO:0000256|ARBA:ARBA00017363};
GN ORFNames=PHYPA_026247 {ECO:0000313|EMBL:PNR32122.1};
OS Physcomitrium patens (Spreading-leaved earth moss) (Physcomitrella patens).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta;
OC Bryophytina; Bryopsida; Funariidae; Funariales; Funariaceae; Physcomitrium.
OX NCBI_TaxID=3218 {ECO:0000313|EMBL:PNR32122.1};
RN [1] {ECO:0000313|EMBL:PNR32122.1, ECO:0000313|Proteomes:UP000006727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Gransden 2004 {ECO:0000313|EnsemblPlants:Pp3c21_15920V3.1,
RC ECO:0000313|Proteomes:UP000006727};
RX PubMed=18079367; DOI=10.1126/science.1150646;
RA Rensing S.A., Lang D., Zimmer A.D., Terry A., Salamov A., Shapiro H.,
RA Nishiyama T., Perroud P.-F., Lindquist E.A., Kamisugi Y., Tanahashi T.,
RA Sakakibara K., Fujita T., Oishi K., Shin-I T., Kuroki Y., Toyoda A.,
RA Suzuki Y., Hashimoto S.-I., Yamaguchi K., Sugano S., Kohara Y.,
RA Fujiyama A., Anterola A., Aoki S., Ashton N., Barbazuk W.B., Barker E.,
RA Bennetzen J.L., Blankenship R., Cho S.H., Dutcher S.K., Estelle M.,
RA Fawcett J.A., Gundlach H., Hanada K., Heyl A., Hicks K.A., Hughes J.,
RA Lohr M., Mayer K., Melkozernov A., Murata T., Nelson D.R., Pils B.,
RA Prigge M., Reiss B., Renner T., Rombauts S., Rushton P.J., Sanderfoot A.,
RA Schween G., Shiu S.-H., Stueber K., Theodoulou F.L., Tu H., Van de Peer Y.,
RA Verrier P.J., Waters E., Wood A., Yang L., Cove D., Cuming A.C., Hasebe M.,
RA Lucas S., Mishler B.D., Reski R., Grigoriev I.V., Quatrano R.S.,
RA Boore J.L.;
RT "The Physcomitrella genome reveals evolutionary insights into the conquest
RT of land by plants.";
RL Science 319:64-69(2008).
RN [2] {ECO:0000313|EMBL:PNR32122.1, ECO:0000313|Proteomes:UP000006727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Gransden 2004 {ECO:0000313|EnsemblPlants:Pp3c21_15920V3.1,
RC ECO:0000313|Proteomes:UP000006727};
RX PubMed=29237241; DOI=10.1111/tpj.13801;
RA Lang D., Ullrich K.K., Murat F., Fuchs J., Jenkins J., Haas F.B.,
RA Piednoel M., Gundlach H., Van Bel M., Meyberg R., Vives C., Morata J.,
RA Symeonidi A., Hiss M., Muchero W., Kamisugi Y., Saleh O., Blanc G.,
RA Decker E.L., van Gessel N., Grimwood J., Hayes R.D., Graham S.W.,
RA Gunter L.E., McDaniel S.F., Hoernstein S.N.W., Larsson A., Li F.W.,
RA Perroud P.F., Phillips J., Ranjan P., Rokshar D.S., Rothfels C.J.,
RA Schneider L., Shu S., Stevenson D.W., Thummler F., Tillich M.,
RA Villarreal Aguilar J.C., Widiez T., Wong G.K., Wymore A., Zhang Y.,
RA Zimmer A.D., Quatrano R.S., Mayer K.F.X., Goodstein D., Casacuberta J.M.,
RA Vandepoele K., Reski R., Cuming A.C., Tuskan G.A., Maumus F., Salse J.,
RA Schmutz J., Rensing S.A.;
RT "The Physcomitrella patens chromosome-scale assembly reveals moss genome
RT structure and evolution.";
RL Plant J. 93:515-533(2018).
RN [3] {ECO:0000313|EnsemblPlants:Pp3c21_15920V3.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (DEC-2020) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the TAF2 family.
CC {ECO:0000256|ARBA:ARBA00010937}.
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DR EMBL; ABEU02000021; PNR32122.1; -; Genomic_DNA.
DR STRING; 3218.A0A2K1IS78; -.
DR PaxDb; 3218-PP1S167_49V6-1; -.
DR EnsemblPlants; Pp3c21_15920V3.1; Pp3c21_15920V3.1; Pp3c21_15920.
DR EnsemblPlants; Pp3c21_15920V3.2; Pp3c21_15920V3.2; Pp3c21_15920.
DR EnsemblPlants; Pp3c21_15920V3.7; Pp3c21_15920V3.7; Pp3c21_15920.
DR Gramene; Pp3c21_15920V3.1; Pp3c21_15920V3.1; Pp3c21_15920.
DR Gramene; Pp3c21_15920V3.2; Pp3c21_15920V3.2; Pp3c21_15920.
DR Gramene; Pp3c21_15920V3.7; Pp3c21_15920V3.7; Pp3c21_15920.
DR Proteomes; UP000006727; Chromosome 21.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005669; C:transcription factor TFIID complex; IEA:InterPro.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd09839; M1_like_TAF2; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR Gene3D; 2.60.40.1730; tricorn interacting facor f3 domain; 1.
DR InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR InterPro; IPR037813; TAF2.
DR PANTHER; PTHR15137; TRANSCRIPTION INITIATION FACTOR TFIID; 1.
DR PANTHER; PTHR15137:SF9; TRANSCRIPTION INITIATION FACTOR TFIID SUBUNIT 2; 1.
DR Pfam; PF01433; Peptidase_M1; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF63737; Leukotriene A4 hydrolase N-terminal domain; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000006727};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 265..288
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 312..509
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT REGION 635..654
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1054..1099
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1206..1414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1076..1099
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1225..1245
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1263..1293
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1299..1331
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1344..1395
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1433 AA; 160216 MW; F3BB8F914BF1407B CRC64;
MAKQRKQKQK EHLPSDVEVV MSDEGFTSSC CAILHQKLCV AIDLSTQRIY GHTELKIAAK
QGGKGGGVIG LHARDLHIEQ VLVDGVEAHF EILNQNNYDE VYINDGPNPA PYTKSNQEAA
DDAYKKYSGD LHVESQPELL IFPPPSKPAG PAQVTETTLE VEAVLEHGFA QTAPDTTSET
TSLVHIVRVD YWVEKPLSGA HFEGNLFYTN NQLRRARCWF PCVDSTLQRC SFDLEFTVHS
EYVAVSNGKL LHQVYSKEGT HLKTYVYSLS IPIAASFVSL VVAPLVVLPD RHHSNVSHLC
MPGMDATLNA SVNTFHSVFS LYEEYLGAPF PFECYKQVFL PGDAVFSTSS VGASLATFSA
DLLADEHIID QAISTRIKLA HALAQQWFGI FIIPDSAGDD WLLEGLAGML TDLFVKRFLG
NNEARFRRYK ANEAVCLVEV EGAPVLSPPA GLDINMCGTE KLGVLGKIRT WKATAVVQML
ERQMGPEPFR KVLQRIIMRA QDPDSKNQTL STTEFRHFAN KLGNLERPFL KDFFPRWVES
SGCPRLRMGF VYSKRRNMVE LAVRRESTSI PKRVGAVGKL EIPDLKLRNS DMGWPGMMSI
RLHELDGMYD HPSLPMAGDC YQLLELQCHS KLAGRRMQRP KKGTKGEAVE DRVDATPAQS
LESPLLWVRG DPELEYLAEL NLIQPEQMWI NQLEKDRDVI GQVQAVAALR AHPRTSFAVV
NALNNCLIDP KVFCRVRIEA AAALASTASE GTSHMGLQNL IKYYKSRRFD PDISLPKPND
FHDFSEYFVL EAIPGAIAEV RGNDGKSPLE ASEFILHILK HNDNNGNVHS DVYWLASVIE
AVGSLEFGKQ DLRTLARILK QIDRFLQYDR LMPSYNGVVA TSCIRTLANI AIRFSYALSI
ERVKLLLKQF KDRDKINWRV RVAALKALLD IEYYSKGLEA AVILALQLIH SEFSFPVKSK
IMKHVGRIAS LIEKGSCKIG SVSVARLMTL LKSSTAFHNV MLRHSVFSFL QVLAGRSASL
YRSAEYLSKL APKHASQDTG SAKAKNAFKL RLRPAQSPVP AQPEPLKLRL VLPSSSKDDA
NRKDIDSSGS EREMDEQKGR FSIKLKLRKS SSALDGPVED ASQALEVSTG AAPMDHHVAS
SPPNCMKEVN LHEVTDSNLG FSQLESSRMQ LLDTQPDDSQ TLLMNTICVG VNGDIQDTSI
KEMKHKDTNG TEGQIPEENE GGGSPGGFNQ GNTHPGRNSR GSMEQQPPFD MYGEDTQDGT
GESSDDMNKS LNESQTVDSK LQRFNSLSGM TGAENCTRDG GLEETESQKR VEKQCDDKKE
RRHDKMDKKD PKEKKKKKKK KKHDKNDSDY LEKKRKRKEE REQRHRQEGH KSLKEEKHRK
EDRDVKVEER PASDAPANNH LHLEDATIEN QGVSDTMKVK FKFKKPRTSA SNI
//
