ID A9U4K2_PHYPA Unreviewed; 1157 AA.
AC A9U4K2;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 28-JUN-2023, entry version 81.
DE SubName: Full=Predicted protein {ECO:0000313|EMBL:EDQ49394.1};
GN ORFNames=PHYPADRAFT_102008 {ECO:0000313|EMBL:EDQ49394.1};
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;
RN [1] {ECO:0000313|EMBL:EDQ49394.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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).
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DR EMBL; DS545391; EDQ49394.1; -; Genomic_DNA.
DR RefSeq; XP_001785787.1; XM_001785735.1.
DR AlphaFoldDB; A9U4K2; -.
DR eggNOG; KOG2135; Eukaryota.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR CDD; cd12257; RRM1_RBM26_like; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR045137; RBM26/27.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR000571; Znf_CCCH.
DR PANTHER; PTHR14398; RNA RECOGNITION RRM/RNP DOMAIN; 1.
DR PANTHER; PTHR14398:SF0; ZINC FINGER PROTEIN SWM; 1.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR PROSITE; PS50102; RRM; 1.
DR PROSITE; PS50103; ZF_C3H1; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00723};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00176}; Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00723};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00723}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1157
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002742019"
FT DOMAIN 428..456
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 692..764
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT ZN_FING 428..456
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 221..339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 495..515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 560..600
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 613..657
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 767..795
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 883..902
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 936..961
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1091..1134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 841..882
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 282..312
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 560..580
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 767..790
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1120..1134
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1157 AA; 123951 MW; 1E061E6D34AB5204 CRC64;
MEVTVLALTL SVWACLAFAL PGVAFRVYGV KEVSCADSGF SVRIRVAHTC KLLVLNYFEE
KLEKKGEKNS SVGAWSRIEH PSNCENLDVT STRRLTRMQC NQCSAGYRSC GSSNDRECCG
YVGRQSNDQR ELSQTDADPT LLSDYVAALL KKSKPKKELH TLCVNQLYDI LGEGTKLFVV
NLFHALDDGT ISSGMEDLAG VKLLDNTESL TGAAEIRISP SHVERLPSAG AQDWEDELEE
EESSDDDRNH KHRRRVSRSR SADRVDEPNV SRYSGGGSND LKRQAGDHRR GGGQSDRERS
LKFDRRSGRD AGGRFSNGDQ AERGLIRGGG PPFRGDAPNV RLDGVRMGRG RGAGNWAGPI
PPPFADAPPL LPPNAGFFPN GRGLGGLGTG WPGGFGHMGG MGAGSLELSH GGRGPPGVMN
LGMGMGIGPV RPRCLDFEER GFCLRGDLCP MDHGSHIVVE DVQSLSKFNL PVNLSNGRGM
AVAAGQLAAS NTMLPAPAPA SSRGSRGNRE PSISPLEAPI MVNGQVPGAE PDLYDPDQPL
WNNDRPEATG RIRKLSAFQA EHSEVGKEKA ELKKSTEGRG IDGGNRGANS SGLHGGDAGS
TVWDRIGPVD VSAASGEAKV EEQRSQGRGV SWQPGRWGDR ESDSGATNLN TNPGRVRGAA
GWAEVGLPLN RSKEGTNLGP RAPGRSTERA QRTLYVNCIP PNSNQQEVLL THFEKFGRVV
DVRIPSHSHR AFVQFATREE AESALASPDA VLGNRFIRLS WANRDSITSD NGASTSSTGQ
PPTTGSEPAG SHAAQLVKGR GKLSLTGLNK VVAGLSGAST VEGSNKATTL NGSASSVPSP
VAVASKKQEE LELMREKIRQ KQEALAQKRD DFRRKLNKLA SQGVTGAEDY QGDHARKRQK
ADNFGDLRPC KVDAAVRSLP SNFGLKKINA VDVTQVGASQ VSSKPTRSPH PRTASGTSTG
HSAVAWGPAR FKLDNRTTAF RVLPPFPFTV SDARKRVWPG LSISSLFSRV YFAFVEVAAV
RDHFAAFGEL SSVEVEAAEG HKADSEHTWS PNSSIRISYT TRWSAERAMM QGRCFHGQSL
NLVWVSAAST SRPSESPAPA GKVAPAEHET TGRGGASEVS EEASAEEVHH VESKLNLKDK
AHLIPARVVD SPITPDA
//
