ID V9FAD4_PHYPR Unreviewed; 1345 AA.
AC V9FAD4;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=EF-hand domain-containing protein {ECO:0000259|PROSITE:PS50222};
GN ORFNames=F443_08424 {ECO:0000313|EMBL:ETI47352.1};
OS Phytophthora parasitica P1569.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=1317065 {ECO:0000313|EMBL:ETI47352.1, ECO:0000313|Proteomes:UP000018721};
RN [1] {ECO:0000313|EMBL:ETI47352.1, ECO:0000313|Proteomes:UP000018721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P1569 {ECO:0000313|EMBL:ETI47352.1,
RC ECO:0000313|Proteomes:UP000018721};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA Machado M., Johnson C.S., Arredondo F., Hong C., Coffey M., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Phytophthora parasitica P1569.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ETI47352.1}.
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DR EMBL; ANIZ01001442; ETI47352.1; -; Genomic_DNA.
DR EnsemblProtists; ETI47352; ETI47352; F443_08424.
DR OrthoDB; 53770at2759; -.
DR Proteomes; UP000018721; Unassembled WGS sequence.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR CDD; cd00051; EFh; 1.
DR Gene3D; 1.10.238.10; EF-hand; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.130.10.30; Regulator of chromosome condensation 1/beta-lactamase-inhibitor protein II; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR009091; RCC1/BLIP-II.
DR InterPro; IPR000408; Reg_chr_condens.
DR PANTHER; PTHR22870; REGULATOR OF CHROMOSOME CONDENSATION; 1.
DR PANTHER; PTHR22870:SF437; X-LINKED RETINITIS PIGMENTOSA GTPASE REGULATOR-RELATED; 1.
DR Pfam; PF13499; EF-hand_7; 1.
DR Pfam; PF00415; RCC1; 3.
DR Pfam; PF13540; RCC1_2; 1.
DR PRINTS; PR00633; RCCNDNSATION.
DR SMART; SM00054; EFh; 3.
DR SUPFAM; SSF47473; EF-hand; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF50985; RCC1/BLIP-II; 1.
DR PROSITE; PS00018; EF_HAND_1; 3.
DR PROSITE; PS50222; EF_HAND_2; 3.
DR PROSITE; PS00626; RCC1_2; 1.
DR PROSITE; PS50012; RCC1_3; 3.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000018721};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 9..44
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 54..89
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 90..125
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT REPEAT 736..793
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 794..850
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 851..906
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REGION 251..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 340..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 445..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1293..1345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 153..181
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 602..632
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 254..269
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..294
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1295..1328
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1329..1345
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1345 AA; 151181 MW; D5AF0FD0FBA16D12 CRC64;
MLPDLGISIS AAKAMRIFRK CDTDGGGEID LTEFKMAMFA VDPVSGNPLG FSPSTLLGPR
DAFELFDEDG TGQIDELEFA DVLEYFGMDV SDEKQEKIFK KYDKDKSGHI DYQEFRSMWI
KLVDVREELT KRGVEVPKHT RLVKLQQMLE TILDEEEARE AAALEEAKRF LQRQRDKELR
EQLGRKAIVR AEDELAAALD AAGQVYIIGS GKYDQFIDDP VTRDEDLFPG FKAVSEIWSY
RVNPIIQEVH TTKPKAATTD HKQAKDTELS PEAANKSAPK NQEVKNTDPP PGNQLNAPAS
KYVRRRVENK RWKFQSPPRL NKQTLSETKI LIRAISREMD NANERNDGEK GAVNSPTNSS
EVVEITHDEN NQEEEELAKL FFENREFVRS LRFRSTTLMT NTGPLWGKSV VQGAISDSVA
FAVTSSGSVF SWGGRSSTWE ASNRRVSGFD SDSDDSIDDT GQEKDKKISE FGMQTKVTPR
SALQKMCTPE QLEGLRDPDV EAREEVLLEI EARQNEENQR YERLKRVAMY YDVWEPPPSN
ATRLLFMEQV VLPKIEYEQL VTSGQLRGLE FQKITKMDLS LALGECFELE IEVKGEAGHA
AFKEMERVIN EYSQDKKRIQ EKQTNMLQAE KDKMLQEWQD VKTLRESRHA KEEEDARARV
IEKINRTDRA YESRAARRVV QMEDMVPEFT TRGENLRIEM SGITTRGPPL HSPRGSIAIA
SVSAGGSHVA LLTQDGSLYS CGIGSSGRLG LQPNERGANC FDSNHPQRVQ AFNGLNLRQV
SCSFSHSAAI DSEGSLYTWG SACTGKLGVG IVEDEYKQYS MTPLLVKFPG KRRIRSVSCG
PSHTGAVSTA GELFMWGSAN GGRLGLGQHV IDIVVVPTLV RDLVNKKIRV WQVSCGTAHS
AFCTEVTSEF NGGSKKLLGG QVYVCGGATA LSRYVLSWER IPQLDGVGVR QVSCGGSHTA
AVSSYGELYT WGRNYHGCTG HDASRRFIEK PELLKCLHVE PYNLALGKIC RQISIYNEQG
PQLAVNGDIE GALATCTHTQ MEDKPWWEVD LGQPAVIEKI RLWNRTDEPL NPSKSRSEYS
GRLFPCWVFV SEFAFKDLEG KEGLRAAKVQ SSAFELFRTN KRMTEWILPT ANAVGQFVRV
QLQNKNFLHF AQVEVFGVYS AFKYVGKVGA VQCSTDATLV IMSPISTQSV LDDYYLRAIQ
ADADHASILR QYDAYERSFR KFGRGTAETL DGPCRLCRVF RDCEICEFYA SAKYSRRAAS
DNGQKPLPVR LVGDRMGLKE LVQVAMAEGT LEAEQQEQLR QEQEAADIAR EAEAERQRAE
EQERNKRQSR LLNPFQGLNF RNKKT
//
