ID W2ZD06_PHYPR Unreviewed; 1319 AA.
AC W2ZD06;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=EF-hand domain-containing protein {ECO:0000259|PROSITE:PS50222};
GN ORFNames=F442_08361 {ECO:0000313|EMBL:ETP45197.1};
OS Phytophthora parasitica P10297.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=1317064 {ECO:0000313|EMBL:ETP45197.1, ECO:0000313|Proteomes:UP000018948};
RN [1] {ECO:0000313|EMBL:ETP45197.1, ECO:0000313|Proteomes:UP000018948}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P10297 {ECO:0000313|EMBL:ETP45197.1,
RC ECO:0000313|Proteomes:UP000018948};
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., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Phytophthora parasitica P10297.";
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:ETP45197.1}.
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DR EMBL; ANIY01001746; ETP45197.1; -; Genomic_DNA.
DR EnsemblProtists; ETP45197; ETP45197; F442_08361.
DR Proteomes; UP000018948; Unassembled WGS sequence.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR CDD; cd00051; EFh; 2.
DR Gene3D; 1.10.238.10; EF-hand; 2.
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; 2.
DR Pfam; PF00415; RCC1; 3.
DR Pfam; PF13540; RCC1_2; 1.
DR PRINTS; PR00633; RCCNDNSATION.
DR SMART; SM00054; EFh; 4.
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; 4.
DR PROSITE; PS50222; EF_HAND_2; 4.
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:UP000018948};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 85..120
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 121..156
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 166..201
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 202..237
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT REPEAT 845..902
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 903..959
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 960..1015
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REGION 1..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 363..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 452..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 557..577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 265..293
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 714..782
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 54..74
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..381
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 386..406
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1319 AA; 147164 MW; 10963A8C59D4C4DA CRC64;
MGLFGKKGNG SRVAEGGGGA LAAASPLTTA SPLKGKSGDL ELFGADSDDS DDDATIDRYA
KDGGDEEMDE KEAAEAEKRK VAVLNSKLSP EELFKKYDTD GSGNISAPEF LAMLPDLGIS
ISAAKAMRIF RKCDTDGGGE IDLTEFKMAM FAVDPVSGNP LGFSPSTLLG PRDAFELFDE
DGTGQIDELE FADVLEYFGM DVSDEKQEKI FKKYDKDKSG HIDYQEFRSM WIKLVDVREE
LTKRGVEVPK HTRLVKLQQM LETILDEEEA REAAALEEAK RFLQRQRDKE LREQLGRKAI
VRAEDELAAA LDAAGQVYII GSGKYDQFID DPVTRDEDLF PGFKAVSEIW SYRVNPIIQE
VHTTKPKAAT TDHKQAKDTE LSPEAANKSA PKNQEVKNTD PPPGNQLNAP ASKYVRRRVE
NKRWKFQSPP RLNKQTISET KILIRAISRE MDNANERNDG EKGAVNSPTN SSEVVEITHD
ENNQEEEELA KLFFENREFV RSLRFRSTTL MTNTGPLWGK SVVQGAISDS VAFAVTSSGS
VFSWGGRSST WEASNRRVSG FDSDSDDSID DTGQEKDKKI SEFGMQTKVT PRSALQKMCT
PEQLEGLRDP DVEAREEVLL AIEARQNEEN QRYERLKRVA MYYDVWEPPP SNATRLLFME
QVVLPKIEYE QLVTSGQLRG LEFQKITKMD LSLALGECFE LEIEVKGEAG HAAFKEMERV
INEYSQDKKR IQEKQTNMLQ AEKDKMLQEW QDVKTLRESR HAKEEEDARA RVIEKINRAD
RAYESRAARR VVQMEDMVPE FTTRGENSRI EMSGITTRGP PLHSPRESYV VIELHVITCG
MLFRRSLYSC GIGSSGRLGL QPNERGANCF DSNHPQRVQA FNGLNLRQVS CSFSHSAAID
SEGSLYTWGS ACTGKLGVGI VEDEYKQYSM TPLLVKFPGK RRIRSVSCGP SHTGAVSTAG
ELFMWGSANG GRLGLGQHVI DIVVVPTLVR DLVNKKIRVW QVSCGTAHSA FCTEVTSEFN
GGSKKLLGGQ VYVCGGATAL SRYVLSWERI PQLDGVGVRQ VSCGGSHTAA VSSYGELYTW
GRNYHGCTGH DASRRFIEKP ELLKCLHVEP YNLALGKICR QISIYNEQGP QLAVNGDIEG
ALATCTHTQM EDKPWWEVDL GQPAVIEKIR LWNRTDEPLN PSKSRSEYSG RLFPCWVFVS
EFAFKDLEGK EGLRAAKVQS SAFELFRTNK RMTEWILPTA NAVGQFVRVQ LQNKNFLHFA
QVEVFGVYSA FKYVGKVGAV QCSTDATLVI MSPISTQRCV RLQYNAVSIS TSLSLQRAG
//
