ID A0A2V1ARZ7_9ASCO Unreviewed; 1760 AA.
AC A0A2V1ARZ7;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=FH2 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=CXQ85_004513 {ECO:0000313|EMBL:PVH20997.1};
OS [Candida] haemuloni.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Metschnikowiaceae; Metschnikowiaceae incertae sedis;
OC Candida/Metschnikowiaceae.
OX NCBI_TaxID=45357 {ECO:0000313|EMBL:PVH20997.1, ECO:0000313|Proteomes:UP000244309};
RN [1] {ECO:0000313|EMBL:PVH20997.1, ECO:0000313|Proteomes:UP000244309}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B11899 {ECO:0000313|EMBL:PVH20997.1,
RC ECO:0000313|Proteomes:UP000244309};
RA Chow N.A., Gade L., Batra D., Rowe L.A., Ben-Ami R., Loparev V.N.,
RA Litvintseva A.P.;
RT "Genome Sequence of a Multidrug-Resistant Candida haemulonii Isolate from a
RT Patient with Chronic Leg Ulcers in Israel.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the formin homology family. BNI1 subfamily.
CC {ECO:0000256|ARBA:ARBA00037935}.
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:PVH20997.1}.
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DR EMBL; PKFO01000004; PVH20997.1; -; Genomic_DNA.
DR STRING; 45357.A0A2V1ARZ7; -.
DR EnsemblFungi; CXQ85_004513-t46_1; CXQ85_004513-t46_1-p1; CXQ85_004513.
DR VEuPathDB; FungiDB:CXQ85_004513; -.
DR OrthoDB; 1118745at2759; -.
DR Proteomes; UP000244309; Unassembled WGS sequence.
DR GO; GO:0015629; C:actin cytoskeleton; IEA:UniProt.
DR GO; GO:0005938; C:cell cortex; IEA:UniProt.
DR GO; GO:0032153; C:cell division site; IEA:UniProt.
DR GO; GO:0003779; F:actin binding; IEA:InterPro.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
DR GO; GO:0051301; P:cell division; IEA:UniProt.
DR Gene3D; 6.10.30.50; -; 1.
DR Gene3D; 1.20.58.2220; Formin, FH2 domain; 1.
DR Gene3D; 1.10.238.150; Formin, FH3 diaphanous domain; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR014767; DAD_dom.
DR InterPro; IPR015425; FH2_Formin.
DR InterPro; IPR042201; FH2_Formin_sf.
DR InterPro; IPR010472; FH3_dom.
DR InterPro; IPR014768; GBD/FH3_dom.
DR InterPro; IPR010473; GTPase-bd.
DR PANTHER; PTHR47102; PROTEIN BNI1; 1.
DR PANTHER; PTHR47102:SF2; PROTEIN BNI1; 1.
DR Pfam; PF06367; Drf_FH3; 1.
DR Pfam; PF06371; Drf_GBD; 1.
DR Pfam; PF02181; FH2; 1.
DR SMART; SM01139; Drf_FH3; 1.
DR SMART; SM01140; Drf_GBD; 1.
DR SMART; SM00498; FH2; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF101447; Formin homology 2 domain (FH2 domain); 1.
DR PROSITE; PS51231; DAD; 1.
DR PROSITE; PS51444; FH2; 1.
DR PROSITE; PS51232; GBD_FH3; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000244309}.
FT DOMAIN 218..659
FT /note="GBD/FH3"
FT /evidence="ECO:0000259|PROSITE:PS51232"
FT DOMAIN 1181..1591
FT /note="FH2"
FT /evidence="ECO:0000259|PROSITE:PS51444"
FT DOMAIN 1605..1637
FT /note="DAD"
FT /evidence="ECO:0000259|PROSITE:PS51231"
FT REGION 1..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 850..893
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 990..1011
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1024..1053
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1065..1184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1645..1760
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 680..846
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1565..1592
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..212
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 863..877
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1037..1053
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1097..1162
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1645..1662
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1663..1678
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1712..1726
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1738..1760
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1760 AA; 198157 MW; 43DA82C9A1B7533B CRC64;
MSSRKRIDPY HAASHNEDME KASSAYYAPL SAPRPSRNQA TSPQQPSSSQ RMSSGSIFSI
RRGKNHQTGD THVDESDNAS VVSGNSLGSS SAFYPSKRHN SMVSVGSGGS GKSSSIVPGP
QVTSSSHSRS GSIYSFNTSS NPYDHVTERS ARGQDSKSHQ NQQSQQPQQA STPQHHQPQS
RAPSFALSRK ATGSSLFSRP SLSTTTTTED VPQPEPLRKP QNPIEIERMF RDLMEKRDFR
SLPQSARQEM LNYSVDKKWM LVQQDALHEH SKQASKSKAS PEYYTRKLIA KTISSDELEN
LWVSLRTEPI DWVREFIYDF QGDVALSSYL IKVHDQMGSQ DIDDIQDDIF NKEFNTLKCL
KCMMNQKLGA ERAKTDDSLY INAITGSLLS PRIATRRIAA ESLTFMIVYY CRVGGDHNKY
HKVLRSLDGL QQKPYYEFVP ASNASMKKTL QRKPPPEESN HRFELWLRLV DKTIDGRGKY
KNSLVGASEE LKYQFAVNGS SVGGPSHVEN QLMEYCLGTM LLVNTIVEYG LDFRVRIHLR
TQFTAAGIEQ LLGKFQDLGY DSLVKQVQKY REMAEADEME LKTKQQIDED LDFNNPVDLV
RSLWTNVQNS EAQGHFLSAM QHIYLNQTEK RDDSEEVTRS LRLLDGLIQN VTGAHTSNDE
SAVGIAINRL YAGLSTDDMY RKAINEVKLY KKIAEEATAE RDEISRQLSI GSEGLITNMT
NEIKEQEIVL RRTRRMNEEL QDELEDLKRK HLREKQEQEV EMRELLIMLN SAQIDSKKDK
GKTTVSVQTS NEKLIKKLQK QIHRKKNEFR LDNKQLGTSV EPSSRLRALR DQMADIENLA
RELEMTDFET YSLPKEEPEP VQEVAEPEPE PETPEPEELP PVPEGPKRSV REDDLEKLEK
LRKKLASLQS ESNDIMKFNN KSLFSKQKYL AMERLRELET NFMDFNIDFD IDENEAALLG
MMDASVKSKI QEELESVKKL NTDLRSQLAA IKDDKSPSKG SSASPSSDML SKIEAKYAQG
KVVVDGSDRA VKGSNSPAKD YKSNRKSTIN TLDPKFLNEL SSKVKEAEAI PSNASSDDEN
FEDSVDKVEE TAVEPPKLTG APPPPPPPLP PALGGAPPPP PPPLPPSLNG GAPPPPPPPP
PPLGGPFGAA PAPPPPAPPL PSGSARSTAS PSPVPQTPHP FEMYPRPKKK LKQLHWEKFD
NGENNSNSFW NESQSQTIAT ELMDKGHFAA KEIKKLATKK KEDVDKVTFL ARDVAQQFGI
NLHSFNNLSD EEVIDKILRC DKEVLTNPAI LEFLGKEEIT EVSNSLARNL EPYSTDYKTE
EISKPEKDPS ELQRPDRIYL ELIYNLQHYW KSRVRSLKTI ANYEKDYDDL VTKLRALDEA
VDKIKQSKEL RSVFDIILAV GNYMNDTSKQ AKGFKLSSLQ RLSFVKDEKN SMSFLHYVEK
TVRTLYPELL TFMEDLALCV PVAKFSIENI SNDCKEYGQA IKNVQSSIDI GNLSDMSNFH
PKDRVLKVVT PTLPRAKKKA DLLQDQANYT LKEFETLMRY FGEDPNDSFV RNSFFSKFTS
FLSEFKKAQR ENLKREEELR VYEQRKKLLE NTTKQNKAKK ESGSEDEDDN VMDSLLEKLK
AAGPQRGEPS SARKRALMKK HLMENLKKSG GATGEEDSRE SSPSRAGSSV TDLSSVEEAE
NQPEAAGDAD VGSRARNLLQ ELRKAEGSDK VSSASAFRQQ RQRRRQLSTV GEVDVPGDSP
SPEEKEAEPK ETSPKETPKE
//
