ID A0A0F8BS98_CERFI Unreviewed; 792 AA.
AC A0A0F8BS98;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=MYND-type zinc finger protein samB {ECO:0000256|ARBA:ARBA00019873};
DE AltName: Full=Suppressor of anucleate metulae protein B {ECO:0000256|ARBA:ARBA00031540};
GN Name=samB {ECO:0000313|EMBL:KKF95448.1};
GN ORFNames=CFO_g2178 {ECO:0000313|EMBL:KKF95448.1};
OS Ceratocystis fimbriata f. sp. platani.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Microascales; Ceratocystidaceae; Ceratocystis.
OX NCBI_TaxID=88771 {ECO:0000313|EMBL:KKF95448.1, ECO:0000313|Proteomes:UP000034841};
RN [1] {ECO:0000313|EMBL:KKF95448.1, ECO:0000313|Proteomes:UP000034841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFO {ECO:0000313|EMBL:KKF95448.1,
RC ECO:0000313|Proteomes:UP000034841};
RA Belbahri L.;
RT "Genome sequence of Ceratocystis platani, a major pathogen of plane
RT trees.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in determination of the onset of polarized growth
CC and morphogenesis. Plays a role in the regulation of branching in
CC hyphae and spore formation. {ECO:0000256|ARBA:ARBA00025097}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the MUB1/samB family.
CC {ECO:0000256|ARBA:ARBA00010655}.
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:KKF95448.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LBBL01000094; KKF95448.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F8BS98; -.
DR Proteomes; UP000034841; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 6.10.140.2220; -; 1.
DR InterPro; IPR002893; Znf_MYND.
DR PANTHER; PTHR47442; MYND-TYPE ZINC FINGER PROTEIN MUB1; 1.
DR PANTHER; PTHR47442:SF1; MYND-TYPE ZINC FINGER PROTEIN MUB1; 1.
DR Pfam; PF01753; zf-MYND; 1.
DR SUPFAM; SSF144232; HIT/MYND zinc finger-like; 1.
DR PROSITE; PS50865; ZF_MYND_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000034841};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00134}.
FT DOMAIN 746..787
FT /note="MYND-type"
FT /evidence="ECO:0000259|PROSITE:PS50865"
FT REGION 134..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 182..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 241..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 345..371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 394..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 446..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 632..693
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..159
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..311
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..461
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 634..660
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 673..692
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 792 AA; 86165 MW; 9AFF7366C489FBDF CRC64;
MREVNFSIPN VNKASVGITT ALYDRRALDC TSTLPLINSL NHLAYLTTSS ARIRDILTVD
GGIERLICIL KQGRSTDVMA MWKWNLAFQC VVNIGVRGTE AVRTRVVEAD VVPVIATILE
NYIRLVDKCQ EKEEQKKKAI AEHHHHHHHH HRSHNHGNHP HGHPTVPSRS LRTTAVPTAI
ALNHHRSSTS TSTSTSASTS TSTSASTSTS TSTSTSISAS TPVAPVITPQ VQLLATSLTS
AATTTSSNLL EPRSGRRGPV PPAIDVSGSY GGNARVSPSR SSPRSTNEAS YTGSQAVNNS
ISTNSNSNPT AILRPLESRR ADRMAYTQAH IVNGLSTVSA QLSVASGQPR TASGSRPERA
MTAPGMGSRP IIQPLGSAAT DLESVLARLA SRPISPTTPV PPHHRPGAAT AAAADMPGAA
GVSPLRLQDA TRDALAPVAR TIVRPQASIA ESENSSGNEG AADESRDIVM TGTDDTTILQ
NTAQLPVGIQ DVNMEHTELL GQEGMDLAVT VPEVVSENQD ATVFNITHDP TGIQVDPVPG
ETTNVNPRVA PLPVTSQPNT TGSVPRFLAD SRASVLNDPQ MLAVIPREED VLMSLQLLAY
VSKYCGLRSY FQHSHLVPKL KIGKEYLRFD DDPSDSSSGL SNNSGNASTL MFSSQHSYQP
TSKPKHKHVH KHDHHQNDDC ENEHHDHGDQ DEEEEYLLPD DFNIFPLVEK FTVRHHSPDM
QYWAGVVMRN LCRKDDSRGG IRQCAYYQCG KWEEFTRQFA KCRRCRRTKY CSKECQKSAW
AFHRHWCVAA SQ
//
