ID   A0A1X7RUI5_ZYMTR        Unreviewed;      1050 AA.
AC   A0A1X7RUI5;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=SWIRM domain-containing protein {ECO:0000259|PROSITE:PS50934};
GN   ORFNames=ZT3D7_G6053 {ECO:0000313|EMBL:SMQ50900.1};
OS   Zymoseptoria tritici ST99CH_3D7.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX   NCBI_TaxID=1276538 {ECO:0000313|EMBL:SMQ50900.1, ECO:0000313|Proteomes:UP000215127};
RN   [1] {ECO:0000313|EMBL:SMQ50900.1, ECO:0000313|Proteomes:UP000215127}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
CC       {ECO:0000256|ARBA:ARBA00005995}.
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DR   EMBL; LT853696; SMQ50900.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X7RUI5; -.
DR   STRING; 1276538.A0A1X7RUI5; -.
DR   Proteomes; UP000215127; Chromosome 5.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0140993; F:histone modifying activity; IEA:UniProt.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProt.
DR   GO; GO:0010558; P:negative regulation of macromolecule biosynthetic process; IEA:UniProt.
DR   CDD; cd00084; HMG-box_SF; 1.
DR   Gene3D; 3.90.660.10; -; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   Gene3D; 1.10.30.10; High mobility group box domain; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR002937; Amino_oxidase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR036910; HMG_box_dom_sf.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR007526; SWIRM.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   PANTHER; PTHR10742; FLAVIN MONOAMINE OXIDASE; 1.
DR   PANTHER; PTHR10742:SF386; LYSINE-SPECIFIC HISTONE DEMETHYLASE 1A; 1.
DR   Pfam; PF01593; Amino_oxidase; 2.
DR   Pfam; PF04433; SWIRM; 1.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF47095; HMG-box; 1.
DR   SUPFAM; SSF46689; Homeodomain-like; 1.
DR   PROSITE; PS50934; SWIRM; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000215127}.
FT   DOMAIN          126..221
FT                   /note="SWIRM"
FT                   /evidence="ECO:0000259|PROSITE:PS50934"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          43..82
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          389..438
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          839..883
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1031..1050
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        43..62
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        839..860
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1050 AA;  115333 MW;  216478AC9CDB0E67 CRC64;
     MSSSVAADDA LSNNITVASP SRKRTIDGQL KFATQKSFQA TSIIGNESSA THTPSPLNSA
     TSGKVPKKRG RPPKPKPLDE NGLLIAKVKA PPKEARSVMV VKPEVVVRPR ASIPSRLPAD
     VFASQCIEAA TSSRLDPYSL HPSEHKLLAD LLMSKEVTVY LNVRNAILRL WTQNPLCSVT
     REEAAGCAKE SRFFGIAEVA YRWLIRNGYI NFGCVEVPKD PSLPKKMSKD MRQRTVVVVG
     AGVSGLTTAR QLESLFMQEA AKWVEMNERP PRVIVLEGRN RIGGRVYSKP LRSQIEGSLP
     DGLRNTAEMG AMIVTGFEHG NPLDTVIRGQ LGLRYHLMRD ALTIYDTDGK PIEEERDMLN
     TELYTDISDR AGAYRAEAQK QDTLRGDEDL INRCRDPPPD GFTAFTLEPL PDAHIKSHKP
     SARRGRRRNA PPGTEKLTGR SQVIEGGSAM HSASRAAKDM GWEVRDGVAK NQSVSLHKAA
     ASRTHPTLGH VMDEAIVQYQ DLIDLTPTDM RLLNWHHANL EYANAAPVTS LSLSGHDQDT
     GNEFEGAHSE IVGGYTQLPR GLMNLPTRLD VRFGRVIDSI HYDNGDDTGS PLTTRIVCTD
     GEVIEADEVV ITAPLGVLKT SMIDFDPPLP DWKRGAINRM GFGLLNKVVL LYDAPFWDDE
     RDMFGLLNEA ERKGSLNPAD YQRKRGRFYL IWNATKISGR PMLVALMAGN AAFDVEQTDT
     TTLLSEVTER LRSVFTSTKV PAPREVIVTR WKRDPFSRGT YSYVAPETRP GDYDLMARSV
     GNLHFAGEAT CGTHPATVHG AFLSGLRVAS EVMDDMAGLI SIPNPLVAAA PIKQEQTSEY
     YPAATSHAEQ SSSTTAPSQP HIKLEPGLEP PLHPLQPLVK GPPQKSVCPS DPSFWYNLNS
     SRTVAASNLS TSTSTSVNET LILATIHARL GDRPLKPARP GVNPFLLFTK SKWEECKAYC
     AAELANSGRD MIRQTIGKWW KAAGEEEKEP FVKASREAQE IADAARREWE EGGKRWDEEA
     ARVRREVVEE LKNEAGGGGG ASVKETDNGV
//