ID V5FRZ3_BYSSN Unreviewed; 1489 AA.
AC V5FRZ3;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE SubName: Full=DNA mismatch repair protein (Pms1), putative {ECO:0000313|EMBL:GAD92421.1};
GN ORFNames=PVAR5_1012 {ECO:0000313|EMBL:GAD92421.1};
OS Byssochlamys spectabilis (strain No. 5 / NBRC 109023) (Paecilomyces
OS variotii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Thermoascaceae; Paecilomyces.
OX NCBI_TaxID=1356009 {ECO:0000313|EMBL:GAD92421.1, ECO:0000313|Proteomes:UP000018001};
RN [1] {ECO:0000313|Proteomes:UP000018001}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=No. 5 / NBRC 109023 {ECO:0000313|Proteomes:UP000018001};
RX PubMed=24407650; DOI=10.1128/genomeA.01162-13;
RA Oka T., Ekino K., Fukuda K., Nomura Y.;
RT "Draft genome sequence of the formaldehyde-resistant fungus Byssochlamys
RT spectabilis No. 5 (anamorph Paecilomyces variotii No. 5) (NBRC109023).";
RL Genome Announc. 2:E0116213-E0116213(2014).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the DNA mismatch repair MutL/HexB family.
CC {ECO:0000256|ARBA:ARBA00006082}.
CC -!- SIMILARITY: Belongs to the TDE1 family.
CC {ECO:0000256|ARBA:ARBA00006665}.
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:GAD92421.1}.
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DR EMBL; BAUL01000025; GAD92421.1; -; Genomic_DNA.
DR eggNOG; KOG1978; Eukaryota.
DR eggNOG; KOG2592; Eukaryota.
DR HOGENOM; CLU_004131_0_1_1; -.
DR InParanoid; V5FRZ3; -.
DR OrthoDB; 4698638at2759; -.
DR Proteomes; UP000018001; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032300; C:mismatch repair complex; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR GO; GO:0030983; F:mismatched DNA binding; IEA:InterPro.
DR GO; GO:0061982; P:meiosis I cell cycle process; IEA:UniProt.
DR GO; GO:0006298; P:mismatch repair; IEA:InterPro.
DR CDD; cd16926; HATPase_MutL-MLH-PMS-like; 1.
DR CDD; cd03484; MutL_Trans_hPMS_2_like; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.1540.20; MutL, C-terminal domain, dimerisation subdomain; 1.
DR Gene3D; 3.30.1370.100; MutL, C-terminal domain, regulatory subdomain; 1.
DR InterPro; IPR014762; DNA_mismatch_repair_CS.
DR InterPro; IPR013507; DNA_mismatch_S5_2-like.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR002099; MutL/Mlh/PMS.
DR InterPro; IPR038973; MutL/Mlh/Pms-like.
DR InterPro; IPR014790; MutL_C.
DR InterPro; IPR042120; MutL_C_dimsub.
DR InterPro; IPR042121; MutL_C_regsub.
DR InterPro; IPR037198; MutL_C_sf.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR InterPro; IPR005016; TDE1/TMS.
DR NCBIfam; TIGR00585; mutl; 1.
DR PANTHER; PTHR10073; DNA MISMATCH REPAIR PROTEIN MLH, PMS, MUTL; 1.
DR PANTHER; PTHR10073:SF52; MISMATCH REPAIR ENDONUCLEASE PMS2; 1.
DR Pfam; PF01119; DNA_mis_repair; 1.
DR Pfam; PF13589; HATPase_c_3; 1.
DR Pfam; PF08676; MutL_C; 1.
DR Pfam; PF03348; Serinc; 1.
DR SMART; SM01340; DNA_mis_repair; 1.
DR SMART; SM00853; MutL_C; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF118116; DNA mismatch repair protein MutL; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR PROSITE; PS00058; DNA_MISMATCH_REPAIR_1; 1.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000018001};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 15..37
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 49..71
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 91..116
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 137..155
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 161..182
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 203..227
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 239..258
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 265..285
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 305..323
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 406..426
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 693..828
FT /note="DNA mismatch repair protein S5"
FT /evidence="ECO:0000259|SMART:SM01340"
FT DOMAIN 1276..1439
FT /note="MutL C-terminal dimerisation"
FT /evidence="ECO:0000259|SMART:SM00853"
FT REGION 341..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 853..889
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 909..1003
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1018..1205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..362
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..395
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 861..889
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 911..933
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 934..948
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 951..1003
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1086..1118
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1119..1141
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1489 AA; 164707 MW; 9F3C48215C2ACDE0 CRC64;
MGALLSIPFM AVPSVGTLLG FGASCCGAAT CSAVCSACGK FQSSMATRIA YAFLLLVNSI
LSWIMLTPWA LKKLQHMTLD YMEIRCDGKE CYGWVAVHRI NFALGLFHLI MALLLLGVRT
SRDSRAALQN GYWGPKVIVW IGFLVMSFFI PESFFFVYGN YIAFIGAILF LLLGLILLVD
LAHSWAEMCL QKIEDNESRA WRGLLIGSTL GMYIASIAMT ILMYIFFASS GCSMNQAAIT
VNLIVFLIIS VVSIQPVVQE HNPRAGLAQA AMVTAYCTYL TMSAVSMEPD DRHCNPLIRA
RGTRTATIVL GAIVTMATIA YTTTRAATQG IALGSTGGHN YTRIGTDDNE HGLVTQQPTS
RREMRAEALR AAVESGSLPA SALDDDDDES DDGYDSKDDE RGSTQYNYSL FHIIFFLATT
WVATLLTQNL DPEANDDFAP VGRTYWASWV KIISAWNARH AFAPTIHHDI QRDGTNMATI
KAIEARSIHQ IQSGQVIVDL CSVVKELVEN SLDAGATSVE VRFKNNGLDL IEVQDNGSGI
SPNNYENIAL KHYTSKLSSY DDLSSLQTFG FRGEALSSLC ALSNFHIVTA QADQAPKATR
LDFEFSGKLK KTQVVAGQKG TTVSVENLFQ KLPVRRRELE KNIKREYGKV LGLLHAYACI
STGVRFSVKN TVGKNKNVVV FTTKANPTTK ENIANVYGAK TLLALIPLEL ELEFEPSAAG
KRKAEQDVNK ILVRGHISRP VFGEGRQTPD RQMFFVNSRP CGLPQIAKAF NEVYKSFNVS
QSPFIFADFR MDTNAYDVNV SPDKRTILLH DSGVLIEVLK ESLVRLFEEA DQTVPQARFQ
TSKQVVLDQH FQVGSQDTRD RGGSPEVEDH AQEEPNDVPS EDDETRHDKA QAKMKSFLSG
LADRRVSVPE QAAVASTSGE AVEATQEASQ EQHHVSQESQ KGDDEMASTG ADAESNGSQQ
DTPRATNELF VEDESHSTPP STNEQNIPAL HASSQQETPN VIQNAFDRMR HRRQPAEIAT
ITVGDKTVTS VIGSGGPRKR NPEITDSPSG QLRSKRRVHT PSRPNIFGQS LRAFAAPGTQ
VSPSSDREED DDDEYIEDAE EGEEANEEEQ EEEADDTRLS PEPDGSTENE TEKRAEQAQS
DESDVDAAET GTGDVSAESD EDYVDEEEKK AQDEARVQDL IREAEANAAL PSQSNTNRAD
KLTKGLTRKD STVHLMGMIN GSISRIESQL NTLRHSLTAC ASTKDTADED QEATSHTAEE
RLSLTVSKDD FSQMRIIGQF NLGFILATRS ATSSSKDELF IIDQHASDEK YNFERLQAET
VVQNQRLVRP KTLDLTAVEE EIIIENRGAL EKNGFIIEVD DSGDEPIGRR CKLVSLPLSK
EVVFDVRDLE ELLVLLSETP ATRTPSTTTS DIYTPRPSKV RKMFAMRACR SSIMIGKSLT
LKQMEKVVRH MGQWNEWDEN QTKDDPESDN LDVWRRYFED HGEEEDIEE
//
