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Database: UniProt
Entry: A1CJ19_ASPCL
LinkDB: A1CJ19_ASPCL
Original site: A1CJ19_ASPCL 
ID   A1CJ19_ASPCL            Unreviewed;      1132 AA.
AC   A1CJ19;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   27-MAR-2024, entry version 90.
DE   SubName: Full=DNA repair protein Rad18, putative {ECO:0000313|EMBL:EAW09143.1};
GN   ORFNames=ACLA_033460 {ECO:0000313|EMBL:EAW09143.1};
OS   Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS   NRRL 1 / QM 1276 / 107).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=344612 {ECO:0000313|EMBL:EAW09143.1, ECO:0000313|Proteomes:UP000006701};
RN   [1] {ECO:0000313|EMBL:EAW09143.1, ECO:0000313|Proteomes:UP000006701}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1
RC   {ECO:0000313|Proteomes:UP000006701};
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
CC   -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
CC       Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the SMC family. SMC6 subfamily.
CC       {ECO:0000256|ARBA:ARBA00006793}.
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DR   EMBL; DS027056; EAW09143.1; -; Genomic_DNA.
DR   RefSeq; XP_001270569.1; XM_001270568.1.
DR   AlphaFoldDB; A1CJ19; -.
DR   STRING; 344612.A1CJ19; -.
DR   EnsemblFungi; EAW09143; EAW09143; ACLA_033460.
DR   GeneID; 4702786; -.
DR   KEGG; act:ACLA_033460; -.
DR   VEuPathDB; FungiDB:ACLA_033460; -.
DR   eggNOG; KOG0250; Eukaryota.
DR   HOGENOM; CLU_009063_0_0_1; -.
DR   OMA; MCHDHFY; -.
DR   OrthoDB; 78166at2759; -.
DR   Proteomes; UP000006701; Unassembled WGS sequence.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR003395; RecF/RecN/SMC_N.
DR   PANTHER; PTHR19306; STRUCTURAL MAINTENANCE OF CHROMOSOMES 5,6 SMC5, SMC6; 1.
DR   PANTHER; PTHR19306:SF6; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN 6; 1.
DR   Pfam; PF02463; SMC_N; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006701}.
FT   DOMAIN          99..1105
FT                   /note="RecF/RecN/SMC N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02463"
FT   REGION          1..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          266..293
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          333..522
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          719..788
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          817..946
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        32..53
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1132 AA;  128675 MW;  D87ABD627E33804B CRC64;
     MPSMKRAQPF AGPDSLDDED GSITLVVNAH SRKRARRSET APSEGESEAS DDEASRPGSI
     AQALNDDEED LVLRNTQWIH EKHSFANDEA NVPAEHGILE RVECYNFMCH DHFQVELGPL
     INFIVGKNGS GKSAVLTAIT LCLGGKASAT NRGQSLKSFI KEGKESATIV VRIKNQGDGA
     YMPDDYGNSI IVERHFSKNG TSGFKIKAEN GRIISTKKAE LDSIIDYFTL QFDNPMNVLS
     QDMARQFLST SSPADKYRFF VKGVQLEQLD QDYRLIEESA DQIEEKLRSR EQDIKILKDF
     KETADRKLER SDQQESLRAR VRNVRNQMAW AQVEEQEQLR DSLDHELARI DEDLATAETE
     LSGVDVTIQH AENECAAAAD FVSQATSRLD QAQSEKNEIK AKWDEQMSER HDLQAEQRQI
     REYQKTTETR LREVQNHIQE ENQRLADLSG GSYARKKEQV EQAKIEVADA QRHFEEHRNN
     LNHFHREADD AEQKVKSAAV PVGRMKADVD QAELNLRSLT REGSRNTGFH ERLPALLREI
     QGERSFSKSP VGPIGNYVRL LKPEWSSILE NSLGATLNSF IVTSKRDMNM LSNIMQRVGC
     VCPIFIGSDG HIDTSEHEPD PQFDTALRVL QIDNELVRRQ LIINHGIEQM LLIERLEEAS
     SVLFDGQRPK NVKRCYCIDR TDRRRGIHLS YSRTGEPSQA PVQAYNGSPR MKSDLASQIR
     LQRDVVAALR RNLSDQEQQL RSAQAHLERC KQAIVRHDRR TKELQVDLQR QEDRVEELAD
     ALERETVKDG HLDVLRATLQ EAEAEKRLNE GSREDSVAAM DAMMKKLKAT KQELAAKDAE
     ISTLQEELRV AQNEELLVQE KRRKAISDKN SAVKRTGDIN LNRTRTQQER EILAARVIEY
     EEKASLVSPR VAIHDGETVA TLTKKLERLH RDIERYNQQL GGSRDEIAAE AEKATAVYNR
     ALKQIEEFRL LADVLKATLK HRKHRWQIFR SHISSRAKAQ FTYLLSERSF RGRLLTDHEG
     KLLDLQVEPD ITKDSAGRGA KTLSGGEKSF SQVCLLLALW EAMGSPVRCL DEFDVYMDHI
     NRKMAIDMLM LAARRSIGRQ FILITPGSRA DITLAPDVRV KEYVNAHRYG CS
//
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