ID A0A177DAK1_ALTAL Unreviewed; 269 AA.
AC A0A177DAK1;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Chromosome segregation in meiosis protein {ECO:0000256|RuleBase:RU366049};
GN ORFNames=CC77DRAFT_944759 {ECO:0000313|EMBL:OAG16210.1};
OS Alternaria alternata (Alternaria rot fungus) (Torula alternata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Alternaria;
OC Alternaria sect. Alternaria; Alternaria alternata complex.
OX NCBI_TaxID=5599 {ECO:0000313|EMBL:OAG16210.1, ECO:0000313|Proteomes:UP000077248};
RN [1] {ECO:0000313|EMBL:OAG16210.1, ECO:0000313|Proteomes:UP000077248}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRC1lrK2f {ECO:0000313|EMBL:OAG16210.1,
RC ECO:0000313|Proteomes:UP000077248};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plays an important role in the control of DNA replication and
CC the maintenance of replication fork stability.
CC {ECO:0000256|RuleBase:RU366049}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|RuleBase:RU366049}.
CC -!- SIMILARITY: Belongs to the CSM3 family. {ECO:0000256|ARBA:ARBA00006075,
CC ECO:0000256|RuleBase:RU366049}.
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DR EMBL; KV441490; OAG16210.1; -; Genomic_DNA.
DR RefSeq; XP_018381631.1; XM_018534982.1.
DR AlphaFoldDB; A0A177DAK1; -.
DR STRING; 5599.A0A177DAK1; -.
DR GeneID; 29120576; -.
DR KEGG; aalt:CC77DRAFT_944759; -.
DR VEuPathDB; FungiDB:CC77DRAFT_944759; -.
DR OMA; ADMDDMW; -.
DR OrthoDB; 1388129at2759; -.
DR Proteomes; UP000077248; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006974; P:DNA damage response; IEA:UniProtKB-KW.
DR GO; GO:0000076; P:DNA replication checkpoint signaling; IEA:UniProtKB-UniRule.
DR GO; GO:0008156; P:negative regulation of DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0031297; P:replication fork processing; IEA:UniProtKB-UniRule.
DR InterPro; IPR012923; Csm3.
DR InterPro; IPR040038; TIPIN/Csm3/Swi3.
DR PANTHER; PTHR13220; TIMELESS INTERACTING-RELATED; 1.
DR PANTHER; PTHR13220:SF11; TIMELESS-INTERACTING PROTEIN; 1.
DR Pfam; PF07962; Swi3; 1.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|RuleBase:RU366049};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|RuleBase:RU366049};
KW DNA replication inhibitor {ECO:0000256|ARBA:ARBA00022880};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU366049};
KW Reference proteome {ECO:0000313|Proteomes:UP000077248}.
FT DOMAIN 71..153
FT /note="Chromosome segregation in meiosis protein 3"
FT /evidence="ECO:0000259|Pfam:PF07962"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 148..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..25
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..206
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..244
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 269 AA; 30240 MW; 8A1B13BD2A56321B CRC64;
MADSSLQVRA HDSDDDLDDI LKDVTNPEEP IQSTENPTQP QYRKSNKSDN AGALGVDEEI
VITKKRIPIP KLDDQRLLSD PGIPRLRKIS KERLRFKGKG HEYGDIARML NMYQLWLDDL
YPRAKFADAL AIIEKVGHTK RMHMMRKDWI DEGKPRRNTG HDVADEDDAT RDKTPQQSTE
EMEGVEHVGQ DSPSRQGERE DPTSNSADHA AEAVASGDPD DDELDALLAE SNQPSTTVPK
TLPTRPAPTQ DDPFADEMEA MADMDDLWD
//
