ID A0A177DWX3_ALTAL Unreviewed; 1478 AA.
AC A0A177DWX3;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Structural maintenance of chromosomes protein {ECO:0000256|PIRNR:PIRNR005719};
GN ORFNames=CC77DRAFT_982509 {ECO:0000313|EMBL:OAG23680.1};
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:OAG23680.1, ECO:0000313|Proteomes:UP000077248};
RN [1] {ECO:0000313|EMBL:OAG23680.1, ECO:0000313|Proteomes:UP000077248}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRC1lrK2f {ECO:0000313|EMBL:OAG23680.1,
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|PIRNR:PIRNR005719}.
CC -!- SIMILARITY: Belongs to the SMC family. SMC4 subfamily.
CC {ECO:0000256|ARBA:ARBA00006005}.
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DR EMBL; KV441472; OAG23680.1; -; Genomic_DNA.
DR RefSeq; XP_018389101.1; XM_018536119.1.
DR STRING; 5599.A0A177DWX3; -.
DR GeneID; 29121713; -.
DR KEGG; aalt:CC77DRAFT_982509; -.
DR VEuPathDB; FungiDB:CC77DRAFT_982509; -.
DR OMA; CPALDNM; -.
DR OrthoDB; 231904at2759; -.
DR Proteomes; UP000077248; Unassembled WGS sequence.
DR GO; GO:0005694; C:chromosome; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0051276; P:chromosome organization; IEA:InterPro.
DR Gene3D; 1.10.287.1490; -; 1.
DR Gene3D; 1.20.1060.20; -; 1.
DR Gene3D; 3.30.70.1620; -; 1.
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 InterPro; IPR024704; SMC.
DR InterPro; IPR010935; SMC_hinge.
DR InterPro; IPR036277; SMC_hinge_sf.
DR PANTHER; PTHR18937:SF172; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN; 1.
DR PANTHER; PTHR18937; STRUCTURAL MAINTENANCE OF CHROMOSOMES SMC FAMILY MEMBER; 1.
DR Pfam; PF06470; SMC_hinge; 1.
DR Pfam; PF02463; SMC_N; 1.
DR PIRSF; PIRSF005719; SMC; 1.
DR SMART; SM00968; SMC_hinge; 1.
DR SUPFAM; SSF90257; Myosin rod fragments; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF75553; Smc hinge domain; 1.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|ARBA:ARBA00022776};
KW Cell division {ECO:0000256|ARBA:ARBA00022618};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Mitosis {ECO:0000256|ARBA:ARBA00022776};
KW Nucleus {ECO:0000256|PIRNR:PIRNR005719};
KW Reference proteome {ECO:0000313|Proteomes:UP000077248}.
FT DOMAIN 802..915
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 1..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 456..490
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 523..655
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 681..785
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 962..1217
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 17..47
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..86
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1478 AA; 165548 MW; CF885F2DE178C71C CRC64;
MASISPRKST RAAATRRKAP VVDDSDHEEN RTPTPEVKQE ADEEDFTPAP APLKTGRGRG
RPRKTAAQNE EATPKPTTRR RTRVTESVEP TQTLTPATER TTRVASPSKA VPKKRGRKPR
SSVAPAPVEE DSHLLTPEPS ISPEPEVEQA SEATITPSSP LAGAADDTAD DIANDAASDV
TMTDRTPEPA PEPEPAPEPV AEVTQIEAKE ETPVPEPKME VDSLPEPQPP AKVAEELSTQ
QTMLEPIDIV VKRRAAAIPA LHEPVAPKQR TVITWLVLNN FKSYAGRQEV GPFHASFSSV
VGPNGSGKSN VIDSLLFVFG FRASKMRQSK LSALIHNSAA FPDLDYCEVE VHFQEVKDLA
NGGHEVIPDS QLVISRRAFK NNSSKYYINK KESTFTIVTN LLKDRGVDLD HKRFLILQGE
VESIAQMKPK AQGEHDDGLL EYLEDIIGTS KYKTPIAESE VEVENLNEVC REKSSRVQHV
EKEKSGLEEK KNKALAYIRD ENELASKQST LYQIYVSEFD DHIQVAQESV GQLQAQLDDE
LQKHQGSEEE IKELEQRYKK GVKECDQLEK RNQEYQKEVA RVDKETVKFE EKKKFLAGKQ
KKLEKTKETS GYGRSEAESL AKQYSADVER YNEEIAELEQ SMEVEAKELE VVRKSLAGKT
QGLSDEIAAK QKSLEPWSAK INEKQSAIAV AQSELDIMRE RENAGAKGIA EVEAKIESLE
EAKQTKAAEL DECKVERKRV EKEVRKTQAK LEEITQQEPM LRSKLSGARA KADEARASLS
SAQTQGNVLT GLMRLKESGR IDGFHGRLGN LGTIDQKYDV AISTACPQLD NMVVDTVESG
QQCIEYLRKN NLGRANFILL DRLAKRDMSP VQTPENVPRL FDLVKPKHEK LKPAFFQVMT
NTLVAENLDQ AERIAYGAKR WRVVTLDGKL IDTAGTMSGG GSRVVKGKMS SKLASDVSKD
QVTKLEHDRD ALEQTFAEFQ QELRELETAL RDLNQQIPEL DTKSQKLALE LESFDRNIAD
CQRRIAELGN EQTSTKTDKG RIASLEKNIA SMEKEVAKLR AETEDIEAEI KGLQDKIMEI
GGVKLRGQKA KVDGLKGQID TLTEQVSNAQ VAKSKEEKQR AKHEKAHNDA IKELEKLAID
AEKVEEDMAS QQRDVSGIRQ QAEEAQEELE TRKEELQLVK KDLDEKLAEL NETRAVEIEM
RNKLEESQKT LNEYQKKQAY FHDKLSKLSY QSVTDLGEEQ EGEGQGLPSY SKDELQDMDK
ATLKDQIAHL EKKNESTQVD LAVLAEYRKR VEEHAARSTD LASAVSARDA AKHKCEELRR
LRKEGFKAGF DIITARLKEM YQMITMGGNA ELEYEDTLDA FSEGIRFSVM PPKKSWKNIS
NLSGGEKTLS SLALVFALHH YKPTPLYVMD EIDAALDFRN VSIVASYIKE RTKNAQFIVI
SLRNNMFELA SRLVGVYKVN HMTKSVTIEN KDYITGRA
//
