ID A1CKN2_ASPCL Unreviewed; 1027 AA.
AC A1CKN2;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE SubName: Full=Spindle pole body component (Alp6), putative {ECO:0000313|EMBL:EAW09706.1};
GN ORFNames=ACLA_039210 {ECO:0000313|EMBL:EAW09706.1};
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:EAW09706.1, ECO:0000313|Proteomes:UP000006701};
RN [1] {ECO:0000313|EMBL:EAW09706.1, 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 -!- SIMILARITY: Belongs to the TUBGCP family.
CC {ECO:0000256|ARBA:ARBA00010337}.
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DR EMBL; DS027056; EAW09706.1; -; Genomic_DNA.
DR RefSeq; XP_001271132.1; XM_001271131.1.
DR AlphaFoldDB; A1CKN2; -.
DR STRING; 344612.A1CKN2; -.
DR EnsemblFungi; EAW09706; EAW09706; ACLA_039210.
DR GeneID; 4702756; -.
DR KEGG; act:ACLA_039210; -.
DR VEuPathDB; FungiDB:ACLA_039210; -.
DR eggNOG; KOG2000; Eukaryota.
DR HOGENOM; CLU_003736_0_0_1; -.
DR OMA; MRMMSVC; -.
DR OrthoDB; 197975at2759; -.
DR Proteomes; UP000006701; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0000923; C:equatorial microtubule organizing center; IEA:EnsemblFungi.
DR GO; GO:0000931; C:gamma-tubulin ring complex; IEA:EnsemblFungi.
DR GO; GO:0008275; C:gamma-tubulin small complex; IEA:EnsemblFungi.
DR GO; GO:0061496; C:half bridge of mitotic spindle pole body; IEA:EnsemblFungi.
DR GO; GO:0061497; C:inner plaque of mitotic spindle pole body; IEA:EnsemblFungi.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0071957; C:old mitotic spindle pole body; IEA:EnsemblFungi.
DR GO; GO:0000922; C:spindle pole; IEA:InterPro.
DR GO; GO:0043015; F:gamma-tubulin binding; IEA:InterPro.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IEA:EnsemblFungi.
DR GO; GO:0007020; P:microtubule nucleation; IEA:InterPro.
DR GO; GO:0090307; P:mitotic spindle assembly; IEA:EnsemblFungi.
DR Gene3D; 1.20.120.1900; Gamma-tubulin complex, C-terminal domain; 1.
DR InterPro; IPR007259; GCP.
DR InterPro; IPR040457; GCP_C.
DR InterPro; IPR042241; GCP_C_sf.
DR InterPro; IPR041470; GCP_N.
DR PANTHER; PTHR19302; GAMMA TUBULIN COMPLEX PROTEIN; 1.
DR PANTHER; PTHR19302:SF14; GAMMA-TUBULIN COMPLEX COMPONENT 3; 1.
DR Pfam; PF04130; GCP_C_terminal; 1.
DR Pfam; PF17681; GCP_N_terminal; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW Reference proteome {ECO:0000313|Proteomes:UP000006701}.
FT DOMAIN 288..587
FT /note="Gamma tubulin complex component protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17681"
FT DOMAIN 590..972
FT /note="Gamma tubulin complex component C-terminal"
FT /evidence="ECO:0000259|Pfam:PF04130"
FT REGION 179..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 871..919
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 977..1027
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..264
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 881..897
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 977..996
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1027 AA; 114293 MW; 386C0AE5C97D8657 CRC64;
MASRHPARPR RIDDALSQLV DSLTPPLSLS ELGDTIPDDA EDLLAEAEDR RHQELLEHAW
RIIDTHPAST NDPASPTAGG AGLGIARRGS LAGGENINNA SDLIKRKLLR ENASPDKAVR
FSNLYSRLLT QPVLSQKWAI LYLLYRLSGS EAPAETGDEH GRSRSPVLEA GNLQNVVLKG
GRGRHAVPTR LAGDSDEDGP AVSSSASQVA AKMERKASLR RPEWERERER ERERERDVEP
EQHGHVAKEG RVAAPRDHHV VEEQKGSFQA PSFTTDSGEK RPAEQGLLRD LPFNLQGLSS
SNLEFSSSSI LKLPSALPIP VLSLLNTLAE PCLLYKGLST YVEDSGGGLL TQSLRAALSN
ELRSYLGLVA TLEGEIRRAL AATGDPQHPK DSSRGLVTLK RCVVWTRDAT MALRLMSLIV
EEARNKKGGQ LVSMIHSFST SHGDPFVYTF AEKLLGHVTR PFYDMLRLWI YDGELSDPYQ
EFFVVEPEFR PSTDPRRIAT SVWEDKYKLD DEMVPSIITQ DFAKKVFLIG KSLNFIRYGC
GDSGWVEAYS KQASKELHYG DTASLETSID EAYKTTMARL IHLMDDKFKL FDHLHALKKY
LLLGQGDFIA LLMESLASNL DRPANSQYRH TLTAQLEHAI RASNAQYDPP DVLRRLDARM
LELSHGEIGW DCFTLEYKID APVDVIITPW GSTQYLKVFN FLWRVKRVEF ALGSTWRRCM
TGARGVLGSV SDKVGADWKL ARCVIAEMIH FVCQLQYYIL FEVIEASWDQ LQAAISKPGC
TLDDLIEAHT KYLNSITHKG LLGSSSSSRT ASGHKQEEGF LTQLHQILKI MLSYKDAVDG
LYSFSVAEFT RRQELSAKIE TRTAQGRWGI TERDLLSSRR PGTHKNSISS LSPSLAQAPG
LGNPGDGFDT PSSLPNHDLS ADDHMLASLR TRLRELSAEF RSRLNVLLGD LAYQPDVDMR
FLGVVMNFND VYEPVRRRRA ATTSSRDKER ARRRATAPGG NGETNPQKEV RRERKDAAGA
DSSGNGA
//
