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Database: UniProt
Entry: F2TRP5_AJEDA
LinkDB: F2TRP5_AJEDA
Original site: F2TRP5_AJEDA 
ID   F2TRP5_AJEDA            Unreviewed;       906 AA.
AC   F2TRP5;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 2.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=Spindle pole body component {ECO:0000256|RuleBase:RU363050};
GN   ORFNames=BDDG_08853 {ECO:0000313|EMBL:EGE85908.2};
OS   Ajellomyces dermatitidis (strain ATCC 18188 / CBS 674.68) (Blastomyces
OS   dermatitidis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX   NCBI_TaxID=653446 {ECO:0000313|EMBL:EGE85908.2};
RN   [1] {ECO:0000313|EMBL:EGE85908.2}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 18188 {ECO:0000313|EMBL:EGE85908.2};
RG   The Broad Institute Genome Sequencing Platform;
RG   Broad Institute Genome Sequencing Center for Infectious Disease.;
RA   Cuomo C., Klein B., Sullivan T., Heitman J., Young S., Zeng Q., Gargeya S.,
RA   Alvarado L., Berlin A.M., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA   Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C.,
RA   Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., White J., Yandava C., Haas B., Nusbaum C.,
RA   Birren B.;
RT   "Annotation of Blastomyces dermatitidis strain ATCC 18188.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC       center {ECO:0000256|RuleBase:RU363050}.
CC   -!- SIMILARITY: Belongs to the TUBGCP family.
CC       {ECO:0000256|ARBA:ARBA00010337, ECO:0000256|RuleBase:RU363050}.
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DR   EMBL; GG749509; EGE85908.2; -; Genomic_DNA.
DR   AlphaFoldDB; F2TRP5; -.
DR   HOGENOM; CLU_010106_0_0_1; -.
DR   Proteomes; UP000007802; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0000930; C:gamma-tubulin complex; IEA:UniProt.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0000922; C:spindle pole; IEA:InterPro.
DR   GO; GO:0005816; C:spindle pole body; IEA:UniProt.
DR   GO; GO:0043015; F:gamma-tubulin binding; IEA:InterPro.
DR   GO; GO:0007020; P:microtubule nucleation; IEA:InterPro.
DR   CDD; cd22572; GCP5_NTD; 1.
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   InterPro; IPR032797; Mod21_N.
DR   PANTHER; PTHR19302; GAMMA TUBULIN COMPLEX PROTEIN; 1.
DR   PANTHER; PTHR19302:SF76; SPINDLE POLE BODY COMPONENT; 1.
DR   Pfam; PF14609; GCP5-Mod21_N; 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, ECO:0000256|RuleBase:RU363050};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212,
KW   ECO:0000256|RuleBase:RU363050};
KW   Microtubule {ECO:0000256|ARBA:ARBA00022701, ECO:0000256|RuleBase:RU363050}.
FT   DOMAIN          66..151
FT                   /note="Gamma-Tubulin ring complex non-core subunit mod21 N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14609"
FT   DOMAIN          231..536
FT                   /note="Gamma tubulin complex component protein N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17681"
FT   DOMAIN          618..893
FT                   /note="Gamma tubulin complex component C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF04130"
FT   REGION          788..840
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        788..805
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   906 AA;  104034 MW;  D20A75E46C0729F7 CRC64;
     MAHSANVSAL TDELIIIITN TPDKGSRRFH RLKSLVERTL KQNNAGRTDH LEVAKRLDGL
     QEKFQVLDND ALSDALHSRL EELNQRRIHR APEALSLLLE LSDRPAVHST IEDLDLLRRP
     ASPPPLTWSD IYASDPLSDE EEIWQDIDYA ALTSGDDLSS TSSGVSIPRI VPQRSKVPLD
     DFKTPDTCFL PVEDEILLSR IQDLELWRNR VAQTNRPTND DDLYLTELQV IRETIFMLQG
     LPTTLFWYLD DSVEVDRRFR LRHASPIAFG NLLRSFSVLG AQLHVIRRFA QHPQKLQFMQ
     MFQREVEFHL CRFNKDLSNM EAEHSGTAES STPSLIRLFS NVYEETSLLR ELSDLINKLA
     DQSPNEAFQC LDLLYDLVCS KQACGDDTTF QHVAKIFFKC FEVYARPIRL WIEKGQLDKT
     LGTFFVSDSG KQLTDLRTLW HEWFVLDEVH GRLYAPDFLR PAAKKIFTTG KSMIFIRRLG
     LDPDVLETPK CMNISYENIC SSDHFSPLLP FPVLLEYSFD RLIDSNHTFA SNLLRKQLDE
     QCGLWISLEA LEYIYLGKDM SLSSIIDHEV FDLIDKGIQS WNDRFFLTEL AQGTFGSLAC
     IDPSRLIIRS KQIGLQDFEY HCRSAQILKA IAMDYILPWP VANIITKQSL SAYRRVSTFL
     MQIRRAKYVV ERQRLLRSLH SETESEKKDD ILGYSIRHHL LWLLNVLYAH LTQLVICTST
     TIMKEALSKA KDVDGMIAAH ESYTSSLEDQ CLLSPNLTPI YQAVISLLDL CIHFSDIQIS
     RHGDNQFDQG NRKSFHSSSG RRYRTSGSLH QRRRRSRSRE IESSSVADDD SVDDADDSMM
     DEGNLTSVSF IETSYRKRLI GVRDKFEHLC SFITAGLRGM GRVDGHNSWE ILAEKLEWRK
     SRGGHV
//
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