ID   F2RQ03_TRIT1            Unreviewed;      1741 AA.
AC   F2RQ03;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   RecName: Full=U3 small nucleolar RNA-associated protein 10 {ECO:0000256|ARBA:ARBA00015399, ECO:0000256|RuleBase:RU367065};
GN   ORFNames=TESG_00934 {ECO:0000313|EMBL:EGD93388.1};
OS   Trichophyton tonsurans (strain CBS 112818) (Scalp ringworm fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=647933 {ECO:0000313|Proteomes:UP000009172};
RN   [1] {ECO:0000313|Proteomes:UP000009172}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 112818 {ECO:0000313|Proteomes:UP000009172};
RX   PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA   Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA   Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA   Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA   Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA   Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT   "Comparative genome analysis of Trichophyton rubrum and related
RT   dermatophytes reveals candidate genes involved in infection.";
RL   MBio 3:E259-E259(2012).
CC   -!- FUNCTION: Involved in nucleolar processing of pre-18S ribosomal RNA.
CC       Involved in ribosome biosynthesis. {ECO:0000256|ARBA:ARBA00025076}.
CC   -!- SUBUNIT: Component of the ribosomal small subunit (SSU) processome.
CC       {ECO:0000256|ARBA:ARBA00011399, ECO:0000256|RuleBase:RU367065}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC       {ECO:0000256|ARBA:ARBA00004604, ECO:0000256|RuleBase:RU367065}.
CC   -!- SIMILARITY: Belongs to the HEATR1/UTP10 family.
CC       {ECO:0000256|ARBA:ARBA00010559, ECO:0000256|RuleBase:RU367065}.
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DR   EMBL; GG698479; EGD93388.1; -; Genomic_DNA.
DR   HOGENOM; CLU_001128_3_1_1; -.
DR   OrthoDB; 5480100at2759; -.
DR   Proteomes; UP000009172; Unassembled WGS sequence.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR012954; BP28_C_dom.
DR   InterPro; IPR022125; U3snoRNP10_N.
DR   InterPro; IPR040191; UTP10.
DR   PANTHER; PTHR13457; BAP28; 1.
DR   PANTHER; PTHR13457:SF1; HEAT REPEAT-CONTAINING PROTEIN 1; 1.
DR   Pfam; PF08146; BP28CT; 1.
DR   Pfam; PF12397; U3snoRNP10; 1.
DR   SMART; SM01036; BP28CT; 1.
DR   SUPFAM; SSF48371; ARM repeat; 2.
PE   3: Inferred from homology;
KW   Kinase {ECO:0000313|EMBL:EGD93388.1};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU367065};
KW   Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274,
KW   ECO:0000256|RuleBase:RU367065};
KW   Ribosome biogenesis {ECO:0000256|ARBA:ARBA00022517,
KW   ECO:0000256|RuleBase:RU367065};
KW   rRNA processing {ECO:0000256|ARBA:ARBA00022552,
KW   ECO:0000256|RuleBase:RU367065}; Transferase {ECO:0000313|EMBL:EGD93388.1}.
FT   DOMAIN          1444..1597
FT                   /note="BP28 C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01036"
SQ   SEQUENCE   1741 AA;  193453 MW;  A94FDD1D0A0BC73E CRC64;
     MASSLAAQLS QVAAKATHQF DLKAQRSAHA QSLIFEKKVA STQDFDTIYQ LYYEGFQELC
     ALDPRFQPFR QNLFSEQSKV EDRSQMTAAQ NKELDIVIED FLALVGGRLL LNPAVKAVDW
     LVRRFRVHEH NTRAIILTFL PYHTTPLFLN LLSILPENLT STFKVLHPYK RSLILPTRAS
     LVHSASTNKE FFSALNSYVM QVGKARAHYQ GLTSFWAGIM TEALSTMLDS AQSGRLEVER
     RNKEDVLIRI LPTLSTGLSL KKAPELVIAC YMLCVVLANK GSLSDNAIDS LMEAVAGSWT
     RDTIASGITC LAVVFQHKEQ LQLPKPVAKS ILRLEDAADV FAGLAASNSI VRLLSGLMNV
     LMENDNEEVA AKCVSLVGQV LQNNIMGAED KTKTIIALLK TIDESHRKGY MSEEVRQLSS
     DTLATFIESK ELDIVLQRAI SESNVDIKAL EITLQLAIDN NLGPAETEDV EMEDIPENST
     QDKEFAAAIT SLSQRRSQQP ENFLVDAINI VTTSILESNG KAIDLQALIP YAISALSDPS
     TPVRREAAAL LTSIDNQYFI PDIEETPWGL GILYGDNERS KAVQWLPGKD IHTLFDKGFM
     PSLEECILDP SQVVETFVQT VKGTSEDGSG LKKSVRRDFF SFICSHIINT PLFATKLRLL
     SIVNRISKIG STPRTQFLSP MLAQCRTIDS DKIKRISTQE HVSIQELEQQ VLSIIYPKDT
     TAISTLLSLV KDSPQSTRAS FLGAVFERMK DTWPFLDEEK ELFASETLLD MCLSTKAQTE
     DLANSSKELL RSVDLSGPVI SKFLSTVTSA SFNIDSQSPA PKRRRMSQSN MAAMSPASRE
     EANIPLRRIS FILELIDASQ PERFPELLGG LFQTLAIVHK LKLQVRSEMS YLLSLNLGIL
     LSIVNKYKGS PKKLDTSVIR ADLIIDCVRT SESQQVQNTA LLLVAALATV APEIVLHSVM
     PIFTFMGSSV LRKDDEYSAL VIDQTIDQVI PPLVRSLRVQ KRDVVTGTSE LLLSFTTAYE
     HIPSYRRLKL FESLVNKLGQ EDFLFAVLAM LATKYGMDRD VLVTMTALAS NAEAQPQLTT
     YARYLSLVQD ALQPKPTISR ILLGIGSEDG REPHKVAVDL LQTLSHLLKF TSLGNKMVQY
     FESDDTEDAK KVHSLFSGML ERLLALGESV RSIKAINIAC GDALATLLGT LSLVDFIDTI
     EVLLQRPKDD LRRQVLRLLE NRLDNSNDRD AASQSKALSF LSVLVGIVET SPDILLKHAA
     VACMEKISEK YGKKNPEKVV EAAIVVAGDK CMGLADNRIR IMSALCLASM TEVIADAIIL
     VLPAALPRSL DLLQSSIQAK EQNPELHDAI YSLLSALFVH IPYMISSEDL DKVLCLSSSS
     AHASLSEDCN INRQETLQLL AKRVDAKEVY NAVERNWDFS VSNGSKAAKE TLEVVKLSIE
     KHSKSDTIKN VPALSKLLWK VFDFRRAQLN LPASDRFEGH QVDDIESSIN DLTIKMIYKL
     NDTIFRPLFT QLTEWATGEL DKSDLPGRQA RLTTFYKFLE TFFGTLKSIV TGYSSYIIEN
     VVDILKNVRP NVKENQALWT AVMRTLRNSF EHDQDEFWQS PSHLGSISSH LISQLSIANS
     KASFKLVTAE ATPAIVALAI AADSPDNQKE LNTHIMKYMR ASGGNADSCK GVNPFTRLAA
     VKCEQSLTEE LGEEWLALLP EMLPFISELM EDDDENVEKE VRKWVLMIED ILGEKLDDML
     A
//