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Database: UniProt
Entry: A0A2H9TLJ1_9FUNG
LinkDB: A0A2H9TLJ1_9FUNG
Original site: A0A2H9TLJ1_9FUNG 
ID   A0A2H9TLJ1_9FUNG        Unreviewed;       881 AA.
AC   A0A2H9TLJ1;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=Peptidase S54 rhomboid domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PSACC_01565 {ECO:0000313|EMBL:PJF18623.1};
OS   Paramicrosporidium saccamoebae.
OC   Eukaryota; Fungi; Fungi incertae sedis; Cryptomycota;
OC   Cryptomycota incertae sedis; Paramicrosporidium.
OX   NCBI_TaxID=1246581 {ECO:0000313|EMBL:PJF18623.1, ECO:0000313|Proteomes:UP000240830};
RN   [1] {ECO:0000313|EMBL:PJF18623.1, ECO:0000313|Proteomes:UP000240830}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KSL3 {ECO:0000313|EMBL:PJF18623.1,
RC   ECO:0000313|Proteomes:UP000240830};
RA   Quandt C.A., Beaudet D., Corsaro D., Michel R., Corradi N., James T.;
RT   "The genome of Paramicrosporidium saccamoebae is the missing link in
RT   understanding Cryptomycota and Microsporidia evolution.";
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Chromosome, centromere, kinetochore
CC       {ECO:0000256|ARBA:ARBA00004629}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}. Nucleus
CC       {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the NDC80/HEC1 family.
CC       {ECO:0000256|ARBA:ARBA00007050}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PJF18623.1}.
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DR   EMBL; MTSL01000112; PJF18623.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2H9TLJ1; -.
DR   STRING; 1246581.A0A2H9TLJ1; -.
DR   Proteomes; UP000240830; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0031262; C:Ndc80 complex; IEA:InterPro.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0051315; P:attachment of mitotic spindle microtubules to kinetochore; IEA:InterPro.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   Gene3D; 6.10.250.1950; -; 1.
DR   Gene3D; 1.10.418.30; Ncd80 complex, Ncd80 subunit; 1.
DR   Gene3D; 1.20.1540.10; Rhomboid-like; 1.
DR   InterPro; IPR040967; DUF5595.
DR   InterPro; IPR005550; Kinetochore_Ndc80.
DR   InterPro; IPR038273; Ndc80_sf.
DR   InterPro; IPR022764; Peptidase_S54_rhomboid_dom.
DR   InterPro; IPR035952; Rhomboid-like_sf.
DR   PANTHER; PTHR10643; KINETOCHORE PROTEIN NDC80; 1.
DR   PANTHER; PTHR10643:SF2; KINETOCHORE PROTEIN NDC80 HOMOLOG; 1.
DR   Pfam; PF18077; DUF5595; 1.
DR   Pfam; PF03801; Ndc80_HEC; 1.
DR   Pfam; PF01694; Rhomboid; 1.
DR   SUPFAM; SSF144091; Rhomboid-like; 1.
PE   3: Inferred from homology;
KW   Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW   Cell division {ECO:0000256|ARBA:ARBA00022618};
KW   Centromere {ECO:0000256|ARBA:ARBA00023328};
KW   Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Kinetochore {ECO:0000256|ARBA:ARBA00022838};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Mitosis {ECO:0000256|ARBA:ARBA00022776};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000240830};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        58..81
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        101..120
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        182..204
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          92..232
FT                   /note="Peptidase S54 rhomboid"
FT                   /evidence="ECO:0000259|Pfam:PF01694"
FT   DOMAIN          490..547
FT                   /note="DUF5595"
FT                   /evidence="ECO:0000259|Pfam:PF18077"
FT   REGION          275..296
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          528..555
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          594..659
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          741..846
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   881 AA;  99445 MW;  F00023468893EEF2 CRC64;
     MVVGGSTVAY SAAMIVDIER DKTRRRRWIS PPKNSIGYDN NASLASWWNG RRESEKTIIS
     LIGINGLVFL AWKFPGLQTF MSRYFMHSTR SHPITMLNSS FSHVSGMHFL VNMIALYSFG
     RMLHEKMGRE QFLAFYLSAG LASSAGSHMV RSIRGDFAKS LGASGAVFAV AAGCAHQPDV
     RVSLIFLPFV SIPIGYALPA MMAYDAIGLV KRWATFDHAA HLSGALFGYI FYTASTRHIW
     PQRYNILKSA GNCFVLAMVE RRLSTAPFQA PTMPSAAPRM SLAGPRQSLG PSRVRGSNVG
     TAVSELAGMS IGTEQRKLSL GRSSLDPRES LNRRSSAFGK NLAGTYAGGK DPRPIREKSY
     QLEVIKNLIN FLAKSGYPHP ISQKILTAPS AKDFQNIFKF LYAQLDPGYD FGKKFEDEVP
     LVMKGLRYPF AGEISKSQLY ACGSMHAWPG LLAMLGWMVD LVNCCDILHA QFETEPSDMT
     DLPGSTQTTA SEKVFFDYLC KSYKLFLAGS DNFDPLISEL GASFERRNEV VYQEVEQLSR
     VVEEEEAEYQ MLITEEPPLA KAQREQSIYK GDIEKFRKFI SHLEVKRTKF DEVIRNTIND
     VEICERELEE HEMLRATLQA QVEAQDICPE DIDRMNSDKE QLVKTLESLS QTKEEANKVF
     WERELLVQKK LDAVEKLVQE YNYSGEQIAV IPQEAVNSKG LSLELAFNPH ATRADQLVNL
     DIRTQVHPSF NSLREECHAM IHQAQDQLLS LQEALDKLNE ACNDKIEELR SNEKKIERTV
     QSYLEEKESC AVENKKTDEE AELLEQTIQK LRSDISSHSI MSQQRLQRAT VEYDQLVTNV
     ASEKERIGTD MYRLLEELIN FKTHVESSLE DLEQAFGRED L
//
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