ID A0A3N2PVY4_9PEZI Unreviewed; 1168 AA.
AC A0A3N2PVY4;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=ARM repeat-containing protein {ECO:0000313|EMBL:ROT38655.1};
GN ORFNames=SODALDRAFT_333273 {ECO:0000313|EMBL:ROT38655.1};
OS Sodiomyces alkalinus F11.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Sodiomyces.
OX NCBI_TaxID=1314773 {ECO:0000313|EMBL:ROT38655.1, ECO:0000313|Proteomes:UP000272025};
RN [1] {ECO:0000313|EMBL:ROT38655.1, ECO:0000313|Proteomes:UP000272025}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F11 {ECO:0000313|EMBL:ROT38655.1,
RC ECO:0000313|Proteomes:UP000272025};
RX PubMed=30368956; DOI=10.1111/mec.14912;
RA Grum-Grzhimaylo A.A., Falkoski D.L., van den Heuvel J.,
RA Valero-Jimenez C.A., Min B., Choi I.G., Lipzen A., Daum C.G., Aanen D.K.,
RA Tsang A., Henrissat B., Bilanenko E.N., de Vries R.P., van Kan J.A.L.,
RA Grigoriev I.V., Debets A.J.M.;
RT "The obligate alkalophilic soda-lake fungus Sodiomyces alkalinus has
RT shifted to a protein diet.";
RL Mol. Ecol. 27:4808-4819(2018).
CC -!- FUNCTION: Microtubule binding protein that promotes the stabilization
CC of dynamic microtubules. Required for mitotic spindle formation.
CC {ECO:0000256|ARBA:ARBA00024889}.
CC -!- SUBUNIT: Interacts with microtubules. {ECO:0000256|ARBA:ARBA00011375}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle
CC {ECO:0000256|ARBA:ARBA00004186}.
CC -!- SIMILARITY: Belongs to the CLASP family.
CC {ECO:0000256|ARBA:ARBA00009549}.
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DR EMBL; ML119055; ROT38655.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N2PVY4; -.
DR STRING; 1314773.A0A3N2PVY4; -.
DR OrthoDB; 1369289at2759; -.
DR Proteomes; UP000272025; Unassembled WGS sequence.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0000278; P:mitotic cell cycle; IEA:UniProt.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 3.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR024395; CLASP_N_dom.
DR InterPro; IPR034085; TOG.
DR PANTHER; PTHR21567; CLASP; 1.
DR PANTHER; PTHR21567:SF9; CLIP-ASSOCIATING PROTEIN; 1.
DR Pfam; PF12348; CLASP_N; 2.
DR SMART; SM01349; TOG; 2.
DR SUPFAM; SSF48371; ARM repeat; 1.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|ARBA:ARBA00022776};
KW Cell division {ECO:0000256|ARBA:ARBA00022618};
KW Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW Mitosis {ECO:0000256|ARBA:ARBA00022776};
KW Reference proteome {ECO:0000313|Proteomes:UP000272025}.
FT DOMAIN 1..227
FT /note="TOG"
FT /evidence="ECO:0000259|SMART:SM01349"
FT DOMAIN 286..524
FT /note="TOG"
FT /evidence="ECO:0000259|SMART:SM01349"
FT REGION 225..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 513..550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 564..703
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 737..788
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 817..851
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 883..920
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..265
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 578..601
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 656..672
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 764..778
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1168 AA; 126878 MW; 1EB417969F428003 CRC64;
MADHITDDQV ADLLRVLRSD AYADVKVQHI NNIKSGIKQH NVPEHLVAQI FDGLRTASVS
QHGVLASAGL TSLNHLLTRL SRQEPKLLAK ELKATLPVVV DKLGDQKDKL RAIASQALTT
LYGAAPADVE RSVRNVAMVG KNPRAKETGM QWLLHMHNQH GLQFRAYVPT LMELLEDADG
MVRDNAKSTV IELFRNAPNA AKSDLKRQLK TFKVRPAIEQ AIVKELAPPG GGLRPETPLD
AAPPRPPSRA NLAASVSSLS SDRPNTPALE LRPEQVEPAY VNTQRELDDM FKEMHLYFDG
RETEQNWLKR EESMTKLRRL IAGNVPQDFP EPFIVSLRGL LDGIIKAVTS LRTSLSKEGC
ALVHDIAVTF GPGMDPMVEL LMQTFIKVAA ATKKISSQQA NFTVETIIGR VTYNNRIMQH
MWAACQDKNV QPRTYASGWL KTLLKKESHH KNHMEHTGGL DLLEKCIKKG LNDPNPGVRE
KMRATYWTFA AMWPARAEVI MDNLESTAQK LLKRDANNPN SSSPKKEEGA RARPGLGLSK
STMGPSKPSL RETVMAQKRA MVGPRNLPAR PGSAMAHISP ARTTSGSSTS ASTTSAGPAA
PLKSTVSGGM SVRPMRPAKR RPDMAPRPAT AGPYSVRSHD DEPGVEAPSP ETLRSKEISA
RPKIEPTPRR AASRVRPGHA SHASESSIPS PMGKPAASKL GASPRVATTR LPQSPTSLPL
RLSSPAKSDE NLTLVVPTVE SLRRSPGPEA AASKLSPRLS PRLSPRLSPQ PSPQQTPTRP
AAPALEEGPI QQVPADDIPA LEEPVLIDHQ DEPIQVAPGQ ETPIRGSPLS AQATPVEKSP
VVPKSPSDDL GATSNQAVKV FEDPFTADEQ QTTNPTIVTP VLEDRPVNEN AGVPAANGGE
PEGNGLLTES PPDKSRQNSR LLESGITRVK ARSLDVHGFR KLQTLIRENK AMFTNDKFDT
LLLGLFEYLE TPLTNLAPGK AQDVKAQILA TIKLLLQKER DSFQPHVSRG LEAVVAARGA
YDSRTHIVSG LELLAEELVG IGDPAEMVMT MTTLLGGGDE EVKATTPTAE GFRSLSMGLH
ILKELLEKRE SFVPTEGELA QLAGLAGRSL ESAESGVRMG AVQLCVALHG RIGDRLFWET
LRDVKDDPKN VITYYIAKRQ RERDGAAV
//
