ID A0A090CEC7_PODAN Unreviewed; 1752 AA.
AC A0A090CEC7;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE SubName: Full=Kinesin-like protein unc-104 {ECO:0000313|EMBL:CDP26080.1};
OS Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383)
OS (Pleurage anserina).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Podosporaceae; Podospora;
OC Podospora anserina.
OX NCBI_TaxID=515849 {ECO:0000313|EMBL:CDP26080.1, ECO:0000313|Proteomes:UP000001197};
RN [1] {ECO:0000313|EMBL:CDP26080.1, ECO:0000313|Proteomes:UP000001197}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383
RC {ECO:0000313|Proteomes:UP000001197};
RX PubMed=18460219; DOI=10.1186/gb-2008-9-5-r77;
RA Espagne E., Lespinet O., Malagnac F., Da Silva C., Jaillon O., Porcel B.M.,
RA Couloux A., Aury J.-M., Segurens B., Poulain J., Anthouard V.,
RA Grossetete S., Khalili H., Coppin E., Dequard-Chablat M., Picard M.,
RA Contamine V., Arnaise S., Bourdais A., Berteaux-Lecellier V., Gautheret D.,
RA de Vries R.P., Battaglia E., Coutinho P.M., Danchin E.G.J., Henrissat B.,
RA El Khoury R., Sainsard-Chanet A., Boivin A., Pinan-Lucarre B., Sellem C.H.,
RA Debuchy R., Wincker P., Weissenbach J., Silar P.;
RT "The genome sequence of the model ascomycete fungus Podospora anserina.";
RL Genome Biol. 9:R77.1-R77.22(2008).
RN [2] {ECO:0000313|Proteomes:UP000001197}
RP GENOME REANNOTATION.
RC STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383
RC {ECO:0000313|Proteomes:UP000001197};
RX PubMed=24558260; DOI=10.1534/genetics.113.159988;
RA Grognet P., Bidard F., Kuchly C., Tong L.C.H., Coppin E., Benkhali J.A.,
RA Couloux A., Wincker P., Debuchy R., Silar P.;
RT "Maintaining two mating types: Structure of the mating type locus and its
RT role in heterokaryosis in Podospora anserina.";
RL Genetics 197:421-432(2014).
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. {ECO:0000256|PROSITE-ProRule:PRU00283}.
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DR EMBL; FO904937; CDP26080.1; -; Genomic_DNA.
DR STRING; 515849.A0A090CEC7; -.
DR eggNOG; KOG0245; Eukaryota.
DR InParanoid; A0A090CEC7; -.
DR Proteomes; UP000001197; Chromosome 2.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR GO; GO:0003777; F:microtubule motor activity; IEA:InterPro.
DR GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR CDD; cd22705; FHA_KIF1; 1.
DR CDD; cd01365; KISc_KIF1A_KIF1B; 1.
DR Gene3D; 2.60.200.20; -; 1.
DR Gene3D; 6.10.250.2520; -; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR022164; Kinesin-like.
DR InterPro; IPR027640; Kinesin-like_fam.
DR InterPro; IPR022140; Kinesin-like_KIF1-typ.
DR InterPro; IPR032405; Kinesin_assoc.
DR InterPro; IPR019821; Kinesin_motor_CS.
DR InterPro; IPR001752; Kinesin_motor_dom.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR PANTHER; PTHR24115:SF802; KINESIN-LIKE PROTEIN UNC-104; 1.
DR PANTHER; PTHR24115; KINESIN-RELATED; 1.
DR Pfam; PF12473; DUF3694; 1.
DR Pfam; PF00498; FHA; 1.
DR Pfam; PF12423; KIF1B; 1.
DR Pfam; PF00225; Kinesin; 1.
DR Pfam; PF16183; Kinesin_assoc; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00240; FHA; 1.
DR SMART; SM00129; KISc; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00283};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00283}; Reference proteome {ECO:0000313|Proteomes:UP000001197}.
FT DOMAIN 14..367
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT DOMAIN 1574..1726
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 621..665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1457..1506
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1529..1553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1728..1752
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 755..832
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 621..652
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1474..1505
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 114..121
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1752 AA; 194650 MW; 69E7216F72B8271D CRC64;
MAPGAGPAGG GGGNIKVVVR CRPFNSREHD RNAKCIIEMK GNQTILTPPD ASAGGGKLSG
KDSAPKAFAF DKSYWSFDKS APNYAGQNHL FDDLGRPLLD NAFQGYNNCI FAYGQTGSGK
SYSMMGYGKD AGIIPMICQD MFERIKVMQQ DKNLKCTVEV SYLEIYNERV RDLLNPANKG
NLKVREHPST GPYVEDLAKL VVGSFQEIEN LMDEGNKART VAATNMNETS SRSHAVFTLM
LTQKRFDPET KMEMEKAAKI SLVDLAGSER ATSTGATGAR LKEGAEINRS LSTLGRVIAA
LADLSTGKKK KGGTGQVPYR DSVLTWLLKD SLGGNSMTAM IAAVSPADIN YDETLSTLRY
ADSAKRIKNH AVVNEDANAR MIRELKEELA LLRNKLGGGG GAPGMPVESY PEGTPLEQQI
VSITAPDGTV KKVSKAEIAE QLNQSEKLLQ DLNQTWEQKL AKTEEIHKER ESALEELGIS
IEKGFIGMST PKKMPHLVNL SDDPLLAECL VYNLKPGITT VGNVESNADH QANIRLNGSK
ILHEHCTFEN APDGTVTVIP KEGAAVMVNG KRVTEPYQLH SGYRIILGDF HIFRFNHPLE
ARAERQERAD KSLLRQSVTA SQLQALERTS PTPSPRPGHD RNLSTAISDF GGSRPDSPSP
FMRNPREADW SFARREAAGA ILGTDQNFAS LSDEELNALF EEVQRVRAER VNGRDDNEDM
ESMASFPVRE KYMSTGTLDN FSLDTALTMP STPKQGEAED RLREIREEMQ TQLEKQKEEF
HDQIKSAEAA NVEVAEIKKE KAKMEETLVK IKAEMQKQLE VQRQEFEKKI EKLDPLKRPK
PKPRLSEEEI ERAKVAVKHW RGRHYVQMAE AVLQHAATLK EAQIMSHELD EHVVFQFTVV
DVGHMMCSSY DMVLNGLTGE GEDPALEDAP KPCIGIRVID YKQSVVHLWS IEKLYDRVRR
MRQMYQYLDQ PEYAQHLSLD NPFIEDCMPQ YTLVGEVDVP LKAVFESRVQ DFTLDVFSPY
TSHTIGIIKL ALEPSSARAP TNTLKFNIVM HEMLGFPERE GTEVHAQLFI PGISEDGITT
TQMIKDFDEG PIRFESVHSM SVPLFAPPQT TLRVAIFAKV SAMHLDKLLS WDDMRDAVPA
NQKPKTPRIS ETQFYTEEKH DLLTRAQILE LNEEGEYKPV EVTQTSEMDN GTFQLHQGLQ
RRISLNLTHS SGDALPWEEV ANMRVGKIQL LDSAGKSPDM GSSGPDLHLK LASKPVFRTN
ANGTRGLTII GQWDSSLHNS LLLDRMTSEK YRVQMTVSWE ILSEKLAEPM KFSMNLCVQI
VSRSFIRQTS MFSSLWQNVR FVHSCTGIFT LQMRPAPIKR AGDLWRMNSQ HDYVKGEELL
TAWTPRGVSL VADFIGSRRK KQMMSEMAVI QSLMKKYGYR ENGHLNGNGI DGGTDDDLLP
PPKINSDADS IAELLKDDTP EVSPTTSPVI SHSELAKDGE ESPESRTTEE PTPPLEEEKP
ASEYDDRQTA LLNKCLKLWQ RYPDSTLKLI SPENTDPPED GVATENNPNG NGNEHHYSAP
TFVATVIRVP KNPSVLKGGY LLVPNADSTR WVKRFVELRR PYLHIHSVAD GEEIGIVSLR
NARVDSQPGI LGLLHSHQDY DHNNFDPDNV AQQQSGGIVG GVASTATGLI SSLTGTPGQG
QGISRLSERL QAGVFAIYGT DNTWLFAARS ERDKLEWIFR IDQSFAQTGS TPAGSVMGAG
SNSGTASPMP RW
//