ID H2B129_KAZAF Unreviewed; 553 AA.
AC H2B129;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 24-JAN-2024, entry version 54.
DE RecName: Full=Actin-binding protein {ECO:0008006|Google:ProtNLM};
GN Name=KAFR0J02650 {ECO:0000313|EMBL:CCF60329.1};
GN ORFNames=KAFR_0J02650 {ECO:0000313|EMBL:CCF60329.1};
OS Kazachstania africana (strain ATCC 22294 / BCRC 22015 / CBS 2517 / CECT
OS 1963 / NBRC 1671 / NRRL Y-8276) (Yeast) (Kluyveromyces africanus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kazachstania.
OX NCBI_TaxID=1071382 {ECO:0000313|EMBL:CCF60329.1, ECO:0000313|Proteomes:UP000005220};
RN [1] {ECO:0000313|EMBL:CCF60329.1, ECO:0000313|Proteomes:UP000005220}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22294 / BCRC 22015 / CBS 2517 / CECT 1963 / NBRC 1671 /
RC NRRL Y-8276 {ECO:0000313|Proteomes:UP000005220};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; HE650830; CCF60329.1; -; Genomic_DNA.
DR RefSeq; XP_003959464.1; XM_003959415.1.
DR AlphaFoldDB; H2B129; -.
DR STRING; 1071382.H2B129; -.
DR GeneID; 13883978; -.
DR KEGG; kaf:KAFR_0J02650; -.
DR eggNOG; KOG3655; Eukaryota.
DR HOGENOM; CLU_459326_0_0_1; -.
DR InParanoid; H2B129; -.
DR OrthoDB; 101008at2759; -.
DR Proteomes; UP000005220; Chromosome 10.
DR GO; GO:0003779; F:actin binding; IEA:InterPro.
DR CDD; cd11281; ADF_drebrin_like; 1.
DR CDD; cd11961; SH3_Abp1_fungi_C2; 1.
DR Gene3D; 3.40.20.10; Severin; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR035718; Abp1_fungi_SH3_C2.
DR InterPro; IPR002108; ADF-H.
DR InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR10829; CORTACTIN AND DREBRIN; 1.
DR PANTHER; PTHR10829:SF25; DREBRIN-LIKE PROTEIN; 1.
DR Pfam; PF00241; Cofilin_ADF; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00102; ADF; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF55753; Actin depolymerizing proteins; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS51263; ADF_H; 1.
DR PROSITE; PS50002; SH3; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000005220};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 7..136
FT /note="ADF-H"
FT /evidence="ECO:0000259|PROSITE:PS51263"
FT DOMAIN 492..553
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 145..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 226..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..265
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..320
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..412
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..474
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 553 AA; 62387 MW; 44505BC0E0FB3472 CRC64;
MALEPINCDS HSRDIEQAYL KVVRGDDDQT KWLILSPNAS KEYFPESTGS DFTEFLASFD
DTKVQYGMAR VSPPGSDVEK LILIGWCPDS APMKTRASFA ANFGTVANNI LKGYHIQVTA
RDEDDLDEKE LLMKVSNAAG ARYSIQKSAS APTKPKISSP PPVKRSIPTP VVAPKRTVPQ
SNEEDDWGEP EIKERDFNKQ PLSANQSTYK PIGKIDLQKV IAEETAKEDP RLVHAEASGS
KINPKDDIAS LKNQSKLQRD NEINSFLKGT KPPVLGNEYK RNDDNVIKGF KTEKTPAQLW
AEKKAKQSAT TESTQVEEPA KSYSAAGEEE EREDEEQEDV NDLKSKFETL STEPTIISPK
PFSKPPVQEA ERQPVKTDYT KIGTRLPGMH QEVSDHEEEQ QNEDDWNDEE EEAAAPSLPS
RKQEIEPEEE EQEEPPTPSL PSRTNVDEEE EQEEQEEEEP APSLPTRDYD EPQQETRAIP
PPPPRRATEQ KEEQPWAIAE YDYEAGEDNE LTFEENDKII NIEFVDDDWW LGELEKNGEK
GLFPSNYVNL GNQ
//
