ID A0A2A2JUM7_9BILA Unreviewed; 1063 AA.
AC A0A2A2JUM7;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=CDK5 regulatory subunit-associated protein 1 {ECO:0008006|Google:ProtNLM};
GN ORFNames=WR25_19297 {ECO:0000313|EMBL:PAV65368.1};
OS Diploscapter pachys.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Diploscapter.
OX NCBI_TaxID=2018661 {ECO:0000313|EMBL:PAV65368.1, ECO:0000313|Proteomes:UP000218231};
RN [1] {ECO:0000313|EMBL:PAV65368.1, ECO:0000313|Proteomes:UP000218231}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PF1309 {ECO:0000313|EMBL:PAV65368.1};
RA Fradin H., Zegar C., Gutwein M., Lucas J., Kovtun M., Corcoran D.,
RA Baugh L.R., Kiontke K., Gunsalus K., Fitch D.H., Piano F.;
RT "Genome architecture and evolution of a unichromosomal asexual nematode.";
RL Curr. Biol. 0:0-0(2017).
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004115}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004115}. Membrane
CC {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: Belongs to the FAD-binding oxidoreductase/transferase type
CC 4 family. {ECO:0000256|ARBA:ARBA00008000}.
CC -!- SIMILARITY: Belongs to the methylthiotransferase family. MiaB
CC subfamily. {ECO:0000256|ARBA:ARBA00009815}.
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:PAV65368.1}.
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; LIAE01010209; PAV65368.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A2JUM7; -.
DR STRING; 2018661.A0A2A2JUM7; -.
DR Proteomes; UP000218231; Unassembled WGS sequence.
DR GO; GO:0098588; C:bounding membrane of organelle; IEA:UniProt.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035596; F:methylthiotransferase activity; IEA:InterPro.
DR GO; GO:0038023; F:signaling receptor activity; IEA:InterPro.
DR GO; GO:0006400; P:tRNA modification; IEA:InterPro.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.30.70.2190; -; 1.
DR Gene3D; 3.30.70.2740; -; 1.
DR Gene3D; 3.40.50.12160; Methylthiotransferase, N-terminal domain; 1.
DR Gene3D; 3.80.30.20; tm_1862 like domain; 1.
DR Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR InterPro; IPR006638; Elp3/MiaA/NifB-like_rSAM.
DR InterPro; IPR004113; FAD-bd_oxidored_4_C.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR InterPro; IPR005839; Methylthiotransferase.
DR InterPro; IPR020612; Methylthiotransferase_CS.
DR InterPro; IPR013848; Methylthiotransferase_N.
DR InterPro; IPR038135; Methylthiotransferase_N_sf.
DR InterPro; IPR006463; MiaB_methiolase.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR InterPro; IPR012493; Renin_rcpt.
DR InterPro; IPR007197; rSAM.
DR InterPro; IPR023404; rSAM_horseshoe.
DR InterPro; IPR002792; TRAM_dom.
DR NCBIfam; TIGR00089; MiaB/RimO family radical SAM methylthiotransferase; 1.
DR PANTHER; PTHR43020; CDK5 REGULATORY SUBUNIT-ASSOCIATED PROTEIN 1; 1.
DR PANTHER; PTHR43020:SF2; MITOCHONDRIAL TRNA METHYLTHIOTRANSFERASE CDK5RAP1; 1.
DR Pfam; PF02913; FAD-oxidase_C; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR Pfam; PF07850; Renin_r; 1.
DR Pfam; PF01938; TRAM; 1.
DR Pfam; PF00919; UPF0004; 1.
DR SFLD; SFLDF00273; (dimethylallyl)adenosine_tRNA; 1.
DR SFLD; SFLDG01082; B12-binding_domain_containing; 1.
DR SFLD; SFLDF00413; CDK5RAP1; 1.
DR SFLD; SFLDS00029; Radical_SAM; 1.
DR SMART; SM00729; Elp3; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 1.
DR SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
DR PROSITE; PS51449; MTTASE_N; 1.
DR PROSITE; PS01278; MTTASE_RADICAL; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
DR PROSITE; PS50926; TRAM; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000218231};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1063
FT /note="CDK5 regulatory subunit-associated protein 1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012245918"
FT TRANSMEM 51..74
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 122..303
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
FT DOMAIN 596..710
FT /note="MTTase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51449"
FT DOMAIN 734..993
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
FT DOMAIN 994..1059
FT /note="TRAM"
FT /evidence="ECO:0000259|PROSITE:PS50926"
FT COILED 975..1002
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1063 AA; 120001 MW; A4A1C6E46E52C2B8 CRC64;
MNRYLILAFV VLAYISLRVN AQLPEPQTPE EKELARWRQE LKVYAFTGQD YPAMFAIFAG
LIIVLVLALI YIVVGMMSMD PSRDSIIYHS DISYFERILP KGSVKTDSED VKEYNIDWMK
QYEGYGKCVL LPTHEDQVSE ILKYCMKKKL ALVPQAGNTG LVGGSIPVHD EIVLSVKKLK
NFRDFDREQG VLTCDAGFIL HDLDEYVKEF GYMMPFDLGA KGSCLIGGNI STCAGGIRLL
RYGSLHAHLL GLHAVIPNEK GEILRLGSIL PKDNTSLHLH HLFLGSEGQL GVITRVTLKT
VPRPKSVQSA MLGTNSFKNV RELLALAKIQ LAEILSSFEF LDRDTMNCLE DNLQLKDVLP
TKSEFNVLVE TSGSNSEHDK AKVENFLQDC MDKNLIDDGI LAESVSEAQT MWRLREDAPM
AVSRDGYVFK HDLSLPLEHF YELTEACHEK FGKMTKRIST YGHVGDGNTH LNITINRGDD
HEKLYKWKNE TPLRSPRKRF RGTGHDPEGP TTMFFLAPKL PYSTVVRLSF RRYVASTSSL
SNAKPQRRTL PDDGKTLHDF IAEGAKRIRK RHPNIVPSIE ETNSYLDPEL FSGKDLKVHY
ITYGCQMNVN DMEIVRSVMK TAEYTEVEEI KMADVVLLMT CSIRDGAEQK VKTMLHQIKK
NSSKKKFVGV LGCMAERVKH ELIERGKLVD VVAGPDSYRD LPRLLAVARG GSSAINVQLS
LDETYADVVP VRQDEAARTA YVSIMRGCDN MCTYCIVPYT RGRERSRPTD SIVEEVIRLR
DEGIKQVTLL GQNVNSYRDL SESVHSYDPS IPSTSTVPGF KTVYKPKIGG RTFLHLLDRL
SSVAPEVRFR FTSPHPKDFP LELIHLIRDR KNICNQLHLP AQSGDDQTLE RMGRGYTKDL
YLRLVHDIRE VLPEVSFTSD FIAGFCGETE EAHQNTVGLV REVKYSFIYS FPYSMREKTK
AHRQLQDDVP DDVKTRRHQE ILAAFREEAE TLNQKYVDTT QLVLVEGTSR RNENDGQGRA
DCGTKVIFPN SEGIYKPGDF VNVQITAANS QTLRGEALGL GSL
//
