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Database: UniProt
Entry: A0A3M0KL30_HIRRU
LinkDB: A0A3M0KL30_HIRRU
Original site: A0A3M0KL30_HIRRU 
ID   A0A3M0KL30_HIRRU        Unreviewed;      1572 AA.
AC   A0A3M0KL30;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:RMC07917.1};
GN   ORFNames=DUI87_15388 {ECO:0000313|EMBL:RMC07917.1};
OS   Hirundo rustica rustica.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Sylvioidea; Hirundinidae;
OC   Hirundo.
OX   NCBI_TaxID=333673 {ECO:0000313|EMBL:RMC07917.1, ECO:0000313|Proteomes:UP000269221};
RN   [1] {ECO:0000313|EMBL:RMC07917.1, ECO:0000313|Proteomes:UP000269221}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Chelidonia {ECO:0000313|EMBL:RMC07917.1};
RC   TISSUE=Blood {ECO:0000313|EMBL:RMC07917.1};
RA   Formenti G., Chiara M., Poveda L., Francoijs K.-J., Bonisoli-Alquati A.,
RA   Canova L., Gianfranceschi L., Horner D.S., Saino N.;
RT   "A high quality draft genome assembly of the barn swallow (H. rustica
RT   rustica).";
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + glycine + L-glutamyl-[protein] = ADP + glycyl-L-
CC         glutamyl-[protein] + H(+) + phosphate; Xref=Rhea:RHEA:67180,
CC         Rhea:RHEA-COMP:10208, Rhea:RHEA-COMP:17207, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29973, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57305, ChEBI:CHEBI:167890, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000256|ARBA:ARBA00036933};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67181;
CC         Evidence={ECO:0000256|ARBA:ARBA00036933};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, flagellum axoneme
CC       {ECO:0000256|ARBA:ARBA00004611}.
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:RMC07917.1}.
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DR   EMBL; QRBI01000119; RMC07917.1; -; Genomic_DNA.
DR   STRING; 333673.A0A3M0KL30; -.
DR   Proteomes; UP000269221; Unassembled WGS sequence.
DR   GO; GO:0005929; C:cilium; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0070735; F:protein-glycine ligase activity; IEA:UniProt.
DR   GO; GO:0036211; P:protein modification process; IEA:InterPro.
DR   Gene3D; 1.10.1200.30; -; 1.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 2.
DR   Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR008916; Retrov_capsid_C.
DR   InterPro; IPR004344; TTL/TTLL_fam.
DR   PANTHER; PTHR45870; TUBULIN MONOGLYCYLASE TTLL3; 1.
DR   PANTHER; PTHR45870:SF2; TUBULIN MONOGLYCYLASE TTLL3; 1.
DR   Pfam; PF00023; Ank; 1.
DR   Pfam; PF12796; Ank_2; 2.
DR   Pfam; PF03133; TTL; 1.
DR   SMART; SM00248; ANK; 7.
DR   SUPFAM; SSF48403; Ankyrin repeat; 2.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 4.
DR   PROSITE; PS50088; ANK_REPEAT; 5.
DR   PROSITE; PS51221; TTL; 1.
PE   4: Predicted;
KW   ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Reference proteome {ECO:0000313|Proteomes:UP000269221}.
FT   REPEAT          84..116
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          117..149
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          429..461
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          465..494
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          495..527
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          560..584
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          690..767
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1303..1341
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1533..1572
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          965..992
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        560..583
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        690..714
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        737..767
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1308..1323
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1572 AA;  177594 MW;  9C222837A1DB2482 CRC64;
     MAAAEADGGP AAAPESSASL CPSERTSLKE DNLPYPGMLP VDKRLLNLQI YKLLQCVHEK
     DKKQIENLIQ KGFPDLINYT EPKEGYSAFH VASMKNDIEM CRFLLEHGAH PNVHDKMGCT
     PAMKAAELGH EVILELLAKA NADMTAVDNE GKGILFYCLS PTRRHSHCLH IALEYGADVN
     NCTTTGRSVL LQACEQAHEV KEMCLIFLEK GADPHATDPI LTIISGYNAD LKLIAMNGCD
     PTWSNLAHLT PREVAKNSGF KAAAAVLRKV EKAFKKPDET LAWYLRVYDW SLQHEDAIRK
     EFETDQEGDG MVSRRDFISV IRKHWGTVER EQIEILAKKH EASGDKSERP LREDGFPTYM
     VEAVPNIPEE QRFKRDQQSA HPVLDDRAWY VDEPKKTLMD INYLVREGDF VSLQKAFDEG
     VPVDIKDKYY KTPLMVACAS GNIVLVEFLL EKGADVNATD NFLWTPLHHA CYHGHLDIIE
     VLVKAGAAVN ATAIGGATPL MRAIEACRLD MVYFLITAGA DVQATNSNGK TVLELAQLFE
     DAKIIELLEN QLQILAEEQE KEEAKPAKGG KPKPVEPPKP VKKEIWSPDT TAIQLAEKRE
     LLRERATLHG HMEDFTTLFN RKFNRQVAAV NIGHHDGRQH AAESERLKKA KLYVEKAIKE
     KKIFAVQGPY PIIRHLLRAR GWVERKLPHK NRQLKQQPGD QKKQQLEKRV GGGGDKQGEA
     VPNPRGGAQR SLGTREPLQH PRPRDKKNKG EREDEDKKED QEQCSENSDD IHDLMSYLVQ
     DQVPNFLWTI RLSNVDQELL PRIEVVNRFP RLYALCTKEG LCQSLQNLTW FEQVDINTFF
     PRCYRLGFTG EQEAFIEDFR LTAARSLLKL ALQKVRDRPV GTEQPPKSDK VPGECMEMAE
     RGGARPCSPL YLQLVEEALE VCEQHLGILE HQDIDRNTPS PSRTCIAWDR FLQEFYHVTH
     EGSRLVLSRE QREQCQDVLQ RLEEQLPQLG IEGNRNIWIL KPSAKSRGRG KARGSMGHTH
     PHGEGISPSL RCPGIVCTTR LEEVLELTQS RPGSSARVCE WVVQKYMERP LTIFGTKFDI
     RQWFVVTDWK PLTVWFYRDC YLRFCSRPFS LCHLEPARHL CNVSIQKKYK TLQPDPRVPP
     DKIWSNTQFQ AHLAQLGRAD AWQQVIVPGM KAAILNALRC ARDHVGSRKG SFELFGADFL
     IGKNFQPWLL EINSCPTMSP SSAVTRRLCA NVQQDTLRLV LDRKDNPTCS IGAFELLYRE
     VKNEGAQEQV LEEMALADAD KQCKAAILSL SIEAAPTLRD MLQRPKSGEP TELNSSGGGQ
     KSSPDGFTRL DGKPGPDSWQ KLEWIHPVGG KTRTGFLAKT GMDSPGWSEN PDRIPGKNWN
     GFTRLERKPG LDSWQKLEWI HPVGAKTRTG FLAKTGMDSP GWSENPDWIP GKNWNGFTRL
     ERKPGPDSWQ KLEWIHPVGA KTRTGFLAKT GMDSPGWSEN PDRIPGKNWN GFTRLERKPG
     LDSWQKLEWI HPVGAKTRTG LPPENWNGFT WLEGKPGPDY PQKTGMDSPG WRGNLDQISP
     RNPECSRLVG FP
//
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