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Database: UniProt
Entry: A0A1V4K8S7_PATFA
LinkDB: A0A1V4K8S7_PATFA
Original site: A0A1V4K8S7_PATFA 
ID   A0A1V4K8S7_PATFA        Unreviewed;      2838 AA.
AC   A0A1V4K8S7;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Dynein heavy chain 1, axonemal {ECO:0000313|EMBL:OPJ80795.1};
GN   Name=DNAH1 {ECO:0000313|EMBL:OPJ80795.1};
GN   ORFNames=AV530_004217 {ECO:0000313|EMBL:OPJ80795.1};
OS   Patagioenas fasciata monilis.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Patagioenas.
OX   NCBI_TaxID=372326 {ECO:0000313|EMBL:OPJ80795.1, ECO:0000313|Proteomes:UP000190648};
RN   [1] {ECO:0000313|EMBL:OPJ80795.1, ECO:0000313|Proteomes:UP000190648}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BTP2013 {ECO:0000313|EMBL:OPJ80795.1};
RC   TISSUE=Blood {ECO:0000313|EMBL:OPJ80795.1};
RA   Soares A.E., Novak B.J., Rice E.S., O'Connell B., Chang D., Weber S.,
RA   Shapiro B.;
RT   "Band-tailed pigeon sequencing and assembly.";
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the dynein heavy chain family.
CC       {ECO:0000256|ARBA:ARBA00008887}.
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:OPJ80795.1}.
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DR   EMBL; LSYS01004144; OPJ80795.1; -; Genomic_DNA.
DR   STRING; 372326.A0A1V4K8S7; -.
DR   Proteomes; UP000190648; Unassembled WGS sequence.
DR   GO; GO:0005930; C:axoneme; IEA:UniProt.
DR   GO; GO:0030286; C:dynein complex; IEA:UniProtKB-KW.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0045505; F:dynein intermediate chain binding; IEA:InterPro.
DR   GO; GO:0051959; F:dynein light intermediate chain binding; IEA:InterPro.
DR   GO; GO:0008569; F:minus-end-directed microtubule motor activity; IEA:InterPro.
DR   GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR   Gene3D; 1.10.287.2620; -; 1.
DR   Gene3D; 1.10.472.130; -; 1.
DR   Gene3D; 1.10.8.710; -; 1.
DR   Gene3D; 1.20.58.1120; -; 1.
DR   Gene3D; 1.20.920.20; -; 1.
DR   Gene3D; 1.20.920.30; -; 1.
DR   Gene3D; 1.20.140.100; Dynein heavy chain, N-terminal domain 2; 1.
DR   Gene3D; 3.20.180.20; Dynein heavy chain, N-terminal domain 2; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR035699; AAA_6.
DR   InterPro; IPR026983; DHC_fam.
DR   InterPro; IPR041589; DNAH3_AAA_lid_1.
DR   InterPro; IPR042222; Dynein_2_N.
DR   InterPro; IPR043157; Dynein_AAA1S.
DR   InterPro; IPR041466; Dynein_AAA5_ext.
DR   InterPro; IPR024317; Dynein_heavy_chain_D4_dom.
DR   InterPro; IPR013602; Dynein_heavy_linker.
DR   InterPro; IPR042228; Dynein_linker_3.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR45703; DYNEIN HEAVY CHAIN; 1.
DR   PANTHER; PTHR45703:SF28; DYNEINS HEAVY CHAIN; 1.
DR   Pfam; PF12774; AAA_6; 1.
DR   Pfam; PF12775; AAA_7; 1.
DR   Pfam; PF12780; AAA_8; 1.
DR   Pfam; PF17857; AAA_lid_1; 1.
DR   Pfam; PF08393; DHC_N2; 1.
DR   Pfam; PF17852; Dynein_AAA_lid; 1.
DR   SMART; SM00382; AAA; 3.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 4.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW   Cilium {ECO:0000256|ARBA:ARBA00023069};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW   Dynein {ECO:0000256|ARBA:ARBA00023017};
KW   Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW   Motor protein {ECO:0000256|ARBA:ARBA00023175};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000190648}.
FT   DOMAIN          1455..1594
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          1736..1893
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          2100..2248
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   COILED          854..881
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          2761..2788
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   2838 AA;  325113 MW;  4E002D15FFB509E6 CRC64;
     MYHSLVSQAN LEQHTPKVTT FQMPEDFASI LDKQRIGPTT EKLIESDFPA QSFQPKVQVA
     FKVLPGQCPR RVEIERRRRL YLSFDIAQLL ASKGIDSNQL MPRHYDPDNM PTIAERADPI
     FPIYLPLKIF DNKEYDCRTP EEWILLGLEP GSCDRKPVPG KALLPTDDVL GHEDPKNQKL
     IYSWIDVGVL DYDKKTELYL VHKTDKNGLV RDEAGRPILN GGMTPEGRAP LLSCQYWVPR
     VCLLFLAEDP RVFAQRVVDA HSLRKKTEAL LRYNLYVDCM PIDGLNSISE EWLECMKLLA
     LQTPRLEKEE RVLDRMCPLE KEVRSDYERT MNKMIFDRVV SSKPQMFYYV TLPDKEEEKV
     PEKGLVSIPD YPFAERRANF NFLSLLTRPE VILLLTQVQD ECNKAAAMSL FNSTLTEHVC
     LEEFEQIQTQ TFTQVQVFLK DTWINTLKTA IKNNLRDSGK GLYDLEQDDW DLYQMSKLHK
     LMTRIKFILQ DSVRYLVQNS LISFTQLLLD ACHDILNCSE DMEWGDDLIN SPYRPQRNPL
     FKTDLVLDSR GVHFSPPVES FEKSLISLFN KGILVTHTVP QLEKYVLENM GITGTPLLNS
     VDLHEPEVEE LRETVWSAIQ KARIPLQAYT KRYEKFLELN NNDIEYFLRE YEEQSPSAQE
     VMTIVNTYLS EKENLQNTLP RSIVIGPFHV STEDVKRNLC KKYKALATSM LDLLAKNLHL
     QVQNICDVYK AVSCKMHEKP NVIEELAELR EWMKGVPEQL AVQEELIHQV VEDYKVLEEF
     LYKLSDKDFS DMWAARHWPH KIAMQTESIQ LQHLEDEEKF RKIQAIDQNV FQDKLEEMQL
     IVYGFSVTVD TNQAHDLAKK AREVKKQLKE LQNLANVYNN RERIFGMKVT KYSTLSKMVK
     DFQPYCDLWT TVSDWMQWHD SWMNDPLVEL EAEQLEKNVN ESSKTMQKCV RQFKDSPACQ
     AVAMEFRDKI EDFKSYVPLI QGLNNPGMKS RHWEMLSEEI NMDIKPEPSL TVGHCLEMNL
     LYHIETITKV AEIAGKEYAI ENALNKMESE WNSVFFIVEP YKDTGTFILK DTDEANQLTD
     DHIVMVQSMS FSPFKKHFEE RMSTWENKLK ITQDVLEEWL NCQCSWLYLE PIFRSEDIKR
     QLPLESQRYQ DMDTEWRNIM KNAKENPEVM SLCPDPVLLE NLRKCNNLLE LVQKGLSEYL
     EMKRRAFPRF YFLSDDELLE ILSQTKDPTA VQPHLRKCFE NIAQLLFQED LQITHMYSAE
     GEEVKLCVSI YPTDNVEEWL LEVEKSMKAS VRDHIERSIG VYPETARTTW VLQWPGQVVI
     AGCQIFWTKE VSEALEAGDL SSRLYPQLTT QLGDLVALVR GHLSKMQRSV LSALIVIEVH
     AKDVAAKLIE ENVTSMNDFE WISQLRYYWT KEDLYIRAVN AEFLYGYEYL GNSGRLVITP
     LTDRCYLTLT GALHLKFGGA PAGPAGTGKT ETTKDLGKAL AIQTVVFNCS DQLDFMAMGK
     FFKGLASAGA WACFDEFNRI DIEVLSVVAQ QITTIQKAQQ QRVDRFMFEG MEIPLVPSCA
     VFITMNPGYA GRTELPDNLK ALFRPVAMMV PDYSMIAEIS LYSFGFNEAK VLAKKITTTF
     KLLSEQLSSQ DHYDFGMRAV KTVISTAGNL KRENPTMDEE LICLRAIRDA NIPKFLQDDL
     RLFRGIVSDL FPKIKEEPVD YGILEKAIRK SCIKENLKDV DGFVTKCIQL YETTVVRHGL
     MLVGPTGSGK TKCYEVLAAA MTSLKGQPAA SGGNYEAVRY FVLNPKSITM GQLYGEFNLL
     THEWTDGILS SLIRQGAAAT DTIKKWYMFD GPVDALWIEN MNTVLDDNKK LCLSSGEIIK
     MTESMTMMFE VQDLAVASPA TVSRCGMVYL EPSILGLEPF IECWLQKIPS IIEPFSKQLA
     SLFKRFLKDA IGFVRRFVKE ITASTDSNLT RSLLVLLECL FQPFIPSEGV RRIPQEKIAR
     IGELIEPWFI FALIWSVGAT GDSQGRTAFS LWLREKMAKE KIQLLFPEDG LVYDYKLYDA
     GLSSPEEDLD EEVIKEVCWE PWLDPTAKFT MVPDTNFCDI IVPTMNTVRM AHLLGLLLTN
     RKPVLCIGPT GTGKTLTITD KLLKNLPPRY VTHFLMFSAR TSANQTQDLI DSKLDKRRKG
     VFGPPVGRYF IFFIDDLNMP MLETYGAQPP IELLRQWMDH GGWYDRKQIG TFKKLVDINF
     VCAMGPPGGG RNAVTPRFTR HFNYLSFTEM EDSSKKAIFS TILGCWMDGL LGERSHREPV
     PEAVAIKDLN EPLVDATIGV YLTITSQLLP TPAKSHYTFN LRDLSKVFQG MLMAEPSKVE
     NKLQLLRLWY HESCRVFCDR LVSKEDRTWF DNLMKSMMED FDTTFEEVVP SQPVLFGDFM
     EPDAIVKQYE AIESQEKLKA VIEDYLEEYN QSNTLELKLV LFMDAIQHIC RISRILRQAP
     GNALLLGVGG SGRQSLTRLA SHMADYECFQ IELSKNYGMT EWRDDVRKIM MKAGIQSLPK
     TFLFVDTQIK NESFLEDINN LLNSGDIPNI YSLDDEDKIT TAMKPVVRDL GQQPTKANLM
     AAYTRRVYSN MHMVLCMSPI GEVFRARLRQ FPSLVNCCTI DWFNKWPAEA LQSVASSVLQ
     EIPHLGASTE DINGMVQVCV EIHQSVAKKC QVYLAELGRH NYVTPKSYLE FLSTFSSLIG
     KKKQELKTAK KRMKGGLDKL LQTAEDVARM QEELESARPL LAQAAKDTEA TMEQLQVDTA
     VAEKTRTAVQ AEEMKANAKA QAAQAIADDA QKDLAEALPA LDAALASLRN LKKNDVTESW
     HEESPVYARL PMPTHKVH
//
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