ID A0A151PG55_ALLMI Unreviewed; 1346 AA.
AC A0A151PG55;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=MAP7 domain-containing protein 1 isoform A {ECO:0000313|EMBL:KYO47973.1};
GN Name=MAP7D1-1 {ECO:0000313|EMBL:KYO47973.1};
GN ORFNames=Y1Q_0022131 {ECO:0000313|EMBL:KYO47973.1};
OS Alligator mississippiensis (American alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=8496 {ECO:0000313|EMBL:KYO47973.1};
RN [1] {ECO:0000313|EMBL:KYO47973.1, ECO:0000313|Proteomes:UP000050525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSC_2009_1 {ECO:0000313|EMBL:KYO47973.1};
RX PubMed=22293439; DOI=10.1186/gb-2012-13-1-415;
RA St John J.A., Braun E.L., Isberg S.R., Miles L.G., Chong A.Y., Gongora J.,
RA Dalzell P., Moran C., Bed'hom B., Abzhanov A., Burgess S.C., Cooksey A.M.,
RA Castoe T.A., Crawford N.G., Densmore L.D., Drew J.C., Edwards S.V.,
RA Faircloth B.C., Fujita M.K., Greenwold M.J., Hoffmann F.G., Howard J.M.,
RA Iguchi T., Janes D.E., Khan S.Y., Kohno S., de Koning A.J., Lance S.L.,
RA McCarthy F.M., McCormack J.E., Merchant M.E., Peterson D.G., Pollock D.D.,
RA Pourmand N., Raney B.J., Roessler K.A., Sanford J.R., Sawyer R.H.,
RA Schmidt C.J., Triplett E.W., Tuberville T.D., Venegas-Anaya M.,
RA Howard J.T., Jarvis E.D., Guillette L.J.Jr., Glenn T.C., Green R.E.,
RA Ray D.A.;
RT "Sequencing three crocodilian genomes to illuminate the evolution of
RT archosaurs and amniotes.";
RL Genome Biol. 13:415-415(2012).
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:KYO47973.1}.
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DR EMBL; AKHW03000275; KYO47973.1; -; Genomic_DNA.
DR Proteomes; UP000050525; Unassembled WGS sequence.
DR GO; GO:0015630; C:microtubule cytoskeleton; IEA:InterPro.
DR GO; GO:0009044; F:xylan 1,4-beta-xylosidase activity; IEA:InterPro.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IEA:InterPro.
DR GO; GO:0045493; P:xylan catabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.1700; Glycoside hydrolase family 3 C-terminal domain; 1.
DR Gene3D; 3.20.20.300; Glycoside hydrolase, family 3, N-terminal domain; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR044993; BXL.
DR InterPro; IPR026891; Fn3-like.
DR InterPro; IPR002772; Glyco_hydro_3_C.
DR InterPro; IPR036881; Glyco_hydro_3_C_sf.
DR InterPro; IPR001764; Glyco_hydro_3_N.
DR InterPro; IPR036962; Glyco_hydro_3_N_sf.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR008604; MAP7_fam.
DR PANTHER; PTHR42721:SF42; FIBRONECTIN TYPE III-LIKE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR42721; SUGAR HYDROLASE-RELATED; 1.
DR Pfam; PF14310; Fn3-like; 1.
DR Pfam; PF00933; Glyco_hydro_3; 1.
DR Pfam; PF01915; Glyco_hydro_3_C; 1.
DR Pfam; PF05672; MAP7; 1.
DR PRINTS; PR00133; GLHYDRLASE3.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000050525};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 26..293
FT /note="Glycoside hydrolase family 3 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00933"
FT DOMAIN 338..567
FT /note="Glycoside hydrolase family 3 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01915"
FT DOMAIN 604..642
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|Pfam:PF14310"
FT REGION 888..1223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 733..789
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 895..911
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 920..969
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1007..1021
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1038..1052
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1054..1210
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1346 AA; 149163 MW; 99CDF0B1160F3F27 CRC64;
MVLQMARGGA RGNGPAPGIE RLGIQPYNWN TECLRGDGEA PGWATAFPQA LGLAASFSPE
LIYRVANATA TEVRAKHTHF MAMGKYSDHT GLSCFSPVLN IMRHPLWGRN QETYGEDPFL
SAELGASFVQ GLQGPHPRYV KASAGCKHFS VHGGPENLPV SRYSFDAKVG ELDWRTTFLP
QFEACVRAGS YSFMCSYNRI NGVPACAHEQ LLMGILREEW GFQGYVVSDE GAVELILLGH
HYTHSFLETA VAAVNAGLNL ELSYGLRKNI FTLIPEAVAQ GNITMETVKA RVRPLFYTRL
RLGEFDPPEM NPYRALGMDT VQSPAHQALA LEAAIKTLVL LKNAEDTLPL RAQDLAGGRI
AVVGPFADSP HVLFGDYAPV PDPRYIVTPR RGLEALPANV SFAAGCREPR CLHYVPAEVK
AAVRGANVVI VCLGTGIDVE SETKDRRDLA LPGHQLQLLQ DAVAEAAGRP VILLLFNAGP
LDVSWAQTHP SVHAILACFF PAQAAGTAVT KVLLGQDGAN PAGRLPATWP AGMHQVPAME
NYTMVGRTYR YYGPEPPLYP FGYGLSYTSF HYRDLVLDPP TLPVCANLSI SVVLENRGPR
DGEEVVQLYL RWGRPSVPAP RWQLVGFRRV PLGAGQADKL LFEEFGVEHF QYRFLFQGSG
NLWLQPAEAR TPARDVVCPE SNQPCAPASP HPAQSDQTYV QKAQARHRQA KERREERAKY
LAAKRVLWLE KEEKAKVLRE KQLEDRRKRL EEQRLKAEQR RAVLEERQRQ KLEKNKERYE
AAIQRSAKKT WAEIRQQRWS WAGALHHGSP AHKDGASRCS VSAVNLPKHV DSIINKRLSK
SSATLWNSPS RNRSLQLSPW ESSIVDRLMT PTLSFLARSR SAVTLAGNGK EQGVPVCPRS
TSASPLSPCN NHRVQHRCWE RRKGTAGSPD VTPRRRAEPL PKRKEKKDKE RENAKERSAL
SRERGLKKRQ SLPGGQPKLL PTAESSPKNR PSSPATPKAR PASPSPALGS PHRPPLPRST
HASPKTPRAT EEPPGAAAPS GAPSPPPAPA TPREAEEQAR RAAEERARRA AEAHRQDEER
RRQDEERQQQ EEREAQERAQ AEQEEMQRLQ KQREEAEARA REEAERQRLE REKHFQREEQ
ERLERKKRLE EIMKRTRKSD TADTKKTEDK KMVNGKEARQ EGDTGSGCEK RLGLLAKEEE
LPEKEMPSTE SPDVRQGTAP EGLPPSPLAK TTAAPVALVN GVQPSKHENG IHAKAAGPGV
VELAHHGSTG DPLIPFGDTE PFLKKAVVSP PQVTEVLSPF LKNRIDLQSE GGCKKELFLD
FGIEEATKVT GYCGRTQGIS QFSNKV
//
