ID A0A162D374_9CRUS Unreviewed; 3228 AA.
AC A0A162D374;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=CCHC-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=APZ42_030316 {ECO:0000313|EMBL:KZS06264.1};
OS Daphnia magna.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Branchiopoda;
OC Diplostraca; Cladocera; Anomopoda; Daphniidae; Daphnia.
OX NCBI_TaxID=35525 {ECO:0000313|EMBL:KZS06264.1, ECO:0000313|Proteomes:UP000076858};
RN [1] {ECO:0000313|EMBL:KZS06264.1, ECO:0000313|Proteomes:UP000076858}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Xinb3 {ECO:0000313|EMBL:KZS06264.1,
RC ECO:0000313|Proteomes:UP000076858};
RC TISSUE=Complete organism {ECO:0000313|EMBL:KZS06264.1};
RA Gilbert D.G., Choi J.-H., Mockaitis K., Colbourne J., Pfrender M.;
RT "EvidentialGene: Evidence-directed Construction of Genes on Genomes.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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:KZS06264.1}.
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DR EMBL; LRGB01002801; KZS06264.1; -; Genomic_DNA.
DR Proteomes; UP000076858; Unassembled WGS sequence.
DR GO; GO:0042575; C:DNA polymerase complex; IEA:UniProt.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0071897; P:DNA biosynthetic process; IEA:UniProt.
DR GO; GO:0015074; P:DNA integration; IEA:InterPro.
DR CDD; cd09272; RNase_HI_RT_Ty1; 1.
DR CDD; cd01647; RT_LTR; 1.
DR Gene3D; 1.10.340.70; -; 1.
DR Gene3D; 3.30.70.270; -; 2.
DR Gene3D; 3.10.10.10; HIV Type 1 Reverse Transcriptase, subunit A, domain 1; 1.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR Gene3D; 4.10.60.10; Zinc finger, CCHC-type; 2.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR005312; DUF1759.
DR InterPro; IPR001584; Integrase_cat-core.
DR InterPro; IPR041588; Integrase_H2C2.
DR InterPro; IPR008042; Retrotrans_Pao.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR000477; RT_dom.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR PANTHER; PTHR22955; RETROTRANSPOSON; 1.
DR PANTHER; PTHR22955:SF69; RNA-DIRECTED DNA POLYMERASE; 1.
DR Pfam; PF03564; DUF1759; 1.
DR Pfam; PF17921; Integrase_H2C2; 1.
DR Pfam; PF05380; Peptidase_A17; 1.
DR Pfam; PF14223; Retrotran_gag_2; 1.
DR Pfam; PF00078; RVT_1; 1.
DR Pfam; PF00098; zf-CCHC; 1.
DR SMART; SM00343; ZnF_C2HC; 2.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 2.
DR SUPFAM; SSF57756; Retrovirus zinc finger-like domains; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR PROSITE; PS50994; INTEGRASE; 1.
DR PROSITE; PS50158; ZF_CCHC; 2.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Reference proteome {ECO:0000313|Proteomes:UP000076858};
KW Transposable element {ECO:0000256|ARBA:ARBA00022464};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00047}.
FT DOMAIN 969..984
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT DOMAIN 2122..2304
FT /note="Integrase catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50994"
FT DOMAIN 2700..2715
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT REGION 192..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 984..1010
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1674..1698
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2300..2339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3167..3203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 984..999
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1678..1698
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2307..2339
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3167..3185
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3186..3200
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3228 AA; 367822 MW; 83F53342B1CD5A70 CRC64;
MERRTLLQRV ASPNVHHSAA TITATSMSHT TLPTNITLPG DKVVLRVISE VYNRFFTTGK
PGSDQLTFKI DSDFLVDEEA TTTANKLTLE EYLLRWGNRL KLQNMSSLFS IKENIITCLM
KQSNSAIFQV HNPSIKNIQQ EITVNMDSSV STCMIESDVL QQQTAETPSG ETSTNASSSF
MYLSSFDGSQ KQTETASTSF THPAGGAQEE RGEEVPSTST LKSNWNSREF RRQRTLLKAS
CAAAQSRIPH YFEILKDIED FTERQENDSL RLQLKNLEDK YSLLQSFQGQ QFEVGLPGQS
LLKRMMQQSI TQNGKSPNKI RHNDAVLEHF CLNVWILGGR RLYEIFYANF PGIFPSPTTI
HQKLVKFDIS VDEDCLNVSK VKEYLVSNGA PLIICLSEDA TGVVGRVEYY AKKNCLMGFS
NPLTSNGFPD STASNARTAQ DILNQFDHHD RASVVMIGMI QPIVVGLPAI RLFAYGRKQQ
VYGRFKRNEG DTEPMASRGF SVSCFSTPQS ELPAAIPVNA LYLRKRWKFF LCDFLRDCIP
VQDTIHLGAK LQTRFWKTQN ILPSGNKIAS PAHIINLIKN IGVTKDKHGL RDRDLELIDK
MNYDAVTRLC NPRLTELLGI VSGSEATRFY LNLMNKVTSS FLDKKLEPLE RVYRLCEAFH
HAERLLVHRN QCPFIEIEAT ILRAKEDSKS TMVSMGVIVS DAECFNFDNR LAWKMNQAVR
QNELSNELDV DEKCESIENQ GNDFLDEVDS FDASVLTSIS NADFKDYREI LERQIVSNCN
ELDHSVSTLI NNYRQMADEL QNVGAPVTYI QMEERILSTL PPSYHAVVAA WETQLRDENR
NILTLTARLI LEETRIKGRD GDKRNLLLTK IKLTRPMQLE VEEVAIKDEE VSEVVDTEEL
EVIVEDTIIV GTEVDPEIIV EVKREIEATI MMVEVYSKLY CSLFHVSKNI YTYQGYNHGS
RPTFGSYDCY ECGEPGHLAR NCRNRRHAEE KKARQGKQDS NRNFNDGGYE NDQRDPTFNC
LSSVCFLAKK TNDWYADSGA THHMTDQRYF FTTFKPVKPG TWHVYGIGSI KMEVHGVGNI
EIHSYDQGEE NVGVLNDALF VPGIGANLFS LGTAMDRKLK ADFEGDLAIF KDKKTDTAVM
EGQKIGKSLY HMKFITSMQI KIYAHASQKI IKKMASIGAV DGLILDKEEG IGGLFTRKVI
GAVRLVYNPE FHQRTKHIKL KWHWIREQVN EDKIVVKLVG TDDQLADIFT KALAGQKFLR
KVLRKISTIE HIKIQGILKY SWNLAYFVHP KVECTTPRSY LHYGTNQYRK AIDVLRDRYG
DEEKLKKPYL AELKAMANTR LSETSALPQW QKLHDGLTNT VAALVSHGVN TKTHEAYLTP
DLLASCPKAL VSRWRDSWDD EEPTFSKILK ALKREIRHRE EDEALSTSCR RPGDKDRSNC
EEILRKCKKG HPTDFSKGLL SEGKDLADDR YITGQQGSQF DIIVGCDFIW SIMQHKTVPG
ANGLVACASK VGWLIFGMIS ENSKMEEQVL SATVDAQRPM TDFKEFWSLE HIRINQQERS
EPAFLEAYQE TIQRAEDEDT WCFSPSKSAI LGAETTKIRP VFDGSAHLKE RPSINDAPET
GPNLNPEVLA VLLRFRQNRI ALTADITQTF LQVEIRQEHR QLIQFIWPVH SQSHHPQAPK
RVRKEIPRDR EETTAEEAEK RIRKANTIFK AAKMELCKWF SNSAELVERL PEVQFKETVT
SVAAESKSVT KTLGVIWDPV SDKFKFDPTN DAYSVVAYLQ RIDGKDPVML YSKTRIAPDS
KISVSIPRLE LLSGLLAARL GSYIEKATRQ QIKRKLLWTD SAIGFWWMKG EASRWEQFVH
NRVTEKRRTV ETEEIRHCPG LQNPADEEEW PQLPSSVTEL QLQEVSVEEK AEETTQCAVS
AETKWYERFS SMRTMVRVLA TMLMAIKKLK GEKDPESPVA TVRHRGRKLK FPVLTVEETR
EATLELYRKV QATHCGAVVT SFRSGILEVP HELRKLGLMW DERDRLLRCR FRHLNWMEYN
KTAALILLST EHIITRRLVE QTHLRLKHTG VKTMMGALRT DFWIPKMRQA IKKETSKCTG
CKRLDSRHFD EIPAPLPSGR LQMSNPFTIT GVDFAGPFQV EPPANSGHRT KVFVCLFTCA
VARAVHLEVT TDQEISTFIF APRRFFAWRE YPRALYSDDA GTFTLADKYL RAAYRDSRVF
NTLVDLNIKW RFSPSLAPWW GGFWERMVQT VKRLLYKTYG SDCMENNFFQ TVLTEIEETI
NTRPLIYVAE DDTKPPKQLV TGYRQQQHHP VDDEEREYSD RENSKHRKTT EKVSIKKPKA
KAVPVDIPTS VQAQRHHVKE CRIEVEKIMN ATQTSPLSFR MRTCPIEKQL KEGERDTNTA
LLSFAINSGL GRFSDAEPLH SIFDLMKDPE YNSSVVVDEF KGLVVKIDSE IVLADTERIV
RQHNIGVNKS AQGALLSDTL CSLSADIQGF FFVSYFIEKI PNLFFELFGS LNHHSSSALQ
YGLNSLLSYG TSYVLHSLLK IIAFFSWEKP KIFRSTSFGV KTKKFRAIFT TIKAATVEIA
ERFRFHQVKQ KPEESEANFL ATLRNLAKDC AFGTFLESAL RNGFVIGFQD QRIQTKLLAE
ATLTLDSAFK LASSMESATQ QTKQLRQTDQ LNVLKPRGHE CWRCGEVHNP TTCYLKTQEC
FYCKKEGHWA SCCPKKTAKK PSQPKPILKP NPTKKAQKSY IHFIEEEEAE TLLVFDPDQD
LNMYYFPDPN RATRPVSSLF VIDGREIRME VDTGAGFTVF SEQDWILHGR PELKDTNVQL
RTYTAYNQLE LDKESQQVCT INTPDGLFQY TRMPFGIASA PGKFQRVMDD LFRDTPWVKC
YLDDILITGR TEEEHWTRVK LVLCKLQKAG VRLQQEKCAF GVREIPYLGF VISKDGLKTS
PEKAKAVQDS RRPHDLTSLR AYLGLINYYG KFIPKLSPVA APLNHLLRKD VEMGRGSREA
KNEGDVVNQF PTSATFSSDF LKTTVLTEEV QKATKKDPVL QEIIQKVHHG WNKADAANDW
SSNYFRKRCE LSMENGLLIS GRQTGVGTNL RPGKNKWLEG NVQQTLGSYL FAVQVGDQLL
KRHTNQLLLR TVANERRQEE AKTSTLRAPE APVQTIQNAR QPIAVAASSQ PMEPTNLEAT
PTVQPTPDQL TPPPPRKPSS RIRKLPSHLQ DFVLDLLTTV HCCNCDTV
//
