NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1189403502|gb|ARO49086|]
View 

recombination activating protein 1, partial [Pennahia macrocephala]

Protein Classification

RAG1 domain-containing protein( domain architecture ID 139673)

RAG1 domain-containing protein such as RAG1, the recombination activating protein 1, which is the catalytic component of the RAG complex, a multiprotein complex that mediates the DNA cleavage phase during V(D)J recombination and also acts as an E3 ubiquitin-protein ligase that mediates monoubiquitination of histone H3

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
RAG1 super family cl20149
Recombination-activation protein 1 (RAG1), recombinase; This family is one of the two ...
1-490 0e+00

Recombination-activation protein 1 (RAG1), recombinase; This family is one of the two different components of the RAG1-RAG2 V(D)J recombinase complex. The RAG complex, consisting of two RAG1 and two RAG2 proteins is a multi-protein complex that mediates DNA cleavage during V(D)J (variable-diversity-joining) recombination. RAG1 mediates DNA-binding to the conserved recombination signal sequences (RSS). Many of the proteins in this family are fragments. Solution of the structure of the complex of RAG1 and RAG2 shows that each protein dimerizes with itself and each pair then complexes together to from the RAG1-RAG2 V(D)J recombinase enzyme. The different structural elements in RAG1 for UniProtKB:P15919 are: an N-terminal nonamer-binding domain from residues 391-459; a dimerization and DNA-binding domain from 459-515; an extended pre-RNase H domain from 515-588; the catalytic RNase H domain from 588-719; a ZnC2 domain from 719-791; and ZnH2 domain from 791-962; and a three-helix C-terminal domain from 962-1008.


The actual alignment was detected with superfamily member pfam12940:

Pssm-ID: 315595  Cd Length: 653  Bit Score: 987.62  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189403502   1 QIFQPLHALRTAEKELLPGFHQFEWQPALKNVSTSCNVGIINGLAGLTSSVDDSPADTITRRFRYDVALVSALKDLEEDV 80
Cdd:pfam12940 115 QIFQPLHTLRAAEKALLPGFHHFEWQPALKNVSPSCDVGIIDGLSGWSPSVDDQPADTITRRFRYDVALVAALKDLEEDI 194
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189403502  81 MEGLKESGLEDSACTSGFSVMIKESCDGMGDVSEKHGGGPVVPEKAVRFSFTIMSVSVLADGEE-EEVTIFTEPKPNSEL 159
Cdd:pfam12940 195 LEGLKEQGLDDSACTEGFSVMIKECCDGMGDVSEKHGGGPAVPEKAVRFSFTIMSVSILADDEEgEEVAIFHELKPNSEL 274
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189403502 160 SCKPLCLTFVDESDHETLTSILWPIVEERNAMKESRLILPIGGLLRSFRFHFRGTGYDEKMVREMEGLEASGSTYICTLC 239
Cdd:pfam12940 275 CCKPLCLMFADESDHETLTAILAPIMAEREAMKESRLILSIGGLLRSFRFHFRGTGYDEKLVRDMEGLEASGSTYICTLC 354
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189403502 240 DSTRAEASQNMVLHSITRSHEENLDRYEIWRTNPFSESAEELRERVKGVSAKPFMETHPTLDALHCDIGNATEFYKIFQD 319
Cdd:pfam12940 355 DSSRAEASKNKVLHAITRSHEENLERYEIWRTNPFSESADDLRDRVKGISAKPFLETQACIDALHCDIGNATEFYKIFQD 434
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189403502 320 EIGEVYEKVNPSREERRSWRAALDKQLRNKMKLKPVMRMNGNYARRLMTMEAAE*VCELVPSEERREALRELMRLYLQMK 399
Cdd:pfam12940 435 EIGEVHKKANPSKEERKRWQAALDKQLRKKMKLKPVMRMNGNFARKLMTQEAVDAVCELVPSEERQEALRELMHLYLQMK 514
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189403502 400 PVWRATCPAKECPDQLCRYSFNSQRFADLLSSAFKYRYNGKITNYLHKTLAHVPEIIERDGSIGAWASEGNESANKLFRR 479
Cdd:pfam12940 515 PVWRATCPAKECPDLLCRYSFNSQRFADLLSTTFKYRYDGKITNYLHKTLAHVPEIIERDGSIGAWASEGNESANKLFRR 594
                         490
                  ....*....|.
gi 1189403502 480 FRKMNARQSKA 490
Cdd:pfam12940 595 FRKMNARQSKS 605
 
Name Accession Description Interval E-value
RAG1 pfam12940
Recombination-activation protein 1 (RAG1), recombinase; This family is one of the two ...
1-490 0e+00

Recombination-activation protein 1 (RAG1), recombinase; This family is one of the two different components of the RAG1-RAG2 V(D)J recombinase complex. The RAG complex, consisting of two RAG1 and two RAG2 proteins is a multi-protein complex that mediates DNA cleavage during V(D)J (variable-diversity-joining) recombination. RAG1 mediates DNA-binding to the conserved recombination signal sequences (RSS). Many of the proteins in this family are fragments. Solution of the structure of the complex of RAG1 and RAG2 shows that each protein dimerizes with itself and each pair then complexes together to from the RAG1-RAG2 V(D)J recombinase enzyme. The different structural elements in RAG1 for UniProtKB:P15919 are: an N-terminal nonamer-binding domain from residues 391-459; a dimerization and DNA-binding domain from 459-515; an extended pre-RNase H domain from 515-588; the catalytic RNase H domain from 588-719; a ZnC2 domain from 719-791; and ZnH2 domain from 791-962; and a three-helix C-terminal domain from 962-1008.


Pssm-ID: 315595  Cd Length: 653  Bit Score: 987.62  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189403502   1 QIFQPLHALRTAEKELLPGFHQFEWQPALKNVSTSCNVGIINGLAGLTSSVDDSPADTITRRFRYDVALVSALKDLEEDV 80
Cdd:pfam12940 115 QIFQPLHTLRAAEKALLPGFHHFEWQPALKNVSPSCDVGIIDGLSGWSPSVDDQPADTITRRFRYDVALVAALKDLEEDI 194
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189403502  81 MEGLKESGLEDSACTSGFSVMIKESCDGMGDVSEKHGGGPVVPEKAVRFSFTIMSVSVLADGEE-EEVTIFTEPKPNSEL 159
Cdd:pfam12940 195 LEGLKEQGLDDSACTEGFSVMIKECCDGMGDVSEKHGGGPAVPEKAVRFSFTIMSVSILADDEEgEEVAIFHELKPNSEL 274
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189403502 160 SCKPLCLTFVDESDHETLTSILWPIVEERNAMKESRLILPIGGLLRSFRFHFRGTGYDEKMVREMEGLEASGSTYICTLC 239
Cdd:pfam12940 275 CCKPLCLMFADESDHETLTAILAPIMAEREAMKESRLILSIGGLLRSFRFHFRGTGYDEKLVRDMEGLEASGSTYICTLC 354
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189403502 240 DSTRAEASQNMVLHSITRSHEENLDRYEIWRTNPFSESAEELRERVKGVSAKPFMETHPTLDALHCDIGNATEFYKIFQD 319
Cdd:pfam12940 355 DSSRAEASKNKVLHAITRSHEENLERYEIWRTNPFSESADDLRDRVKGISAKPFLETQACIDALHCDIGNATEFYKIFQD 434
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189403502 320 EIGEVYEKVNPSREERRSWRAALDKQLRNKMKLKPVMRMNGNYARRLMTMEAAE*VCELVPSEERREALRELMRLYLQMK 399
Cdd:pfam12940 435 EIGEVHKKANPSKEERKRWQAALDKQLRKKMKLKPVMRMNGNFARKLMTQEAVDAVCELVPSEERQEALRELMHLYLQMK 514
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189403502 400 PVWRATCPAKECPDQLCRYSFNSQRFADLLSSAFKYRYNGKITNYLHKTLAHVPEIIERDGSIGAWASEGNESANKLFRR 479
Cdd:pfam12940 515 PVWRATCPAKECPDLLCRYSFNSQRFADLLSTTFKYRYDGKITNYLHKTLAHVPEIIERDGSIGAWASEGNESANKLFRR 594
                         490
                  ....*....|.
gi 1189403502 480 FRKMNARQSKA 490
Cdd:pfam12940 595 FRKMNARQSKS 605
 
Name Accession Description Interval E-value
RAG1 pfam12940
Recombination-activation protein 1 (RAG1), recombinase; This family is one of the two ...
1-490 0e+00

Recombination-activation protein 1 (RAG1), recombinase; This family is one of the two different components of the RAG1-RAG2 V(D)J recombinase complex. The RAG complex, consisting of two RAG1 and two RAG2 proteins is a multi-protein complex that mediates DNA cleavage during V(D)J (variable-diversity-joining) recombination. RAG1 mediates DNA-binding to the conserved recombination signal sequences (RSS). Many of the proteins in this family are fragments. Solution of the structure of the complex of RAG1 and RAG2 shows that each protein dimerizes with itself and each pair then complexes together to from the RAG1-RAG2 V(D)J recombinase enzyme. The different structural elements in RAG1 for UniProtKB:P15919 are: an N-terminal nonamer-binding domain from residues 391-459; a dimerization and DNA-binding domain from 459-515; an extended pre-RNase H domain from 515-588; the catalytic RNase H domain from 588-719; a ZnC2 domain from 719-791; and ZnH2 domain from 791-962; and a three-helix C-terminal domain from 962-1008.


Pssm-ID: 315595  Cd Length: 653  Bit Score: 987.62  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189403502   1 QIFQPLHALRTAEKELLPGFHQFEWQPALKNVSTSCNVGIINGLAGLTSSVDDSPADTITRRFRYDVALVSALKDLEEDV 80
Cdd:pfam12940 115 QIFQPLHTLRAAEKALLPGFHHFEWQPALKNVSPSCDVGIIDGLSGWSPSVDDQPADTITRRFRYDVALVAALKDLEEDI 194
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189403502  81 MEGLKESGLEDSACTSGFSVMIKESCDGMGDVSEKHGGGPVVPEKAVRFSFTIMSVSVLADGEE-EEVTIFTEPKPNSEL 159
Cdd:pfam12940 195 LEGLKEQGLDDSACTEGFSVMIKECCDGMGDVSEKHGGGPAVPEKAVRFSFTIMSVSILADDEEgEEVAIFHELKPNSEL 274
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189403502 160 SCKPLCLTFVDESDHETLTSILWPIVEERNAMKESRLILPIGGLLRSFRFHFRGTGYDEKMVREMEGLEASGSTYICTLC 239
Cdd:pfam12940 275 CCKPLCLMFADESDHETLTAILAPIMAEREAMKESRLILSIGGLLRSFRFHFRGTGYDEKLVRDMEGLEASGSTYICTLC 354
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189403502 240 DSTRAEASQNMVLHSITRSHEENLDRYEIWRTNPFSESAEELRERVKGVSAKPFMETHPTLDALHCDIGNATEFYKIFQD 319
Cdd:pfam12940 355 DSSRAEASKNKVLHAITRSHEENLERYEIWRTNPFSESADDLRDRVKGISAKPFLETQACIDALHCDIGNATEFYKIFQD 434
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189403502 320 EIGEVYEKVNPSREERRSWRAALDKQLRNKMKLKPVMRMNGNYARRLMTMEAAE*VCELVPSEERREALRELMRLYLQMK 399
Cdd:pfam12940 435 EIGEVHKKANPSKEERKRWQAALDKQLRKKMKLKPVMRMNGNFARKLMTQEAVDAVCELVPSEERQEALRELMHLYLQMK 514
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189403502 400 PVWRATCPAKECPDQLCRYSFNSQRFADLLSSAFKYRYNGKITNYLHKTLAHVPEIIERDGSIGAWASEGNESANKLFRR 479
Cdd:pfam12940 515 PVWRATCPAKECPDLLCRYSFNSQRFADLLSTTFKYRYDGKITNYLHKTLAHVPEIIERDGSIGAWASEGNESANKLFRR 594
                         490
                  ....*....|.
gi 1189403502 480 FRKMNARQSKA 490
Cdd:pfam12940 595 FRKMNARQSKS 605
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH