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Conserved domains on  [gi|289472321|gb|ADC97403|]
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REC8, partial [Daphnia pulex]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
An_peroxidase_like super family cl14561
Animal heme peroxidases and related proteins; A diverse family of enzymes, which includes ...
 1-113 6.73e-65

Animal heme peroxidases and related proteins; A diverse family of enzymes, which includes prostaglandin G/H synthase, thyroid peroxidase, myeloperoxidase, linoleate diol synthase, lactoperoxidase, peroxinectin, peroxidasin, and others. Despite its name, this family is not restricted to metazoans: members are found in fungi, plants, and bacteria as well.


The actual alignment was detected with superfamily member cd09823:

Pssm-ID: 353811 [Multi-domain]  Cd Length: 378  Bit Score: 203.19  E-value: 6.73e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289472321   1 LPGYNSYRELCGLPRARDFNDLLDVIPPKIVEKFESVYDTVDDIDLFIAGVSERPAKGAMVGPIFQCIIADQFLRLKRGD 80
Cdd:cd09823  266 LPGYNDYREFCGLPRATTFDDLLGIMSPETIQKLRRLYKSVDDIDLYVGGLSEKPVPGGLVGPTFACIIGEQFRRLRRGD 345

                         90       100       110
                 ....*....|....*....|....*....|...
gi 289472321  81 RYFYDLGGQAGSFTQEQLDEIRKISYSRIVCDN 113
Cdd:cd09823  346 RFWYENGGQPSSFTPAQLNEIRKVSLARIICDN 378
Rad21_Rec8_N super family cl04781
N terminus of Rad21 / Rec8 like protein; This family represents a conserved N-terminal region ...
 130-156 1.06e-04

N terminus of Rad21 / Rec8 like protein; This family represents a conserved N-terminal region found in eukaryotic cohesins of the Rad21, Rec8 and Scc1 families. Members of this family mediate sister chromatid cohesion during mitosis and meiosis, as part of the cohesin complex. Cohesion is necessary for homologous recombination (including double-strand break repair) and correct chromatid segregation. These proteins may also be involved in chromosome condensation. Dissociation at the metaphase to anaphase transition causes loss of cohesion and chromatid segregation.


The actual alignment was detected with superfamily member pfam04825:

Pssm-ID: 461446  Cd Length: 104  Bit Score: 39.46  E-value: 1.06e-04
                          10        20
                  ....*....|....*....|....*....
gi 289472321  130 MFYDIDILNRRGGkFGIIWLAAN--KKLR 156
Cdd:pfam04825   1 MFYSHEILSKKGP-LATVWLAATlgKKLS 28
 
Name Accession Description Interval E-value
peroxinectin_like cd09823
peroxinectin_like animal heme peroxidases; Peroxinectin is an arthropod protein that plays a ...
 1-113 6.73e-65

peroxinectin_like animal heme peroxidases; Peroxinectin is an arthropod protein that plays a role in invertebrate immunity mechanisms. Specifically, peroxinectins are secreted as cell-adhesive and opsonic peroxidases. The immunity mechanism appears to involve an interaction between peroxinectin and a transmembrane receptor of the integrin family. Human myeloperoxidase, which is included in this wider family, has also been reported to interact with integrins.


Pssm-ID: 188655 [Multi-domain]  Cd Length: 378  Bit Score: 203.19  E-value: 6.73e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289472321   1 LPGYNSYRELCGLPRARDFNDLLDVIPPKIVEKFESVYDTVDDIDLFIAGVSERPAKGAMVGPIFQCIIADQFLRLKRGD 80
Cdd:cd09823  266 LPGYNDYREFCGLPRATTFDDLLGIMSPETIQKLRRLYKSVDDIDLYVGGLSEKPVPGGLVGPTFACIIGEQFRRLRRGD 345

                         90       100       110
                 ....*....|....*....|....*....|...
gi 289472321  81 RYFYDLGGQAGSFTQEQLDEIRKISYSRIVCDN 113
Cdd:cd09823  346 RFWYENGGQPSSFTPAQLNEIRKVSLARIICDN 378
An_peroxidase pfam03098
Animal haem peroxidase;
1-124 7.69e-65

Animal haem peroxidase;


Pssm-ID: 460804 [Multi-domain]  Cd Length: 531  Bit Score: 207.41  E-value: 7.69e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289472321    1 LPGYNSYRELCGLPRARDFNDLLDVIPPKIVEKFESVYDTVDDIDLFIAGVSERPAKGAMVGPIFQCIIADQFLRLKRGD 80
Cdd:pfam03098 408 LPGYNDYREFCGLPPAKSFEDLTDVIPNEVIAKLRELYGSVDDIDLWVGGLAEKPLPGGLVGPTFACIIGDQFRRLRDGD 487

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 289472321   81 RYFYDLGGQaGSFTQEQLDEIRKISYSRIVCDNSFV-QFIQPLFF 124
Cdd:pfam03098 488 RFWYENGNQ-GSFTPEQLEEIRKTSLARVICDNTDIiETIQPNVF 531
Rad21_Rec8_N pfam04825
N terminus of Rad21 / Rec8 like protein; This family represents a conserved N-terminal region ...
 130-156 1.06e-04

N terminus of Rad21 / Rec8 like protein; This family represents a conserved N-terminal region found in eukaryotic cohesins of the Rad21, Rec8 and Scc1 families. Members of this family mediate sister chromatid cohesion during mitosis and meiosis, as part of the cohesin complex. Cohesion is necessary for homologous recombination (including double-strand break repair) and correct chromatid segregation. These proteins may also be involved in chromosome condensation. Dissociation at the metaphase to anaphase transition causes loss of cohesion and chromatid segregation.


Pssm-ID: 461446  Cd Length: 104  Bit Score: 39.46  E-value: 1.06e-04
                          10        20
                  ....*....|....*....|....*....
gi 289472321  130 MFYDIDILNRRGGkFGIIWLAAN--KKLR 156
Cdd:pfam04825   1 MFYSHEILSKKGP-LATVWLAATlgKKLS 28
 
Name Accession Description Interval E-value
peroxinectin_like cd09823
peroxinectin_like animal heme peroxidases; Peroxinectin is an arthropod protein that plays a ...
 1-113 6.73e-65

peroxinectin_like animal heme peroxidases; Peroxinectin is an arthropod protein that plays a role in invertebrate immunity mechanisms. Specifically, peroxinectins are secreted as cell-adhesive and opsonic peroxidases. The immunity mechanism appears to involve an interaction between peroxinectin and a transmembrane receptor of the integrin family. Human myeloperoxidase, which is included in this wider family, has also been reported to interact with integrins.


Pssm-ID: 188655 [Multi-domain]  Cd Length: 378  Bit Score: 203.19  E-value: 6.73e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289472321   1 LPGYNSYRELCGLPRARDFNDLLDVIPPKIVEKFESVYDTVDDIDLFIAGVSERPAKGAMVGPIFQCIIADQFLRLKRGD 80
Cdd:cd09823  266 LPGYNDYREFCGLPRATTFDDLLGIMSPETIQKLRRLYKSVDDIDLYVGGLSEKPVPGGLVGPTFACIIGEQFRRLRRGD 345

                         90       100       110
                 ....*....|....*....|....*....|...
gi 289472321  81 RYFYDLGGQAGSFTQEQLDEIRKISYSRIVCDN 113
Cdd:cd09823  346 RFWYENGGQPSSFTPAQLNEIRKVSLARIICDN 378
An_peroxidase pfam03098
Animal haem peroxidase;
1-124 7.69e-65

Animal haem peroxidase;


Pssm-ID: 460804 [Multi-domain]  Cd Length: 531  Bit Score: 207.41  E-value: 7.69e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289472321    1 LPGYNSYRELCGLPRARDFNDLLDVIPPKIVEKFESVYDTVDDIDLFIAGVSERPAKGAMVGPIFQCIIADQFLRLKRGD 80
Cdd:pfam03098 408 LPGYNDYREFCGLPPAKSFEDLTDVIPNEVIAKLRELYGSVDDIDLWVGGLAEKPLPGGLVGPTFACIIGDQFRRLRDGD 487

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 289472321   81 RYFYDLGGQaGSFTQEQLDEIRKISYSRIVCDNSFV-QFIQPLFF 124
Cdd:pfam03098 488 RFWYENGNQ-GSFTPEQLEEIRKTSLARVICDNTDIiETIQPNVF 531
peroxidasin_like cd09826
Animal heme peroxidase domain of peroxidasin and related proteins; Peroxidasin is a secreted ...
 1-114 2.14e-41

Animal heme peroxidase domain of peroxidasin and related proteins; Peroxidasin is a secreted heme peroxidase which is involved in hydrogen peroxide metabolism and peroxidative reactions in the cardiovascular system. The domain co-occurs with extracellular matrix domains and may play a role in the formation of the extracellular matrix.


Pssm-ID: 188658  Cd Length: 440  Bit Score: 143.99  E-value: 2.14e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289472321   1 LPGYNSYRELCGLPRARDFNDLLDVIP-PKIVEKFESVYDTVDDIDLFIAGVSERPAKGAMVGPIFQCIIADQFLRLKRG 79
Cdd:cd09826  304 LPGYNDYRKFCNLSVAETFEDLKNEIKnDDVREKLKRLYGHPGNIDLFVGGILEDLLPGARVGPTLACLLAEQFRRLRDG 383

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 289472321  80 DRYFYDlggQAGSFTQEQLDEIRKISYSRIVCDNS 114
Cdd:cd09826  384 DRFWYE---NPGVFSPAQLTQIKKTSLARVLCDNG 415
peroxinectin_like_bacterial cd09822
Uncharacterized family of heme peroxidases, mostly bacterial; Animal heme peroxidases are ...
 1-126 7.19e-31

Uncharacterized family of heme peroxidases, mostly bacterial; Animal heme peroxidases are diverse family of enzymes which are not restricted to animals. Members are also found in metazoans, fungi, and plants, and also in bacteria - like most members of this family of uncharacterized proteins.


Pssm-ID: 188654 [Multi-domain]  Cd Length: 420  Bit Score: 115.49  E-value: 7.19e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289472321   1 LPGYNSYRELCGLPRARDFNDLLDviPPKIVEKFESVYDTVDDIDLFIAGVSERPAKGAMVGPIFQCIIADQFLRLKRGD 80
Cdd:cd09822  301 LPSYNQLREALGLPAVTSFSDITS--DPDLAARLASVYGDVDQIDLWVGGLAEDHVNGGLVGETFSTIIADQFTRLRDGD 378

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 289472321  81 RYFYDLGGqagsFTQEQLDEIRKISYSRIVCDNSFVQFIQPLFFKA 126
Cdd:cd09822  379 RFFYENDD----LLLDEIADIENTTLADVIRRNTDVDDIQDNVFLV 420
thyroid_peroxidase cd09825
Thyroid peroxidase (TPO); TPO is a member of the animal heme peroxidase family, which is ...
 1-114 1.58e-29

Thyroid peroxidase (TPO); TPO is a member of the animal heme peroxidase family, which is expressed in the thyroid and involved in the processing of iodine and iodine compounds. Specifically, TPO oxidizes iodide via hydrogen peroxide to form active iodine, which is then, for example, incorporated into the tyrosine residues of thyroglobulin to yield mono- and di-iodotyrosines.


Pssm-ID: 188657 [Multi-domain]  Cd Length: 565  Bit Score: 113.30  E-value: 1.58e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289472321   1 LPGYNSYRELCGLPRARDFNDLLDVIPPKIV-EKFESVYDTVDDIDLFIAGVSERPAKGAMVGPIFQCIIADQFLRLKRG 79
Cdd:cd09825  419 LPGYNDWREFCGLPRLATPADLATAIADQAVaDKILDLYKHPDNIDVWLGGLAEDFLPGARTGPLFACLIGKQMKALRDG 498

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 289472321  80 DRYFYDlggQAGSFTQEQLDEIRKISYSRIVCDNS 114
Cdd:cd09825  499 DRFWWE---NSNVFTDAQRRELRKHSLSRVICDNT 530
myeloperoxidase_like cd09824
Myeloperoxidases, eosinophil peroxidases, and lactoperoxidases; This well conserved family of ...
 1-114 1.00e-28

Myeloperoxidases, eosinophil peroxidases, and lactoperoxidases; This well conserved family of animal heme peroxidases contains members with somewhat diverse functions. Myeloperoxidases are lysosomal proteins found in azurophilic granules of neutrophils and the lysosomes of monocytes. They are involved in the formation of microbicidal agents upon activation of activated neutrophils (neutrophils undergoing respiratory bursts as a result of phagocytosis), by catalyzing the conversion of hydrogen peroxide to hypochlorous acid. As a heme protein, myeloperoxidase is responsible for the greenish tint of pus, which is rich in neutrophils. Eosinophil peroxidases are haloperoxidases as well, preferring bromide over chloride. Expressed by eosinophil granulocytes, they are involved in attacking multicellular parasites and play roles in various inflammatory diseases such as asthma. The haloperoxidase lactoperoxidase is secreted from mucosal glands and provides antibacterial activity by oxidizing a variety of substrates such as bromide or chloride in the presence of hydrogen peroxide.


Pssm-ID: 188656 [Multi-domain]  Cd Length: 411  Bit Score: 109.82  E-value: 1.00e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289472321   1 LPGYNSYRELCGLPRARDFNDLLDVIP-PKIVEKFESVYDTVDDIDLFIAGVSERPAKGAMVGPIFQCIIADQFLRLKRG 79
Cdd:cd09824  280 LPGYNAWRRFCGLSQPQNLAELAAVLNnTVLARKLLDLYGTPDNIDIWIGGVAEPLVPGGRVGPLLACLISRQFRRIRDG 359

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 289472321  80 DRYFYDlggQAGSFTQEQLDEIRKISYSRIVCDNS 114
Cdd:cd09824  360 DRFWWE---NPGVFTEEQRESLRSVSLSRIICDNT 391
An_peroxidase_like cd05396
Animal heme peroxidases and related proteins; A diverse family of enzymes, which includes ...
 1-113 7.77e-22

Animal heme peroxidases and related proteins; A diverse family of enzymes, which includes prostaglandin G/H synthase, thyroid peroxidase, myeloperoxidase, linoleate diol synthase, lactoperoxidase, peroxinectin, peroxidasin, and others. Despite its name, this family is not restricted to metazoans: members are found in fungi, plants, and bacteria as well.


Pssm-ID: 188647 [Multi-domain]  Cd Length: 370  Bit Score: 90.56  E-value: 7.77e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289472321   1 LPGYNSYRELCGLPRARDFNDLLDviPPKIVEKFESVYDTVDDIDLFIAGVSERPAKGAMVGPIFQCIIADQFLRLKRGD 80
Cdd:cd05396  262 LPSYNEVRRFIGLKPPTSFQDILT--DPELAKKLAELYGDPDDVDLWVGGLLEKKVPPARLGELLATIILEQFKRLVDGD 339

                         90       100       110
                 ....*....|....*....|....*....|...
gi 289472321  81 RYFYDLGGQAGSFTQEQLDEIRKIsySRIVCDN 113
Cdd:cd05396  340 RFYYVNYNPFGKSGKEELEKLISL--ADIICLN 370
dual_peroxidase_like cd09820
Dual oxidase and related animal heme peroxidases; Animal heme peroxidases of the dual-oxidase ...
 1-105 7.65e-19

Dual oxidase and related animal heme peroxidases; Animal heme peroxidases of the dual-oxidase like subfamily play vital roles in the innate mucosal immunity of gut epithelia. They provide reactive oxygen species which help control infection.


Pssm-ID: 188652 [Multi-domain]  Cd Length: 558  Bit Score: 82.73  E-value: 7.65e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289472321   1 LPGYNSYRELCGLPRARDFNDLLDV---IPPKIVEKFESVY-DTVDDIDLFIAGVSErpAKGAMVGPIFQCIIADQFLRL 76
Cdd:cd09820  398 LPDYNTAREAFGLPPRTTWSDINPDlfkKDPELLERLAELYgNDLSKLDLYVGGMLE--SKGGGPGELFRAIILDQFQRL 475

                         90       100
                 ....*....|....*....|....*....
gi 289472321  77 KRGDRYFYDlGGQAGSFTQEQLDEIRKIS 105
Cdd:cd09820  476 RDGDRFWFE-NVKNGLFTAEEIEEIRNTT 503
prostaglandin_endoperoxide_synthase cd09816
Animal prostaglandin endoperoxide synthase and related bacterial proteins; Animal ...
 1-63 1.46e-09

Animal prostaglandin endoperoxide synthase and related bacterial proteins; Animal prostaglandin endoperoxide synthases, including prostaglandin H2 synthase and a set of similar bacterial proteins which may function as cyclooxygenases. Prostaglandin H2 synthase catalyzes the synthesis of prostaglandin H2 from arachidonic acid. In two reaction steps, arachidonic acid is converted to Prostaglandin G2, a peroxide (cyclooxygenase activity) and subsequently converted to the end product via the enzyme's peroxidase activity. Prostaglandin H2 synthase is the target of aspirin and other non-steroid anti-inflammatory drugs such as ibuprofen, which block the substrate's access to the active site and may acetylate a conserved serine residue. In humans and other mammals, prostaglandin H2 synthase (PGHS), also called cyclooxygenase (COX) is present as at least two isozymes, PGHS-1 (or COX-1) and PGHS-2 (or COX-2), respectively. PGHS-1 is expressed constitutively in most mammalian cells, while the expression of PGHS-2 is induced via inflammation response in endothelial cells, activated macrophages, and others. COX-3 is a splice variant of COX-1.


Pssm-ID: 188648 [Multi-domain]  Cd Length: 490  Bit Score: 55.73  E-value: 1.46e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 289472321   1 LPGYNSYRELCGLPRARDFNDLL-DvipPKIVEKFESVYDTVDDIDLFIAGVSERPAKGAMVGP 63
Cdd:cd09816  373 LASFNDYRKRFGLPPYTSFEELTgD---PEVAAELEELYGDVDAVEFYVGLFAEDPRPNSPLPP 433
An_peroxidase_bacterial_2 cd09821
Uncharacterized bacterial family of heme peroxidases; Animal heme peroxidases are diverse ...
 41-100 5.16e-08

Uncharacterized bacterial family of heme peroxidases; Animal heme peroxidases are diverse family of enzymes which are not restricted to metazoans; members are also found in fungi, and plants, and in bacteria - like this family of uncharacterized proteins.


Pssm-ID: 188653 [Multi-domain]  Cd Length: 570  Bit Score: 51.26  E-value: 5.16e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 289472321  41 VDDIDLFIAGVSERPAK-GAMVGPIFQCIIADQFLRLKRGDRyFYDLGGQAGSFTQEQLDE 100
Cdd:cd09821  483 LDNVDLWVGGLAEKQVPfGGMLGSTFNFVFEEQMDRLQDGDR-FYYLSRTAGLDLLNQLEN 542
linoleate_diol_synthase_like cd09817
Linoleate (8R)-dioxygenase and related enzymes; These fungal enzymes, related to animal heme ...
 4-85 7.35e-05

Linoleate (8R)-dioxygenase and related enzymes; These fungal enzymes, related to animal heme peroxidases, catalyze the oxygenation of linoleate and similar targets. Linoleate (8R)-dioxygenase, also called linoleate:oxygen 7S,8S-oxidoreductase, generates (9Z,12Z)-(7S,8S)-dihydroxyoctadeca-9,12-dienoate as a product. Other members are 5,8-linoleate dioxygenase (LDS, ppoA) and linoleate 10R-dioxygenase (ppoC), involved in the biosynthesis of oxylipins.


Pssm-ID: 188649 [Multi-domain]  Cd Length: 550  Bit Score: 42.32  E-value: 7.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289472321   4 YNSYRELCGLPRARDFNDLLDviPPKIVEKFESVYDTVDDIDLFIAGVSERpAKGAMVGPIFQCI-------IADQFLRL 76
Cdd:cd09817  391 LNEFRKFFGLKPYETFEDINS--DPEVAEALELLYGHPDNVELYPGLVAED-AKPPMPPGSGLCPgytisraILSDAVAL 467


                 ....*....
gi 289472321  77 KRGDRyFYD 85
Cdd:cd09817  468 VRGDR-FYT 475
Rad21_Rec8_N pfam04825
N terminus of Rad21 / Rec8 like protein; This family represents a conserved N-terminal region ...
 130-156 1.06e-04

N terminus of Rad21 / Rec8 like protein; This family represents a conserved N-terminal region found in eukaryotic cohesins of the Rad21, Rec8 and Scc1 families. Members of this family mediate sister chromatid cohesion during mitosis and meiosis, as part of the cohesin complex. Cohesion is necessary for homologous recombination (including double-strand break repair) and correct chromatid segregation. These proteins may also be involved in chromosome condensation. Dissociation at the metaphase to anaphase transition causes loss of cohesion and chromatid segregation.


Pssm-ID: 461446  Cd Length: 104  Bit Score: 39.46  E-value: 1.06e-04
                          10        20
                  ....*....|....*....|....*....
gi 289472321  130 MFYDIDILNRRGGkFGIIWLAAN--KKLR 156
Cdd:pfam04825   1 MFYSHEILSKKGP-LATVWLAATlgKKLS 28
 
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.
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