104 kDa microneme/rhoptry antigen; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221331079 432 EALTDSDASPSKysacgGTGSSGNPPVAL--TSGSGGDGAGPAFSLSPKtlnqfSHKLPQEVNElggydsdaTDMSSTSS 509
Cdd:PTZ00449 501 EEDSDKHDEPPE-----GPEASGLPPKAPgdKEGEEGEHEDSKESDEPK-----EGGKPGETKE--------GEVGKKPG 562

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221331079 510 VGHSGGSSSPSTAASQRSG-KGSKSQRRATALRKKRRHETRETTLASKSA---EALEAPlrKSPKRDSAPSVARadTPEA 585
Cdd:PTZ00449 563 PAKEHKPSKIPTLSKKPEFpKDPKHPKDPEEPKKPKRPRSAQRPTRPKSPklpELLDIP--KSPKRPESPKSPK--RPPP 638

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 221331079 586 EQRPSTSK--QSSHSPQKNVDSKSPTEQSYSSFYQELLEaSYANEGANESE 634
Cdd:PTZ00449 639 PQRPSSPErpEGPKIIKSPKPPKSPKPPFDPKFKEKFYD-DYLDAAAKSKE 688

OTU-like cysteine protease; This family is comprised of a group of predicted cysteine proteases, homologous to the Ovarian Tumour (OTU) gene in Drosophila. Members include proteins from eukaryotes, viruses and pathogenic bacterium. The conserved cysteine and histidine, and possibly the aspartate, represent the catalytic residues in this putative group of proteases.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221331079  224 DGACLFRSISLQIY-----GDEEMHDVIRQHTMDYIHENREYFGQFVTEDINSYIQRKRARDAHGNHIEIQAISEIYSRT 298
Cdd:pfam02338   3 DGNCLYRSISHQLWgvhdvLRKMLVQELRETLAEYMREHKEEFEPFLEDDETGDIIEIEQTGAWGGEIEIFALAHILRRP 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 221331079  299 VEVYcYQSNPINIFNSEQSQAGYP-----PLRLSYQR-----GSHY 334
Cdd:pfam02338  83 IIVY-KSEGGEELGGLKEYGIYLPlgwdpSLCLVYPRhlyylGGHY 127

OTU (ovarian tumor) domain of deubiquitinating enzyme OTU6 from plants and similar proteins; Deubiquitinating enzyme OTU6, also called OTU domain-containing protein 6 or otubain-like deubiquitinase 1 (OTLD1), is a deubiquitinase (DUB) or ubiquitin thiolesterase (EC 3.4.19.12) that catalyzes the thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin, a small regulatory protein that can be conjugated to a large range of target proteins. Protein ubiquitination is a post-translational modification of mostly Lys residues that regulates many cellular processes, including protein degradation, intracellular trafficking, cell signaling, autophagy, transcription, translation, and the DNA damage response. OTU6 binds chromatin and has enzymatic histone deubiquitinase activity specific for the H2B histone. OTU6 belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221331079 214 RGYELKPVEEDGACLFRSISLQIYGDEEMHDVIRQHTMDYIHENREYFGQFVTEDINSYIQRKRARDAHGNHIEIQAISE 293
Cdd:cd22796    3 KGLEIRRMDGDGNCLFRAVADQVYGDQEMHDEVREMCMDYMEKERDHFSQFVTEDFTQYVKRKRRDRVFGNNLEIQAMSE 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 221331079 294 IYSRTVEVYCYQSN-PINIFNsEQSQAGYPPLRLSYQRGSHYNAILD 339
Cdd:cd22796   83 IYNRPIEVYSYSNGePINIFH-GSYEGDDPPIRLSYHDGNHYNSIID 128

OTU (ovarian tumor) domain family; The OTU family of cysteine proteases use a conserved cysteine and histidine, and in most cases an aspartate, as the catalytic triad. OTU domains typically function as deubiquitinases (DUBs)/ubiquitin thiolesterases (EC 3.4.19.12) that catalyze the thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin, a small regulatory protein that can be conjugated to a large range of target proteins. Protein ubiquitination is a post-translational modification of mostly Lys residues that regulates many cellular processes, including protein degradation, intracellular trafficking, cell signaling, autophagy, transcription, translation, and the DNA damage response. These DUBs may play important regulatory roles at the level of protein turnover by preventing degradation.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221331079 217 ELKPVEEDGACLFRSISLQIYGDEEMHDVIRQHTMDYIHENREYF------GQFVTEDINSYIQRKRARDAHGNHIEIQA 290
Cdd:cd22744    1 RVVDVPGDGNCLFRALAHALYGDQESHRELRQEVVDYLRENPDLYepaelaDEDDGEDFDEYLQRMRKPGTWGGELELQA 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 221331079 291 ISEIYSRTVEVY--CYQSNPINIFNSEQsQAGYPPLRLSYQRGSHYNAI 337
Cdd:cd22744   81 LANALNVPIVVYseDGGFLPVSVFGPGP-GPSGRPIHLLYTGGNHYDAL 128

OTU (ovarian tumor) domain of Invertebrate iridescent virus putative ubiquitin thioesterase 232R and similar proteins; This subfamily contains putative ubiquitin thioesterases 232R from Invertebrate iridescent virus and L96 from Tipula iridescent virus (TIV), Dictyostelium discoideum OTU domain-containing protein DDB_G0284757, and similar proteins. L96 may be involved in TIV genomic DNA packaging in a manner related to the Gag polyproteins of the mammalian viruses. Proteins in this subfamily contain an OTU domain. OTU domains typically function as deubiquitinases (DUBs)/ubiquitin thiolesterases (EC 3.4.19.12) that catalyze the thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin, a small regulatory protein that can be conjugated to a large range of target proteins. Protein ubiquitination is a post-translational modification of mostly Lys residues that regulates many cellular processes, including protein degradation, intracellular trafficking, cell signaling, autophagy, transcription, translation, and the DNA damage response. These DUBs may play important regulatory roles at the level of protein turnover by preventing degradation. They belong to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221331079 212 EQRGYELKPVEEDGACLFRSISLQIYGD--EEMHDVIRQHTMDYIHENREYFG------QFVTEDINSYIQRKRARDAHG 283
Cdd:cd22758    2 KENGFEIRDVPGDGNCFFHAVSDQLYGNgiEHSHKELRQQAVNYLRENPELYDgfflseFDEEESWEEYLNRMSKDGTWG 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 221331079 284 NHIEIQAISEIYSRTVEVY-CYQSNPINIFNSEQSQAGyPPLRLSYQRGSHY 334
Cdd:cd22758   82 DHIILQAAANLFNVRIVIIsSDGSDETTIIEPGNSKNG-RTIYLGHIGENHY 132

OTU (ovarian tumor) domain of OTU domain-containing proteins 6A, 6B, and similar proteins; This subfamily is composed of mammalian OTU domain-containing protein 6A (OTUD6A, also called DUBA-2, vertebrate OTU domain-containing protein 6B (OTUD6B, also called DUBA-5), fungal OTU domain-containing protein 2 (OTU2), and similar proteins. OTUD6A, OTUD6B, and Schizosaccharomyces pombe OTU2 are deubiquitinating enzymes/ubiquitinyl hydrolases (EC 3.4.19.12). OTUD6A hydrolyzes 'Lys-27'-, 'Lys-29'-, and 'Lys-33'-linked polyubiquitin chains, and may also be able to hydrolyze 'Lys-11'-linked ubiquitin chains. It deubiquitylates and stabilizes dynamin-related protein 1 (Drp1), a cytosolic protein responsible for mitochondrial fission and is essential in the initiation and development of several human diseases including cancer, thereby facilitating tumorigenesis. OTUD6B is a functional deubiquitinase in in vitro enzyme assays. It may play a role in the ubiquitin-dependent regulation of protein synthesis downstream of mTORC1, and may modify the ubiquitination of the protein synthesis initiation complex to repress translation. Biallelic variants in OTUD6B cause an intellectual disability syndrome that is associated with seizures and dysmorphic features. This subfamily belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221331079 214 RGYELKPVEEDGACLFRSISLQI---YGDEEMHDV--IRQHTMDYIHENREYFGQFVT---------EDINSYIQRKRAR 279
Cdd:cd22748    4 LGLRIKEIPPDGHCLYRAIADQLklrGGSEEPYSYkeLRKLAADYMRAHRDDFLPFLTnddgdlmteEEFEEYCDKIENT 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 221331079 280 DAHGNHIEIQAISEIYSRTVEVYCYQSNPINIfnSEQSQAGyPPLRLSYQR-----GSHYNAI 337
Cdd:cd22748   84 AEWGGQLELRALSKALKRPIHVYQAGSPPLVI--GEEFDSG-EPLRLSYHRhayglGEHYNSV 143

OTU (ovarian tumor) domain of bifunctional UDP-N-acetylglucosamine transferase and deubiquitinase ALG13 and similar proteins; Bifunctional UDP-N-acetylglucosamine transferase and deubiquitinase ALG13 is alco called asparagine-linked glycosylation 13 homolog, glycosyltransferase 28 domain-containing protein 1 (GLT28D1), or UDP-N-acetylglucosamine transferase subunit ALG13 homolog. It displays both glycosyltransferase (EC 2.4.1.141) and deubiquitinase (DUB)/ubiquitin thioesterase (EC 3.4.19.12) activities. With ALG14, it forms a UDP-N-acetylglucosamine transferase that catalyzes the second step of eukaryotic N-linked glycosylation in the endoplasmic reticulum. ALG13 variants cause a form of early infantile epileptic encephalopathy known as EIEE36 refractory seizures, neurodevelopmental impairment, and poor prognosis; given the essential role of ALG13 in glycosylation, it is also considered a congenital disorder of glycosylation (CDG). This subfamily also contains OTU domain-containing protein 4 (OTUD4), also called HIV-1-induced protein HIN-1, a DUB that specifically deubiquitinates 'Lys-63'-polyubiquitinated MYD88 adapter protein upon phosphorylation, triggering down-regulation of NF-kappa-B-dependent transcription of inflammatory mediators. This subfamily belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221331079 211 MEQRGYELKPVEEDGACLFRSISLQIYGDEEMHDVIRQHTMDYIHENREYFGQFVTEDINSYIQRKRARDAHGNHIEIQA 290
Cdd:cd22753    5 LDSLGLYRKHIPRDGSCLFRAVSEQLFFTQSYHQQVRQACVEYLEKNREEFEKFSEISFDDYLERLSDPKEWGGLLELEA 84

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 221331079 291 ISEIYSRTVEVYC-YQSNPINIFNSeqsqaGYP-PLRLSYQRGSHYNAILD 339
Cdd:cd22753   85 LSLLYKVDFIVYSiPDQPPSNITNN-----GYPkKIMLCYSGGNHYDSVYS 130

OTU (ovarian tumor) domain of OTU domain-containing protein 4 and similar proteins; OTU domain-containing protein 4 (OTUD4), also called HIV-1-induced protein HIN-1, is a deubiquitinase that specifically deubiquitinates 'Lys-63'-polyubiquitinated MYD88 adapter protein upon phosphorylation, triggering down-regulation of NF-kappa-B-dependent transcription of inflammatory mediators. OTUD4 belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221331079 214 RGYELKPVEEDGACLFRSISLQIYGDEEMHDVIRQHTMDYIHENREYFGQFVTEDINSYIQRKRARDAHGNHIEIQAISE 293
Cdd:cd22794    8 LGLYRKQIAKDGSCLFRAVAEQVFHTQSRHLEVRKACVDYLRRNREKFEAFIEGPFEQYLKNLENPKEWAGQVEISALSL 87

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 221331079 294 IYSRTVEVYcyqsNPINIFNSEQSQAGYP-PLRLSYQRGSHYNAI 337
Cdd:cd22794   88 MYKRDFIIY----QEPGKPPSNVTENGFPdKILLCFSNGNHYDSV 128

OTU (ovarian tumor) domain of nucleopolyhedrovirus P87/VP80 protein and similar proteins; The VP80 protein is a capsid-associated structural protein that was first identified as P87 in Orgyia pseudotsugata multicapsid nuclear polyhedrosis virus (OpMNPV); its homologs are found only in NPV genomes. The Autographa californica multicapsid nucleopolyhedrovirus (AcMNPV) VP80 protein is essential for the formation of both budded virus (BV) and occlusion-derived virus (ODV). It has also been shown to interact with the virus-triggered, nuclear F-actin cytoskeleton. P87/VP80 contains an N-terminal OTU domain. OTU domains typically function as deubiquitinases (DUBs)/ubiquitin thiolesterases (EC 3.4.19.12) that catalyze the thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin, a small regulatory protein that can be conjugated to a large range of target proteins. Protein ubiquitination is a post-translational modification of mostly Lys residues that regulates many cellular processes, including protein degradation, intracellular trafficking, cell signaling, autophagy, transcription, translation, and the DNA damage response. These DUBs may play important regulatory roles at the level of protein turnover by preventing degradation. They belong to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221331079 216 YELKPVEEDGACLFRSISLQIYGDEEMHDVIRQHTMDYIHENREYFGQFVTEDI-NSYIQRKRARDA------HGNHIEI 288
Cdd:cd22757    1 FRVIPIPGDGACLFRALSYLLYGTQSRHLEVRKEVVDYVVNNWDEFSIYTHDSEgNNYKSAEEYRADmskpgtYGTLCEL 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 221331079 289 QAISEIYSRTVEVYCyqsNPINIFNSEQSQAGYPPLRLSYQRGS-HYNAIL 338
Cdd:cd22757   81 VAAAELYPFHFEVYR---NGKLYASFGDPSNPVKRLKFSGDLSNgHFDVLE 128

OTU (ovarian tumor) domain of OTU domain-containing protein 3 and similar proteins; OTU domain-containing protein 3 (OTUD3) is a deubiquitinase (DUB)/ubiquitin thioesterase (EC 3.4.19.12) that hydrolyzes 'Lys-6'- and 'Lys-11'-linked polyubiquitin. It is an acetylation-dependent deubiquitinase that restricts innate antiviral immune signaling. It directly hydrolyzes lysine 63 (Lys63)-linked polyubiquitination of MAVS (mitochondrial antiviral-signaling protein) and shuts off innate antiviral immune response. OTUD3 can elicit tumor-suppressing or tumor-promoting activities in a cell- and tissue-dependent manner. It is a DUB for PTEN (phosphatase and tension homologue deleted on chromosome 10); the OTUD3-PTEN signaling axis plays a critical role in suppression of breast tumorigenesis. OTUD3 is also a DUB for glucose-regulated protein GRP78, stabilizing it and promoting lung tumorigenesis. It belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221331079 207 FAKCMEQRGYELKPVEEDGACLFRSISLQIYGDEEMHDVIRQHTMDYIHENREYFGQFVTEDI--NSYIQRKRARDAHGN 284
Cdd:cd22770    5 FANQLQALGLKLRDIPGDGNCLFRALGDQLEGHSRNHLKHRQETVQYMIEHREDFEPFVEDDVpfDKHVANLSKPGTYAG 84

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 221331079 285 HIEIQAISEIYSRTVEVYCYQSNPINIFNSEQSQAgyPPLRLSYQRGSHYNAI 337
Cdd:cd22770   85 NDAIVAFARLHQVNVVIHQLNAPLWQIRGTEKSSS--RELHISYHNGDHYSSV 135

OTU (ovarian tumor) domain of deubiquitinating enzymes OTU3 and OTU4 from plants, and similar proteins; Deubiquitinating enzyme OTU3 (also called OTU domain-containing protein 3) and deubiquitinating enzyme OTU4 (also called OTU domain-containing protein 4) are deubiquitinases (DUBs) or ubiquitin thiolesterases (EC 3.4.19.12) that catalyze the thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin, a small regulatory protein that can be conjugated to a large range of target proteins. Protein ubiquitination is a post-translational modification of mostly Lys residues that regulates many cellular processes, including protein degradation, intracellular trafficking, cell signaling, autophagy, transcription, translation, and the DNA damage response. OTU3 and OTU4 may play important regulatory roles at the level of protein turnover by preventing degradation. They belong to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221331079 220 PVEEDGACLFRSI--SLQIYG-----DEEM------------HDVIRQHtmdyiHENREYFGQFVTEDINSYIQRKRARD 280
Cdd:cd22746    6 PVKGDGRCLFRAVarGLALATggrplSERReradadalrkavVEEIRKR-----RDELFEGSLVIEGDFDAYCQRMSHPD 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 221331079 281 AHGNHIEIQAISEIYSRTVEVYCYQ---SNPINIFNSEQSQAGYPPLRLSYQRGSHYNAIL 338
Cdd:cd22746   81 TWGGEPELLMLADVLQRPIAVYLPTpgkGGLRKIQEYGEEYLGGEPIRLLYNGGNHYDLLL 141

OTU (ovarian tumor) domain of deubiquitinating enzyme OTU5 from plants and similar proteins; Deubiquitinating enzyme OTU5, also called OTU domain-containing protein 6, is a deubiquitinase (DUB) or ubiquitin thiolesterase (EC 3.4.19.12) that catalyzes the thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin, a small regulatory protein that can be conjugated to a large range of target proteins. Protein ubiquitination is a post-translational modification of mostly Lys residues that regulates many cellular processes, including protein degradation, intracellular trafficking, cell signaling, autophagy, transcription, translation, and the DNA damage response. OTU5 is an inactive cysteine protease. It regulates gene expression by contributing to chromatin organization and DNA methylation patterns (e.g. H3K4me3 and H3K27me3). It is required for phosphate (Pi) homeostasis. OTU5 belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221331079 214 RGYELKPVEEDGACLFRSISLQI---YGDEEMHDV--IRQHTMDYIHENREYFGQFV---------TEDINSYIQRKRAR 279
Cdd:cd22797    8 LGLAIKEIKADGHCLYRAVEDQLqlrGGGAPAPDYqqLRELAADYMRAHPDDFLPFLededeggdgDEAFEAYCREVEST 87

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 221331079 280 DAHGNHIEIQAISEIYSRTVEVYCYQSNPINIfnSEQSQAGYPPLRLSYQR-----GSHYNAI 337
Cdd:cd22797   88 AAWGGQLELGALAHALRRHIKVYSAGMPDVEM--GEEYAGTGPPLRLCYHRhafglGEHYNSV 148

OTU (ovarian tumor) domain of ubiquitin thioesterase OTU1 and similar proteins; Ubiquitin thioesterase (EC 3.4.19.12) OTU1 is also called OTU domain-containing protein 1 in yeast, while human OTU1 is also called HIV-1-induced protease 7 (HIN7), DUBA-8, or OTU domain-containing protein 2 (OTUD2). OTU1 is a deubiquitinase (DUB) that catalyzes the thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin, a small regulatory protein that can be conjugated to a large range of target proteins. Protein ubiquitination is a post-translational modification of mostly Lys residues that regulates many cellular processes, including protein degradation, intracellular trafficking, cell signaling, autophagy, transcription, translation, and the DNA damage response. OTU1 has been implicated in the ER-associated degradation (ERAD) pathway. In yeast, it counteracts the activity of Ufd2 by deubiquitinating Ufd2 substrates; Ufd2 is a E4 ubiquitin ligase that interacts with Cdc48, an AAA ATPase that plays a central role in the ERAD pathway by chaperoning proteins to the proteasome for destruction. OTU1 also functions as a substrate-processing factor of valosin-containing protein (VCP, the mammalian counterpart of yeast Cdc48) that is required for the retrotranslocation of the ERAD pathway. OTU1 has been shown to preferentially hydrolyze polyubiquitin chains with Lys48 linkages. It contains ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, a C2H2-type zinc finger, and an OTU (ovarian tumor) domain. This model represents the OTU domain that interacts with ubiquitin and possesses catalytic activity. OTU1 belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad. This family also contains plant OTU1 and OTU2.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221331079 218 LKPVEEDGACLFRSISLQIYGDEEMH-DVIRQHTMDYIHENREYFgqfvTEDI----NS-YIQRKRARDAHGNHIEIQAI 291
Cdd:cd22745    5 RRVVPDDNSCLFTSISYLLEGGLLDSaPELREIVADAILSDPDTY----NEAIlgkpPDeYCAWILKPDSWGGAIELSIL 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 221331079 292 SEIYSrtVEVYCY--QSNPINIFNSEQsqagYPPLR--LSYQrGSHYNAI 337
Cdd:cd22745   81 SKHFG--VEICVVdvQTGRVDRFGEDK----GYSKRifLLYS-GIHYDAL 123

OTU (ovarian tumor) domain of vertnin and similar proteins; Vertnin (VRTN) is an OTU domain-containing protein that is required for the development of thoracic vertebrae in mammals. OTU domains typically function as deubiquitinases (DUBs)/ubiquitin thiolesterases (EC 3.4.19.12) that catalyze the thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin, a small regulatory protein that can be conjugated to a large range of target proteins. Protein ubiquitination is a post-translational modification of mostly Lys residues that regulates many cellular processes, including protein degradation, intracellular trafficking, cell signaling, autophagy, transcription, translation, and the DNA damage response. These DUBs may play important regulatory roles at the level of protein turnover by preventing degradation. Vertnin and some subfamily members do not possess the conserved catalytic residues and may not have DUB activity. VRTN gene is associated with variations in vertebral number.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221331079 224 DGACLFRSISLQIYGDEEMHDVIRQHTMDYIHENREYFgqfvtedinSYIQRKRARDAHGNH-----IEIQAISEIYSRT 298
Cdd:cd22791    9 DGNCLFRAASLLLFGDESLHLELRLRTVLELVLNSEFY---------EAIYEAEIKATCKPGsysgiWHIYALSSVLQRP 79

                 ....*
gi 221331079 299 VEVYC 303
Cdd:cd22791   80 IFSVY 84