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Conserved domains on  [gi|2009535425|ref|XP_040116140|]
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probable C-mannosyltransferase DPY19L1 [Oryx dammah]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Dpy19L1 cd20178
C-mannosyltransferase Dpy-19-like protein 1 (Dpy19L1); Dpy19 proteins are ...
92-743 0e+00

C-mannosyltransferase Dpy-19-like protein 1 (Dpy19L1); Dpy19 proteins are C-mannosyltransferases that mediate C-mannosylation of tryptophan residues on target proteins. C-mannosylation is the attachment of alpha-mannose to the indole C2 carbon of the first tryptophan residue in the consensus amino acid sequence Trp-Xaa-Xaa-Trp/Cys through a C-C bond. This reaction takes place in the endoplasmic reticulum (ER) lumen. Dpy19 is a transmembrane domain family whose name is derived from the Caenorhabditis elegans Dumpy mutant. Dpy19L1 (also called protein Dpy-19 homolog 1) regulates neurite extension during development.


:

Pssm-ID: 439131  Cd Length: 652  Bit Score: 1258.22  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009535425  92 RTWTTLLLAAFAAVLHWSHITHLFENDRHFSHLSTLEREMAFRTEMGLYYSYFKTIVEAPSFLNGVWMIMNDKLTEYPLV 171
Cdd:cd20178     1 KIWVTLLLAALAGVLHWSHITHLFENDRHFSHLSTLEREMAFRTEMGLYYSYFKTIIEAPSFLNGVWMIMNDRLTEYPLV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009535425 172 INTLKRFNLYPEVILASWYRIYTKIMDLIGIQTKICWTVTRGEGLSPIESCEGLGDPACFYVAVIFILNGLMMALFFIYG 251
Cdd:cd20178    81 INTLKRFNLYPEVVLASWYRIYTGIMDFFGIQTKTCWTVNRGEGLSPVESCEGLGDPAYFYVAVIFLLNGLMMSLFFIYG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009535425 252 TYLSGSRLGGLVTVLCFFFNHGECTRVMWTPPLRESFSYPFLVLQMLLVTHILRATKLYRGSLIALCISNVFFMLPWQFA 331
Cdd:cd20178   161 TYLSGSRLGGVVTVLCFFFNHGECTRVMWTPPLRESFSYPFLVLQMLLVTYILRAPNLGRGSLIALCISNVLFMLPWQFA 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009535425 332 QFVLLTQIASLFALYVVGYIDISKLRKIIYMHMISLALCFVLMFGNSMLLTSYYASSLVIIWGLLAMKPYFLKINVSELS 411
Cdd:cd20178   241 QFVLLTQIASLFAVYVVGYIDSCKLQKILYAHMISLVVCFVLMFGNSMLLTSYYASSLVIIWGILALRPKFLKVNKSEVS 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009535425 412 LWVIQGCFWLFGTVILKYLTSKIFGIADDAHIGNLLTSKFFSYKDFDTLLYTCAAEFDFMEKETPLRYTKTLLLPVVLVV 491
Cdd:cd20178   321 LWVIQGCAWLFGTVILKYLTSKVFGIADDAHIGNLLKSKFTSYKDFDTLMYTCAAEFDFMEKETPLRYTKTLLLPVVLVV 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009535425 492 FIVIIRKVVSDMWVVLTKQQTHIRKHQFDHGELVYHALQLLAYTVLGVLIMRLKLFLTPHMCVMASLICSRQLFGWLFCK 571
Cdd:cd20178   401 FAAIARKTIKDLWGVLAKKATHTRKEQFAHGELVYHALQLLAYAVLAILIMRLKLFLTPHMCVMASLVCSRQLFGWLFCK 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009535425 572 VHPGAVVFAVLAAMSIQGSANLQTQWNIVGEFSNLPQEELIEWIKYSTKPDAVFAGAMPTMASVKLSALRPIVNHPHYED 651
Cdd:cd20178   481 VHPQAVVFAILAAMAIQGSANLQTQWNIIGEFSNLPQEELLEWIKYNTKPDAVFAGAMPTMASVKLSALRPIVNHPHYED 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009535425 652 AGLRARTKIVYSMYSRKAAEEVKRELIKLQVNYYILEESWCIRRSKPGCSMPEIWDVEDPANAGKPPLCNLLVKESKPHF 731
Cdd:cd20178   561 AGLRARTKIVYSMYSRKPAEEVKRELMKLGVNYYILEESWCVRRSKPGCSMPEIWDVEDPDNAGKTPLCTLMSKDSRPHF 640
                         650
                  ....*....|..
gi 2009535425 732 TTVFQNSVYKVL 743
Cdd:cd20178   641 TTVFENSVYKVL 652
Brme1 super family cl25823
Break repair meiotic recombinase recruitment factor 1; Brme1 (also known as Meiok21) is a ...
9-52 2.04e-04

Break repair meiotic recombinase recruitment factor 1; Brme1 (also known as Meiok21) is a component of meiotic recombination bridges involved in meiotic double-strand break repair. The C-terminal domain of Brme1 physically interacts with the N-terminal domain of HSF2BP. BRME1 facilitates the loading of RAD51 and DMC1 recombinases onto DSBs (DNA double-strand breaks) through interaction with MEILB2/HSF2BP and replacing ssDNA binding proteins. Brme1 is highly expressed in mice testes and fetal ovaries. Knockout of Brme1 results in male mice infertility.


The actual alignment was detected with superfamily member pfam15710:

Pssm-ID: 464816 [Multi-domain]  Cd Length: 667  Bit Score: 44.92  E-value: 2.04e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2009535425   9 HREAAPKPPQPPRASQsplrGSPDVGAGEPGPERAPPSPRRKGA 52
Cdd:pfam15710 484 HREAAGGPPQEAGAQQ----GSPDAPTDLAGQPQHPPDSSDQAT 523
 
Name Accession Description Interval E-value
Dpy19L1 cd20178
C-mannosyltransferase Dpy-19-like protein 1 (Dpy19L1); Dpy19 proteins are ...
92-743 0e+00

C-mannosyltransferase Dpy-19-like protein 1 (Dpy19L1); Dpy19 proteins are C-mannosyltransferases that mediate C-mannosylation of tryptophan residues on target proteins. C-mannosylation is the attachment of alpha-mannose to the indole C2 carbon of the first tryptophan residue in the consensus amino acid sequence Trp-Xaa-Xaa-Trp/Cys through a C-C bond. This reaction takes place in the endoplasmic reticulum (ER) lumen. Dpy19 is a transmembrane domain family whose name is derived from the Caenorhabditis elegans Dumpy mutant. Dpy19L1 (also called protein Dpy-19 homolog 1) regulates neurite extension during development.


Pssm-ID: 439131  Cd Length: 652  Bit Score: 1258.22  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009535425  92 RTWTTLLLAAFAAVLHWSHITHLFENDRHFSHLSTLEREMAFRTEMGLYYSYFKTIVEAPSFLNGVWMIMNDKLTEYPLV 171
Cdd:cd20178     1 KIWVTLLLAALAGVLHWSHITHLFENDRHFSHLSTLEREMAFRTEMGLYYSYFKTIIEAPSFLNGVWMIMNDRLTEYPLV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009535425 172 INTLKRFNLYPEVILASWYRIYTKIMDLIGIQTKICWTVTRGEGLSPIESCEGLGDPACFYVAVIFILNGLMMALFFIYG 251
Cdd:cd20178    81 INTLKRFNLYPEVVLASWYRIYTGIMDFFGIQTKTCWTVNRGEGLSPVESCEGLGDPAYFYVAVIFLLNGLMMSLFFIYG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009535425 252 TYLSGSRLGGLVTVLCFFFNHGECTRVMWTPPLRESFSYPFLVLQMLLVTHILRATKLYRGSLIALCISNVFFMLPWQFA 331
Cdd:cd20178   161 TYLSGSRLGGVVTVLCFFFNHGECTRVMWTPPLRESFSYPFLVLQMLLVTYILRAPNLGRGSLIALCISNVLFMLPWQFA 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009535425 332 QFVLLTQIASLFALYVVGYIDISKLRKIIYMHMISLALCFVLMFGNSMLLTSYYASSLVIIWGLLAMKPYFLKINVSELS 411
Cdd:cd20178   241 QFVLLTQIASLFAVYVVGYIDSCKLQKILYAHMISLVVCFVLMFGNSMLLTSYYASSLVIIWGILALRPKFLKVNKSEVS 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009535425 412 LWVIQGCFWLFGTVILKYLTSKIFGIADDAHIGNLLTSKFFSYKDFDTLLYTCAAEFDFMEKETPLRYTKTLLLPVVLVV 491
Cdd:cd20178   321 LWVIQGCAWLFGTVILKYLTSKVFGIADDAHIGNLLKSKFTSYKDFDTLMYTCAAEFDFMEKETPLRYTKTLLLPVVLVV 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009535425 492 FIVIIRKVVSDMWVVLTKQQTHIRKHQFDHGELVYHALQLLAYTVLGVLIMRLKLFLTPHMCVMASLICSRQLFGWLFCK 571
Cdd:cd20178   401 FAAIARKTIKDLWGVLAKKATHTRKEQFAHGELVYHALQLLAYAVLAILIMRLKLFLTPHMCVMASLVCSRQLFGWLFCK 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009535425 572 VHPGAVVFAVLAAMSIQGSANLQTQWNIVGEFSNLPQEELIEWIKYSTKPDAVFAGAMPTMASVKLSALRPIVNHPHYED 651
Cdd:cd20178   481 VHPQAVVFAILAAMAIQGSANLQTQWNIIGEFSNLPQEELLEWIKYNTKPDAVFAGAMPTMASVKLSALRPIVNHPHYED 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009535425 652 AGLRARTKIVYSMYSRKAAEEVKRELIKLQVNYYILEESWCIRRSKPGCSMPEIWDVEDPANAGKPPLCNLLVKESKPHF 731
Cdd:cd20178   561 AGLRARTKIVYSMYSRKPAEEVKRELMKLGVNYYILEESWCVRRSKPGCSMPEIWDVEDPDNAGKTPLCTLMSKDSRPHF 640
                         650
                  ....*....|..
gi 2009535425 732 TTVFQNSVYKVL 743
Cdd:cd20178   641 TTVFENSVYKVL 652
Dpy19 pfam10034
Q-cell neuroblast polarization; Dyp-19, formerly known as DUF2211, is a transmembrane domain ...
107-745 0e+00

Q-cell neuroblast polarization; Dyp-19, formerly known as DUF2211, is a transmembrane domain family that is required to orient the neuroblast cells, QR and QL accurately on the anterior-posterior axis: QL and QR are born in the same anterior-posterior position, but polarise and migrate left-right asymmetrically, QL migrating towards the posterior and QR migrating towards the anterior. It is also required, with unc-40, to express mab-5 correctly in the Q cell descendants. The Dpy-19 protein derives from the C. elegans DUMPY mutant, Swiss:P34413.


Pssm-ID: 462945  Cd Length: 646  Bit Score: 910.06  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009535425 107 HWSHITHLFENDRHFSHLSTLEREMAFRTEMGLYYSYFKTIVEAPSFLNGVWMIMNDKLTEYPLVINTLKRFNLYPEVIL 186
Cdd:pfam10034   7 YALHVSTLFENDRWFSHLSELEREISFRTEMGLYYSYYKTIIEAPSFLEGLYQLMNDNRTEYPDTINALQRFNLYPEVIL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009535425 187 ASWYRIYTKIMDLIGiqtkicwtvtrgeglspiesceglgDPACFYVAVIFILNGLMMALFFIYGTYLSGSRLGGLVTVL 266
Cdd:pfam10034  87 AILYRIFRGIQNYLG-------------------------EPVYFYIYFVFGLQGVYVSALFLYGWYLSGSWLGGILAVL 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009535425 267 CFFFNHGECTRVMWTPPLRESFSYPFLVLQMLLVTHILRATKLY----RGSLIALCISNVFFMLPWQFAQFVLLTQIASL 342
Cdd:pfam10034 142 WFFFNHGETTRVEWTPPLRENFALPFFALQMLALTYILKRKNISsaseLFCYILLSASTFLFLLTWQFSQFVLLTQILSL 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009535425 343 FALYVVGYIDISKLRKIIYMHMISLALCFVLMFGNSMLLTSYYASSLVIIWGLLAMKPYFLKI-NVSELSLWVIQGCFWL 421
Cdd:pfam10034 222 FLLDSLGLVPSKKVAKIYLSHLISLLLAFVLQFGNSMLLTSPLLSSLISILLIRYLQPNMKKGrFSFRLLKLLLHGLLVL 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009535425 422 FGTVILKYLTSKIFGIADDAHIGNLLTSKFF--SYKDFDTLLYTCAAEFDFMEKETPLRYTKTLLLPVVLVVFIVIIRKV 499
Cdd:pfam10034 302 FGTLTLKLLIKKLLNVEDDAHIFDFLKAKFGlnSTRDFDTNLYTCAEEFDFLSKETFLRLTKTLLLPFYILVLLILLIKV 381
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009535425 500 VSD--------------MWVVLTKQQTHIRKHQFDHGELVYHALQLLAYTVLGVLIMRLKLFLTPHMCVMASLICSRQLF 565
Cdd:pfam10034 382 LQSiyrrlkryklsqapMQESLPLEDGRIGERPELNGEVVYHVLQLLAFGLLALLIMRLKLLWTPHMCVFASLGASKQLW 461
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009535425 566 GWLFCKVHPGAVVFAVLAAMSIQGSANLQTQWNIVGEFSNLPQEELIEWIKYSTKPDAVFAGAMPTMASVKLSALRPIVN 645
Cdd:pfam10034 462 HFLFKKIFSSAVPTVILASMSYKGFPNIQEELSILGEFYNPDTEELMEWIKSNTPKDAVFAGSMPLMATVKLSTGRPIVN 541
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009535425 646 HPHYEDAGLRARTKIVYSMYSRKAAEEVKRELIKLQVNYYILEESWCIRRSK-PGCSMPEIWDVED---PANAGKPPLCN 721
Cdd:pfam10034 542 HPHYEDAGLRERTEDVYSVYSRKPAEDVYKILTSLKVNYVILEDSICSERSRrRGCRMLDIWDVEDghcPANRKGPRFCH 621
                         650       660
                  ....*....|....*....|....*
gi 2009535425 722 LLV-KESKPHFTTVFQNSVYKVLEV 745
Cdd:pfam10034 622 EIKlSNYVPYFTRVFWNRSYHVYKV 646
Brme1 pfam15710
Break repair meiotic recombinase recruitment factor 1; Brme1 (also known as Meiok21) is a ...
9-52 2.04e-04

Break repair meiotic recombinase recruitment factor 1; Brme1 (also known as Meiok21) is a component of meiotic recombination bridges involved in meiotic double-strand break repair. The C-terminal domain of Brme1 physically interacts with the N-terminal domain of HSF2BP. BRME1 facilitates the loading of RAD51 and DMC1 recombinases onto DSBs (DNA double-strand breaks) through interaction with MEILB2/HSF2BP and replacing ssDNA binding proteins. Brme1 is highly expressed in mice testes and fetal ovaries. Knockout of Brme1 results in male mice infertility.


Pssm-ID: 464816 [Multi-domain]  Cd Length: 667  Bit Score: 44.92  E-value: 2.04e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2009535425   9 HREAAPKPPQPPRASQsplrGSPDVGAGEPGPERAPPSPRRKGA 52
Cdd:pfam15710 484 HREAAGGPPQEAGAQQ----GSPDAPTDLAGQPQHPPDSSDQAT 523
PHA03201 PHA03201
uracil DNA glycosylase; Provisional
14-66 1.01e-03

uracil DNA glycosylase; Provisional


Pssm-ID: 165468  Cd Length: 318  Bit Score: 41.80  E-value: 1.01e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2009535425  14 PKPPQPPRASQSPLRGSPDVGAGEPGPERA--PPSPRRKGAAGRKGPRAESAAPP 66
Cdd:PHA03201   20 PTPPRSPDASPEETPPSPPGPGAEPPPGRAagPAAPRRRPRGCPAGVTFSSSAPP 74
 
Name Accession Description Interval E-value
Dpy19L1 cd20178
C-mannosyltransferase Dpy-19-like protein 1 (Dpy19L1); Dpy19 proteins are ...
92-743 0e+00

C-mannosyltransferase Dpy-19-like protein 1 (Dpy19L1); Dpy19 proteins are C-mannosyltransferases that mediate C-mannosylation of tryptophan residues on target proteins. C-mannosylation is the attachment of alpha-mannose to the indole C2 carbon of the first tryptophan residue in the consensus amino acid sequence Trp-Xaa-Xaa-Trp/Cys through a C-C bond. This reaction takes place in the endoplasmic reticulum (ER) lumen. Dpy19 is a transmembrane domain family whose name is derived from the Caenorhabditis elegans Dumpy mutant. Dpy19L1 (also called protein Dpy-19 homolog 1) regulates neurite extension during development.


Pssm-ID: 439131  Cd Length: 652  Bit Score: 1258.22  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009535425  92 RTWTTLLLAAFAAVLHWSHITHLFENDRHFSHLSTLEREMAFRTEMGLYYSYFKTIVEAPSFLNGVWMIMNDKLTEYPLV 171
Cdd:cd20178     1 KIWVTLLLAALAGVLHWSHITHLFENDRHFSHLSTLEREMAFRTEMGLYYSYFKTIIEAPSFLNGVWMIMNDRLTEYPLV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009535425 172 INTLKRFNLYPEVILASWYRIYTKIMDLIGIQTKICWTVTRGEGLSPIESCEGLGDPACFYVAVIFILNGLMMALFFIYG 251
Cdd:cd20178    81 INTLKRFNLYPEVVLASWYRIYTGIMDFFGIQTKTCWTVNRGEGLSPVESCEGLGDPAYFYVAVIFLLNGLMMSLFFIYG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009535425 252 TYLSGSRLGGLVTVLCFFFNHGECTRVMWTPPLRESFSYPFLVLQMLLVTHILRATKLYRGSLIALCISNVFFMLPWQFA 331
Cdd:cd20178   161 TYLSGSRLGGVVTVLCFFFNHGECTRVMWTPPLRESFSYPFLVLQMLLVTYILRAPNLGRGSLIALCISNVLFMLPWQFA 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009535425 332 QFVLLTQIASLFALYVVGYIDISKLRKIIYMHMISLALCFVLMFGNSMLLTSYYASSLVIIWGLLAMKPYFLKINVSELS 411
Cdd:cd20178   241 QFVLLTQIASLFAVYVVGYIDSCKLQKILYAHMISLVVCFVLMFGNSMLLTSYYASSLVIIWGILALRPKFLKVNKSEVS 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009535425 412 LWVIQGCFWLFGTVILKYLTSKIFGIADDAHIGNLLTSKFFSYKDFDTLLYTCAAEFDFMEKETPLRYTKTLLLPVVLVV 491
Cdd:cd20178   321 LWVIQGCAWLFGTVILKYLTSKVFGIADDAHIGNLLKSKFTSYKDFDTLMYTCAAEFDFMEKETPLRYTKTLLLPVVLVV 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009535425 492 FIVIIRKVVSDMWVVLTKQQTHIRKHQFDHGELVYHALQLLAYTVLGVLIMRLKLFLTPHMCVMASLICSRQLFGWLFCK 571
Cdd:cd20178   401 FAAIARKTIKDLWGVLAKKATHTRKEQFAHGELVYHALQLLAYAVLAILIMRLKLFLTPHMCVMASLVCSRQLFGWLFCK 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009535425 572 VHPGAVVFAVLAAMSIQGSANLQTQWNIVGEFSNLPQEELIEWIKYSTKPDAVFAGAMPTMASVKLSALRPIVNHPHYED 651
Cdd:cd20178   481 VHPQAVVFAILAAMAIQGSANLQTQWNIIGEFSNLPQEELLEWIKYNTKPDAVFAGAMPTMASVKLSALRPIVNHPHYED 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009535425 652 AGLRARTKIVYSMYSRKAAEEVKRELIKLQVNYYILEESWCIRRSKPGCSMPEIWDVEDPANAGKPPLCNLLVKESKPHF 731
Cdd:cd20178   561 AGLRARTKIVYSMYSRKPAEEVKRELMKLGVNYYILEESWCVRRSKPGCSMPEIWDVEDPDNAGKTPLCTLMSKDSRPHF 640
                         650
                  ....*....|..
gi 2009535425 732 TTVFQNSVYKVL 743
Cdd:cd20178   641 TTVFENSVYKVL 652
Dpy19 cd20177
C-mannosyltransferase Dpy19; Dpy19 proteins are C-mannosyltransferases that mediate ...
107-742 0e+00

C-mannosyltransferase Dpy19; Dpy19 proteins are C-mannosyltransferases that mediate C-mannosylation of tryptophan residues on target proteins. C-mannosylation is the attachment of alpha-mannose to the indole C2 carbon of the first tryptophan residue in the consensus amino acid sequence Trp-Xaa-Xaa-Trp/Cys through a C-C bond. This reaction takes place in the endoplasmic reticulum (ER) lumen. Dpy19 is a transmembrane domain family whose name is derived from the Caenorhabditis elegans Dumpy mutant.


Pssm-ID: 439130  Cd Length: 657  Bit Score: 935.53  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009535425 107 HWSHITHLFENDRHFSHLSTLEREMAFRTEMGLYYSYFKTIVEAPSFLNGVWMIMNDKLTEYPLVINTLKRFNLYPEVIL 186
Cdd:cd20177    16 YSLHLSTLFENDRHFSHLSELEREMTFRTEMGLYYSYYKQLIEAPSFLEGLYKLTHDNVTEYPHTINTLKRFNLYPEVIL 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009535425 187 ASWYRIYTKIMDLIGIQTKICWTVtRGEGLSPIESCEGLGDPACFYVAVIFILNGLMMALFFIYGTYLSGSRLGGLVTVL 266
Cdd:cd20177    96 AILYRVFPSIANYFGIPTKQCWQV-RGEDLPPVESCEGLGEPAYFYIYVVFGLNGLVAGLLFLYGWLLSGSILGGLLTVA 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009535425 267 CFFFNHGECTRVMWTPPLRESFSYPFLVLQMLLVTHILRATKLYRGSLIALCISNVFFMLPWQFAQFVLLTQIASLFALY 346
Cdd:cd20177   175 FFFFNHGEATRVQWTPPLRESFAYPFLLLQILLITIYLRSNIGKRFHLLAISISTFLFMLMWQFSQFALLTQILSLFALY 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009535425 347 VVGYIDISKLRKIIYMHMISLALCFVLMFGNSMLLTSYYASSLVIIWGLLAMKPYFLKINVSELSLWVIQGCFWLFGTVI 426
Cdd:cd20177   255 VLGYIPSSKVQTIILSHLISLLLAFVLLFGNEMLLTSLYLSSLLAFLIILYLQLRLKKSFKFKLIIWLLQLILVFLGTLG 334
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009535425 427 LKYLTSKIFGIADDAHIGNLLTSKFFSYKDFDTLLYTCAAEFDFMEKETPLRYTKTL---LLPVVLVVFIVIIRKVVSDM 503
Cdd:cd20177   335 LKLLLSKLLNVEDDAHIFKILKSKFGDYRDFDTRLYTCAAEFDFLSLETFLRLSKTLllpLYIVVLVVIAFLFLRVRLLT 414
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009535425 504 WVVLTKQQTHI--RKHQFDHGELVYHALQLLAYTVLGVLIMRLKLFLTPHMCVMASLICSRQLFGWLFCKVHPG-AVVFA 580
Cdd:cd20177   415 LNDSTLKESVNftDSRLILNPEIVYNVLQLLAFGLLAILIMRLKLFWTPHMCILASLLLSKKLLWKLLLKKIFRlAVLFA 494
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009535425 581 VLAAMSIQGSANLQTQWNIVGEFSNLPQEELIEWIKYSTKPDAVFAGAMPTMASVKLSALRPIVNHPHYEDAGLRARTKI 660
Cdd:cd20177   495 LLASMSYPGIPNLQEELSILGEFSNPDTEELMEWIKDNTPPDAVFAGSMPLMANVKLSTGRPIVNHPHYEDAGLRERTKQ 574
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009535425 661 VYSMYSRKAAEEVKRELIKLQVNYYILEESWCIRRSKPGCSMPEIWDVEDPANAGKPPLC-NLLVKESKPHFTTVFQNSV 739
Cdd:cd20177   575 VYSMYSRRPAEEVYNILKKLGVNYIILEDSICLSRRRDGCSLPDIWDLEDPHNRGKPPLCiRLLLEDYVPYFKLVFSNKT 654

                  ...
gi 2009535425 740 YKV 742
Cdd:cd20177   655 YRV 657
Dpy19 pfam10034
Q-cell neuroblast polarization; Dyp-19, formerly known as DUF2211, is a transmembrane domain ...
107-745 0e+00

Q-cell neuroblast polarization; Dyp-19, formerly known as DUF2211, is a transmembrane domain family that is required to orient the neuroblast cells, QR and QL accurately on the anterior-posterior axis: QL and QR are born in the same anterior-posterior position, but polarise and migrate left-right asymmetrically, QL migrating towards the posterior and QR migrating towards the anterior. It is also required, with unc-40, to express mab-5 correctly in the Q cell descendants. The Dpy-19 protein derives from the C. elegans DUMPY mutant, Swiss:P34413.


Pssm-ID: 462945  Cd Length: 646  Bit Score: 910.06  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009535425 107 HWSHITHLFENDRHFSHLSTLEREMAFRTEMGLYYSYFKTIVEAPSFLNGVWMIMNDKLTEYPLVINTLKRFNLYPEVIL 186
Cdd:pfam10034   7 YALHVSTLFENDRWFSHLSELEREISFRTEMGLYYSYYKTIIEAPSFLEGLYQLMNDNRTEYPDTINALQRFNLYPEVIL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009535425 187 ASWYRIYTKIMDLIGiqtkicwtvtrgeglspiesceglgDPACFYVAVIFILNGLMMALFFIYGTYLSGSRLGGLVTVL 266
Cdd:pfam10034  87 AILYRIFRGIQNYLG-------------------------EPVYFYIYFVFGLQGVYVSALFLYGWYLSGSWLGGILAVL 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009535425 267 CFFFNHGECTRVMWTPPLRESFSYPFLVLQMLLVTHILRATKLY----RGSLIALCISNVFFMLPWQFAQFVLLTQIASL 342
Cdd:pfam10034 142 WFFFNHGETTRVEWTPPLRENFALPFFALQMLALTYILKRKNISsaseLFCYILLSASTFLFLLTWQFSQFVLLTQILSL 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009535425 343 FALYVVGYIDISKLRKIIYMHMISLALCFVLMFGNSMLLTSYYASSLVIIWGLLAMKPYFLKI-NVSELSLWVIQGCFWL 421
Cdd:pfam10034 222 FLLDSLGLVPSKKVAKIYLSHLISLLLAFVLQFGNSMLLTSPLLSSLISILLIRYLQPNMKKGrFSFRLLKLLLHGLLVL 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009535425 422 FGTVILKYLTSKIFGIADDAHIGNLLTSKFF--SYKDFDTLLYTCAAEFDFMEKETPLRYTKTLLLPVVLVVFIVIIRKV 499
Cdd:pfam10034 302 FGTLTLKLLIKKLLNVEDDAHIFDFLKAKFGlnSTRDFDTNLYTCAEEFDFLSKETFLRLTKTLLLPFYILVLLILLIKV 381
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009535425 500 VSD--------------MWVVLTKQQTHIRKHQFDHGELVYHALQLLAYTVLGVLIMRLKLFLTPHMCVMASLICSRQLF 565
Cdd:pfam10034 382 LQSiyrrlkryklsqapMQESLPLEDGRIGERPELNGEVVYHVLQLLAFGLLALLIMRLKLLWTPHMCVFASLGASKQLW 461
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009535425 566 GWLFCKVHPGAVVFAVLAAMSIQGSANLQTQWNIVGEFSNLPQEELIEWIKYSTKPDAVFAGAMPTMASVKLSALRPIVN 645
Cdd:pfam10034 462 HFLFKKIFSSAVPTVILASMSYKGFPNIQEELSILGEFYNPDTEELMEWIKSNTPKDAVFAGSMPLMATVKLSTGRPIVN 541
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009535425 646 HPHYEDAGLRARTKIVYSMYSRKAAEEVKRELIKLQVNYYILEESWCIRRSK-PGCSMPEIWDVED---PANAGKPPLCN 721
Cdd:pfam10034 542 HPHYEDAGLRERTEDVYSVYSRKPAEDVYKILTSLKVNYVILEDSICSERSRrRGCRMLDIWDVEDghcPANRKGPRFCH 621
                         650       660
                  ....*....|....*....|....*
gi 2009535425 722 LLV-KESKPHFTTVFQNSVYKVLEV 745
Cdd:pfam10034 622 EIKlSNYVPYFTRVFWNRSYHVYKV 646
Dpy19L2 cd20179
C-mannosyltransferase Dpy-19-like protein 2 (Dpy19L2); Dpy19 proteins are ...
107-742 0e+00

C-mannosyltransferase Dpy-19-like protein 2 (Dpy19L2); Dpy19 proteins are C-mannosyltransferases that mediate C-mannosylation of tryptophan residues on target proteins. C-mannosylation is the attachment of alpha-mannose to the indole C2 carbon of the first tryptophan residue in the consensus amino acid sequence Trp-Xaa-Xaa-Trp/Cys through a C-C bond. This reaction takes place in the endoplasmic reticulum (ER) lumen. Dpy19 is a transmembrane domain family whose name is derived from the Caenorhabditis elegans Dumpy mutant. Dpy19L2 (also called protein Dpy-19 homolog 2) deletion is a major cause of globozoospermia.


Pssm-ID: 439132  Cd Length: 652  Bit Score: 881.69  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009535425 107 HWSHITHLFENDRHFSHLSTLEREMAFRTEMGLYYSYFKTIVEAPSFLNGVWMIMNDKLTEYPLVINTLKRFNLYPEVIL 186
Cdd:cd20179    18 HWLHLVTLFENDRHFSHLSSLEREMTFRTEMGLYYSYFKTIIEAPSFLEGLWMIMNDRLTEYPLIINAIKRFHLYPEVII 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009535425 187 ASWYRIYTKIMDLIGIQTKICWTVTRGEGLSPIESCEGLGDPACFYVAVIFILNGLMMALFFIYGTYLSGSRLGGLVTVL 266
Cdd:cd20179    98 ASWYCTFMGIMNLFGLETKTCWNVTRIEPLNEVQSCEGLGDPACFYVGVIFILNGLMMGLFFMYGAYLSGTQLGGLITVL 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009535425 267 CFFFNHGECTRVMWTPPLRESFSYPFLVLQMLLVTHILRATKLYRGSLIALCISNVFFMLPWQFAQFVLLTQIASLFALY 346
Cdd:cd20179   178 CFFFNHGEATRVMWTPPLRESFSYPFLVLQMCILTLILRTSSNDRRPFIALCLSNVAFMLPWQFAQFILFTQIASLFPMY 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009535425 347 VVGYIDISKLRKIIYMHMISLALCFVLMFGNSMLLTSYYASSLVIIWGLLAMKPYFLKINVSELSLWVIQGCFWLFGTVI 426
Cdd:cd20179   258 VVGYIEPSKFQKIIYMNMISVTLSFILMFGNSMYLSSYYSSSLLMTWAIILKRNEIQKLGVSKLNFWLIQGSAWWCGTII 337
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009535425 427 LKYLTSKIFGIADDAHIGNLLTSKFFSYKDFDTLLYTCAAEFDFMEKETPLRYTKTLLLPVVLVVFIVIIRKVVSDMWVV 506
Cdd:cd20179   338 LKFLTSKILGVSDHIRLSDLIAARILRYTDFDTLIYTCAPEFDFMEKATPLRYTKTLLLPVVMVITCFIFKKTVRDISYV 417
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009535425 507 LTkQQTHIRKHQFDHGELVYHALQLLAYTVLGVLIMRLKLFLTPHMCVMASLICSRQLFGWLFCKVHPGAVVFAVLAAMS 586
Cdd:cd20179   418 LA-TNIYLRKQLLEHSELAFHTLQLLVFTALAILIMRLKMFLTPHMCVMASLICSRQLFGWLFRRVRFEKVIFGILTVMS 496
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009535425 587 IQGSANLQTQWNIVGEFSNLPQEELIEWIKYSTKPDAVFAGAMPTMASVKLSALRPIVNHPHYEDAGLRARTKIVYSMYS 666
Cdd:cd20179   497 IQGYANLRNQWSIIGEFNNLPQEELLQWIKYSTTSDAVFAGAMPTMASIKLSTLHPIVNHPHYEDADLRARTKIVYSTYS 576
                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2009535425 667 RKAAEEVKRELIKLQVNYYILEESWCIRRSKPGCSMPEIWDVEDPANAGKPPLCNLLVKESKPHFTTVFQNSVYKV 742
Cdd:cd20179   577 RKSAKEVRDKLLELHVNYYVLEEAWCVVRTKPGCSMLEIWDVEDPSNAANPPLCSVLLEDARPYFTTVFQNSVYRV 652
Dpy19L3 cd20181
C-mannosyltransferase Dpy-19-like protein 3 (Dpy19L3); Dpy19 proteins are ...
110-742 7.83e-88

C-mannosyltransferase Dpy-19-like protein 3 (Dpy19L3); Dpy19 proteins are C-mannosyltransferases that mediate C-mannosylation of tryptophan residues on target proteins. C-mannosylation is the attachment of alpha-mannose to the indole C2 carbon of the first tryptophan residue in the consensus amino acid sequence Trp-Xaa-Xaa-Trp/Cys through a C-C bond. This reaction takes place in the endoplasmic reticulum (ER) lumen. Dpy19 is a transmembrane domain family whose name is derived from the Caenorhabditis elegans Dumpy mutant. In humans Dpy19L3 (also called protein Dpy-19 homolog 3) is a C-mannosyltransferase of R-spondin.


Pssm-ID: 439134  Cd Length: 667  Bit Score: 290.20  E-value: 7.83e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009535425 110 HITHLFENDRHFSHLSTLEREMAFRTEMGLYYSYFKTIVEAPSFLNGVWMIMNDKLTEYPLVINTLKRFNLYPEVILASW 189
Cdd:cd20181    19 YVATLHENDLWFSNIKEVEREISFRTECGLYYSYYKQMLQAPSIQQGFHGLIYDNKTESMRTINLLQRMNIYQEVFLSVL 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009535425 190 YRIYtkimdligiqtkicwtvtrgeglsPIEScegLGDPACFYVAVIFILNGLMMALFFIYGTYLSGSRLGGLVTVLCFF 269
Cdd:cd20181    99 YRVL------------------------PIQK---YLEPVYFYIYTLFGLQAVYVIALYITSWLLSGTWLSGLLAAVWYI 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009535425 270 FNHGECTRVMWTPPLRESFSYPFLVLQMLLVTHILRaTKLY----RGSLIALCISNVFFMLPWQFAQFVLLTQIASLFAL 345
Cdd:cd20181   152 TNRIDTTRVEFTIPLRENWALPFFAIQIAAITYFLR-PNLQplqeRLTLLAIFISTFLFSLTWQFNQFMMLIQALVLFTL 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009535425 346 YVVGYIDISKLRKIIYMHMISLALCFVLMFGNSMLLtsyyaSSLVIIWGLLAMKPYFLKINVSELSLWVIQG-------- 417
Cdd:cd20181   231 DCLDMLPTAKVTWLYGIQISGLLLVCILQFFNSMIL-----GSLLLSFNLSVLIVRKLQKNLKTGSFLNRLGklllhlal 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009535425 418 CFWLfgTVILKYLTSKIFGIADDAHIGNLLTSKFF--SYKDFDTLLYTCAAEFDFME-------KETPLRYTKTLLLPVV 488
Cdd:cd20181   306 VLCL--TLFLNNIIKKILNLKSDEHIFKFLKAKFGfgATRDFDANLYLCEEAFGLLPfntferlSDTLLFYAYIFVLLLT 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009535425 489 LVVFIVIIRKVVSDMWVVLTKQQThiRKHQFD-HGELVYHALQLLAYTVLGVLIMRLKLFLTPHMCVMASL-ICSRQLFG 566
Cdd:cd20181   384 VIVAAVVAFHNLSDSTNQQSMGKM--EKGTVDlKPEVAYNLIHTILFGFLALSTMRMKYLWTSHMCVFASFgLCSTELWE 461
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009535425 567 WLFCKVH----------PGAVVFAVLAAMSIQGSANLQTQWNIVGEFSNLPQEELIEWIKYSTKPDAVFAGAMPTMASVK 636
Cdd:cd20181   462 LLLKSVHlynpkrirvmRYSVPILTLLYLCYKFWPGLMDELSELREFYDPDTVELMNWINSNTPRKAVFAGSMQLLAGVK 541
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009535425 637 LSALRPIVNHPHYEDAGLRARTKIVYSMYSRKAAEEVKRELIKLQVNYYILEESWCI-RRSKPGCSMPEIWDVE------ 709
Cdd:cd20181   542 LCTGRTLTNHPHYEDKSLRERTRQVYQIYAKRSPEEVHALLRSFGTDYVILEDSICYeRRHRRGCRLRDLLDIAnghimd 621
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|...
gi 2009535425 710 -------DPANAGKPPLCNLLVKESKP---HFTTVFQNSVYKV 742
Cdd:cd20181   622 gpgendpDLKPADHPRFCEEIKRNLPSyaaYFTRVFQNKTFHV 664
Dpy19L4 cd20180
C-mannosyltransferase Dpy-19-like protein 4 (Dpy19L4); Dpy19 proteins are ...
121-708 7.66e-48

C-mannosyltransferase Dpy-19-like protein 4 (Dpy19L4); Dpy19 proteins are C-mannosyltransferases that mediate C-mannosylation of tryptophan residues on target proteins. C-mannosylation is the attachment of alpha-mannose to the indole C2 carbon of the first tryptophan residue in the consensus amino acid sequence Trp-Xaa-Xaa-Trp/Cys through a C-C bond. This reaction takes place in the endoplasmic reticulum (ER) lumen. Dpy19 is a transmembrane domain family whose name is derived from the Caenorhabditis elegans Dumpy mutant. The function of Dpy19L4 (also called protein Dpy-19 homolog 4) is unknown.


Pssm-ID: 439133  Cd Length: 664  Bit Score: 180.03  E-value: 7.66e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009535425 121 FSHLSTLEREMAFRTEMGLYYSYFKTIVEAPSFLNGVWMIMNDKLTEYPLVINTLKRFNLYPEVILASWYRIyTKIMDLI 200
Cdd:cd20180    30 FSNRQELEREITFQGDSAIYYSYYKDMLKAPSFERGVYELTHNNKTVSLKTINAVQQMSLYPELIASVLYQA-TGSNEVI 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009535425 201 giqtkicwtvtrgeglspiesceglgDPACFYVAVIFILNGLMMALFFIYGTYLSGSRLGGLVTVLCFFFNHGECTRVMW 280
Cdd:cd20180   109 --------------------------EPVYFYIGIVFGLQGIYVTALFVTSWLMSGTWLAGMLTVAWFIINRVDTTRIEY 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009535425 281 TPPLRESFSYPFLVLQMLLVTHILR---ATKLYRGSLIALCISNVFFMLPWQFAQFVLLTQIASLFALYVVGYIDISKLR 357
Cdd:cd20180   163 SIPLRENWALPYFACQVAALTGYLKsnlNTYAERFCYLLMSASTYTFMMMWEYSHYVLFLQAISLFLLDSFSLEQSDKVY 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009535425 358 KIIYMHMISLALCFVLMFGNSMLLTSyyaSSLVIIWGLLAMKpyFLKINVSELSLWVIQGCFWLFG-----TVILKYLTS 432
Cdd:cd20180   243 EVYKVYLFSLFLGYLLQFENPALLVS---PLLSLVAALMLAK--CLQLNMKKGPFVAKMIKVLHFYlvctlTITLNFIMK 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009535425 433 KIFGIADDAHIGNLLTSKF--FSYKDFDTLLYTCAAEFDFMEKETPLRYTKTLLLPVVLVVFIVIIRKVVSDMWVVLTKQ 510
Cdd:cd20180   318 MFVPHKENEHLLKFLEVKFglNTTKNFTMNWLLCQESLQAPSQDFFLRLTQSSLLPFYILVLIICLLSMLQVIFRRLSGK 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009535425 511 --QTHIRKHQFDHGE---LVYHALQLLAYTVLGVLIMRLKLFLTPHMCVMASL-ICSRQL----FGWLFCK-VHPgaVVF 579
Cdd:cd20180   398 plKETVTLEDGRIGErpeIVYHVIHTILLGSLAMLFEGMKYLWTPYVCMLAAFgVCSPELwmtlFKWLRLRtVHP--ILL 475
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009535425 580 AVLAAMSI----------QGSANLQTQWNIVGEFSNLPQEELIEWIKYSTKPDAVFAGAMPTMASVKLSALRPIVNHPHY 649
Cdd:cd20180   476 ALILSMAVptiigfslwkEFFPRLMTELSELQEFYDPDTVELMTWIKRQAPVAAVFAGSPQLMGTIKLCTGWMVTSLPLY 555
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009535425 650 EDAGLRARTKIVYSMYSRKAAEEVKRELIKLQVNYYILEESWCIRRS-KPGCSMPEIWDV 708
Cdd:cd20180   556 NDDDLLKRNENIYQIYSKRSAEDIYKILTSYKANYLIIEDAICNEVGpVRGCRVKDLLDI 615
Brme1 pfam15710
Break repair meiotic recombinase recruitment factor 1; Brme1 (also known as Meiok21) is a ...
9-52 2.04e-04

Break repair meiotic recombinase recruitment factor 1; Brme1 (also known as Meiok21) is a component of meiotic recombination bridges involved in meiotic double-strand break repair. The C-terminal domain of Brme1 physically interacts with the N-terminal domain of HSF2BP. BRME1 facilitates the loading of RAD51 and DMC1 recombinases onto DSBs (DNA double-strand breaks) through interaction with MEILB2/HSF2BP and replacing ssDNA binding proteins. Brme1 is highly expressed in mice testes and fetal ovaries. Knockout of Brme1 results in male mice infertility.


Pssm-ID: 464816 [Multi-domain]  Cd Length: 667  Bit Score: 44.92  E-value: 2.04e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2009535425   9 HREAAPKPPQPPRASQsplrGSPDVGAGEPGPERAPPSPRRKGA 52
Cdd:pfam15710 484 HREAAGGPPQEAGAQQ----GSPDAPTDLAGQPQHPPDSSDQAT 523
PHA03201 PHA03201
uracil DNA glycosylase; Provisional
14-66 1.01e-03

uracil DNA glycosylase; Provisional


Pssm-ID: 165468  Cd Length: 318  Bit Score: 41.80  E-value: 1.01e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2009535425  14 PKPPQPPRASQSPLRGSPDVGAGEPGPERA--PPSPRRKGAAGRKGPRAESAAPP 66
Cdd:PHA03201   20 PTPPRSPDASPEETPPSPPGPGAEPPPGRAagPAAPRRRPRGCPAGVTFSSSAPP 74
 
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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