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Conserved domains on  [gi|1907136182|ref|XP_036015055|]
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myelin transcription factor 1 isoform X11 [Mus musculus]

Protein Classification

MYT1 and zf-C2HC domain-containing protein( domain architecture ID 10479154)

protein containing domains MYT1, zf-C2HC, and Com_YlbF

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MYT1 super family cl07191
Myelin transcription factor 1; This domain is found in the myelin transcription factor 1 (MYT1) ...
 474-705 9.05e-81

Myelin transcription factor 1; This domain is found in the myelin transcription factor 1 (MYT1) of chordates. MYT1 contains C2HC zinc finger domains (pfam01530) and is expressed in developing neurons of the central nervous system where it is involved in the selection of neuronal precursor cells.


The actual alignment was detected with superfamily member pfam08474:

Pssm-ID: 462489 [Multi-domain]  Cd Length: 237  Bit Score: 262.38  E-value: 9.05e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136182  474 YRPNVAPATPRANLAKELEKFSKVTFDYASFDAQVFGKRMLAPKIQTSETSPKAFQC----------------------- 530
Cdd:pfam08474    1 YRNNVPTTTPRANLAKELEKYSKTSFDYASFDAQVFGKRTLAPKVQGQDTSPKGFDAkkyfckpsspsssltssyapsss 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136182  531 ------FDYSHDAEAAHMAATAILNLSTRCWEMPENLSTKPQDLPSKAVDIEVDENGTLDLSMHKHRKRENTfpsssscs 604
Cdd:pfam08474   81 ssssssYDYTHDMEAAHMAATAILNLSTRCREMPENLSTKPQDLSAKPDDIEVDENGTLDLSMKKNRPRGVT-------- 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136182  605 sSPGVKSPDVSQRQSSTSAPSSSMTSPQSsqaSRQDEWDRPLDYTKPSRLREEEpeesepaahsfaSSEADDQEVSEENF 684
Cdd:pfam08474  153 -SGSVLTPLPPMSPQRQASLLNSRCYQAL---CAQDCWDLPVDYTKIKRIDEEE------------KEEPEDLDPFQELL 216

                          250       260
                   ....*....|....*....|.
gi 1907136182  685 EERKYPGEVTLTNFKLKFLSK 705
Cdd:pfam08474  217 EERKYPGEVTIPSPKPKYPPC 237
zf-C2HC pfam01530
Zinc finger, C2HC type; This is a DNA binding zinc finger domain.
 734-762 5.27e-17

Zinc finger, C2HC type; This is a DNA binding zinc finger domain.


:

Pssm-ID: 460240  Cd Length: 29  Bit Score: 74.88  E-value: 5.27e-17
                           10        20
                   ....*....|....*....|....*....
gi 1907136182  734 RCPTPGCDGSGHITGNYASHRSLSGCPRA 762
Cdd:pfam01530    1 KCPTPGCDGSGHVSGKYATHRSLSGCPYA 29
zf-C2HC pfam01530
Zinc finger, C2HC type; This is a DNA binding zinc finger domain.
 783-811 8.30e-15

Zinc finger, C2HC type; This is a DNA binding zinc finger domain.


:

Pssm-ID: 460240  Cd Length: 29  Bit Score: 68.71  E-value: 8.30e-15
                           10        20
                   ....*....|....*....|....*....
gi 1907136182  783 KCPVPGCVGLGHISGKYASHRSASGCPLA 811
Cdd:pfam01530    1 KCPTPGCDGSGHVSGKYATHRSLSGCPYA 29
zf-C2HC pfam01530
Zinc finger, C2HC type; This is a DNA binding zinc finger domain.
 836-864 9.89e-15

Zinc finger, C2HC type; This is a DNA binding zinc finger domain.


:

Pssm-ID: 460240  Cd Length: 29  Bit Score: 68.71  E-value: 9.89e-15
                           10        20
                   ....*....|....*....|....*....
gi 1907136182  836 TCPTPGCDGSGHANGSFLTHRSLSGCPRA 864
Cdd:pfam01530    1 KCPTPGCDGSGHVSGKYATHRSLSGCPYA 29
zf-C2HC pfam01530
Zinc finger, C2HC type; This is a DNA binding zinc finger domain.
 399-427 2.27e-14

Zinc finger, C2HC type; This is a DNA binding zinc finger domain.


:

Pssm-ID: 460240  Cd Length: 29  Bit Score: 67.56  E-value: 2.27e-14
                           10        20
                   ....*....|....*....|....*....
gi 1907136182  399 KCPTPGCTGQGHVNSNRNTHRSLSGCPIA 427
Cdd:pfam01530    1 KCPTPGCDGSGHVSGKYATHRSLSGCPYA 29
zf-C2HC pfam01530
Zinc finger, C2HC type; This is a DNA binding zinc finger domain.
 355-381 2.73e-14

Zinc finger, C2HC type; This is a DNA binding zinc finger domain.


:

Pssm-ID: 460240  Cd Length: 29  Bit Score: 67.17  E-value: 2.73e-14
                           10        20
                   ....*....|....*....|....*..
gi 1907136182  355 KCPTPGCDGTGHVTGLYPHHRSLSGCP 381
Cdd:pfam01530    1 KCPTPGCDGSGHVSGKYATHRSLSGCP 27
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
893-961 2.28e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


:

Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 51.06  E-value: 2.28e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907136182  893 EEIKQLNQEIRDLNESNSEMEAAMVQLQSQISSMEKNLKNIEEENKLIEEQNEALFLELSGLSQALIQS 961
Cdd:COG4372    115 EELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQ 183
 
Name Accession Description Interval E-value
MYT1 pfam08474
Myelin transcription factor 1; This domain is found in the myelin transcription factor 1 (MYT1) ...
 474-705 9.05e-81

Myelin transcription factor 1; This domain is found in the myelin transcription factor 1 (MYT1) of chordates. MYT1 contains C2HC zinc finger domains (pfam01530) and is expressed in developing neurons of the central nervous system where it is involved in the selection of neuronal precursor cells.


Pssm-ID: 462489 [Multi-domain]  Cd Length: 237  Bit Score: 262.38  E-value: 9.05e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136182  474 YRPNVAPATPRANLAKELEKFSKVTFDYASFDAQVFGKRMLAPKIQTSETSPKAFQC----------------------- 530
Cdd:pfam08474    1 YRNNVPTTTPRANLAKELEKYSKTSFDYASFDAQVFGKRTLAPKVQGQDTSPKGFDAkkyfckpsspsssltssyapsss 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136182  531 ------FDYSHDAEAAHMAATAILNLSTRCWEMPENLSTKPQDLPSKAVDIEVDENGTLDLSMHKHRKRENTfpsssscs 604
Cdd:pfam08474   81 ssssssYDYTHDMEAAHMAATAILNLSTRCREMPENLSTKPQDLSAKPDDIEVDENGTLDLSMKKNRPRGVT-------- 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136182  605 sSPGVKSPDVSQRQSSTSAPSSSMTSPQSsqaSRQDEWDRPLDYTKPSRLREEEpeesepaahsfaSSEADDQEVSEENF 684
Cdd:pfam08474  153 -SGSVLTPLPPMSPQRQASLLNSRCYQAL---CAQDCWDLPVDYTKIKRIDEEE------------KEEPEDLDPFQELL 216

                          250       260
                   ....*....|....*....|.
gi 1907136182  685 EERKYPGEVTLTNFKLKFLSK 705
Cdd:pfam08474  217 EERKYPGEVTIPSPKPKYPPC 237
zf-C2HC pfam01530
Zinc finger, C2HC type; This is a DNA binding zinc finger domain.
 734-762 5.27e-17

Zinc finger, C2HC type; This is a DNA binding zinc finger domain.


Pssm-ID: 460240  Cd Length: 29  Bit Score: 74.88  E-value: 5.27e-17
                           10        20
                   ....*....|....*....|....*....
gi 1907136182  734 RCPTPGCDGSGHITGNYASHRSLSGCPRA 762
Cdd:pfam01530    1 KCPTPGCDGSGHVSGKYATHRSLSGCPYA 29
zf-C2HC pfam01530
Zinc finger, C2HC type; This is a DNA binding zinc finger domain.
 783-811 8.30e-15

Zinc finger, C2HC type; This is a DNA binding zinc finger domain.


Pssm-ID: 460240  Cd Length: 29  Bit Score: 68.71  E-value: 8.30e-15
                           10        20
                   ....*....|....*....|....*....
gi 1907136182  783 KCPVPGCVGLGHISGKYASHRSASGCPLA 811
Cdd:pfam01530    1 KCPTPGCDGSGHVSGKYATHRSLSGCPYA 29
zf-C2HC pfam01530
Zinc finger, C2HC type; This is a DNA binding zinc finger domain.
 836-864 9.89e-15

Zinc finger, C2HC type; This is a DNA binding zinc finger domain.


Pssm-ID: 460240  Cd Length: 29  Bit Score: 68.71  E-value: 9.89e-15
                           10        20
                   ....*....|....*....|....*....
gi 1907136182  836 TCPTPGCDGSGHANGSFLTHRSLSGCPRA 864
Cdd:pfam01530    1 KCPTPGCDGSGHVSGKYATHRSLSGCPYA 29
zf-C2HC pfam01530
Zinc finger, C2HC type; This is a DNA binding zinc finger domain.
 399-427 2.27e-14

Zinc finger, C2HC type; This is a DNA binding zinc finger domain.


Pssm-ID: 460240  Cd Length: 29  Bit Score: 67.56  E-value: 2.27e-14
                           10        20
                   ....*....|....*....|....*....
gi 1907136182  399 KCPTPGCTGQGHVNSNRNTHRSLSGCPIA 427
Cdd:pfam01530    1 KCPTPGCDGSGHVSGKYATHRSLSGCPYA 29
zf-C2HC pfam01530
Zinc finger, C2HC type; This is a DNA binding zinc finger domain.
 355-381 2.73e-14

Zinc finger, C2HC type; This is a DNA binding zinc finger domain.


Pssm-ID: 460240  Cd Length: 29  Bit Score: 67.17  E-value: 2.73e-14
                           10        20
                   ....*....|....*....|....*..
gi 1907136182  355 KCPTPGCDGTGHVTGLYPHHRSLSGCP 381
Cdd:pfam01530    1 KCPTPGCDGSGHVSGKYATHRSLSGCP 27
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
893-961 2.28e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 51.06  E-value: 2.28e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907136182  893 EEIKQLNQEIRDLNESNSEMEAAMVQLQSQISSMEKNLKNIEEENKLIEEQNEALFLELSGLSQALIQS 961
Cdd:COG4372    115 EELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQ 183
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 884-956 2.51e-06

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 51.56  E-value: 2.51e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907136182  884 KTSDVLENDEEIKQLNQEIRDLNESNSEMEAAMVQLQSQISSMEKNLKNIEEENKLIEEQNEALFLELSGLSQ 956
Cdd:TIGR04523  354 SESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEK 426
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 892-941 4.03e-05

Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family includes Saccharomyces cerevisiae Atg16 (also called cytoplasm to vacuole targeting protein 11, CVT11, or SAP18), human autophagy-related protein 16-1 (also called APG16-like 1, ATG16L1, or APG16L) and autophagy-related protein 16-2 (also called APG16-like 2, ATG16L2, WD repeat-containing protein 80 or WDR80), and similar proteins. Atg16 stabilizes the Atg5-Atg12 conjugate and mediates the formation of the 350 kDa complex, which is necessary for autophagy. The Atg5-Atg12/Atg16 complex is required for efficient promotion of Atg8-conjugation to phosphatidylethanolamine and Atg8 localization to the pre-autophagosomal structure (PAS). Similarly, human ATG16L1 plays an essential role in autophagy and acts as a molecular scaffold which mediates protein-protein interactions essential for autophagosome formation. ATG16L2, though structurally similar to ATG16L1 and able to form a complex with the autophagy proteins Atg5 and Atg12, is not essential for autophagy. Single-nucleotide polymorphisms in ATG16L1 is associated with an increased risk of developing Crohn disease. Saccharomyces cerevisiae Atg16 contains an N-terminal domain (NTD) that interacts with the Atg5-Atg12 protein conjugate and a coiled-coil domain (CCD) that dimerizes and mediates self-assembly. Human ATG16L1 and ATG16L2 also contains an N-terminal region that binds Atg5, a CCD homologous to the yeast CCD, and a WD40 domain that represents approximately 50% of the full-length protein. This model corresponds to the CCD of Atg16 family proteins.


Pssm-ID: 439196 [Multi-domain]  Cd Length: 91  Bit Score: 43.32  E-value: 4.03e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1907136182  892 DEEIKQLNQEIRDLNESNSEMEAAMVQLQSQISSMEKNLKNIEEEN-KLIE 941
Cdd:cd22887     24 EEEIKDLEEELKEKNKANEILNDELIALQIENNLLEEKLRKLQEENdELVE 74
CCDC22 pfam05667
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ...
 844-947 6.72e-04

Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.


Pssm-ID: 461708 [Multi-domain]  Cd Length: 600  Bit Score: 43.48  E-value: 6.72e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136182  844 GSGHANGSFLTHRslsgcpratfagKKGKLSGDEILSPKFKTSDVLENDEEIKQLNQEIRDLNESNSEMEAAMVQLQSQI 923
Cdd:pfam05667  291 DTGLTKGSRFTHT------------EKLQFTNEAPAATSSPPTKVETEEELQQQREEELEELQEQLEDLESSIQELEKEI 358

                           90       100
                   ....*....|....*....|....
gi 1907136182  924 SSMEKNLKNIEEENKLIEEQNEAL 947
Cdd:pfam05667  359 KKLESSIKQVEEELEELKEQNEEL 382
t_SNARE smart00397
Helical region found in SNAREs; All alpha-helical motifs that form twisted and parallel ...
 885-938 3.78e-03

Helical region found in SNAREs; All alpha-helical motifs that form twisted and parallel four-helix bundles in target soluble N-ethylmaleimide-sensitive factor (NSF) attachment protein (SNAP) receptor proteins. This motif found in "Q-SNAREs".


Pssm-ID: 197699 [Multi-domain]  Cd Length: 66  Bit Score: 36.79  E-value: 3.78e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 1907136182   885 TSDVLENDEEIKQLNQEIRDLNESNSEMeAAMVQLQS-QISSMEKNLKNIEEENK 938
Cdd:smart00397    4 LAREEERDEELEQLEKSIQELKQIFLDM-GTELEEQGeQLDRIEDNVDDADVNLK 57
 
Name Accession Description Interval E-value
MYT1 pfam08474
Myelin transcription factor 1; This domain is found in the myelin transcription factor 1 (MYT1) ...
 474-705 9.05e-81

Myelin transcription factor 1; This domain is found in the myelin transcription factor 1 (MYT1) of chordates. MYT1 contains C2HC zinc finger domains (pfam01530) and is expressed in developing neurons of the central nervous system where it is involved in the selection of neuronal precursor cells.


Pssm-ID: 462489 [Multi-domain]  Cd Length: 237  Bit Score: 262.38  E-value: 9.05e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136182  474 YRPNVAPATPRANLAKELEKFSKVTFDYASFDAQVFGKRMLAPKIQTSETSPKAFQC----------------------- 530
Cdd:pfam08474    1 YRNNVPTTTPRANLAKELEKYSKTSFDYASFDAQVFGKRTLAPKVQGQDTSPKGFDAkkyfckpsspsssltssyapsss 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136182  531 ------FDYSHDAEAAHMAATAILNLSTRCWEMPENLSTKPQDLPSKAVDIEVDENGTLDLSMHKHRKRENTfpsssscs 604
Cdd:pfam08474   81 ssssssYDYTHDMEAAHMAATAILNLSTRCREMPENLSTKPQDLSAKPDDIEVDENGTLDLSMKKNRPRGVT-------- 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136182  605 sSPGVKSPDVSQRQSSTSAPSSSMTSPQSsqaSRQDEWDRPLDYTKPSRLREEEpeesepaahsfaSSEADDQEVSEENF 684
Cdd:pfam08474  153 -SGSVLTPLPPMSPQRQASLLNSRCYQAL---CAQDCWDLPVDYTKIKRIDEEE------------KEEPEDLDPFQELL 216

                          250       260
                   ....*....|....*....|.
gi 1907136182  685 EERKYPGEVTLTNFKLKFLSK 705
Cdd:pfam08474  217 EERKYPGEVTIPSPKPKYPPC 237
zf-C2HC pfam01530
Zinc finger, C2HC type; This is a DNA binding zinc finger domain.
 734-762 5.27e-17

Zinc finger, C2HC type; This is a DNA binding zinc finger domain.


Pssm-ID: 460240  Cd Length: 29  Bit Score: 74.88  E-value: 5.27e-17
                           10        20
                   ....*....|....*....|....*....
gi 1907136182  734 RCPTPGCDGSGHITGNYASHRSLSGCPRA 762
Cdd:pfam01530    1 KCPTPGCDGSGHVSGKYATHRSLSGCPYA 29
zf-C2HC pfam01530
Zinc finger, C2HC type; This is a DNA binding zinc finger domain.
 783-811 8.30e-15

Zinc finger, C2HC type; This is a DNA binding zinc finger domain.


Pssm-ID: 460240  Cd Length: 29  Bit Score: 68.71  E-value: 8.30e-15
                           10        20
                   ....*....|....*....|....*....
gi 1907136182  783 KCPVPGCVGLGHISGKYASHRSASGCPLA 811
Cdd:pfam01530    1 KCPTPGCDGSGHVSGKYATHRSLSGCPYA 29
zf-C2HC pfam01530
Zinc finger, C2HC type; This is a DNA binding zinc finger domain.
 836-864 9.89e-15

Zinc finger, C2HC type; This is a DNA binding zinc finger domain.


Pssm-ID: 460240  Cd Length: 29  Bit Score: 68.71  E-value: 9.89e-15
                           10        20
                   ....*....|....*....|....*....
gi 1907136182  836 TCPTPGCDGSGHANGSFLTHRSLSGCPRA 864
Cdd:pfam01530    1 KCPTPGCDGSGHVSGKYATHRSLSGCPYA 29
zf-C2HC pfam01530
Zinc finger, C2HC type; This is a DNA binding zinc finger domain.
 399-427 2.27e-14

Zinc finger, C2HC type; This is a DNA binding zinc finger domain.


Pssm-ID: 460240  Cd Length: 29  Bit Score: 67.56  E-value: 2.27e-14
                           10        20
                   ....*....|....*....|....*....
gi 1907136182  399 KCPTPGCTGQGHVNSNRNTHRSLSGCPIA 427
Cdd:pfam01530    1 KCPTPGCDGSGHVSGKYATHRSLSGCPYA 29
zf-C2HC pfam01530
Zinc finger, C2HC type; This is a DNA binding zinc finger domain.
 355-381 2.73e-14

Zinc finger, C2HC type; This is a DNA binding zinc finger domain.


Pssm-ID: 460240  Cd Length: 29  Bit Score: 67.17  E-value: 2.73e-14
                           10        20
                   ....*....|....*....|....*..
gi 1907136182  355 KCPTPGCDGTGHVTGLYPHHRSLSGCP 381
Cdd:pfam01530    1 KCPTPGCDGSGHVSGKYATHRSLSGCP 27
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
893-961 2.28e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 51.06  E-value: 2.28e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907136182  893 EEIKQLNQEIRDLNESNSEMEAAMVQLQSQISSMEKNLKNIEEENKLIEEQNEALFLELSGLSQALIQS 961
Cdd:COG4372    115 EELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQ 183
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 884-956 2.51e-06

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 51.56  E-value: 2.51e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907136182  884 KTSDVLENDEEIKQLNQEIRDLNESNSEMEAAMVQLQSQISSMEKNLKNIEEENKLIEEQNEALFLELSGLSQ 956
Cdd:TIGR04523  354 SESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEK 426
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 892-941 4.03e-05

Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family includes Saccharomyces cerevisiae Atg16 (also called cytoplasm to vacuole targeting protein 11, CVT11, or SAP18), human autophagy-related protein 16-1 (also called APG16-like 1, ATG16L1, or APG16L) and autophagy-related protein 16-2 (also called APG16-like 2, ATG16L2, WD repeat-containing protein 80 or WDR80), and similar proteins. Atg16 stabilizes the Atg5-Atg12 conjugate and mediates the formation of the 350 kDa complex, which is necessary for autophagy. The Atg5-Atg12/Atg16 complex is required for efficient promotion of Atg8-conjugation to phosphatidylethanolamine and Atg8 localization to the pre-autophagosomal structure (PAS). Similarly, human ATG16L1 plays an essential role in autophagy and acts as a molecular scaffold which mediates protein-protein interactions essential for autophagosome formation. ATG16L2, though structurally similar to ATG16L1 and able to form a complex with the autophagy proteins Atg5 and Atg12, is not essential for autophagy. Single-nucleotide polymorphisms in ATG16L1 is associated with an increased risk of developing Crohn disease. Saccharomyces cerevisiae Atg16 contains an N-terminal domain (NTD) that interacts with the Atg5-Atg12 protein conjugate and a coiled-coil domain (CCD) that dimerizes and mediates self-assembly. Human ATG16L1 and ATG16L2 also contains an N-terminal region that binds Atg5, a CCD homologous to the yeast CCD, and a WD40 domain that represents approximately 50% of the full-length protein. This model corresponds to the CCD of Atg16 family proteins.


Pssm-ID: 439196 [Multi-domain]  Cd Length: 91  Bit Score: 43.32  E-value: 4.03e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1907136182  892 DEEIKQLNQEIRDLNESNSEMEAAMVQLQSQISSMEKNLKNIEEEN-KLIE 941
Cdd:cd22887     24 EEEIKDLEEELKEKNKANEILNDELIALQIENNLLEEKLRKLQEENdELVE 74
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 869-968 4.20e-04

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 44.24  E-value: 4.20e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136182  869 KKGKLSG--DEILSPKF-KTSDVLEndEEIKQLNQEIRDLNESNSEMEAAMVQLQ--------------SQISSMEKNLK 931
Cdd:TIGR04523  536 KESKISDleDELNKDDFeLKKENLE--KEIDEKNKEIEELKQTQKSLKKKQEEKQelidqkekekkdliKEIEEKEKKIS 613

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1907136182  932 NIEEENKLIEEQNEALFLELSGL---SQALIQSLANIRLP 968
Cdd:TIGR04523  614 SLEKELEKAKKENEKLSSIIKNIkskKNKLKQEVKQIKET 653
CCDC22 pfam05667
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ...
 844-947 6.72e-04

Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.


Pssm-ID: 461708 [Multi-domain]  Cd Length: 600  Bit Score: 43.48  E-value: 6.72e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136182  844 GSGHANGSFLTHRslsgcpratfagKKGKLSGDEILSPKFKTSDVLENDEEIKQLNQEIRDLNESNSEMEAAMVQLQSQI 923
Cdd:pfam05667  291 DTGLTKGSRFTHT------------EKLQFTNEAPAATSSPPTKVETEEELQQQREEELEELQEQLEDLESSIQELEKEI 358

                           90       100
                   ....*....|....*....|....
gi 1907136182  924 SSMEKNLKNIEEENKLIEEQNEAL 947
Cdd:pfam05667  359 KKLESSIKQVEEELEELKEQNEEL 382
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
886-960 1.25e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.20  E-value: 1.25e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907136182  886 SDVLENDEEIKQLNQEIRDLNESNSEMEAAMVQLQSQISSMEKNLKNIEEENKLIEEQNEALFLELSGLSQALIQ 960
Cdd:COG4372     73 SELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAE 147
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 890-958 2.21e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 41.67  E-value: 2.21e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907136182  890 ENDEEIKQLNQEIRDLNESNSEMEAAMVQLQSQISSMEKNLKNIEEENKLIEEQNEALFLELSGLSQAL 958
Cdd:COG4942     31 QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 893-941 2.81e-03

Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.


Pssm-ID: 462536 [Multi-domain]  Cd Length: 176  Bit Score: 39.92  E-value: 2.81e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1907136182  893 EEIKQLNQEIRDLNESNSEMEAAMVQLQSQISSMEKNLKNIEEENK-LIE 941
Cdd:pfam08614  113 EKLKDREEELREKRKLNQDLQDELVALQLQLNMAEEKLRKLEKENReLVE 162
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
890-947 2.98e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.04  E-value: 2.98e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907136182  890 ENDEEIKQLNQEIRDLNESNSEMEAAMVQLQSQISSMEKNLKNIEEENKLIEEQNEAL 947
Cdd:COG4372     70 QARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDL 127
t_SNARE smart00397
Helical region found in SNAREs; All alpha-helical motifs that form twisted and parallel ...
 885-938 3.78e-03

Helical region found in SNAREs; All alpha-helical motifs that form twisted and parallel four-helix bundles in target soluble N-ethylmaleimide-sensitive factor (NSF) attachment protein (SNAP) receptor proteins. This motif found in "Q-SNAREs".


Pssm-ID: 197699 [Multi-domain]  Cd Length: 66  Bit Score: 36.79  E-value: 3.78e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 1907136182   885 TSDVLENDEEIKQLNQEIRDLNESNSEMeAAMVQLQS-QISSMEKNLKNIEEENK 938
Cdd:smart00397    4 LAREEERDEELEQLEKSIQELKQIFLDM-GTELEEQGeQLDRIEDNVDDADVNLK 57
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 882-950 4.05e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 41.16  E-value: 4.05e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907136182  882 KFKTSDVLENDEEIKQLNQEIRDLNESNSEMEAAMVQLQSQISSMEKNLKNIEEENKLIEEQNEALFLE 950
Cdd:TIGR04523  492 KSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLE 560
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 884-947 4.87e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.58  E-value: 4.87e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907136182  884 KTSDVLENDEEIKQLNQEIRDLNESNSEMEAAMVQLQSQISSMEKNLKNIEEE----NKLIEEQNEAL 947
Cdd:COG3883     21 KQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEiaeaEAEIEERREEL 88
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 890-1015 5.82e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.13  E-value: 5.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136182  890 ENDEEIKQLNQEIRDLNESNSEMEAAMVQLQSQISSMEKNLKNIEEENKLIEEQNEALFLELSGLSQALIQSLANIrlph 969
Cdd:COG4942     24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL---- 99

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1907136182  970 mepicEQNFDAYVNTLTDMYSNQdcyQNPENKGLL--ETIKQAVRGIQ 1015
Cdd:COG4942    100 -----EAQKEELAELLRALYRLG---RQPPLALLLspEDFLDAVRRLQ 139
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 890-954 5.88e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 40.77  E-value: 5.88e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907136182  890 END---EEIKQLNQEIRDLNESNSEMEAAMVQLQSQISSMEKNLKNIEEENKLIEEQNEALFLELSGL 954
Cdd:TIGR04523  378 ENQsykQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDL 445
SNARE_Qa cd15840
SNARE motif, subgroup Qa; SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein ...
 890-935 9.64e-03

SNARE motif, subgroup Qa; SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins consist of coiled-coil helices (called SNARE motifs) which mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complex mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle. Their SNARE motifs form twisted and parallel heterotetrameric helix bundles. Examples for members of the Qa SNAREs are syntaxin 18, syntaxin 5, syntaxin 16, and syntaxin 1.


Pssm-ID: 277193 [Multi-domain]  Cd Length: 59  Bit Score: 35.57  E-value: 9.64e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1907136182  890 ENDEEIKQLNQEIRDLNESNSEMeAAMVQLQS-QISSMEKNLKNIEE 935
Cdd:cd15840      3 EREEEIREIESSIGEVNEIFKDL-ATLVTEQGeQIDNIENNIEEAAA 48
 
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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