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Conserved domains on  [gi|665391394|ref|NP_001285258|]
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highwire, isoform B [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PHR pfam08005
PHR domain; This domain is called PHR as it was original found in the proteins PAM, highwire ...
 1436-1586 5.63e-60

PHR domain; This domain is called PHR as it was original found in the proteins PAM, highwire and RPM. This domain can be duplicated in the highwire, PFAM and PRM sequence. The C-terminal region of the protein BTBD1 includes the PHR domain and is known to interact with Topoisomerase I, an enzyme which relaxes DNA supercoils.


:

Pssm-ID: 462339  Cd Length: 150  Bit Score: 204.01  E-value: 5.63e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391394  1436 NRFDNFGGGWGYSGHSVEAIRFSADTDIVICGFGMFGGRG---EYSCKLKLFDlggdGGGYEKEGILISETKEVPYECGA 1512
Cdd:pfam08005    1 NRFQSTGGGWGYSGGSPDAIRFSVDRDIFLVGFGLYGSIGgpaDYSVKIELID----GERWESLGEVLGENDTTFSSDGS 76

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665391394  1513 RSKHHILLPKPVSAVAGRWYLVWARIAGPSSDCGSCGQASVTTEDQVVFSFKSSKKANNGTDVNSGQIPAILYR 1586
Cdd:pfam08005   77 NDIFRVLFDEPVEIEPNVKYTASAKIKGPSSYYGTNGLREVTCDGGVTFQFSSSSLSNNGTSVNRGQIPELLYY 150
PHR pfam08005
PHR domain; This domain is called PHR as it was original found in the proteins PAM, highwire ...
 2015-2168 4.85e-41

PHR domain; This domain is called PHR as it was original found in the proteins PAM, highwire and RPM. This domain can be duplicated in the highwire, PFAM and PRM sequence. The C-terminal region of the protein BTBD1 includes the PHR domain and is known to interact with Topoisomerase I, an enzyme which relaxes DNA supercoils.


:

Pssm-ID: 462339  Cd Length: 150  Bit Score: 150.08  E-value: 4.85e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391394  2015 RFARCdvSRTWNTGNFGPDAIAFAVDRpGVAIAGAMVYSGSGS---YDYQLELlydntadlQPQHKWETLESVSGSYDQD 2091
Cdd:pfam08005    2 RFQST--GGGWGYSGGSPDAIRFSVDR-DIFLVGFGLYGSIGGpadYSVKIEL--------IDGERWESLGEVLGENDTT 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391394  2092 AV---HNDLAEIKFDHPVHIKENARYALRLCSQGARTCSGDAGMPAVRGPCGAQFHFYACDLSFNGTTPARGQLPCILYY 2168
Cdd:pfam08005   71 FSsdgSNDIFRVLFDEPVEIEPNVKYTASAKIKGPSSYYGTNGLREVTCDGGVTFQFSSSSLSNNGTSVNRGQIPELLYY 150
RING-H2_PHR cd16463
RING finger, H2 subclass, found in the PHR (Pam/Highwire/RPM-1) protein family; The PHR ...
 4988-5042 1.62e-34

RING finger, H2 subclass, found in the PHR (Pam/Highwire/RPM-1) protein family; The PHR protein family represents an evolutionally conserved family of large proteins including human E3 ubiquitin ligase protein associated with Myc (Pam) and its homologs, Phr1 in mouse, Highwire (HIW) in Drosophila, RPM-1 (regulator of presynaptic morphology 1) in Caenorhabditis elegans, and Esrom in zebrafish. Those proteins are large E3 ubiquitin ligases containing regulator of chromosome condensation (RCC) homology domains (RHD-1 and RHD-2) with inferred guanine exchange factor (GEF) activity, a Myc-binding domain, a B-box zinc finger, and a C-terminal C3H2C3-type RING-H2 finger with E3 ubiquitin (Ub) ligase activity. They play an important role in axon guidance and synaptogenesis. They regulate synapse formation and growth in mammals, zebrafish, Drosophila, and Caenorhabditis elegans, and may control a variety of signaling pathways, including cAMP signaling in mammalian cells, JNK/p38 MAPK signaling in Drosophila and C. elegans, and bone morphogenetic protein signaling in Drosophila. Pam also known as Myc-binding protein 2 (MYCBP2), or Pam/highwire/rpm-1 protein (PHR1), negatively regulates neuronal growth, synaptogenesis and synaptic plasticity by modulating several signaling pathways including the p38 MAPK signaling cascade. It also participates in receptor and ion channel internalization, such as regulating internalization of transient receptor potential vanilloid receptor 1 (TRPV1) in peripheral sensory neurons, as well as duration of thermal hyperalgesia through p38 MAPK. It interacts with neuron-specific electroneutral potassium (K+) and chloride (Cl-) cotransporter KCC2 and modulates its function. Moreover, Pam genetically interacts with Robo2 to modulate axon guidance in the olfactory system. It also associates with tuberous sclerosis complex (TSC) proteins, ubiquitinating TSC2 and regulating mammalian/mechanistic target of rapamycin (mTOR) signaling. Furthermore, Pam is the longest lasting nontranscriptional regulator of adenylyl cyclase activity, and can mediate sustained inhibition of cAMP signaling by sphingosine-1-phosphate. It is also involved in spinal nociceptive processing. Phr1 is an essential regulator of retinal ganglion cell projection during both dorsal lateral geniculate nucleus (dLGN) and superior colliculus (SC) topographic map development. RPM-1 positively regulates a Rab GTPase pathway to promote vesicular trafficking via late endosomes, thereby regulating synapse formation and axon termination. Esrom has E3 ligase activity and modulates the amount of phosphorylated Tuberin, a tumor suppressor, in growth cones. It is required for the formation of the retinotectal projection.


:

Pssm-ID: 438126 [Multi-domain]  Cd Length: 55  Bit Score: 127.84  E-value: 1.62e-34
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 665391394 4988 DDMCMICFVEALSCAPSIHLECGHVFHYHCCKAVLEKRWSGPRITFGFSLCPICK 5042
Cdd:cd16463     1 DDMCMICFTEALSAAPAIQLDCGHVFHLHCCRRVLENRWPGPRITFGFLKCPICK 55
Bbox2_MYCBP2 cd19799
B-box-type 2 zinc finger found in Myc-binding protein 2 (MYCBP2) and similar proteins; MYCBP2, ...
 4809-4857 7.92e-23

B-box-type 2 zinc finger found in Myc-binding protein 2 (MYCBP2) and similar proteins; MYCBP2, also termed protein associated with Myc (Pam), is an atypical E3 ubiquitin-protein ligase which specifically mediates ubiquitination of threonine and serine residues on target proteins, instead of ubiquitinating lysine residues. MYCBP2 harbors a B-box motif that shows high sequence similarity with B-Box-type zinc finger 2 found in tripartite motif-containing proteins (TRIMs). The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif.


:

Pssm-ID: 380857  Cd Length: 50  Bit Score: 94.00  E-value: 7.92e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 665391394 4809 PLCSNHDDGETAAIIQCETCGS-LCGDCDRFLHLNRKTRSHKRTVCKEEE 4857
Cdd:cd19799     1 PTCDNHDDGETAAIIFCCDCGNyLCAECDRFLHLHRKNRSHQRQVFKEEE 50
ATS1 super family cl34932
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 961-1050 6.06e-20

Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];


The actual alignment was detected with superfamily member COG5184:

Pssm-ID: 444065 [Multi-domain]  Cd Length: 343  Bit Score: 95.04  E-value: 6.06e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391394  961 QLTSSSPVVQVACGLHHTVVLTLAGEVYTFGSNQYGQLGSGDLQPVSGPVRVQVPGAISQVAAGSNHTVLLTSKGMVYTF 1040
Cdd:COG5184   244 QVAGLTGVVAIAAGGSHTCALKSDGTVWCWGDNSYGQLGDGTTTDRSTPVKVPGLSGVVAVAAGSSHTCALLTDGTVWCW 323

                          90
                  ....*....|
gi 665391394 1041 GNYQKGQLGR 1050
Cdd:COG5184   324 GDNAYGQLGD 333
ATS1 super family cl34932
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 589-784 1.45e-09

Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];


The actual alignment was detected with superfamily member COG5184:

Pssm-ID: 444065 [Multi-domain]  Cd Length: 343  Bit Score: 63.46  E-value: 1.45e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391394  589 PAPCRDADVDVMGMACGKEFGLVRASNGRVYYYGKSAA--LGLkcvgRTPTLKLTELVISKAANIVHVAVGHDgiHALLV 666
Cdd:COG5184   141 PVQVDAGLSGVVAIAAGGYHTCALKSDGTVWCWGANSYgqLGD----GTTTDRPTPVQVGGLSGVVAVAAGGD--HSCAL 214

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391394  667 NDDGTVFFAGTARRGEDGD-SSKNRRQPKAVkpkkmtkIDGHVVVHAACNNGTSAFVTKTGKLIMYGK---------DTA 736
Cdd:COG5184   215 KSDGTVWCWGSNSSGQLGDgTTTDRATPVQV-------AGLTGVVAIAAGGSHTCALKSDGTVWCWGDnsygqlgdgTTT 287

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 665391394  737 HCDAMGFVSELLeqHVTKVALGKAHCVALNAKGQLFSFGLNNKGQCGR 784
Cdd:COG5184   288 DRSTPVKVPGLS--GVVAVAAGSSHTCALLTDGTVWCWGDNAYGQLGD 333
 
Name Accession Description Interval E-value
PHR pfam08005
PHR domain; This domain is called PHR as it was original found in the proteins PAM, highwire ...
 1436-1586 5.63e-60

PHR domain; This domain is called PHR as it was original found in the proteins PAM, highwire and RPM. This domain can be duplicated in the highwire, PFAM and PRM sequence. The C-terminal region of the protein BTBD1 includes the PHR domain and is known to interact with Topoisomerase I, an enzyme which relaxes DNA supercoils.


Pssm-ID: 462339  Cd Length: 150  Bit Score: 204.01  E-value: 5.63e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391394  1436 NRFDNFGGGWGYSGHSVEAIRFSADTDIVICGFGMFGGRG---EYSCKLKLFDlggdGGGYEKEGILISETKEVPYECGA 1512
Cdd:pfam08005    1 NRFQSTGGGWGYSGGSPDAIRFSVDRDIFLVGFGLYGSIGgpaDYSVKIELID----GERWESLGEVLGENDTTFSSDGS 76

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665391394  1513 RSKHHILLPKPVSAVAGRWYLVWARIAGPSSDCGSCGQASVTTEDQVVFSFKSSKKANNGTDVNSGQIPAILYR 1586
Cdd:pfam08005   77 NDIFRVLFDEPVEIEPNVKYTASAKIKGPSSYYGTNGLREVTCDGGVTFQFSSSSLSNNGTSVNRGQIPELLYY 150
PHR pfam08005
PHR domain; This domain is called PHR as it was original found in the proteins PAM, highwire ...
 2015-2168 4.85e-41

PHR domain; This domain is called PHR as it was original found in the proteins PAM, highwire and RPM. This domain can be duplicated in the highwire, PFAM and PRM sequence. The C-terminal region of the protein BTBD1 includes the PHR domain and is known to interact with Topoisomerase I, an enzyme which relaxes DNA supercoils.


Pssm-ID: 462339  Cd Length: 150  Bit Score: 150.08  E-value: 4.85e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391394  2015 RFARCdvSRTWNTGNFGPDAIAFAVDRpGVAIAGAMVYSGSGS---YDYQLELlydntadlQPQHKWETLESVSGSYDQD 2091
Cdd:pfam08005    2 RFQST--GGGWGYSGGSPDAIRFSVDR-DIFLVGFGLYGSIGGpadYSVKIEL--------IDGERWESLGEVLGENDTT 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391394  2092 AV---HNDLAEIKFDHPVHIKENARYALRLCSQGARTCSGDAGMPAVRGPCGAQFHFYACDLSFNGTTPARGQLPCILYY 2168
Cdd:pfam08005   71 FSsdgSNDIFRVLFDEPVEIEPNVKYTASAKIKGPSSYYGTNGLREVTCDGGVTFQFSSSSLSNNGTSVNRGQIPELLYY 150
RING-H2_PHR cd16463
RING finger, H2 subclass, found in the PHR (Pam/Highwire/RPM-1) protein family; The PHR ...
 4988-5042 1.62e-34

RING finger, H2 subclass, found in the PHR (Pam/Highwire/RPM-1) protein family; The PHR protein family represents an evolutionally conserved family of large proteins including human E3 ubiquitin ligase protein associated with Myc (Pam) and its homologs, Phr1 in mouse, Highwire (HIW) in Drosophila, RPM-1 (regulator of presynaptic morphology 1) in Caenorhabditis elegans, and Esrom in zebrafish. Those proteins are large E3 ubiquitin ligases containing regulator of chromosome condensation (RCC) homology domains (RHD-1 and RHD-2) with inferred guanine exchange factor (GEF) activity, a Myc-binding domain, a B-box zinc finger, and a C-terminal C3H2C3-type RING-H2 finger with E3 ubiquitin (Ub) ligase activity. They play an important role in axon guidance and synaptogenesis. They regulate synapse formation and growth in mammals, zebrafish, Drosophila, and Caenorhabditis elegans, and may control a variety of signaling pathways, including cAMP signaling in mammalian cells, JNK/p38 MAPK signaling in Drosophila and C. elegans, and bone morphogenetic protein signaling in Drosophila. Pam also known as Myc-binding protein 2 (MYCBP2), or Pam/highwire/rpm-1 protein (PHR1), negatively regulates neuronal growth, synaptogenesis and synaptic plasticity by modulating several signaling pathways including the p38 MAPK signaling cascade. It also participates in receptor and ion channel internalization, such as regulating internalization of transient receptor potential vanilloid receptor 1 (TRPV1) in peripheral sensory neurons, as well as duration of thermal hyperalgesia through p38 MAPK. It interacts with neuron-specific electroneutral potassium (K+) and chloride (Cl-) cotransporter KCC2 and modulates its function. Moreover, Pam genetically interacts with Robo2 to modulate axon guidance in the olfactory system. It also associates with tuberous sclerosis complex (TSC) proteins, ubiquitinating TSC2 and regulating mammalian/mechanistic target of rapamycin (mTOR) signaling. Furthermore, Pam is the longest lasting nontranscriptional regulator of adenylyl cyclase activity, and can mediate sustained inhibition of cAMP signaling by sphingosine-1-phosphate. It is also involved in spinal nociceptive processing. Phr1 is an essential regulator of retinal ganglion cell projection during both dorsal lateral geniculate nucleus (dLGN) and superior colliculus (SC) topographic map development. RPM-1 positively regulates a Rab GTPase pathway to promote vesicular trafficking via late endosomes, thereby regulating synapse formation and axon termination. Esrom has E3 ligase activity and modulates the amount of phosphorylated Tuberin, a tumor suppressor, in growth cones. It is required for the formation of the retinotectal projection.


Pssm-ID: 438126 [Multi-domain]  Cd Length: 55  Bit Score: 127.84  E-value: 1.62e-34
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 665391394 4988 DDMCMICFVEALSCAPSIHLECGHVFHYHCCKAVLEKRWSGPRITFGFSLCPICK 5042
Cdd:cd16463     1 DDMCMICFTEALSAAPAIQLDCGHVFHLHCCRRVLENRWPGPRITFGFLKCPICK 55
Bbox2_MYCBP2 cd19799
B-box-type 2 zinc finger found in Myc-binding protein 2 (MYCBP2) and similar proteins; MYCBP2, ...
 4809-4857 7.92e-23

B-box-type 2 zinc finger found in Myc-binding protein 2 (MYCBP2) and similar proteins; MYCBP2, also termed protein associated with Myc (Pam), is an atypical E3 ubiquitin-protein ligase which specifically mediates ubiquitination of threonine and serine residues on target proteins, instead of ubiquitinating lysine residues. MYCBP2 harbors a B-box motif that shows high sequence similarity with B-Box-type zinc finger 2 found in tripartite motif-containing proteins (TRIMs). The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif.


Pssm-ID: 380857  Cd Length: 50  Bit Score: 94.00  E-value: 7.92e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 665391394 4809 PLCSNHDDGETAAIIQCETCGS-LCGDCDRFLHLNRKTRSHKRTVCKEEE 4857
Cdd:cd19799     1 PTCDNHDDGETAAIIFCCDCGNyLCAECDRFLHLHRKNRSHQRQVFKEEE 50
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 961-1050 6.06e-20

Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];


Pssm-ID: 444065 [Multi-domain]  Cd Length: 343  Bit Score: 95.04  E-value: 6.06e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391394  961 QLTSSSPVVQVACGLHHTVVLTLAGEVYTFGSNQYGQLGSGDLQPVSGPVRVQVPGAISQVAAGSNHTVLLTSKGMVYTF 1040
Cdd:COG5184   244 QVAGLTGVVAIAAGGSHTCALKSDGTVWCWGDNSYGQLGDGTTTDRSTPVKVPGLSGVVAVAAGSSHTCALLTDGTVWCW 323

                          90
                  ....*....|
gi 665391394 1041 GNYQKGQLGR 1050
Cdd:COG5184   324 GDNAYGQLGD 333
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
985-1031 8.11e-13

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 65.62  E-value: 8.11e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 665391394   985 GEVYTFGSNQYGQLGSGDLQPVSGPVRVQVPGA--ISQVAAGSNHTVLL 1031
Cdd:pfam00415    2 GRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGnkVVQVACGGDHTVAL 50
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 589-784 1.45e-09

Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];


Pssm-ID: 444065 [Multi-domain]  Cd Length: 343  Bit Score: 63.46  E-value: 1.45e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391394  589 PAPCRDADVDVMGMACGKEFGLVRASNGRVYYYGKSAA--LGLkcvgRTPTLKLTELVISKAANIVHVAVGHDgiHALLV 666
Cdd:COG5184   141 PVQVDAGLSGVVAIAAGGYHTCALKSDGTVWCWGANSYgqLGD----GTTTDRPTPVQVGGLSGVVAVAAGGD--HSCAL 214

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391394  667 NDDGTVFFAGTARRGEDGD-SSKNRRQPKAVkpkkmtkIDGHVVVHAACNNGTSAFVTKTGKLIMYGK---------DTA 736
Cdd:COG5184   215 KSDGTVWCWGSNSSGQLGDgTTTDRATPVQV-------AGLTGVVAIAAGGSHTCALKSDGTVWCWGDnsygqlgdgTTT 287

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 665391394  737 HCDAMGFVSELLeqHVTKVALGKAHCVALNAKGQLFSFGLNNKGQCGR 784
Cdd:COG5184   288 DRSTPVKVPGLS--GVVAVAAGSSHTCALLTDGTVWCWGDNAYGQLGD 333
zf-RING_2 pfam13639
Ring finger domain;
4989-5042 2.62e-05

Ring finger domain;


Pssm-ID: 433370 [Multi-domain]  Cd Length: 44  Bit Score: 44.32  E-value: 2.62e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 665391394  4989 DMCMICFVEALSCAPSIHLECGHVFHYHCCKAVLEKRwsgpritfgfSLCPICK 5042
Cdd:pfam13639    1 DECPICLEEFEEGDKVVVLPCGHHFHRECLDKWLRSS----------NTCPLCR 44
RCC1_2 pfam13540
Regulator of chromosome condensation (RCC1) repeat;
752-781 2.09e-04

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 463914 [Multi-domain]  Cd Length: 30  Bit Score: 41.26  E-value: 2.09e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 665391394   752 VTKVALGKAHCVALNAKGQLFSFGLNNKGQ 781
Cdd:pfam13540    1 VVSVAAGDNHTLALTSDGRVYCWGDNSYGQ 30
RING smart00184
Ring finger; E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and ...
 4991-5041 6.71e-04

Ring finger; E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and is likely to be a general function of this domain; Various RING fingers exhibit binding activity towards E2 ubiquitin-conjugating enzymes (Ubc' s)


Pssm-ID: 214546 [Multi-domain]  Cd Length: 40  Bit Score: 40.18  E-value: 6.71e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|.
gi 665391394   4991 CMICFvEALSCAPSIhLECGHVFHYHCCkavleKRWsgprITFGFSLCPIC 5041
Cdd:smart00184    1 CPICL-EEYLKDPVI-LPCGHTFCRSCI-----RKW----LESGNNTCPIC 40
BBOX smart00336
B-Box-type zinc finger;
4808-4850 6.64e-03

B-Box-type zinc finger;


Pssm-ID: 197662 [Multi-domain]  Cd Length: 42  Bit Score: 37.32  E-value: 6.64e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 665391394   4808 RPLCSNHDDgETAAIIqCETCGS-LCGDCDRFLHlnrktRSHKR 4850
Cdd:smart00336    3 APKCDSHGD-EPAEFF-CEECGAlLCRTCDEAEH-----RGHTV 39
 
Name Accession Description Interval E-value
PHR pfam08005
PHR domain; This domain is called PHR as it was original found in the proteins PAM, highwire ...
 1436-1586 5.63e-60

PHR domain; This domain is called PHR as it was original found in the proteins PAM, highwire and RPM. This domain can be duplicated in the highwire, PFAM and PRM sequence. The C-terminal region of the protein BTBD1 includes the PHR domain and is known to interact with Topoisomerase I, an enzyme which relaxes DNA supercoils.


Pssm-ID: 462339  Cd Length: 150  Bit Score: 204.01  E-value: 5.63e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391394  1436 NRFDNFGGGWGYSGHSVEAIRFSADTDIVICGFGMFGGRG---EYSCKLKLFDlggdGGGYEKEGILISETKEVPYECGA 1512
Cdd:pfam08005    1 NRFQSTGGGWGYSGGSPDAIRFSVDRDIFLVGFGLYGSIGgpaDYSVKIELID----GERWESLGEVLGENDTTFSSDGS 76

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665391394  1513 RSKHHILLPKPVSAVAGRWYLVWARIAGPSSDCGSCGQASVTTEDQVVFSFKSSKKANNGTDVNSGQIPAILYR 1586
Cdd:pfam08005   77 NDIFRVLFDEPVEIEPNVKYTASAKIKGPSSYYGTNGLREVTCDGGVTFQFSSSSLSNNGTSVNRGQIPELLYY 150
PHR pfam08005
PHR domain; This domain is called PHR as it was original found in the proteins PAM, highwire ...
 2015-2168 4.85e-41

PHR domain; This domain is called PHR as it was original found in the proteins PAM, highwire and RPM. This domain can be duplicated in the highwire, PFAM and PRM sequence. The C-terminal region of the protein BTBD1 includes the PHR domain and is known to interact with Topoisomerase I, an enzyme which relaxes DNA supercoils.


Pssm-ID: 462339  Cd Length: 150  Bit Score: 150.08  E-value: 4.85e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391394  2015 RFARCdvSRTWNTGNFGPDAIAFAVDRpGVAIAGAMVYSGSGS---YDYQLELlydntadlQPQHKWETLESVSGSYDQD 2091
Cdd:pfam08005    2 RFQST--GGGWGYSGGSPDAIRFSVDR-DIFLVGFGLYGSIGGpadYSVKIEL--------IDGERWESLGEVLGENDTT 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391394  2092 AV---HNDLAEIKFDHPVHIKENARYALRLCSQGARTCSGDAGMPAVRGPCGAQFHFYACDLSFNGTTPARGQLPCILYY 2168
Cdd:pfam08005   71 FSsdgSNDIFRVLFDEPVEIEPNVKYTASAKIKGPSSYYGTNGLREVTCDGGVTFQFSSSSLSNNGTSVNRGQIPELLYY 150
RING-H2_PHR cd16463
RING finger, H2 subclass, found in the PHR (Pam/Highwire/RPM-1) protein family; The PHR ...
 4988-5042 1.62e-34

RING finger, H2 subclass, found in the PHR (Pam/Highwire/RPM-1) protein family; The PHR protein family represents an evolutionally conserved family of large proteins including human E3 ubiquitin ligase protein associated with Myc (Pam) and its homologs, Phr1 in mouse, Highwire (HIW) in Drosophila, RPM-1 (regulator of presynaptic morphology 1) in Caenorhabditis elegans, and Esrom in zebrafish. Those proteins are large E3 ubiquitin ligases containing regulator of chromosome condensation (RCC) homology domains (RHD-1 and RHD-2) with inferred guanine exchange factor (GEF) activity, a Myc-binding domain, a B-box zinc finger, and a C-terminal C3H2C3-type RING-H2 finger with E3 ubiquitin (Ub) ligase activity. They play an important role in axon guidance and synaptogenesis. They regulate synapse formation and growth in mammals, zebrafish, Drosophila, and Caenorhabditis elegans, and may control a variety of signaling pathways, including cAMP signaling in mammalian cells, JNK/p38 MAPK signaling in Drosophila and C. elegans, and bone morphogenetic protein signaling in Drosophila. Pam also known as Myc-binding protein 2 (MYCBP2), or Pam/highwire/rpm-1 protein (PHR1), negatively regulates neuronal growth, synaptogenesis and synaptic plasticity by modulating several signaling pathways including the p38 MAPK signaling cascade. It also participates in receptor and ion channel internalization, such as regulating internalization of transient receptor potential vanilloid receptor 1 (TRPV1) in peripheral sensory neurons, as well as duration of thermal hyperalgesia through p38 MAPK. It interacts with neuron-specific electroneutral potassium (K+) and chloride (Cl-) cotransporter KCC2 and modulates its function. Moreover, Pam genetically interacts with Robo2 to modulate axon guidance in the olfactory system. It also associates with tuberous sclerosis complex (TSC) proteins, ubiquitinating TSC2 and regulating mammalian/mechanistic target of rapamycin (mTOR) signaling. Furthermore, Pam is the longest lasting nontranscriptional regulator of adenylyl cyclase activity, and can mediate sustained inhibition of cAMP signaling by sphingosine-1-phosphate. It is also involved in spinal nociceptive processing. Phr1 is an essential regulator of retinal ganglion cell projection during both dorsal lateral geniculate nucleus (dLGN) and superior colliculus (SC) topographic map development. RPM-1 positively regulates a Rab GTPase pathway to promote vesicular trafficking via late endosomes, thereby regulating synapse formation and axon termination. Esrom has E3 ligase activity and modulates the amount of phosphorylated Tuberin, a tumor suppressor, in growth cones. It is required for the formation of the retinotectal projection.


Pssm-ID: 438126 [Multi-domain]  Cd Length: 55  Bit Score: 127.84  E-value: 1.62e-34
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 665391394 4988 DDMCMICFVEALSCAPSIHLECGHVFHYHCCKAVLEKRWSGPRITFGFSLCPICK 5042
Cdd:cd16463     1 DDMCMICFTEALSAAPAIQLDCGHVFHLHCCRRVLENRWPGPRITFGFLKCPICK 55
Bbox2_MYCBP2 cd19799
B-box-type 2 zinc finger found in Myc-binding protein 2 (MYCBP2) and similar proteins; MYCBP2, ...
 4809-4857 7.92e-23

B-box-type 2 zinc finger found in Myc-binding protein 2 (MYCBP2) and similar proteins; MYCBP2, also termed protein associated with Myc (Pam), is an atypical E3 ubiquitin-protein ligase which specifically mediates ubiquitination of threonine and serine residues on target proteins, instead of ubiquitinating lysine residues. MYCBP2 harbors a B-box motif that shows high sequence similarity with B-Box-type zinc finger 2 found in tripartite motif-containing proteins (TRIMs). The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif.


Pssm-ID: 380857  Cd Length: 50  Bit Score: 94.00  E-value: 7.92e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 665391394 4809 PLCSNHDDGETAAIIQCETCGS-LCGDCDRFLHLNRKTRSHKRTVCKEEE 4857
Cdd:cd19799     1 PTCDNHDDGETAAIIFCCDCGNyLCAECDRFLHLHRKNRSHQRQVFKEEE 50
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 961-1050 6.06e-20

Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];


Pssm-ID: 444065 [Multi-domain]  Cd Length: 343  Bit Score: 95.04  E-value: 6.06e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391394  961 QLTSSSPVVQVACGLHHTVVLTLAGEVYTFGSNQYGQLGSGDLQPVSGPVRVQVPGAISQVAAGSNHTVLLTSKGMVYTF 1040
Cdd:COG5184   244 QVAGLTGVVAIAAGGSHTCALKSDGTVWCWGDNSYGQLGDGTTTDRSTPVKVPGLSGVVAVAAGSSHTCALLTDGTVWCW 323

                          90
                  ....*....|
gi 665391394 1041 GNYQKGQLGR 1050
Cdd:COG5184   324 GDNAYGQLGD 333
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 961-1050 2.93e-19

Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];


Pssm-ID: 444065 [Multi-domain]  Cd Length: 343  Bit Score: 92.73  E-value: 2.93e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391394  961 QLTSSSPVVQVACGLHHTVVLTLAGEVYTFGSNQYGQLGSGDLQPVSGPVRVQVPGAISQVAAGSNHTVLLTSKGMVYTF 1040
Cdd:COG5184    43 RVPGLSNVVAVAAGGDHTCALKADGTVWCWGNNSYGQLGDGTTTDRTTPVKVPGLTGVVAVAAGYYHSCALKSDGTVWCW 122

                          90
                  ....*....|
gi 665391394 1041 GNYQKGQLGR 1050
Cdd:COG5184   123 GDNSSGQLGD 132
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 961-1068 4.24e-19

Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];


Pssm-ID: 444065 [Multi-domain]  Cd Length: 343  Bit Score: 92.35  E-value: 4.24e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391394  961 QLTSSSPVVQVACGLHHTVVLTLAGEVYTFGSNQYGQLGSGDLQPVSGPVRVQVPGAISQVAAGSNHTVLLTSKGMVYTF 1040
Cdd:COG5184   194 QVGGLSGVVAVAAGGDHSCALKSDGTVWCWGSNSSGQLGDGTTTDRATPVQVAGLTGVVAIAAGGSHTCALKSDGTVWCW 273

                          90       100
                  ....*....|....*....|....*...
gi 665391394 1041 GNYQKGQLGRLPSDYGLKPPPQDDDSPV 1068
Cdd:COG5184   274 GDNSYGQLGDGTTTDRSTPVKVPGLSGV 301
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 966-1049 3.27e-18

Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];


Pssm-ID: 444065 [Multi-domain]  Cd Length: 343  Bit Score: 89.65  E-value: 3.27e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391394  966 SPVVQVACGLHHTVVLTLAGEVYTFGSNQYGQLGSGDLQPVSGPVRVQVPGAISQVAAGSNHTVLLTSKGMVYTFGNYQK 1045
Cdd:COG5184   149 SGVVAIAAGGYHTCALKSDGTVWCWGANSYGQLGDGTTTDRPTPVQVGGLSGVVAVAAGGDHSCALKSDGTVWCWGSNSS 228


                  ....
gi 665391394 1046 GQLG 1049
Cdd:COG5184   229 GQLG 232
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 969-1068 1.32e-17

Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];


Pssm-ID: 444065 [Multi-domain]  Cd Length: 343  Bit Score: 87.72  E-value: 1.32e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391394  969 VQVACGLHHTVVLTLAGEVYTFGSNQYGQLGSGDLQPVSGPVRVQVPGAISQVAAGSNHTVLLTSKGMVYTFGNYQKGQL 1048
Cdd:COG5184     1 TQVAAGGSHSCALKSDGTVWCWGDNSYGQLGDGTTTDRSTPVRVPGLSNVVAVAAGGDHTCALKADGTVWCWGNNSYGQL 80

                          90       100
                  ....*....|....*....|
gi 665391394 1049 GRLPSDYGLKPPPQDDDSPV 1068
Cdd:COG5184    81 GDGTTTDRTTPVKVPGLTGV 100
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
985-1031 8.11e-13

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 65.62  E-value: 8.11e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 665391394   985 GEVYTFGSNQYGQLGSGDLQPVSGPVRVQVPGA--ISQVAAGSNHTVLL 1031
Cdd:pfam00415    2 GRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGnkVVQVACGGDHTVAL 50
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 598-1010 1.39e-10

Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];


Pssm-ID: 444065 [Multi-domain]  Cd Length: 343  Bit Score: 66.54  E-value: 1.39e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391394  598 DVMGMACGKEFGLVRASNGRVY-----YYGkSAALGLKCVGRTPTLkltelvISKAANIVHVAVGHDgiHALLVNDDGTV 672
Cdd:COG5184    49 NVVAVAAGGDHTCALKADGTVWcwgnnSYG-QLGDGTTTDRTTPVK------VPGLTGVVAVAAGYY--HSCALKSDGTV 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391394  673 FFAGTARRGEDGD-SSKNRRQPKAVKPkkmtkiDGHVVVHAACNNGTSAFVTKTGKLIMYGK---------DTAHCDAMG 742
Cdd:COG5184   120 WCWGDNSSGQLGDgTTTNRLTPVQVDA------GLSGVVAIAAGGYHTCALKSDGTVWCWGAnsygqlgdgTTTDRPTPV 193

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391394  743 FVSELleQHVTKVALGKAHCVALNAKGQLFSFGLNNKGQCGR--IFNKLQPVKdVPPFASSSTAAAcfasllpldkrlkl 820
Cdd:COG5184   194 QVGGL--SGVVAVAAGGDHSCALKSDGTVWCWGSNSSGQLGDgtTTDRATPVQ-VAGLTGVVAIAA-------------- 256

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391394  821 dfstlcdyddhnlvqgqcrvcvicrectGYNVSCvsALnvpldqRLAGSICPCGHGDAGcakcglcaacialQDSDEAKT 900
Cdd:COG5184   257 ----------------------------GGSHTC--AL------KSDGTVWCWGDNSYG-------------QLGDGTTT 287

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391394  901 elkpppsdvqqrqqrsktlimrrkerkgeletgaaggGAATPTdldkdppRVAPLapqllqltssSPVVQVACGLHHTVV 980
Cdd:COG5184   288 -------------------------------------DRSTPV-------KVPGL----------SGVVAVAAGSSHTCA 313

                         410       420       430
                  ....*....|....*....|....*....|
gi 665391394  981 LTLAGEVYTFGSNQYGQLGSGDLQPVSGPV 1010
Cdd:COG5184   314 LLTDGTVWCWGDNAYGQLGDGTTTDRSTPV 343
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 589-784 1.45e-09

Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];


Pssm-ID: 444065 [Multi-domain]  Cd Length: 343  Bit Score: 63.46  E-value: 1.45e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391394  589 PAPCRDADVDVMGMACGKEFGLVRASNGRVYYYGKSAA--LGLkcvgRTPTLKLTELVISKAANIVHVAVGHDgiHALLV 666
Cdd:COG5184   141 PVQVDAGLSGVVAIAAGGYHTCALKSDGTVWCWGANSYgqLGD----GTTTDRPTPVQVGGLSGVVAVAAGGD--HSCAL 214

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391394  667 NDDGTVFFAGTARRGEDGD-SSKNRRQPKAVkpkkmtkIDGHVVVHAACNNGTSAFVTKTGKLIMYGK---------DTA 736
Cdd:COG5184   215 KSDGTVWCWGSNSSGQLGDgTTTDRATPVQV-------AGLTGVVAIAAGGSHTCALKSDGTVWCWGDnsygqlgdgTTT 287

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 665391394  737 HCDAMGFVSELLeqHVTKVALGKAHCVALNAKGQLFSFGLNNKGQCGR 784
Cdd:COG5184   288 DRSTPVKVPGLS--GVVAVAAGSSHTCALLTDGTVWCWGDNAYGQLGD 333
RCC1_2 pfam13540
Regulator of chromosome condensation (RCC1) repeat;
968-997 3.77e-08

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 463914 [Multi-domain]  Cd Length: 30  Bit Score: 52.04  E-value: 3.77e-08
                           10        20        30
                   ....*....|....*....|....*....|
gi 665391394   968 VVQVACGLHHTVVLTLAGEVYTFGSNQYGQ 997
Cdd:pfam13540    1 VVSVAAGDNHTLALTSDGRVYCWGDNSYGQ 30
RING-H2 cd16448
H2 subclass of RING (RING-H2) fingers and its variants; The RING finger is a specialized type ...
 4991-5042 4.25e-07

H2 subclass of RING (RING-H2) fingers and its variants; The RING finger is a specialized type of Zn-finger of 40 to 60 residues that binds two atoms of zinc. It is defined by the "cross-brace" motif that chelates zinc atoms by eight amino acid residues, typically Cys or His, arranged in a characteristic spacing. Canonical RING motifs have been categorized into two major subclasses, RING-HC (C3HC4-type) and RING-H2 (C3H2C3-type), according to their Cys/His content. There are also many variants of RING fingers: some have different Cys/His patterns while some lack a single Cys or His residue at typical Zn ligand positions (the fourth or eighth zinc ligand is prevalently exchanged for an Asp, which can indeed chelate Zn in a RING finger as well). This family corresponds to the H2 subclass of RING (RING-H2) finger proteins that are characterized by containing C3H2C3-type canonical RING-H2 fingers or noncanonical RING-H2 finger variants, including C4HC3- (RING-CH alias RINGv), C3H3C2-, C3H2C2D-, C3DHC3-, and C4HC2H-type modified RING-H2 fingers. The canonical RING-H2 finger has been defined as C-X2-C-X(9-39)-C-X(1-3)-H-X(2-3)-H-X2-C-X(4-48)-C-X2-C, X is any amino acid and the number of X residues varies in different fingers. It binds two Zn ions in a unique "cross-brace" arrangement, which distinguishes it from tandem zinc fingers and other similar motifs. RING-H2 finger can be found in a group of diverse proteins with a variety of cellular functions, including oncogenesis, development, viral replication, signal transduction, the cell cycle and apoptosis. Many of them are ubiquitin-protein ligases (E3s) that serves as a scaffold for binding to ubiquitin-conjugating enzymes (E2s, also referred to as ubiquitin carrier proteins or UBCs) in close proximity to substrate proteins, which enables efficient transfer of ubiquitin from E2 to the substrates.


Pssm-ID: 438112 [Multi-domain]  Cd Length: 43  Bit Score: 49.32  E-value: 4.25e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 665391394 4991 CMICFVEALSCAPSIHLECGHVFHYHCCKAVLEkrwsgpritFGFSLCPICK 5042
Cdd:cd16448     1 CVICLEEFEEGDVVRLLPCGHVFHLACILRWLE---------SGNNTCPLCR 43
RCC1_2 pfam13540
Regulator of chromosome condensation (RCC1) repeat;
1018-1047 6.37e-06

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 463914 [Multi-domain]  Cd Length: 30  Bit Score: 45.49  E-value: 6.37e-06
                           10        20        30
                   ....*....|....*....|....*....|
gi 665391394  1018 ISQVAAGSNHTVLLTSKGMVYTFGNYQKGQ 1047
Cdd:pfam13540    1 VVSVAAGDNHTLALTSDGRVYCWGDNSYGQ 30
zf-RING_2 pfam13639
Ring finger domain;
4989-5042 2.62e-05

Ring finger domain;


Pssm-ID: 433370 [Multi-domain]  Cd Length: 44  Bit Score: 44.32  E-value: 2.62e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 665391394  4989 DMCMICFVEALSCAPSIHLECGHVFHYHCCKAVLEKRwsgpritfgfSLCPICK 5042
Cdd:pfam13639    1 DECPICLEEFEEGDKVVVLPCGHHFHRECLDKWLRSS----------NTCPLCR 44
RING-H2_RHA1-like cd23121
RING finger, H2 subclass, found in Arabidopsis thaliana RING-H2 finger A1a (RHA1A), A1b (RHA1B) ...
 4988-5044 4.06e-05

RING finger, H2 subclass, found in Arabidopsis thaliana RING-H2 finger A1a (RHA1A), A1b (RHA1B) and similar proteins; This subfamily includes Arabidopsis thaliana RHA1A, RHA1B and XERICO. RHA1A is a probable E3 ubiquitin-protein ligase that may possess E3 ubiquitin ligase activity in vitro. RHA1B possesses E3 ubiquitin-protein ligase activity when associated with the E2 enzyme UBC8 in vitro. XERICO functions on abscisic acid homeostasis at post-translational level, probably through ubiquitin/proteasome-dependent substrate-specific degradation. Members of this subfamily contain a C3H2C3-type RING-H2 finger.


Pssm-ID: 438483 [Multi-domain]  Cd Length: 50  Bit Score: 44.01  E-value: 4.06e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391394 4988 DDMCMIC---FVEalSCAPSIHLECGHVFHYHCckavLEkRWsgprITFGFSLCPICKAD 5044
Cdd:cd23121     1 DDCCAIClsdFNS--DEKLRQLPKCGHIFHHHC----LD-RW----IRYNKITCPLCRAD 49
RCC1_2 pfam13540
Regulator of chromosome condensation (RCC1) repeat;
752-781 2.09e-04

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 463914 [Multi-domain]  Cd Length: 30  Bit Score: 41.26  E-value: 2.09e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 665391394   752 VTKVALGKAHCVALNAKGQLFSFGLNNKGQ 781
Cdd:pfam13540    1 VVSVAAGDNHTLALTSDGRVYCWGDNSYGQ 30
RING smart00184
Ring finger; E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and ...
 4991-5041 6.71e-04

Ring finger; E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and is likely to be a general function of this domain; Various RING fingers exhibit binding activity towards E2 ubiquitin-conjugating enzymes (Ubc' s)


Pssm-ID: 214546 [Multi-domain]  Cd Length: 40  Bit Score: 40.18  E-value: 6.71e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|.
gi 665391394   4991 CMICFvEALSCAPSIhLECGHVFHYHCCkavleKRWsgprITFGFSLCPIC 5041
Cdd:smart00184    1 CPICL-EEYLKDPVI-LPCGHTFCRSCI-----RKW----LESGNNTCPIC 40
RING-H2_synoviolin cd16479
RING finger, H2 subclass, found in synoviolin and similar proteins; Synoviolin, also known as ...
 4988-5042 1.49e-03

RING finger, H2 subclass, found in synoviolin and similar proteins; Synoviolin, also known as synovial apoptosis inhibitor 1 (Syvn1), Hrd1, or Der3, is an endoplasmic reticulum (ER)-anchoring E3 ubiquitin ligase that functions as a suppressor of ER stress-induced apoptosis and plays a role in homeostasis maintenance. It also targets tumor suppressor gene p53 for proteasomal degradation, suggesting crosstalk between ER associated degradation (ERAD) and p53 mediated apoptotic pathway under ER stress. Moreover, synoviolin controls body weight and mitochondrial biogenesis through negative regulation of the thermogenic coactivator peroxisome proliferator-activated receptor coactivator (PGC)-1beta. It upregulates amyloid beta production by targeting a negative regulator of gamma-secretase, Retention in endoplasmic reticulum 1 (Rer1), for degradation. It is also involved in the degradation of endogenous immature nicastrin, and affects amyloid beta-protein generation. Moreover, synoviolin is highly expressed in rheumatoid synovial cells and may be involved in the pathogenesis of rheumatoid arthritis (RA). It functions as an anti-apoptotic factor that is responsible for the outgrowth of synovial cells during the development of RA. It promotes inositol-requiring enzyme 1 (IRE1) ubiquitination and degradation in synovial fibroblasts with collagen-induced arthritis. Furthermore, the upregulation of synoviolin may represent a protective response against neurodegeneration in Parkinson's disease (PD). In addition, synoviolin is involved in liver fibrogenesis. Synoviolin contains a C3H2C2-type RING-H2 finger.


Pssm-ID: 438142 [Multi-domain]  Cd Length: 43  Bit Score: 39.26  E-value: 1.49e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 665391394 4988 DDMCMICFVEALSCAPSihLECGHVFHYHCCKAVLEKRWSgpritfgfslCPICK 5042
Cdd:cd16479     1 DNTCIICREEMTVGAKK--LPCGHIFHLSCLRSWLQRQQT----------CPTCR 43
mRING-HC-C3HC5_MAPL cd16648
Modified RING finger, HC subclass (C3HC5-type), found in mitochondrial-anchored protein ligase ...
 4988-5045 6.15e-03

Modified RING finger, HC subclass (C3HC5-type), found in mitochondrial-anchored protein ligase (MAPL) and similar proteins; MAPL, also known as MULAN, mitochondrial ubiquitin ligase activator of NFKB 1, E3 SUMO-protein ligase MUL1, E3 ubiquitin-protein ligase MUL1, growth inhibition and death E3 ligase (GIDE), putative NF-kappa-B-activating protein 266, or RING finger protein 218 (RNF218), is a multifunctional mitochondrial outer membrane protein involved in several processes specific to metazoan (multicellular animal) cells, such as NF-kappaB activation, innate immunity and antiviral signaling, suppression of PINK1/parkin defects, mitophagy in skeletal muscle, and caspase-dependent apoptosis. MAPL contains a unique BAM (beside a membrane)/GIDE (growth inhibition death E3 ligase) domain and a C-terminal modified cytosolic C3HC5-type RING-HC finger which is distinguished from typical C3HC4-type RING-HC finger due to the existence of the additional cysteine residue in the middle portion of the RING finger domain.


Pssm-ID: 438310 [Multi-domain]  Cd Length: 52  Bit Score: 37.83  E-value: 6.15e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 665391394 4988 DDMCMICFVEALSCapsIHLECGHVFhyhCCKAVLEKRWSGPRitfgfslCPICKADI 5045
Cdd:cd16648     1 DNACVICLSNPRSC---VFLECGHVC---SCIECYEALPSPKK-------CPICRSFI 45
RING-H2_RNF103 cd16473
RING finger, H2 subclass, found in RING finger protein 103 (RNF103) and similar proteins; ...
 4985-5045 6.62e-03

RING finger, H2 subclass, found in RING finger protein 103 (RNF103) and similar proteins; RNF103, also known as KF-1 or zinc finger protein 103 homolog (Zfp-103), is an endoplasmic reticulum (ER)-resident E3 ubiquitin-protein ligase that is widely expressed in many different organs, including brain, heart, kidney, spleen, and lung. It is involved in the ER-associated degradation (ERAD) pathway by interacting with components of the ERAD pathway, including Derlin-1 and VCP. RNF103 contains several hydrophobic regions at its N-terminal and middle regions, as well as a C-terminal C3H2C3-type RING-H2 finger.


Pssm-ID: 438136 [Multi-domain]  Cd Length: 55  Bit Score: 37.64  E-value: 6.62e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665391394 4985 QDADDMCMICFVEALSCAPSIHLECGHVFHYHCCKAVLEKrwsgpritfGFSLCPICKADI 5045
Cdd:cd16473     1 MLECEECAICLENYQNGDLLRGLPCGHVFHQNCIDVWLER---------DNHCCPVCRWPV 52
BBOX smart00336
B-Box-type zinc finger;
4808-4850 6.64e-03

B-Box-type zinc finger;


Pssm-ID: 197662 [Multi-domain]  Cd Length: 42  Bit Score: 37.32  E-value: 6.64e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 665391394   4808 RPLCSNHDDgETAAIIqCETCGS-LCGDCDRFLHlnrktRSHKR 4850
Cdd:smart00336    3 APKCDSHGD-EPAEFF-CEECGAlLCRTCDEAEH-----RGHTV 39
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
957-981 7.90e-03

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 37.50  E-value: 7.90e-03
                           10        20
                   ....*....|....*....|....*
gi 665391394   957 PQLLQLTSSSPVVQVACGLHHTVVL 981
Cdd:pfam00415   26 PQKVEGLSGNKVVQVACGGDHTVAL 50
RING-H2_TTC3 cd16481
RING finger, H2 subclass, found in Tetratricopeptide repeat protein 3 (TTC3) and similar ...
 4991-5045 9.24e-03

RING finger, H2 subclass, found in Tetratricopeptide repeat protein 3 (TTC3) and similar proteins; TTC3, also known as protein DCRR1, TPR repeat protein D, TPR repeat protein 3, or RING finger protein 105 (RNF105), is an E3 ubiquitin-protein ligase encoded by a gene within the Down syndrome (DS) critical region on chromosome 21. It affects differentiation and Golgi compactness in neurons through specific actin-regulating pathways. It inhibits the neuronal-like differentiation of pheocromocytoma cells by activating RhoA and by binding to Citron proteins. TTC3 is an Akt-specific E3 ligase that binds to phosphorylated Akt and facilitates its ubiquitination and degradation within the nucleus. It contains four N-terminal TPR motifs, a potential coiled-coil region and a Citron binding region in the central part, and a C-terminal C3H2C2-type RING-H2 finger.


Pssm-ID: 438144 [Multi-domain]  Cd Length: 45  Bit Score: 36.94  E-value: 9.24e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 665391394 4991 CMICFvEALSCAPSIHLECGHVFHYHCCKAVLEKRwsgpritfgfSLCPICKADI 5045
Cdd:cd16481     2 CIICH-DDLKPDQLAKLECGHIFHKECIKQWLKEQ----------STCPTCRVHV 45
 
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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