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Conserved domains on  [gi|2119497975|ref|XP_044525223|]
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E3 ubiquitin-protein ligase HERC2 [Gracilinanus agilis]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
APC10-HERC2 cd08664
APC10-like DOC1 domain present in HERC2 (HECT domain and RLD2); This model represents the ...
2766-2911 2.79e-89

APC10-like DOC1 domain present in HERC2 (HECT domain and RLD2); This model represents the APC10/DOC1 domain present in HERC2 (HECT domain and RLD2), a large multi-domain protein with three RCC1-like domains (RLDs), additional internal domains including a zinc finger ZZ-type and Cyt-b5 (Cytochrome b5-like Heme/Steroid binding) domains, and a C-terminal HECT (Homologous to the E6-AP Carboxyl Terminus) domain. The APC10/DOC1 domain of HERC2 is a homolog of the APC10 subunit and the DOC1 domain present in E3 ubiquitin ligases which mediate substrate ubiquitination (or ubiquitylation), a component of the ubiquitin-26S proteasome pathway for selective proteolytic degradation. As suggested by structural relationships between HERC2 and other proteins such as HERC1, the proposed role for HERC2 in protein trafficking and degradation pathways is consistent with observations that mutations in HERC2 lead to neuromuscular secretory vesicle and sperm acrosome defects, other developmental abnormalities, and juvenile lethality of jdf2 mice. Recent studies have shown that the protein complex, HERC2-RNF8, coordinates ubiquitin-dependent assembly of DNA repair factors on damaged chromosomes.


:

Pssm-ID: 176485  Cd Length: 152  Bit Score: 287.73  E-value: 2.79e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497975 2766 KQLKRCHSSQP------GMLLDNWSRIVKNLNVSSSVNQASRLIDGSEPCWQSSGSQGKHWIRLEIFPDVLVHRLKMIVD 2839
Cdd:cd08664      1 GKPGKYHRNDPelnageGDLIDDWSRCVRSLTVSSNENQAKRLIDGSGSYWQSSGSQGKHWIRLELHPDVLIHSLKIIVD 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2119497975 2840 PADSSYMPSLVVVSGGNSLNNLIELKTININPADTTVPLLTDCTEYHRYIEVAIKQCRSSGIDCKIHGLIIL 2911
Cdd:cd08664     81 PADSSYMPSLVVVSGGDSLNSLKELKTINVNATDTLVTLLQDVKEYYRYIEIAIKQCRNNGIDCKIHGLNII 152
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
2962-3302 1.39e-78

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: 265.30  E-value: 1.39e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497975 2962 VFVWGLNDKDQLGGLKGSKIKVPSFSETLSalNVVQVAGGSKSLFAVTVEGKVYACGEATNGRLGLGiSSGTVPIPRQIT 3041
Cdd:COG5184     19 VWCWGDNSYGQLGDGTTTDRSTPVRVPGLS--NVVAVAAGGDHTCALKADGTVWCWGNNSYGQLGDG-TTTDRTTPVKVP 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497975 3042 ALSNYVvkkvAVHSGGRHAMALTVDGKVFSWGEGDDGKLGHFSRMNCDKPRLIeALKTKRIRDIACGSSHSAAITSSGEL 3121
Cdd:COG5184     96 GLTGVV----AVAAGYYHSCALKSDGTVWCWGDNSSGQLGDGTTTNRLTPVQV-DAGLSGVVAIAAGGYHTCALKSDGTV 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497975 3122 YTWGLGEYGRLGHGDNTTQLKPkmVKVLLGHRVIQVACGsrDAQTLALTDEGLVFSWGDGDFGKLGRGGSEGCNIPQNIE 3201
Cdd:COG5184    171 WCWGANSYGQLGDGTTTDRPTP--VQVGGLSGVVAVAAG--GDHSCALKSDGTVWCWGSNSSGQLGDGTTTDRATPVQVA 246
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497975 3202 rlNGQGVCQIECGAQFSLALTKSGVVWTWGKGDYFRLGHGTDVHVRKPQVVEGLRGkkIVHVAVGALHCLAVTDTGQVYA 3281
Cdd:COG5184    247 --GLTGVVAIAAGGSHTCALKSDGTVWCWGDNSYGQLGDGTTTDRSTPVKVPGLSG--VVAVAAGSSHTCALLTDGTVWC 322
                          330       340
                   ....*....|....*....|.
gi 2119497975 3282 WGDNDHGQQGNGTTTVNRKPT 3302
Cdd:COG5184    323 WGDNAYGQLGDGTTTDRSTPV 343
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
3947-4295 8.93e-78

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: 262.99  E-value: 8.93e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497975 3947 WTLSAGGS--------GTIYGWGHNHRGQLGGieGAKVKVPTPCEALAALRPIQLIGGEQTLFAVTADGKLYATGYGAGG 4018
Cdd:COG5184      1 TQVAAGGShscalksdGTVWCWGDNSYGQLGD--GTTTDRSTPVRVPGLSNVVAVAAGGDHTCALKADGTVWCWGNNSYG 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497975 4019 RLGIGGTESVSTPTLLESIQHVfikkVAVNSGGKHCLALSSEGEVYSWGEAEDGKLGHGNRSPCDRPRVIeSLRGIEVVD 4098
Cdd:COG5184     79 QLGDGTTTDRTTPVKVPGLTGV----VAVAAGYYHSCALKSDGTVWCWGDNSSGQLGDGTTTNRLTPVQV-DAGLSGVVA 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497975 4099 IAAGGAHSACITAAGDLYTWGKGRYGRLGHGDSEDQLKPKLVEALQGyrVIDIACGsgDAQTLCLTDDDTVWSWGDGDYG 4178
Cdd:COG5184    154 IAAGGYHTCALKSDGTVWCWGANSYGQLGDGTTTDRPTPVQVGGLSG--VVAVAAG--GDHSCALKSDGTVWCWGSNSSG 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497975 4179 KLGRGGSDGCKVPMKIDSLTGlgVVKVECGSQFSVALTKSGSVYTWGKGDYHRLGHGSDDHVRRPRQVQGLQGkkVIAIA 4258
Cdd:COG5184    230 QLGDGTTTDRATPVQVAGLTG--VVAIAAGGSHTCALKSDGTVWCWGDNSYGQLGDGTTTDRSTPVKVPGLSG--VVAVA 305
                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 2119497975 4259 TGSLHCVCCTEDGEVYTWGDNDEGQLGDGTTNAIQRP 4295
Cdd:COG5184    306 AGSSHTCALLTDGTVWCWGDNAYGQLGDGTTTDRSTP 342
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
443-741 6.39e-62

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: 217.15  E-value: 6.39e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497975  443 PIQCEGLANlgITQIACAEKRFLILSRNGRVYM----------QAYNSDTLGPQLVQGLAsrNIVKIAAhsDGHHYLALA 512
Cdd:COG5184     41 PVRVPGLSN--VVAVAAGGDHTCALKADGTVWCwgnnsygqlgDGTTTDRTTPVKVPGLT--GVVAVAA--GYYHSCALK 114
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497975  513 ATGEVFSWGCGDGGRLGHGDTVPLEEPKMISA-LSGkqagkhVVHIACGSTYSAAITAEGELYTWGRGNYGRLGHGSSED 591
Cdd:COG5184    115 SDGTVWCWGDNSSGQLGDGTTTNRLTPVQVDAgLSG------VVAIAAGGYHTCALKSDGTVWCWGANSYGQLGDGTTTD 188
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497975  592 QTIPMLVTGLKGlkVIDVSCgsGDAQTLAVTENGQVWSWGDGDYGKLGRGGSDGCKTPKLIEKLQdlDVVKVRCGSQFSV 671
Cdd:COG5184    189 RPTPVQVGGLSG--VVAVAA--GGDHSCALKSDGTVWCWGSNSSGQLGDGTTTDRATPVQVAGLT--GVVAIAAGGSHTC 262
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497975  672 ALTKDGQVYSWGKGDNQRLGHGTEEHVRYPKLLEGLQGkkVVDVAAGSTHCLALTEDSEVHSWGSNDQCQ 741
Cdd:COG5184    263 ALKSDGTVWCWGDNSYGQLGDGTTTDRSTPVKVPGLSG--VVAVAAGSSHTCALLTDGTVWCWGDNAYGQ 330
Cul7 pfam11515
Mouse development and cellular proliferation protein Cullin-7; The Cullin Ring Ligase family ...
2555-2632 1.66e-46

Mouse development and cellular proliferation protein Cullin-7; The Cullin Ring Ligase family member, Cul7, is required for normal mouse development and cellular proliferation. Cul7 has a CPH domain which is a p53 interaction domain. The CPH domain interaction surface of P53 is present in the tetramerization domain.


:

Pssm-ID: 463286  Cd Length: 78  Bit Score: 162.52  E-value: 1.66e-46
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2119497975 2555 RADFLSNDDYAVYVRENIQVGMMVRCCRTYEEVCEGDIGKVIKLDRDGLHDLNVQCDWQQKGSTYWVRYIHVELIGFP 2632
Cdd:pfam11515    1 RSDFASRDDYAEYVRDNLAPGMRVRCCRDYEEVSAGDEGEVIQSNRGGLHDLNVQVDWQSKGRTYWVHWHHVEILGFP 78
ZZ_HERC2 cd02344
Zinc finger, ZZ type. Zinc finger present in HERC2 and related proteins. HERC2 is a potential ...
2707-2751 3.83e-29

Zinc finger, ZZ type. Zinc finger present in HERC2 and related proteins. HERC2 is a potential E3 ubiquitin protein ligase and/or guanine nucleotide exchange factor. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding.


:

Pssm-ID: 239084  Cd Length: 45  Bit Score: 111.91  E-value: 3.83e-29
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 2119497975 2707 VTCDGCQMFPINGPRFKCRNCDDFDFCETCFKTRKHNTRHTFGRI 2751
Cdd:cd02344      1 VTCDGCQMFPINGPRFKCRNCDDFDFCENCFKTRKHNTRHTFGRI 45
MIB_HERC2 pfam06701
Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain ...
1872-1932 1.03e-27

Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain (either Ring or Hect).


:

Pssm-ID: 461991  Cd Length: 66  Bit Score: 108.46  E-value: 1.03e-27
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2119497975 1872 GTRVMRGVDWKWGDQDGPPPGLGRVI-----GELGEDGWIRVQWDTGSTNSYRMGKEGKYDLKLAE 1932
Cdd:pfam06701    1 GARVVRGPDWKWGDQDGGEGHVGTVVeirdwDSESPRSTVRVQWDNGSTNVYRVGYEGKYDLKVVD 66
UBA_HERC2 cd14402
UBA domain found in probable E3 ubiquitin-protein ligase HERC2 and similar proteins; HERC2, ...
2463-2507 1.32e-23

UBA domain found in probable E3 ubiquitin-protein ligase HERC2 and similar proteins; HERC2, also called HECT domain and RCC1-like domain-containing protein 2, is a SUMO-regulated E3 ubiquitin ligase that plays an important role in the SUMO-dependent pathway which orchestrates the DNA double-strand break (DSB) response. Moreover, HERC2 functions as a RNF8 auxiliary factor that regulates ubiquitin-dependent retention of repair proteins on damaged chromosomes. In addition to a ubiquitin-association (UBA) domain, HERC2 contains more than one RCC1-like domains (RLDs) and a C-terminal HECT E3 ubiquitin ligase domain.


:

Pssm-ID: 270585  Cd Length: 45  Bit Score: 95.90  E-value: 1.32e-23
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 2119497975 2463 PIVVQLMEMGFPRKNIEFALKSLTGSASGLPGVEALVGWLLDHPD 2507
Cdd:cd14402      1 PIVQQLMEMGFPRKNVEFALKSLSGSSGGLPTPEALVAWLLEHPD 45
Cyt-b5 pfam00173
Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from ...
1212-1284 1.54e-08

Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from a diverse range of proteins. This family also includes proteins that bind to steroids. The family includes progesterone receptors. Many members of this subfamily are membrane anchored by an N-terminal transmembrane alpha helix. This family also includes a domain in some chitin synthases. There is no known ligand for this domain in the chitin synthases.


:

Pssm-ID: 459698 [Multi-domain]  Cd Length: 74  Bit Score: 54.16  E-value: 1.54e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2119497975 1212 RKADLENHNKDGGFWTVIDGKVYDIKDFQTQSLTGNSILAQFAGDDPVVALEAALQFEDTRESMHA-FCVGQYM 1284
Cdd:pfam00173    1 TLEELSKHNGDGDCWVAINGKVYDVTKFLKEHPGGEDVILSAAGKDATDAFEAIGHSEDAAEKLLKkYRIGELA 74
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
728-777 2.93e-03

Regulator of chromosome condensation (RCC1) repeat;


:

Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 38.27  E-value: 2.93e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2119497975  728 DSEVHSWGSNDQCQhfdtL----RITKPEPTALPGLDTKHIVGIACGPAQSFAW 777
Cdd:pfam00415    1 DGRVYTWGRNDYGQ----LglgtTENVLVPQKVEGLSGNKVVQVACGGDHTVAL 50
SH3_15 super family cl39691
Mind bomb SH3 repeat domain; The REP domain of Mind bomb which serves as the substrate ...
2640-2697 4.01e-03

Mind bomb SH3 repeat domain; The REP domain of Mind bomb which serves as the substrate recognition domain for a second, membrane-distal epitope of the Notch ligand (C-box). Although the first Mib repeat of REP may play a dominant role in ligand binding, the two repeats appear to cooperate in the engagement of the Jag1 tail. Mind bomb (Mib) proteins are large, multi-domain E3 ligases that promote ubiquitination of the cytoplasmic tails of Notch ligands. The structure and functional analysis, show that Mib1 contains two independent substrate recognition domains that engage two distinct epitopes from the cytoplasmic tail of the ligand Jagged1, one in the intracellular membrane proximal region and the other near the C terminus. REP domains have a five-stranded anti-parallel twisted beta sheet topology similar to that of SH3 domains.


The actual alignment was detected with superfamily member pfam18346:

Pssm-ID: 465720  Cd Length: 67  Bit Score: 38.76  E-value: 4.01e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2119497975 2640 IKIGDKVRVKTSVTTPK------YKWG---SVTHRSVGVVKAFSANGkDVIVDFPQQSH-WTGLLSEM 2697
Cdd:pfam18346    1 FEVGDWVRVKDDLEKVKplqeghGGWNggmAETLGSVGTVVKVDADG-DLRVQFPGGGRrWTLNPAAL 67
 
Name Accession Description Interval E-value
APC10-HERC2 cd08664
APC10-like DOC1 domain present in HERC2 (HECT domain and RLD2); This model represents the ...
2766-2911 2.79e-89

APC10-like DOC1 domain present in HERC2 (HECT domain and RLD2); This model represents the APC10/DOC1 domain present in HERC2 (HECT domain and RLD2), a large multi-domain protein with three RCC1-like domains (RLDs), additional internal domains including a zinc finger ZZ-type and Cyt-b5 (Cytochrome b5-like Heme/Steroid binding) domains, and a C-terminal HECT (Homologous to the E6-AP Carboxyl Terminus) domain. The APC10/DOC1 domain of HERC2 is a homolog of the APC10 subunit and the DOC1 domain present in E3 ubiquitin ligases which mediate substrate ubiquitination (or ubiquitylation), a component of the ubiquitin-26S proteasome pathway for selective proteolytic degradation. As suggested by structural relationships between HERC2 and other proteins such as HERC1, the proposed role for HERC2 in protein trafficking and degradation pathways is consistent with observations that mutations in HERC2 lead to neuromuscular secretory vesicle and sperm acrosome defects, other developmental abnormalities, and juvenile lethality of jdf2 mice. Recent studies have shown that the protein complex, HERC2-RNF8, coordinates ubiquitin-dependent assembly of DNA repair factors on damaged chromosomes.


Pssm-ID: 176485  Cd Length: 152  Bit Score: 287.73  E-value: 2.79e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497975 2766 KQLKRCHSSQP------GMLLDNWSRIVKNLNVSSSVNQASRLIDGSEPCWQSSGSQGKHWIRLEIFPDVLVHRLKMIVD 2839
Cdd:cd08664      1 GKPGKYHRNDPelnageGDLIDDWSRCVRSLTVSSNENQAKRLIDGSGSYWQSSGSQGKHWIRLELHPDVLIHSLKIIVD 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2119497975 2840 PADSSYMPSLVVVSGGNSLNNLIELKTININPADTTVPLLTDCTEYHRYIEVAIKQCRSSGIDCKIHGLIIL 2911
Cdd:cd08664     81 PADSSYMPSLVVVSGGDSLNSLKELKTINVNATDTLVTLLQDVKEYYRYIEIAIKQCRNNGIDCKIHGLNII 152
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
2962-3302 1.39e-78

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: 265.30  E-value: 1.39e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497975 2962 VFVWGLNDKDQLGGLKGSKIKVPSFSETLSalNVVQVAGGSKSLFAVTVEGKVYACGEATNGRLGLGiSSGTVPIPRQIT 3041
Cdd:COG5184     19 VWCWGDNSYGQLGDGTTTDRSTPVRVPGLS--NVVAVAAGGDHTCALKADGTVWCWGNNSYGQLGDG-TTTDRTTPVKVP 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497975 3042 ALSNYVvkkvAVHSGGRHAMALTVDGKVFSWGEGDDGKLGHFSRMNCDKPRLIeALKTKRIRDIACGSSHSAAITSSGEL 3121
Cdd:COG5184     96 GLTGVV----AVAAGYYHSCALKSDGTVWCWGDNSSGQLGDGTTTNRLTPVQV-DAGLSGVVAIAAGGYHTCALKSDGTV 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497975 3122 YTWGLGEYGRLGHGDNTTQLKPkmVKVLLGHRVIQVACGsrDAQTLALTDEGLVFSWGDGDFGKLGRGGSEGCNIPQNIE 3201
Cdd:COG5184    171 WCWGANSYGQLGDGTTTDRPTP--VQVGGLSGVVAVAAG--GDHSCALKSDGTVWCWGSNSSGQLGDGTTTDRATPVQVA 246
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497975 3202 rlNGQGVCQIECGAQFSLALTKSGVVWTWGKGDYFRLGHGTDVHVRKPQVVEGLRGkkIVHVAVGALHCLAVTDTGQVYA 3281
Cdd:COG5184    247 --GLTGVVAIAAGGSHTCALKSDGTVWCWGDNSYGQLGDGTTTDRSTPVKVPGLSG--VVAVAAGSSHTCALLTDGTVWC 322
                          330       340
                   ....*....|....*....|.
gi 2119497975 3282 WGDNDHGQQGNGTTTVNRKPT 3302
Cdd:COG5184    323 WGDNAYGQLGDGTTTDRSTPV 343
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
3947-4295 8.93e-78

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: 262.99  E-value: 8.93e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497975 3947 WTLSAGGS--------GTIYGWGHNHRGQLGGieGAKVKVPTPCEALAALRPIQLIGGEQTLFAVTADGKLYATGYGAGG 4018
Cdd:COG5184      1 TQVAAGGShscalksdGTVWCWGDNSYGQLGD--GTTTDRSTPVRVPGLSNVVAVAAGGDHTCALKADGTVWCWGNNSYG 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497975 4019 RLGIGGTESVSTPTLLESIQHVfikkVAVNSGGKHCLALSSEGEVYSWGEAEDGKLGHGNRSPCDRPRVIeSLRGIEVVD 4098
Cdd:COG5184     79 QLGDGTTTDRTTPVKVPGLTGV----VAVAAGYYHSCALKSDGTVWCWGDNSSGQLGDGTTTNRLTPVQV-DAGLSGVVA 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497975 4099 IAAGGAHSACITAAGDLYTWGKGRYGRLGHGDSEDQLKPKLVEALQGyrVIDIACGsgDAQTLCLTDDDTVWSWGDGDYG 4178
Cdd:COG5184    154 IAAGGYHTCALKSDGTVWCWGANSYGQLGDGTTTDRPTPVQVGGLSG--VVAVAAG--GDHSCALKSDGTVWCWGSNSSG 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497975 4179 KLGRGGSDGCKVPMKIDSLTGlgVVKVECGSQFSVALTKSGSVYTWGKGDYHRLGHGSDDHVRRPRQVQGLQGkkVIAIA 4258
Cdd:COG5184    230 QLGDGTTTDRATPVQVAGLTG--VVAIAAGGSHTCALKSDGTVWCWGDNSYGQLGDGTTTDRSTPVKVPGLSG--VVAVA 305
                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 2119497975 4259 TGSLHCVCCTEDGEVYTWGDNDEGQLGDGTTNAIQRP 4295
Cdd:COG5184    306 AGSSHTCALLTDGTVWCWGDNAYGQLGDGTTTDRSTP 342
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
443-741 6.39e-62

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: 217.15  E-value: 6.39e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497975  443 PIQCEGLANlgITQIACAEKRFLILSRNGRVYM----------QAYNSDTLGPQLVQGLAsrNIVKIAAhsDGHHYLALA 512
Cdd:COG5184     41 PVRVPGLSN--VVAVAAGGDHTCALKADGTVWCwgnnsygqlgDGTTTDRTTPVKVPGLT--GVVAVAA--GYYHSCALK 114
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497975  513 ATGEVFSWGCGDGGRLGHGDTVPLEEPKMISA-LSGkqagkhVVHIACGSTYSAAITAEGELYTWGRGNYGRLGHGSSED 591
Cdd:COG5184    115 SDGTVWCWGDNSSGQLGDGTTTNRLTPVQVDAgLSG------VVAIAAGGYHTCALKSDGTVWCWGANSYGQLGDGTTTD 188
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497975  592 QTIPMLVTGLKGlkVIDVSCgsGDAQTLAVTENGQVWSWGDGDYGKLGRGGSDGCKTPKLIEKLQdlDVVKVRCGSQFSV 671
Cdd:COG5184    189 RPTPVQVGGLSG--VVAVAA--GGDHSCALKSDGTVWCWGSNSSGQLGDGTTTDRATPVQVAGLT--GVVAIAAGGSHTC 262
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497975  672 ALTKDGQVYSWGKGDNQRLGHGTEEHVRYPKLLEGLQGkkVVDVAAGSTHCLALTEDSEVHSWGSNDQCQ 741
Cdd:COG5184    263 ALKSDGTVWCWGDNSYGQLGDGTTTDRSTPVKVPGLSG--VVAVAAGSSHTCALLTDGTVWCWGDNAYGQ 330
Cul7 pfam11515
Mouse development and cellular proliferation protein Cullin-7; The Cullin Ring Ligase family ...
2555-2632 1.66e-46

Mouse development and cellular proliferation protein Cullin-7; The Cullin Ring Ligase family member, Cul7, is required for normal mouse development and cellular proliferation. Cul7 has a CPH domain which is a p53 interaction domain. The CPH domain interaction surface of P53 is present in the tetramerization domain.


Pssm-ID: 463286  Cd Length: 78  Bit Score: 162.52  E-value: 1.66e-46
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2119497975 2555 RADFLSNDDYAVYVRENIQVGMMVRCCRTYEEVCEGDIGKVIKLDRDGLHDLNVQCDWQQKGSTYWVRYIHVELIGFP 2632
Cdd:pfam11515    1 RSDFASRDDYAEYVRDNLAPGMRVRCCRDYEEVSAGDEGEVIQSNRGGLHDLNVQVDWQSKGRTYWVHWHHVEILGFP 78
ZZ_HERC2 cd02344
Zinc finger, ZZ type. Zinc finger present in HERC2 and related proteins. HERC2 is a potential ...
2707-2751 3.83e-29

Zinc finger, ZZ type. Zinc finger present in HERC2 and related proteins. HERC2 is a potential E3 ubiquitin protein ligase and/or guanine nucleotide exchange factor. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding.


Pssm-ID: 239084  Cd Length: 45  Bit Score: 111.91  E-value: 3.83e-29
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 2119497975 2707 VTCDGCQMFPINGPRFKCRNCDDFDFCETCFKTRKHNTRHTFGRI 2751
Cdd:cd02344      1 VTCDGCQMFPINGPRFKCRNCDDFDFCENCFKTRKHNTRHTFGRI 45
MIB_HERC2 pfam06701
Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain ...
1872-1932 1.03e-27

Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain (either Ring or Hect).


Pssm-ID: 461991  Cd Length: 66  Bit Score: 108.46  E-value: 1.03e-27
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2119497975 1872 GTRVMRGVDWKWGDQDGPPPGLGRVI-----GELGEDGWIRVQWDTGSTNSYRMGKEGKYDLKLAE 1932
Cdd:pfam06701    1 GARVVRGPDWKWGDQDGGEGHVGTVVeirdwDSESPRSTVRVQWDNGSTNVYRVGYEGKYDLKVVD 66
UBA_HERC2 cd14402
UBA domain found in probable E3 ubiquitin-protein ligase HERC2 and similar proteins; HERC2, ...
2463-2507 1.32e-23

UBA domain found in probable E3 ubiquitin-protein ligase HERC2 and similar proteins; HERC2, also called HECT domain and RCC1-like domain-containing protein 2, is a SUMO-regulated E3 ubiquitin ligase that plays an important role in the SUMO-dependent pathway which orchestrates the DNA double-strand break (DSB) response. Moreover, HERC2 functions as a RNF8 auxiliary factor that regulates ubiquitin-dependent retention of repair proteins on damaged chromosomes. In addition to a ubiquitin-association (UBA) domain, HERC2 contains more than one RCC1-like domains (RLDs) and a C-terminal HECT E3 ubiquitin ligase domain.


Pssm-ID: 270585  Cd Length: 45  Bit Score: 95.90  E-value: 1.32e-23
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 2119497975 2463 PIVVQLMEMGFPRKNIEFALKSLTGSASGLPGVEALVGWLLDHPD 2507
Cdd:cd14402      1 PIVQQLMEMGFPRKNVEFALKSLSGSSGGLPTPEALVAWLLEHPD 45
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
676-725 5.24e-17

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 77.56  E-value: 5.24e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2119497975  676 DGQVYSWGKGDNQRLGHGTEEHVRYPKLLEGLQGKKVVDVAAGSTHCLAL 725
Cdd:pfam00415    1 DGRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQVACGGDHTVAL 50
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
3277-3325 1.00e-15

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 73.71  E-value: 1.00e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 2119497975 3277 GQVYAWGDNDHGQQGNGTTTVNRKPTLVQGLEGQKITRVACGSSHSVAW 3325
Cdd:pfam00415    2 GRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQVACGGDHTVAL 50
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
4113-4163 1.29e-14

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 70.62  E-value: 1.29e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2119497975 4113 GDLYTWGKGRYGRLGHGDSEDQLKPKLVEALQGYRVIDIACGSGdaQTLCL 4163
Cdd:pfam00415    2 GRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQVACGGD--HTVAL 50
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
2703-2746 1.34e-11

Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain present in dystrophin-like proteins, and CREB-binding protein/p300 homologues. The ZZ in dystrophin appears to bind calmodulin. A missense mutation of one of the conserved cysteines in dystrophin results in a patient with Duchenne muscular dystrophy.


Pssm-ID: 197633 [Multi-domain]  Cd Length: 44  Bit Score: 62.07  E-value: 1.34e-11
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 2119497975  2703 IHPGVTCDGCQmFPINGPRFKCRNCDDFDFCETCFKTRKHNTRH 2746
Cdd:smart00291    1 VHHSYSCDTCG-KPIVGVRYHCLVCPDYDLCQSCFAKGSAGGEH 43
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
2703-2742 3.44e-09

Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds calmodulin. Putative zinc finger; binding not yet shown. Four to six cysteine residues in its sequence are responsible for coordinating zinc ions, to reinforce the structure.


Pssm-ID: 395451  Cd Length: 45  Bit Score: 55.18  E-value: 3.44e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 2119497975 2703 IHPGVTCDGCQMFPINGPRFKCRNCDDFDFCETCFKTRKH 2742
Cdd:pfam00569    1 IHKVYTCNGCSNDPSIGVRYHCLRCSDYDLCQSCFQTHKG 40
Cyt-b5 pfam00173
Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from ...
1212-1284 1.54e-08

Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from a diverse range of proteins. This family also includes proteins that bind to steroids. The family includes progesterone receptors. Many members of this subfamily are membrane anchored by an N-terminal transmembrane alpha helix. This family also includes a domain in some chitin synthases. There is no known ligand for this domain in the chitin synthases.


Pssm-ID: 459698 [Multi-domain]  Cd Length: 74  Bit Score: 54.16  E-value: 1.54e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2119497975 1212 RKADLENHNKDGGFWTVIDGKVYDIKDFQTQSLTGNSILAQFAGDDPVVALEAALQFEDTRESMHA-FCVGQYM 1284
Cdd:pfam00173    1 TLEELSKHNGDGDCWVAINGKVYDVTKFLKEHPGGEDVILSAAGKDATDAFEAIGHSEDAAEKLLKkYRIGELA 74
ANAPC10 pfam03256
Anaphase-promoting complex, subunit 10 (APC10);
2804-2870 2.26e-03

Anaphase-promoting complex, subunit 10 (APC10);


Pssm-ID: 367420  Cd Length: 185  Bit Score: 42.43  E-value: 2.26e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2119497975 2804 DGSEPCWQSSGSQgKHWIRLEIFPDVLVHRLKMIVDPA-DSSYMPSLVVVSGGNSLNNLIELKTININ 2870
Cdd:pfam03256   48 DNLDTYWQSDGSQ-PHLVNIQFRKKTPVKYVAIYLDYKlDESYTPSKISVRAGTGFNDLQEVRVVDLE 114
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
728-777 2.93e-03

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 38.27  E-value: 2.93e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2119497975  728 DSEVHSWGSNDQCQhfdtL----RITKPEPTALPGLDTKHIVGIACGPAQSFAW 777
Cdd:pfam00415    1 DGRVYTWGRNDYGQ----LglgtTENVLVPQKVEGLSGNKVVQVACGGDHTVAL 50
SH3_15 pfam18346
Mind bomb SH3 repeat domain; The REP domain of Mind bomb which serves as the substrate ...
2640-2697 4.01e-03

Mind bomb SH3 repeat domain; The REP domain of Mind bomb which serves as the substrate recognition domain for a second, membrane-distal epitope of the Notch ligand (C-box). Although the first Mib repeat of REP may play a dominant role in ligand binding, the two repeats appear to cooperate in the engagement of the Jag1 tail. Mind bomb (Mib) proteins are large, multi-domain E3 ligases that promote ubiquitination of the cytoplasmic tails of Notch ligands. The structure and functional analysis, show that Mib1 contains two independent substrate recognition domains that engage two distinct epitopes from the cytoplasmic tail of the ligand Jagged1, one in the intracellular membrane proximal region and the other near the C terminus. REP domains have a five-stranded anti-parallel twisted beta sheet topology similar to that of SH3 domains.


Pssm-ID: 465720  Cd Length: 67  Bit Score: 38.76  E-value: 4.01e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2119497975 2640 IKIGDKVRVKTSVTTPK------YKWG---SVTHRSVGVVKAFSANGkDVIVDFPQQSH-WTGLLSEM 2697
Cdd:pfam18346    1 FEVGDWVRVKDDLEKVKplqeghGGWNggmAETLGSVGTVVKVDADG-DLRVQFPGGGRrWTLNPAAL 67
 
Name Accession Description Interval E-value
APC10-HERC2 cd08664
APC10-like DOC1 domain present in HERC2 (HECT domain and RLD2); This model represents the ...
2766-2911 2.79e-89

APC10-like DOC1 domain present in HERC2 (HECT domain and RLD2); This model represents the APC10/DOC1 domain present in HERC2 (HECT domain and RLD2), a large multi-domain protein with three RCC1-like domains (RLDs), additional internal domains including a zinc finger ZZ-type and Cyt-b5 (Cytochrome b5-like Heme/Steroid binding) domains, and a C-terminal HECT (Homologous to the E6-AP Carboxyl Terminus) domain. The APC10/DOC1 domain of HERC2 is a homolog of the APC10 subunit and the DOC1 domain present in E3 ubiquitin ligases which mediate substrate ubiquitination (or ubiquitylation), a component of the ubiquitin-26S proteasome pathway for selective proteolytic degradation. As suggested by structural relationships between HERC2 and other proteins such as HERC1, the proposed role for HERC2 in protein trafficking and degradation pathways is consistent with observations that mutations in HERC2 lead to neuromuscular secretory vesicle and sperm acrosome defects, other developmental abnormalities, and juvenile lethality of jdf2 mice. Recent studies have shown that the protein complex, HERC2-RNF8, coordinates ubiquitin-dependent assembly of DNA repair factors on damaged chromosomes.


Pssm-ID: 176485  Cd Length: 152  Bit Score: 287.73  E-value: 2.79e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497975 2766 KQLKRCHSSQP------GMLLDNWSRIVKNLNVSSSVNQASRLIDGSEPCWQSSGSQGKHWIRLEIFPDVLVHRLKMIVD 2839
Cdd:cd08664      1 GKPGKYHRNDPelnageGDLIDDWSRCVRSLTVSSNENQAKRLIDGSGSYWQSSGSQGKHWIRLELHPDVLIHSLKIIVD 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2119497975 2840 PADSSYMPSLVVVSGGNSLNNLIELKTININPADTTVPLLTDCTEYHRYIEVAIKQCRSSGIDCKIHGLIIL 2911
Cdd:cd08664     81 PADSSYMPSLVVVSGGDSLNSLKELKTINVNATDTLVTLLQDVKEYYRYIEIAIKQCRNNGIDCKIHGLNII 152
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
2962-3302 1.39e-78

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: 265.30  E-value: 1.39e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497975 2962 VFVWGLNDKDQLGGLKGSKIKVPSFSETLSalNVVQVAGGSKSLFAVTVEGKVYACGEATNGRLGLGiSSGTVPIPRQIT 3041
Cdd:COG5184     19 VWCWGDNSYGQLGDGTTTDRSTPVRVPGLS--NVVAVAAGGDHTCALKADGTVWCWGNNSYGQLGDG-TTTDRTTPVKVP 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497975 3042 ALSNYVvkkvAVHSGGRHAMALTVDGKVFSWGEGDDGKLGHFSRMNCDKPRLIeALKTKRIRDIACGSSHSAAITSSGEL 3121
Cdd:COG5184     96 GLTGVV----AVAAGYYHSCALKSDGTVWCWGDNSSGQLGDGTTTNRLTPVQV-DAGLSGVVAIAAGGYHTCALKSDGTV 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497975 3122 YTWGLGEYGRLGHGDNTTQLKPkmVKVLLGHRVIQVACGsrDAQTLALTDEGLVFSWGDGDFGKLGRGGSEGCNIPQNIE 3201
Cdd:COG5184    171 WCWGANSYGQLGDGTTTDRPTP--VQVGGLSGVVAVAAG--GDHSCALKSDGTVWCWGSNSSGQLGDGTTTDRATPVQVA 246
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497975 3202 rlNGQGVCQIECGAQFSLALTKSGVVWTWGKGDYFRLGHGTDVHVRKPQVVEGLRGkkIVHVAVGALHCLAVTDTGQVYA 3281
Cdd:COG5184    247 --GLTGVVAIAAGGSHTCALKSDGTVWCWGDNSYGQLGDGTTTDRSTPVKVPGLSG--VVAVAAGSSHTCALLTDGTVWC 322
                          330       340
                   ....*....|....*....|.
gi 2119497975 3282 WGDNDHGQQGNGTTTVNRKPT 3302
Cdd:COG5184    323 WGDNAYGQLGDGTTTDRSTPV 343
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
3947-4295 8.93e-78

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: 262.99  E-value: 8.93e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497975 3947 WTLSAGGS--------GTIYGWGHNHRGQLGGieGAKVKVPTPCEALAALRPIQLIGGEQTLFAVTADGKLYATGYGAGG 4018
Cdd:COG5184      1 TQVAAGGShscalksdGTVWCWGDNSYGQLGD--GTTTDRSTPVRVPGLSNVVAVAAGGDHTCALKADGTVWCWGNNSYG 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497975 4019 RLGIGGTESVSTPTLLESIQHVfikkVAVNSGGKHCLALSSEGEVYSWGEAEDGKLGHGNRSPCDRPRVIeSLRGIEVVD 4098
Cdd:COG5184     79 QLGDGTTTDRTTPVKVPGLTGV----VAVAAGYYHSCALKSDGTVWCWGDNSSGQLGDGTTTNRLTPVQV-DAGLSGVVA 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497975 4099 IAAGGAHSACITAAGDLYTWGKGRYGRLGHGDSEDQLKPKLVEALQGyrVIDIACGsgDAQTLCLTDDDTVWSWGDGDYG 4178
Cdd:COG5184    154 IAAGGYHTCALKSDGTVWCWGANSYGQLGDGTTTDRPTPVQVGGLSG--VVAVAAG--GDHSCALKSDGTVWCWGSNSSG 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497975 4179 KLGRGGSDGCKVPMKIDSLTGlgVVKVECGSQFSVALTKSGSVYTWGKGDYHRLGHGSDDHVRRPRQVQGLQGkkVIAIA 4258
Cdd:COG5184    230 QLGDGTTTDRATPVQVAGLTG--VVAIAAGGSHTCALKSDGTVWCWGDNSYGQLGDGTTTDRSTPVKVPGLSG--VVAVA 305
                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 2119497975 4259 TGSLHCVCCTEDGEVYTWGDNDEGQLGDGTTNAIQRP 4295
Cdd:COG5184    306 AGSSHTCALLTDGTVWCWGDNAYGQLGDGTTTDRSTP 342
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
2996-3327 3.15e-77

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: 261.45  E-value: 3.15e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497975 2996 VQVAGGSKSLFAVTVEGKVYACGEATNGRLGLGiSSGTVPIPRQITALSNYVvkkvAVHSGGRHAMALTVDGKVFSWGEG 3075
Cdd:COG5184      1 TQVAAGGSHSCALKSDGTVWCWGDNSYGQLGDG-TTTDRSTPVRVPGLSNVV----AVAAGGDHTCALKADGTVWCWGNN 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497975 3076 DDGKLGHFSRMNCDKPRLIEALKTkrIRDIACGSSHSAAITSSGELYTWGLGEYGRLGHGDNTTQLKPkmVKVLLG-HRV 3154
Cdd:COG5184     76 SYGQLGDGTTTDRTTPVKVPGLTG--VVAVAAGYYHSCALKSDGTVWCWGDNSSGQLGDGTTTNRLTP--VQVDAGlSGV 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497975 3155 IQVACGsrDAQTLALTDEGLVFSWGDGDFGKLGRGGSEGCNIPQNIERLNGqgVCQIECGAQFSLALTKSGVVWTWGKGD 3234
Cdd:COG5184    152 VAIAAG--GYHTCALKSDGTVWCWGANSYGQLGDGTTTDRPTPVQVGGLSG--VVAVAAGGDHSCALKSDGTVWCWGSNS 227
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497975 3235 YFRLGHGTDVHVRKPQVVEGLRGkkIVHVAVGALHCLAVTDTGQVYAWGDNDHGQQGNGTTTVNRKPTLVQGLEGqkITR 3314
Cdd:COG5184    228 SGQLGDGTTTDRATPVQVAGLTG--VVAIAAGGSHTCALKSDGTVWCWGDNSYGQLGDGTTTDRSTPVKVPGLSG--VVA 303
                          330
                   ....*....|...
gi 2119497975 3315 VACGSSHSVAWTT 3327
Cdd:COG5184    304 VAAGSSHTCALLT 316
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
3995-4322 6.40e-70

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: 240.26  E-value: 6.40e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497975 3995 GGEQTLfAVTADGKLYATGYGAGGRLGIGGTESVSTPTLLESIQHVfikkVAVNSGGKHCLALSSEGEVYSWGEAEDGKL 4074
Cdd:COG5184      6 GGSHSC-ALKSDGTVWCWGDNSYGQLGDGTTTDRSTPVRVPGLSNV----VAVAAGGDHTCALKADGTVWCWGNNSYGQL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497975 4075 GHGNRSPCDRPRVIESLRGieVVDIAAGGAHSACITAAGDLYTWGKGRYGRLGHGDSEDQLKPKLVeALQGYRVIDIAcg 4154
Cdd:COG5184     81 GDGTTTDRTTPVKVPGLTG--VVAVAAGYYHSCALKSDGTVWCWGDNSSGQLGDGTTTNRLTPVQV-DAGLSGVVAIA-- 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497975 4155 SGDAQTLCLTDDDTVWSWGDGDYGKLGRGGSDGCKVPMKIDSLTGlgVVKVECGSQFSVALTKSGSVYTWGKGDYHRLGH 4234
Cdd:COG5184    156 AGGYHTCALKSDGTVWCWGANSYGQLGDGTTTDRPTPVQVGGLSG--VVAVAAGGDHSCALKSDGTVWCWGSNSSGQLGD 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497975 4235 GSDDHVRRPRQVQGLQGkkVIAIATGSLHCVCCTEDGEVYTWGDNDEGQLGDGTTNAIQRPRLVAALQGkkINRVACGSA 4314
Cdd:COG5184    234 GTTTDRATPVQVAGLTG--VVAIAAGGSHTCALKSDGTVWCWGDNSYGQLGDGTTTDRSTPVKVPGLSG--VVAVAAGSS 309

                   ....*...
gi 2119497975 4315 HTLAWSTS 4322
Cdd:COG5184    310 HTCALLTD 317
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
4045-4318 4.97e-66

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: 229.09  E-value: 4.97e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497975 4045 VAVNSGGKHCLALSSEGEVYSWGEAEDGKLGHGNRSPCDRPRVIESLRGieVVDIAAGGAHSACITAAGDLYTWGKGRYG 4124
Cdd:COG5184      1 TQVAAGGSHSCALKSDGTVWCWGDNSYGQLGDGTTTDRSTPVRVPGLSN--VVAVAAGGDHTCALKADGTVWCWGNNSYG 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497975 4125 RLGHGDSEDQLKPKLVEALQGyrVIDIACGSGdaQTLCLTDDDTVWSWGDGDYGKLGRGGSDGCKVPMKIDsLTGLGVVK 4204
Cdd:COG5184     79 QLGDGTTTDRTTPVKVPGLTG--VVAVAAGYY--HSCALKSDGTVWCWGDNSSGQLGDGTTTNRLTPVQVD-AGLSGVVA 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497975 4205 VECGSQFSVALTKSGSVYTWGKGDYHRLGHGSDDHVRRPRQVQGLQGkkVIAIATGSLHCVCCTEDGEVYTWGDNDEGQL 4284
Cdd:COG5184    154 IAAGGYHTCALKSDGTVWCWGANSYGQLGDGTTTDRPTPVQVGGLSG--VVAVAAGGDHSCALKSDGTVWCWGSNSSGQL 231
                          250       260       270
                   ....*....|....*....|....*....|....
gi 2119497975 4285 GDGTTNAIQRPRLVAALQGkkINRVACGSAHTLA 4318
Cdd:COG5184    232 GDGTTTDRATPVQVAGLTG--VVAIAAGGSHTCA 263
APC10-like1 cd08365
APC10-like DOC1 domains of E3 ubiquitin ligases that mediate substrate ubiquitination; This ...
2787-2911 1.96e-62

APC10-like DOC1 domains of E3 ubiquitin ligases that mediate substrate ubiquitination; This model represens the APC10-like DOC1 domain of multi-domain proteins present in E3 ubiquitin ligases. E3 ubiquitin ligases mediate substrate ubiquitination (or ubiquitylation), a component of the ubiquitin-26S proteasome pathway for selective proteolytic degradation. APC10/DOC1 domains such as those present in HECT (Homologous to the E6-AP Carboxyl Terminus) and Cullin-RING (Really Interesting New Gene) E3 ubiquitin ligase proteins, HECTD3, and CUL7, respectively, are also included here. CUL7 is a member of the Cullin-RING ligase family and functions as a molecular scaffold assembling a SCF-ROC1-like E3 ubiquitin ligase complex consisting of Skp1, CUL7, Fbx29 F-box protein, and ROC1 (RING-box protein 1) and promotes ubiquitination. CUL7 is a multi-domain protein with a C-terminal cullin domain that binds ROC1 and a centrally positioned APC10/DOC1 domain. HECTD3 contains a C-terminal HECT domain which contains the active site for ubiquitin transfer onto substrates, and an N-terminal APC10/DOC1 domain which is responsible for substrate recognition and binding. An APC10/DOC1 domain homolog is also present in HERC2 (HECT domain and RLD2), a large multi-domain protein with three RCC1-like domains (RLDs), additional internal domains including zinc finger ZZ-type and Cyt-b5 (Cytochrome b5-like Heme/Steroid binding) domains, and a C-terminal HECT domain. Recent studies have shown that the protein complex HERC2-RNF8 coordinates ubiquitin-dependent assembly of DNA repair factors on damaged chromosomes. Also included in this hierarchy is an uncharacterized APC10/DOC1-like domain found in a multi-domain protein, which also contains CUB, zinc finger ZZ-type, and EF-hand domains. The APC10/DOC1 domain forms a beta-sandwich structure that is related in architecture to the galactose-binding domain-like fold; their sequences are quite dissimilar, however, and are not included here.


Pssm-ID: 176483  Cd Length: 131  Bit Score: 210.05  E-value: 1.96e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497975 2787 VKNLNVSSSVNQASRLIDG-SEPCWQSSGSQGKHWIRLEIFPDVLVHRLKMIVDPADSSYMPSLVVVSGGNSLNNLIELK 2865
Cdd:cd08365      5 VESIEVSSNPADASRLTDGnTSTYWQSDGSQGSHWIRLKMKPDVLVRHLSLAVDATDSSYMPQRVVVAGGRSASNLQELR 84
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 2119497975 2866 TININPA-DTTVPLLTDCTEYHRYIEVAIKQCRSSGIDCKIHGLIIL 2911
Cdd:cd08365     85 DVNIPPSvTGYVTLLEDATISQPYIEIRIKRCRSDGIDTRIHGLRIL 131
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
443-741 6.39e-62

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: 217.15  E-value: 6.39e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497975  443 PIQCEGLANlgITQIACAEKRFLILSRNGRVYM----------QAYNSDTLGPQLVQGLAsrNIVKIAAhsDGHHYLALA 512
Cdd:COG5184     41 PVRVPGLSN--VVAVAAGGDHTCALKADGTVWCwgnnsygqlgDGTTTDRTTPVKVPGLT--GVVAVAA--GYYHSCALK 114
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497975  513 ATGEVFSWGCGDGGRLGHGDTVPLEEPKMISA-LSGkqagkhVVHIACGSTYSAAITAEGELYTWGRGNYGRLGHGSSED 591
Cdd:COG5184    115 SDGTVWCWGDNSSGQLGDGTTTNRLTPVQVDAgLSG------VVAIAAGGYHTCALKSDGTVWCWGANSYGQLGDGTTTD 188
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497975  592 QTIPMLVTGLKGlkVIDVSCgsGDAQTLAVTENGQVWSWGDGDYGKLGRGGSDGCKTPKLIEKLQdlDVVKVRCGSQFSV 671
Cdd:COG5184    189 RPTPVQVGGLSG--VVAVAA--GGDHSCALKSDGTVWCWGSNSSGQLGDGTTTDRATPVQVAGLT--GVVAIAAGGSHTC 262
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497975  672 ALTKDGQVYSWGKGDNQRLGHGTEEHVRYPKLLEGLQGkkVVDVAAGSTHCLALTEDSEVHSWGSNDQCQ 741
Cdd:COG5184    263 ALKSDGTVWCWGDNSYGQLGDGTTTDRSTPVKVPGLSG--VVAVAAGSSHTCALLTDGTVWCWGDNAYGQ 330
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
505-776 7.32e-61

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: 214.07  E-value: 7.32e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497975  505 GHHYLALAATGEVFSWGCGDGGRLGHGDTVPLEEPKMISALSGkqagkhVVHIACGSTYSAAITAEGELYTWGRGNYGRL 584
Cdd:COG5184      7 GSHSCALKSDGTVWCWGDNSYGQLGDGTTTDRSTPVRVPGLSN------VVAVAAGGDHTCALKADGTVWCWGNNSYGQL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497975  585 GHGSSEDQTIPMLVTGLKGlkVIDVSCGSGdaQTLAVTENGQVWSWGDGDYGKLGRGGSDGCKTPKLIEkLQDLDVVKVR 664
Cdd:COG5184     81 GDGTTTDRTTPVKVPGLTG--VVAVAAGYY--HSCALKSDGTVWCWGDNSSGQLGDGTTTNRLTPVQVD-AGLSGVVAIA 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497975  665 CGSQFSVALTKDGQVYSWGKGDNQRLGHGTEEHVRYPKLLEGLQGkkVVDVAAGSTHCLALTEDSEVHSWGSNDQCQHFD 744
Cdd:COG5184    156 AGGYHTCALKSDGTVWCWGANSYGQLGDGTTTDRPTPVQVGGLSG--VVAVAAGGDHSCALKSDGTVWCWGSNSSGQLGD 233
                          250       260       270
                   ....*....|....*....|....*....|..
gi 2119497975  745 TLRITKPEPTALPGLDTkhIVGIACGPAQSFA 776
Cdd:COG5184    234 GTTTDRATPVQVAGLTG--VVAIAAGGSHTCA 263
APC10-like cd08159
APC10-like DOC1 domains in E3 ubiquitin ligases that mediate substrate ubiquitination; This ...
2781-2911 7.86e-60

APC10-like DOC1 domains in E3 ubiquitin ligases that mediate substrate ubiquitination; This family contains the single domain protein, APC10, a subunit of the anaphase-promoting complex (APC), as well as the DOC1 domain of multi-domain proteins present in E3 ubiquitin ligases. E3 ubiquitin ligases mediate substrate ubiquitination (or ubiquitylation), a component of the ubiquitin-26S proteasome pathway for selective proteolytic degradation. The APC, a multi-protein complex (or cyclosome), is a cell cycle-regulated, E3 ubiquitin ligase that controls important transitions in mitosis and the G1 phase by ubiquitinating regulatory proteins, thereby targeting them for degradation. APC10-like DOC1 domains such as those present in HECT (Homologous to the E6-AP Carboxyl Terminus) and Cullin-RING (Really Interesting New Gene) E3 ubiquitin ligase proteins, HECTD3, and CUL7, respectively, are also included in this hierarchy. CUL7 is a member of the Cullin-RING ligase family and functions as a molecular scaffold assembling a SCF-ROC1-like E3 ubiquitin ligase complex consisting of Skp1, CUL7, Fbx29 F-box protein, and ROC1 (RING-box protein 1) and promotes ubiquitination. CUL7 is a multi-domain protein with a C-terminal cullin domain that binds ROC1 and a centrally positioned APC10/DOC1 domain. HECTD3 contains a C-terminal HECT domain which contains the active site for ubiquitin transfer onto substrates, and an N-terminal APC10 domain which is responsible for substrate recognition and binding. An APC10/DOC1 domain homolog is also present in HERC2 (HECT domain and RLD2), a large multi-domain protein with three RCC1-like domains (RLDs), additional internal domains including zinc finger ZZ-type and Cyt-b5 (Cytochrome b5-like Heme/Steroid binding) domains, and a C-terminal HECT domain. Recent studies have shown that the protein complex HERC2-RNF8 coordinates ubiquitin-dependent assembly of DNA repair factors on damaged chromosomes. Also included in this hierarchy is an uncharacterized APC10/DOC1-like domain found in a multi-domain protein, which also contains CUB, zinc finger ZZ-type, and EF-hand domains. The APC10/DOC1 domain forms a beta-sandwich structure that is related in architecture to the galactose-binding domain-like fold; their sequences are quite dissimilar, however, and are not included here.


Pssm-ID: 176482  Cd Length: 129  Bit Score: 202.70  E-value: 7.86e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497975 2781 DNWSrivKNLNVSSSVNQASRLIDG-SEPCWQSSGSQGKHWIRLEIFPDVLVHRLKMIVDPADSSYMPSLVVVSGGNSLN 2859
Cdd:cd08159      1 KCYT---ASIEVSSNPLPVSRLTDGnYDTYWQSDGSQGSHWIRLFMKKDVLIRVLAIFVDMADSSYMPSLVVVYGGHSPS 77
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2119497975 2860 NLIELKTININPADTTVPLLTDCTEYHRYIEVAIKQCRSSGIDCKIHGLIIL 2911
Cdd:cd08159     78 DLRELKDVNIRPSNGWVALLEDDTLKCPYIEIRIKRCRSDGIDTRIRGLRLL 129
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
443-701 3.68e-50

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: 183.25  E-value: 3.68e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497975  443 PIQCEGLANlgITQIACAEKRFLILSRNGRVYMQAYNS----------DTLGPQLVqGLASRNIVKIAAhsDGHHYLALA 512
Cdd:COG5184     91 PVKVPGLTG--VVAVAAGYYHSCALKSDGTVWCWGDNSsgqlgdgtttNRLTPVQV-DAGLSGVVAIAA--GGYHTCALK 165
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497975  513 ATGEVFSWGCGDGGRLGHGDTVPLEEPKMISALSGkqagkhVVHIACGSTYSAAITAEGELYTWGRGNYGRLGHGSSEDQ 592
Cdd:COG5184    166 SDGTVWCWGANSYGQLGDGTTTDRPTPVQVGGLSG------VVAVAAGGDHSCALKSDGTVWCWGSNSSGQLGDGTTTDR 239
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497975  593 TIPMLVTGLKGlkVIDVSCGSGdaQTLAVTENGQVWSWGDGDYGKLGRGGSDGCKTPKLIEKLqdLDVVKVRCGSQFSVA 672
Cdd:COG5184    240 ATPVQVAGLTG--VVAIAAGGS--HTCALKSDGTVWCWGDNSYGQLGDGTTTDRSTPVKVPGL--SGVVAVAAGSSHTCA 313
                          250       260
                   ....*....|....*....|....*....
gi 2119497975  673 LTKDGQVYSWGKGDNQRLGHGTEEHVRYP 701
Cdd:COG5184    314 LLTDGTVWCWGDNAYGQLGDGTTTDRSTP 342
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
555-776 1.39e-48

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: 178.63  E-value: 1.39e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497975  555 VHIACGSTYSAAITAEGELYTWGRGNYGRLGHGSSEDQTIPMLVTGLKGlkVIDVSCGSgdAQTLAVTENGQVWSWGDGD 634
Cdd:COG5184      1 TQVAAGGSHSCALKSDGTVWCWGDNSYGQLGDGTTTDRSTPVRVPGLSN--VVAVAAGG--DHTCALKADGTVWCWGNNS 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497975  635 YGKLGRGGSDGCKTPKLIEKLqdLDVVKVRCGSQFSVALTKDGQVYSWGKGDNQRLGHGTEEHVRYP-KLLEGLQGkkVV 713
Cdd:COG5184     77 YGQLGDGTTTDRTTPVKVPGL--TGVVAVAAGYYHSCALKSDGTVWCWGDNSSGQLGDGTTTNRLTPvQVDAGLSG--VV 152
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2119497975  714 DVAAGSTHCLALTEDSEVHSWGSNDQCQHFDTLRITKPEPTALPGLDTkhIVGIACGPAQSFA 776
Cdd:COG5184    153 AIAAGGYHTCALKSDGTVWCWGANSYGQLGDGTTTDRPTPVQVGGLSG--VVAVAAGGDHSCA 213
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
2961-3198 4.03e-47

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: 174.39  E-value: 4.03e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497975 2961 KVFVWGLNDKDQLG-GLKGSK---IKVPsfsetLSALNVVQVAGGSKSLFAVTVEGKVYACGEATNGRLGLGiSSGTVPI 3036
Cdd:COG5184    118 TVWCWGDNSSGQLGdGTTTNRltpVQVD-----AGLSGVVAIAAGGYHTCALKSDGTVWCWGANSYGQLGDG-TTTDRPT 191
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497975 3037 PRQITALSNyvVKKVAVhsGGRHAMALTVDGKVFSWGEGDDGKLGHFSRMNCDKPRLIEALKTkrIRDIACGSSHSAAIT 3116
Cdd:COG5184    192 PVQVGGLSG--VVAVAA--GGDHSCALKSDGTVWCWGSNSSGQLGDGTTTDRATPVQVAGLTG--VVAIAAGGSHTCALK 265
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497975 3117 SSGELYTWGLGEYGRLGHGDNTTQLKPkmVKVLLGHRVIQVACGSrdAQTLALTDEGLVFSWGDGDFGKLGRGGSEGCNI 3196
Cdd:COG5184    266 SDGTVWCWGDNSYGQLGDGTTTDRSTP--VKVPGLSGVVAVAAGS--SHTCALLTDGTVWCWGDNAYGQLGDGTTTDRST 341

                   ..
gi 2119497975 3197 PQ 3198
Cdd:COG5184    342 PV 343
Cul7 pfam11515
Mouse development and cellular proliferation protein Cullin-7; The Cullin Ring Ligase family ...
2555-2632 1.66e-46

Mouse development and cellular proliferation protein Cullin-7; The Cullin Ring Ligase family member, Cul7, is required for normal mouse development and cellular proliferation. Cul7 has a CPH domain which is a p53 interaction domain. The CPH domain interaction surface of P53 is present in the tetramerization domain.


Pssm-ID: 463286  Cd Length: 78  Bit Score: 162.52  E-value: 1.66e-46
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2119497975 2555 RADFLSNDDYAVYVRENIQVGMMVRCCRTYEEVCEGDIGKVIKLDRDGLHDLNVQCDWQQKGSTYWVRYIHVELIGFP 2632
Cdd:pfam11515    1 RSDFASRDDYAEYVRDNLAPGMRVRCCRDYEEVSAGDEGEVIQSNRGGLHDLNVQVDWQSKGRTYWVHWHHVEILGFP 78
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
2949-3143 1.62e-33

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: 134.72  E-value: 1.62e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497975 2949 SSGLESAATIRT--KVFVWGLNDKDQLGglKGSKIKVPSFSETLSALNVVQVAGGSKSLFAVTVEGKVYACGEATNGRLG 3026
Cdd:COG5184    155 AAGGYHTCALKSdgTVWCWGANSYGQLG--DGTTTDRPTPVQVGGLSGVVAVAAGGDHSCALKSDGTVWCWGSNSSGQLG 232
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497975 3027 LGiSSGTVPIPRQITALSNYvvkkVAVHSGGRHAMALTVDGKVFSWGEGDDGKLGHFSRMNCDKPRLIEALKTkrIRDIA 3106
Cdd:COG5184    233 DG-TTTDRATPVQVAGLTGV----VAIAAGGSHTCALKSDGTVWCWGDNSYGQLGDGTTTDRSTPVKVPGLSG--VVAVA 305
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 2119497975 3107 CGSSHSAAITSSGELYTWGLGEYGRLGHGDNTTQLKP 3143
Cdd:COG5184    306 AGSSHTCALLTDGTVWCWGDNAYGQLGDGTTTDRSTP 342
APC10-HECTD3 cd08666
APC10-like DOC1 domain of HECTD3, a HECT E3 ubiquitin ligase protein that mediates substrate ...
2781-2910 9.43e-30

APC10-like DOC1 domain of HECTD3, a HECT E3 ubiquitin ligase protein that mediates substrate ubiquitination; This model represents the APC10/DOC1 domain present in HECTD3, a HECT (Homologous to the E6-AP Carboxyl Terminus) E3 ubiquitin ligase protein. HECT E3 ubiquitin ligases mediate substrate ubiquitination (or ubiquitylation), and are a component of the ubiquitin-26S proteasome pathway for selective proteolytic degradation. They also regulate the trafficking of many receptors, channels, transporters and viral proteins. HECTD3 (HECT domain-containing protein3) contains a C-terminal HECT domain with the active site for ubiquitin transfer onto substrates, and an N-terminal APC10/DOC1 domain, which is responsible for substrate recognition and binding. HECTD3 specifically recognizes the Trio-binding protein, Tara (Trio-associated repeat on actin), implicated in regulating actin cytoskeletal, cell motility and cell growth. Tara also binds to TRF1 and may participate in telomere maintenance and/or mitotic regulation through interacting with TRF1. HECTD3 interacts with and promotes the ubiquitination of Syntaxin 8, an endosomal syntaxin proposed to mediate distinct steps of endosomal protein trafficking. HECTD3-mediated Syntaxin 8 degradation has been suggested to contribute to the pathophysiology of neurodegenerative diseases.


Pssm-ID: 176487  Cd Length: 134  Bit Score: 116.74  E-value: 9.43e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497975 2781 DNWSRIVKNLNVSSSV--NQASRLIDG-SEPCWQSSGSQGKHWIRLEIFPDVLVHRLKMIVDPADSSYMPSLVVVSGGNS 2857
Cdd:cd08666      1 GSVKQYVESIEVSSYTddFNVSCLTDGdPDTYWESDGSQGQHWIRLHMKKGTIIKKLLLTVDATDDNYMPKRVAVYGGEG 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2119497975 2858 lNNLIELKTININPADTT-VPLLTDCTEYHRYIEVAIKQCRSSGIDCKIHGLII 2910
Cdd:cd08666     81 -DNLKKLNDVSIDETLIGdVCILEDMTTHLPVIEIRIKECKDEGIDVRIRGIKI 133
ZZ_HERC2 cd02344
Zinc finger, ZZ type. Zinc finger present in HERC2 and related proteins. HERC2 is a potential ...
2707-2751 3.83e-29

Zinc finger, ZZ type. Zinc finger present in HERC2 and related proteins. HERC2 is a potential E3 ubiquitin protein ligase and/or guanine nucleotide exchange factor. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding.


Pssm-ID: 239084  Cd Length: 45  Bit Score: 111.91  E-value: 3.83e-29
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 2119497975 2707 VTCDGCQMFPINGPRFKCRNCDDFDFCETCFKTRKHNTRHTFGRI 2751
Cdd:cd02344      1 VTCDGCQMFPINGPRFKCRNCDDFDFCENCFKTRKHNTRHTFGRI 45
MIB_HERC2 pfam06701
Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain ...
1872-1932 1.03e-27

Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain (either Ring or Hect).


Pssm-ID: 461991  Cd Length: 66  Bit Score: 108.46  E-value: 1.03e-27
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2119497975 1872 GTRVMRGVDWKWGDQDGPPPGLGRVI-----GELGEDGWIRVQWDTGSTNSYRMGKEGKYDLKLAE 1932
Cdd:pfam06701    1 GARVVRGPDWKWGDQDGGEGHVGTVVeirdwDSESPRSTVRVQWDNGSTNVYRVGYEGKYDLKVVD 66
APC10-CUL7 cd08665
APC10-like DOC1 domain of CUL7, subunit of the SCF-ROC1-like E3 ubiquitin ligase complex that ...
2783-2912 7.46e-26

APC10-like DOC1 domain of CUL7, subunit of the SCF-ROC1-like E3 ubiquitin ligase complex that mediates substrate ubiquitination; This model represents the APC10/DOC1 domain present in CUL7, a subunit of the SCF-ROC1-like E3 Ubiquitin (Ub) ligase complex, which mediates substrate ubiquitination (or ubiquitylation), and is a component of the ubiquitin-26S proteasome pathway for selective proteolytic degradation. CUL7 is a member of the Cullin-RING ligase family and functions as a molecular scaffold assembling the SCF-ROC1-like E3 Ub ligase complex consisting of the adapter protein Skp1, CUL7, the WD40 repeat-containing F-box Fbw8 (also known as Fbx29), and ROC1 (RING-box protein 1). CUL7 is a large protein with a C-terminal cullin domain that binds ROC1 and additional domains, including an APC10/DOC1 domain. While the Fbw8 protein is responsible for substrate protein recognition, the ROC1 RING domain recruits an Ub-charged E2 Ub-conjugating enzyme for substrate ubiquitination. It remains to be determined how CUL7 binds to the Skp1-Fbw8 heterodimer. The CUL7 E3 Ub ligase has been implicated in the proteasomal degradation of the cellular proteins, cyclin D1, an important regulator of the G1 to S-phase cell cycle progression, and insulin receptor substrate 1, a critical component of the signaling pathways downstream of the insulin and insulin-like growth factor 1 receptor. CUL7 appears to be an important regulator of placental development. Germ line mutations of CUL7 are linked to 3-M syndrome and Yakuts short stature syndrome.


Pssm-ID: 176486  Cd Length: 131  Bit Score: 105.78  E-value: 7.46e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497975 2783 WSRIvknlNVSSSVNQASRLIDGS-EPCWQSSGSQGKHWIRLEIFPDVLVHRLKMIVDPADSSYMPSLVVVSGGNSLNNL 2861
Cdd:cd08665      4 WEKV----EVSSNPHRANKLTDGNpKTYWESNGSTGSHYINIHMHRGVVIRQLYMLVASEDSSYMPARVVVLGGDSPSCI 79
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2119497975 2862 -IELKTININPADTTVPLLTDCTEYHRYIEVAIKQCRSSGIDCKIHGLIILG 2912
Cdd:cd08665     80 tTELNAVNVSPTASRVVLLENMTRFWPIIQIRIKRCQQGGIDTRVRGLEILG 131
APC10-ZZEF1 cd08667
APC10/DOC1-like domain of uncharacterized Zinc finger ZZ-type and EF-hand domain-containing ...
2788-2912 2.98e-24

APC10/DOC1-like domain of uncharacterized Zinc finger ZZ-type and EF-hand domain-containing protein 1 (ZZEF1) and homologs; This model represents the APC10/DOC1-like domain present in the uncharacterized Zinc finger ZZ-type and EF-hand domain-containing protein 1 (ZZEF1) of Mus musculus. Members of this family contain EF-hand, APC10, CUB, and zinc finger ZZ-type domains. ZZEF1-like APC10 domains are homologous to the APC10 subunit/DOC1 domains present in E3 ubiquitin ligases, which mediate substrate ubiquitination (or ubiquitylation), and are components of the ubiquitin-26S proteasome pathway for selective proteolytic degradation.


Pssm-ID: 176488  Cd Length: 131  Bit Score: 101.14  E-value: 2.98e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497975 2788 KNLNVSSSVNQASRLIDGS-EPCWQSSGSQGKHWIRLEIFPDVLVHRLKMIVDPADSSYMPSLVVVSGGNSLNNLIELKT 2866
Cdd:cd08667      5 AYIEVSSNSADIDRMTDGEtSTYWQSDGSARSHWIRLKMKPDVVLRHLSIAVAATDQSYMPQQVTVSVGRSASSLQEVRD 84
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 2119497975 2867 INInPADTT--VPLLTDCTEYHRYIEVAIKQCRSSGIDCKIHGLIILG 2912
Cdd:cd08667     85 VHI-PSNVTgyVTLLENANISYLVVQINIKRCHSDGCDTRIHGLKTIG 131
UBA_HERC2 cd14402
UBA domain found in probable E3 ubiquitin-protein ligase HERC2 and similar proteins; HERC2, ...
2463-2507 1.32e-23

UBA domain found in probable E3 ubiquitin-protein ligase HERC2 and similar proteins; HERC2, also called HECT domain and RCC1-like domain-containing protein 2, is a SUMO-regulated E3 ubiquitin ligase that plays an important role in the SUMO-dependent pathway which orchestrates the DNA double-strand break (DSB) response. Moreover, HERC2 functions as a RNF8 auxiliary factor that regulates ubiquitin-dependent retention of repair proteins on damaged chromosomes. In addition to a ubiquitin-association (UBA) domain, HERC2 contains more than one RCC1-like domains (RLDs) and a C-terminal HECT E3 ubiquitin ligase domain.


Pssm-ID: 270585  Cd Length: 45  Bit Score: 95.90  E-value: 1.32e-23
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 2119497975 2463 PIVVQLMEMGFPRKNIEFALKSLTGSASGLPGVEALVGWLLDHPD 2507
Cdd:cd14402      1 PIVQQLMEMGFPRKNVEFALKSLSGSSGGLPTPEALVAWLLEHPD 45
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
676-725 5.24e-17

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 77.56  E-value: 5.24e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2119497975  676 DGQVYSWGKGDNQRLGHGTEEHVRYPKLLEGLQGKKVVDVAAGSTHCLAL 725
Cdd:pfam00415    1 DGRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQVACGGDHTVAL 50
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
570-621 8.27e-16

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 74.09  E-value: 8.27e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2119497975  570 EGELYTWGRGNYGRLGHGSSEDQTIPMLVTGLKGLKVIDVSCGSGdaQTLAV 621
Cdd:pfam00415    1 DGRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQVACGGD--HTVAL 50
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
3277-3325 1.00e-15

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 73.71  E-value: 1.00e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 2119497975 3277 GQVYAWGDNDHGQQGNGTTTVNRKPTLVQGLEGQKITRVACGSSHSVAW 3325
Cdd:pfam00415    2 GRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQVACGGDHTVAL 50
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
3224-3273 4.56e-15

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 71.78  E-value: 4.56e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2119497975 3224 SGVVWTWGKGDYFRLGHGTDVHVRKPQVVEGLRGKKIVHVAVGALHCLAV 3273
Cdd:pfam00415    1 DGRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQVACGGDHTVAL 50
ZZ cd02249
Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ...
2707-2751 5.84e-15

Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ZZ motif coordinates one or two zinc ions and most likely participates in ligand binding or molecular scaffolding. Many proteins containing ZZ motifs have other zinc-binding motifs as well, and the majority serve as scaffolds in pathways involving acetyltransferase, protein kinase, or ubiqitin-related activity. ZZ proteins can be grouped into the following functional classes: chromatin modifying, cytoskeletal scaffolding, ubiquitin binding or conjugating, and membrane receptor or ion-channel modifying proteins.


Pssm-ID: 239069 [Multi-domain]  Cd Length: 46  Bit Score: 71.31  E-value: 5.84e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 2119497975 2707 VTCDGCQMfPINGPRFKCRNCDDFDFCETCFKTR--KHNTRHTFGRI 2751
Cdd:cd02249      1 YSCDGCLK-PIVGVRYHCLVCEDFDLCSSCYAKGkkGHPPDHSFTEI 46
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
4113-4163 1.29e-14

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 70.62  E-value: 1.29e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2119497975 4113 GDLYTWGKGRYGRLGHGDSEDQLKPKLVEALQGYRVIDIACGSGdaQTLCL 4163
Cdd:pfam00415    2 GRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQVACGGD--HTVAL 50
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
3066-3115 1.73e-14

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 70.24  E-value: 1.73e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2119497975 3066 DGKVFSWGEGDDGKLGHFSRMNCDKPRLIEALKTKRIRDIACGSSHSAAI 3115
Cdd:pfam00415    1 DGRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQVACGGDHTVAL 50
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
4218-4266 1.99e-14

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 70.24  E-value: 1.99e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 2119497975 4218 SGSVYTWGKGDYHRLGHGSDDHVRRPRQVQGLQGKKVIAIATGSLHCVC 4266
Cdd:pfam00415    1 DGRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQVACGGDHTVA 49
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
4270-4319 2.39e-14

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 69.85  E-value: 2.39e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2119497975 4270 DGEVYTWGDNDEGQLGDGTTNAIQRPRLVAALQGKKINRVACGSAHTLAW 4319
Cdd:pfam00415    1 DGRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQVACGGDHTVAL 50
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
4060-4109 4.34e-14

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 69.08  E-value: 4.34e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2119497975 4060 EGEVYSWGEAEDGKLGHGNRSPCDRPRVIESLRGIEVVDIAAGGAHSACI 4109
Cdd:pfam00415    1 DGRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQVACGGDHTVAL 50
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
3118-3169 9.86e-14

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 67.93  E-value: 9.86e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2119497975 3118 SGELYTWGLGEYGRLGHGDNTTQLKPKMVKVLLGHRVIQVACGSRdaQTLAL 3169
Cdd:pfam00415    1 DGRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQVACGGD--HTVAL 50
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
4166-4215 2.67e-13

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 66.77  E-value: 2.67e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2119497975 4166 DDTVWSWGDGDYGKLGRGGSDGCKVPMKIDSLTGLGVVKVECGSQFSVAL 4215
Cdd:pfam00415    1 DGRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQVACGGDHTVAL 50
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
3172-3221 2.80e-13

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 66.77  E-value: 2.80e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2119497975 3172 EGLVFSWGDGDFGKLGRGGSEGCNIPQNIERLNGQGVCQIECGAQFSLAL 3221
Cdd:pfam00415    1 DGRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQVACGGDHTVAL 50
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
624-673 3.75e-13

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 66.39  E-value: 3.75e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2119497975  624 NGQVWSWGDGDYGKLGRGGSDGCKTPKLIEKLQDLDVVKVRCGSQFSVAL 673
Cdd:pfam00415    1 DGRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQVACGGDHTVAL 50
UBA_HERC1_2 cd14331
UBA domain found in probable E3 ubiquitin-protein ligase HERC1, HERC2 and similar proteins; ...
2465-2505 1.75e-12

UBA domain found in probable E3 ubiquitin-protein ligase HERC1, HERC2 and similar proteins; HERC1, also called HECT domain and RCC1-like domain-containing protein 1, p532, or p619, is an ubiquitously expressed giant protein involved in ubiquitin-dependent intracellular membrane trafficking through its interaction with vesicle coat proteins such as clathrin and ARF. Moreover, it has been identified as a tuberous sclerosis complex TSC2-interacting protein that may play a role in TSC-mTOR (mammalian target of rapamycin) pathway. HERC2, also called HECT domain and RCC1-like domain-containing protein 2, is a SUMO-regulated E3 ubiquitin ligase that plays an important role in the SUMO-dependent pathway which orchestrates the DNA double-strand break (DSB) response. Moreover, HERC2 functions as a RNF8 auxiliary factor that regulates ubiquitin-dependent retention of repair proteins on damaged chromosomes. HERC1 and HERC2 are multi-domain proteins with different domain organizations. Both of them contain a ubiquitin-association (UBA) domain, more than one RCC1-like domains (RLDs) and a C-terminal HECT E3 ubiquitin ligase domain.


Pssm-ID: 270516  Cd Length: 40  Bit Score: 64.36  E-value: 1.75e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 2119497975 2465 VVQLMEMGFPRKNIEFALKSlTGSASGLPGVEALVGWLLDH 2505
Cdd:cd14331      1 IVQLMEMGFSRRQIEMAMQA-LGSESDAPNIENLVNWLLEH 40
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
515-567 2.95e-12

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 64.08  E-value: 2.95e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2119497975  515 GEVFSWGCGDGGRLGHGDTVPLEEPKMISALSgkqaGKHVVHIACGSTYSAAI 567
Cdd:pfam00415    2 GRVYTWGRNDYGQLGLGTTENVLVPQKVEGLS----GNKVVQVACGGDHTVAL 50
ZZ_Mind_bomb cd02339
Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. ...
2707-2751 5.01e-12

Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Mind bomb is an E3 ubiqitin ligase that has been shown to regulate signaling by the Notch ligand Delta in Drosophila melanogaster.


Pssm-ID: 239079  Cd Length: 45  Bit Score: 63.25  E-value: 5.01e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 2119497975 2707 VTCDGCQMFPINGPRFKCRNCDDFDFCETCFKTRKHNTRHTFGRI 2751
Cdd:cd02339      1 IICDTCRKQGIIGIRWKCAECPNYDLCTTCYHGDKHDLEHRFYRY 45
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
2703-2746 1.34e-11

Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain present in dystrophin-like proteins, and CREB-binding protein/p300 homologues. The ZZ in dystrophin appears to bind calmodulin. A missense mutation of one of the conserved cysteines in dystrophin results in a patient with Duchenne muscular dystrophy.


Pssm-ID: 197633 [Multi-domain]  Cd Length: 44  Bit Score: 62.07  E-value: 1.34e-11
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 2119497975  2703 IHPGVTCDGCQmFPINGPRFKCRNCDDFDFCETCFKTRKHNTRH 2746
Cdd:smart00291    1 VHHSYSCDTCG-KPIVGVRYHCLVCPDYDLCQSCFAKGSAGGEH 43
ZZ_NBR1_like cd02340
Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 ...
2707-2751 1.40e-11

Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Drosophila ref(2)P appears to control the multiplication of sigma rhabdovirus. NBR1 (Next to BRCA1 gene 1 protein) interacts with fasciculation and elongation protein zeta-1 (FEZ1) and calcium and integrin binding protein (CIB), and may function in cell signalling pathways. Sequestosome 1 is a phosphotyrosine independent ligand for the Lck SH2 domain and binds noncovalently to ubiquitin via its UBA domain.


Pssm-ID: 239080  Cd Length: 43  Bit Score: 61.89  E-value: 1.40e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 2119497975 2707 VTCDGCQmFPINGPRFKCRNCDDFDFCETCFKTRKHNTrHTFGRI 2751
Cdd:cd02340      1 VICDGCQ-GPIVGVRYKCLVCPDYDLCESCEAKGVHPE-HAMLKI 43
ZZ_PCMF_like cd02338
Zinc finger, ZZ type. Zinc finger present in potassium channel modulatory factor (PCMF) 1 and ...
2707-2749 3.41e-10

Zinc finger, ZZ type. Zinc finger present in potassium channel modulatory factor (PCMF) 1 and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Human potassium channel modulatory factor 1 or FIGC has been shown to possess intrinsic E3 ubiquitin ligase activity and to promote ubiquitination.


Pssm-ID: 239078  Cd Length: 49  Bit Score: 58.13  E-value: 3.41e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 2119497975 2707 VTCDGCQMFPINGPRFKCRNCDDFDFCETCFKTRKHNTRHTFG 2749
Cdd:cd02338      1 VSCDGCGKSNFTGRRYKCLICYDYDLCADCYDSGVTTERHLFD 43
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
2703-2742 3.44e-09

Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds calmodulin. Putative zinc finger; binding not yet shown. Four to six cysteine residues in its sequence are responsible for coordinating zinc ions, to reinforce the structure.


Pssm-ID: 395451  Cd Length: 45  Bit Score: 55.18  E-value: 3.44e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 2119497975 2703 IHPGVTCDGCQMFPINGPRFKCRNCDDFDFCETCFKTRKH 2742
Cdd:pfam00569    1 IHKVYTCNGCSNDPSIGVRYHCLRCSDYDLCQSCFQTHKG 40
RCC1_2 pfam13540
Regulator of chromosome condensation (RCC1) repeat;
3260-3289 7.83e-09

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 463914 [Multi-domain]  Cd Length: 30  Bit Score: 53.58  E-value: 7.83e-09
                           10        20        30
                   ....*....|....*....|....*....|
gi 2119497975 3260 IVHVAVGALHCLAVTDTGQVYAWGDNDHGQ 3289
Cdd:pfam13540    1 VVSVAAGDNHTLALTSDGRVYCWGDNSYGQ 30
Cyt-b5 pfam00173
Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from ...
1212-1284 1.54e-08

Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from a diverse range of proteins. This family also includes proteins that bind to steroids. The family includes progesterone receptors. Many members of this subfamily are membrane anchored by an N-terminal transmembrane alpha helix. This family also includes a domain in some chitin synthases. There is no known ligand for this domain in the chitin synthases.


Pssm-ID: 459698 [Multi-domain]  Cd Length: 74  Bit Score: 54.16  E-value: 1.54e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2119497975 1212 RKADLENHNKDGGFWTVIDGKVYDIKDFQTQSLTGNSILAQFAGDDPVVALEAALQFEDTRESMHA-FCVGQYM 1284
Cdd:pfam00173    1 TLEELSKHNGDGDCWVAINGKVYDVTKFLKEHPGGEDVILSAAGKDATDAFEAIGHSEDAAEKLLKkYRIGELA 74
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
3011-3063 3.16e-08

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 52.52  E-value: 3.16e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2119497975 3011 EGKVYACGEATNGRLGLGiSSGTVPIPRQITALSNYVVKKVAvhSGGRHAMAL 3063
Cdd:pfam00415    1 DGRVYTWGRNDYGQLGLG-TTENVLVPQKVEGLSGNKVVQVA--CGGDHTVAL 50
APC10 cd08366
APC10 subunit of the anaphase-promoting complex (APC) that mediates substrate ubiquitination; ...
2792-2912 8.39e-08

APC10 subunit of the anaphase-promoting complex (APC) that mediates substrate ubiquitination; This model represents the single domain protein APC10, a subunit of the anaphase-promoting complex (APC), which is a multi-subunit E3 ubiquitin ligase. E3 ubiquitin ligases mediate substrate ubiquitination (or ubiquitylation), a vital component of the ubiquitin-26S proteasome pathway for selective proteolytic degradation. The APC (also known as the cyclosome), is a cell cycle-regulated E3 ubiquitin ligase that controls important transitions in mitosis and the G1 phase by ubiquitinating regulatory proteins, thereby targeting them for degradation. In mitosis, the APC initiates sister chromatid separation by ubiquitinating the anaphase inhibitor securin and triggers exit from mitosis by ubiquitinating cyclin B. The C-terminus of APC10 binds to CDC27/APC3, an APC subunit that contains multiple tetratrico peptide repeats. APC10 domains are homologous to the DOC1 domains present in the HECT (Homologous to the E6-AP Carboxyl Terminus) E3 ubiquitin ligase protein, and the Cullin-RING (Really Interesting New Gene) E3 ubiquitin ligase complex. The APC10/DOC1 domain forms a beta-sandwich structure that is related in architecture to the galactose-binding domain-like fold; their sequences are quite dissimilar, however, and are not included here.


Pssm-ID: 176484  Cd Length: 139  Bit Score: 54.10  E-value: 8.39e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497975 2792 VSSS-----VNQasrLIDGS-EPCWQSSGSQgKHWIRLEIFPDVLVHRLKMIVD-PADSSYMPSLVVVSGGNSLNNLIEL 2864
Cdd:cd08366     11 LSSAkpgngVDQ---LRDDSlDTYWQSDGPQ-PHLINIQFSKKTDISAVALYLDyKLDESYTPSKISIRAGTSPHDLQEV 86
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2119497975 2865 KT-----------ININPADTTVPLLTDCteyhryIEVAIKQCRSSGIDCKIHGLIILG 2912
Cdd:cd08366     87 RTveleepngwvhIPLEDNRDGKPLRTFF------LQIAILSNHQNGRDTHIRQIKVYG 139
RCC1_2 pfam13540
Regulator of chromosome condensation (RCC1) repeat;
4254-4283 1.23e-07

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 463914 [Multi-domain]  Cd Length: 30  Bit Score: 50.12  E-value: 1.23e-07
                           10        20        30
                   ....*....|....*....|....*....|
gi 2119497975 4254 VIAIATGSLHCVCCTEDGEVYTWGDNDEGQ 4283
Cdd:pfam13540    1 VVSVAAGDNHTLALTSDGRVYCWGDNSYGQ 30
RCC1_2 pfam13540
Regulator of chromosome condensation (RCC1) repeat;
3102-3131 1.67e-07

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 463914 [Multi-domain]  Cd Length: 30  Bit Score: 49.73  E-value: 1.67e-07
                           10        20        30
                   ....*....|....*....|....*....|
gi 2119497975 3102 IRDIACGSSHSAAITSSGELYTWGLGEYGR 3131
Cdd:pfam13540    1 VVSVAAGDNHTLALTSDGRVYCWGDNSYGQ 30
ZZ_dystrophin cd02334
Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif ...
2707-2746 3.95e-07

Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Dystrophin attaches actin filaments to an integral membrane glycoprotein complex in muscle cells. The ZZ domain in dystrophin has been shown to be essential for binding to the membrane protein beta-dystroglycan.


Pssm-ID: 239074  Cd Length: 49  Bit Score: 49.28  E-value: 3.95e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 2119497975 2707 VTCDGCQMFPINGPRFKCRNCDDFDFCETCF----KTRKHNTRH 2746
Cdd:cd02334      1 AKCNICKEFPITGFRYRCLKCFNYDLCQSCFfsgrTSKSHKNSH 44
ZZ_UBA_plant cd02342
Zinc finger, ZZ type. Zinc finger present in plant ubiquitin-associated (UBA) proteins. The ZZ ...
2707-2737 6.21e-07

Zinc finger, ZZ type. Zinc finger present in plant ubiquitin-associated (UBA) proteins. The ZZ motif coordinates a zinc ion and most likely participates in ligand binding or molecular scaffolding.


Pssm-ID: 239082  Cd Length: 43  Bit Score: 48.73  E-value: 6.21e-07
                           10        20        30
                   ....*....|....*....|....*....|.
gi 2119497975 2707 VTCDGCQMFPINGPRFKCRNCDDFDFCETCF 2737
Cdd:cd02342      1 IQCDGCGVLPITGPRYKSKVKEDYDLCTICF 31
ZZ_ADA2 cd02335
Zinc finger, ZZ type. Zinc finger present in ADA2, a putative transcriptional adaptor, and ...
2708-2748 2.79e-06

Zinc finger, ZZ type. Zinc finger present in ADA2, a putative transcriptional adaptor, and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding.


Pssm-ID: 239075 [Multi-domain]  Cd Length: 49  Bit Score: 46.90  E-value: 2.79e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 2119497975 2708 TCDGCQMFPINGPRFKCRNCDDFDFCETCFK----TRKHNTRHTF 2748
Cdd:cd02335      2 HCDYCSKDITGTIRIKCAECPDFDLCLECFSagaeIGKHRNDHNY 46
RCC1_2 pfam13540
Regulator of chromosome condensation (RCC1) repeat;
712-738 3.76e-06

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 463914 [Multi-domain]  Cd Length: 30  Bit Score: 45.88  E-value: 3.76e-06
                           10        20
                   ....*....|....*....|....*..
gi 2119497975  712 VVDVAAGSTHCLALTEDSEVHSWGSND 738
Cdd:pfam13540    1 VVSVAAGDNHTLALTSDGRVYCWGDNS 27
RCC1_2 pfam13540
Regulator of chromosome condensation (RCC1) repeat;
554-583 5.62e-06

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 463914 [Multi-domain]  Cd Length: 30  Bit Score: 45.49  E-value: 5.62e-06
                           10        20        30
                   ....*....|....*....|....*....|
gi 2119497975  554 VVHIACGSTYSAAITAEGELYTWGRGNYGR 583
Cdd:pfam13540    1 VVSVAAGDNHTLALTSDGRVYCWGDNSYGQ 30
ZZ_ZZZ3 cd02341
Zinc finger, ZZ type. Zinc finger present in ZZZ3 (ZZ finger containing 3) and related ...
2707-2746 7.19e-06

Zinc finger, ZZ type. Zinc finger present in ZZZ3 (ZZ finger containing 3) and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding.


Pssm-ID: 239081  Cd Length: 48  Bit Score: 45.89  E-value: 7.19e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 2119497975 2707 VTCDGCQMFPINGPRFKCRNCD--DFDFCETCF-KTRKHNTRH 2746
Cdd:cd02341      1 FKCDSCGIEPIPGTRYHCSECDdgDFDLCQDCVvKGESHQEDH 43
RCC1_2 pfam13540
Regulator of chromosome condensation (RCC1) repeat;
660-687 7.47e-06

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 463914 [Multi-domain]  Cd Length: 30  Bit Score: 45.11  E-value: 7.47e-06
                           10        20
                   ....*....|....*....|....*...
gi 2119497975  660 VVKVRCGSQFSVALTKDGQVYSWGKGDN 687
Cdd:pfam13540    1 VVSVAAGDNHTLALTSDGRVYCWGDNSY 28
RCC1_2 pfam13540
Regulator of chromosome condensation (RCC1) repeat;
4202-4231 9.36e-06

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 463914 [Multi-domain]  Cd Length: 30  Bit Score: 45.11  E-value: 9.36e-06
                           10        20        30
                   ....*....|....*....|....*....|
gi 2119497975 4202 VVKVECGSQFSVALTKSGSVYTWGKGDYHR 4231
Cdd:pfam13540    1 VVSVAAGDNHTLALTSDGRVYCWGDNSYGQ 30
RCC1_2 pfam13540
Regulator of chromosome condensation (RCC1) repeat;
4096-4125 5.97e-05

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 463914 [Multi-domain]  Cd Length: 30  Bit Score: 42.80  E-value: 5.97e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 2119497975 4096 VVDIAAGGAHSACITAAGDLYTWGKGRYGR 4125
Cdd:pfam13540    1 VVSVAAGDNHTLALTSDGRVYCWGDNSYGQ 30
UBA_HERC1 cd14401
UBA domain found in probable E3 ubiquitin-protein ligase HERC1 and similar proteins; HERC1, ...
2464-2506 1.06e-04

UBA domain found in probable E3 ubiquitin-protein ligase HERC1 and similar proteins; HERC1, also called HECT domain and RCC1-like domain-containing protein 1, or p532, or p619, is an ubiquitously expressed multi-domain protein involved in ubiquitin-dependent intracellular membrane trafficking through its interaction with vesicle coat proteins such as clathrin and ARF. Moreover, it has been identified as a tuberous sclerosis complex TSC2-interacting protein that may play a role in TSC-mTOR (mammalian target of rapamycin) pathway. In addition to a ubiquitin-association (UBA) domain, HERC1 contains more than one RCC1-like domains (RLDs) and a C-terminal HECT E3 ubiquitin ligase domain. At this point, it may function as both E3 ubiquitin ligases and guanine nucleotide exchange factors (GEFs).


Pssm-ID: 270584  Cd Length: 44  Bit Score: 42.37  E-value: 1.06e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 2119497975 2464 IVVQLMEMGFPRKNIEFALKSlTGSASGL--PGVEALVGWLLDHP 2506
Cdd:cd14401      1 IAVPLLEMGFSLRHITRAMEA-TGTRGEAdaRNINVLATWMIEHP 44
UBA1_atUBP14 cd14295
UBA1 domain found in Arabidopsis thaliana ubiquitin carboxyl-terminal hydrolase 14 (atUBP14) ...
2464-2507 1.26e-04

UBA1 domain found in Arabidopsis thaliana ubiquitin carboxyl-terminal hydrolase 14 (atUBP14) and similar proteins; atUBP14, also called deubiquitinating enzyme 14, TITAN-6 protein, ubiquitin thioesterase 14, or ubiquitin-specific-processing protease 14, is related to the isopeptidase T class of deubiquitinating enzymes that recycle polyubiquitin chains following protein degradation. atUBP14 is essential for early plant development. It can disassemble multi-ubiquitin chains linked internally via epsilon-amino isopeptide bonds using Lys48 and can process some, but not all, translational fusions of ubiquitin linked via alpha-amino peptide bonds. atUBP14 contains two ubiquitin-association (UBA) domains. This model corresponds to the UBA1 domain.


Pssm-ID: 270481 [Multi-domain]  Cd Length: 45  Bit Score: 42.36  E-value: 1.26e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 2119497975 2464 IVVQLMEMGFPRKNIEFALKsLTGSAsglpGVEALVGWLLDHPD 2507
Cdd:cd14295      4 LVAQLMEMGFPKVRAEKALF-FTQNK----GLEEAMEWLEEHSE 42
UBA_UBXN1 cd14302
UBA domain found in UBX domain-containing protein 1 (UBXN1) and similar proteins; UBXN1, also ...
2467-2507 1.75e-04

UBA domain found in UBX domain-containing protein 1 (UBXN1) and similar proteins; UBXN1, also called SAPK substrate protein 1 (SAKS1) or UBA/UBX 33.3 kDa protein, is a widely expressed protein containing an N-terminal ubiquitin-associated (UBA) domain, a coiled-coil region, and a C-terminal ubiquitin-like (UBX) domain. It binds polyubiquitin and valosin-containing protein (VCP), and has been identified as a substrate for stress-activated protein kinases (SAPKs). Moreover, UBXN1 specifically binds to Homer2b. It may also interact with ubiquitin (Ub) and may be involved in the Ub-proteasome proteolytic pathways. In addition, UBXN1 can associate with autoubiquitinated BRCA1 tumor suppressor and inhibit its enzymatic function through its UBA domain.


Pssm-ID: 270487 [Multi-domain]  Cd Length: 41  Bit Score: 41.51  E-value: 1.75e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 2119497975 2467 QLMEMGFPRKNIEFALksltgSASGLPGVEALVGWLLDHPD 2507
Cdd:cd14302      5 TLIEMGFSRNRAEKAL-----AKTGNQGVEAAMEWLLAHED 40
RCC1_2 pfam13540
Regulator of chromosome condensation (RCC1) repeat;
3208-3235 1.86e-04

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 463914 [Multi-domain]  Cd Length: 30  Bit Score: 41.26  E-value: 1.86e-04
                           10        20
                   ....*....|....*....|....*...
gi 2119497975 3208 VCQIECGAQFSLALTKSGVVWTWGKGDY 3235
Cdd:pfam13540    1 VVSVAAGDNHTLALTSDGRVYCWGDNSY 28
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
3944-4014 2.60e-04

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: 46.51  E-value: 2.60e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497975 3944 PDDWT-LSAGGS--------GTIYGWGHNHRGQLGGieGAKVKVPTPcEALAALRPIQLI-GGEQTLFAVTADGKLYATG 4013
Cdd:COG5184    248 LTGVVaIAAGGShtcalksdGTVWCWGDNSYGQLGD--GTTTDRSTP-VKVPGLSGVVAVaAGSSHTCALLTDGTVWCWG 324

                   .
gi 2119497975 4014 Y 4014
Cdd:COG5184    325 D 325
RCC1_2 pfam13540
Regulator of chromosome condensation (RCC1) repeat;
3154-3184 4.25e-04

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 463914 [Multi-domain]  Cd Length: 30  Bit Score: 40.10  E-value: 4.25e-04
                           10        20        30
                   ....*....|....*....|....*....|.
gi 2119497975 3154 VIQVACGSRdaQTLALTDEGLVFSWGDGDFG 3184
Cdd:pfam13540    1 VVSVAAGDN--HTLALTSDGRVYCWGDNSYG 29
ZZ_CBP cd02337
Zinc finger, ZZ type. Zinc finger present in CBP/p300 and related proteins. The ZZ motif ...
2708-2742 4.70e-04

Zinc finger, ZZ type. Zinc finger present in CBP/p300 and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. CREB-binding protein (CBP) is a large multidomain protein that provides binding sites for transcriptional coactivators, the role of the ZZ domain in CBP/p300 is unclear.


Pssm-ID: 239077  Cd Length: 41  Bit Score: 40.62  E-value: 4.70e-04
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 2119497975 2708 TCDGCQMFPINgpRFKCRNCDDFDFCETCFKTRKH 2742
Cdd:cd02337      2 TCNECKHHVET--RWHCTVCEDYDLCITCYNTKNH 34
ZZ_dah cd02345
Zinc finger, ZZ type. Zinc finger present in Drosophila dah and related proteins. The ZZ motif ...
2708-2751 5.04e-04

Zinc finger, ZZ type. Zinc finger present in Drosophila dah and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Dah (discontinuous actin hexagon) is a membrane associated protein essential for cortical furrow formation in Drosophila.


Pssm-ID: 239085  Cd Length: 49  Bit Score: 40.65  E-value: 5.04e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 2119497975 2708 TCDGCQMFPINGPRFKCRNCDDFDFCETCF----KTRKHNTRHTFGRI 2751
Cdd:cd02345      2 SCSACRKQDISGIRFPCQVCRDYSLCLGCYtkgrETKRHNSLHIMYEL 49
RCC1_2 pfam13540
Regulator of chromosome condensation (RCC1) repeat;
3048-3078 8.20e-04

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 463914 [Multi-domain]  Cd Length: 30  Bit Score: 39.33  E-value: 8.20e-04
                           10        20        30
                   ....*....|....*....|....*....|.
gi 2119497975 3048 VKKVAvhSGGRHAMALTVDGKVFSWGEGDDG 3078
Cdd:pfam13540    1 VVSVA--AGDNHTLALTSDGRVYCWGDNSYG 29
TFP_LU_ECD_Sax cd23600
extracellular domain (ECD) found in Drosophila melanogaster Saxophone and similar proteins; ...
2720-2775 1.14e-03

extracellular domain (ECD) found in Drosophila melanogaster Saxophone and similar proteins; Saxophone (Sax) is the Drosophila bone morphogenetic protein (BMP) type I receptor that transmits signal through Mad. It functions as a Dpp (Decapentaplegic) receptor in Drosophila embryos, but that its activity is normally inhibited by the O-linked glycosyltransferase Sxc (Super sex combs). Saxophone is the ortholog of the human activin receptor-like kinase (ALK)-1/2. It contains an extracellular domain (ECD), which belongs to Ly-6 antigen/uPA receptor-like (LU) superfamily and exhibits a snake toxin-like fold (also known as three-finger toxin/3FTx fold or three-fingered protein/TFP domain fold).


Pssm-ID: 467129  Cd Length: 89  Bit Score: 40.75  E-value: 1.14e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2119497975 2720 PRFKCRNCDDFD-----FCE---TCFK--TRKHNTRHTFGR--INEPGQSPVFCG---RSGKQLKRCHSSQ 2775
Cdd:cd23600      2 KRFKCYSCEPPDcdpttVCSnaiQCWKsrVRDSDGKERVSRgcITEPDQVPFTCNtksHSGSSKKKPNSGQ 72
UBA1_scUBP14_like cd14296
UBA1 domain found in Saccharomyces cerevisiae ubiquitin carboxyl-terminal hydrolase 14 ...
2464-2505 1.95e-03

UBA1 domain found in Saccharomyces cerevisiae ubiquitin carboxyl-terminal hydrolase 14 (scUBP14) and similar proteins; scUBP14, also called deubiquitinating enzyme 14, glucose-induced degradation protein 6, ubiquitin thioesterase 14, or ubiquitin-specific-processing protease 14, is the yeast ortholog of human Isopeptidase T (USP5), a deubiquitinating enzyme known to bind the 29-linked polyubiquitin chains. scUBP14 has been identified as a K29-linked polyubiquitin binding protein as well. It is involved in K29-linked polyubiquitin metabolism by binding to the 29-linked Ub4 resin and serving as an internal positive control in budding yeast. Members in this family contain two tandem ubiquitin-association (UBA) domains. This model corresponds to the UBA1 domain.


Pssm-ID: 270482 [Multi-domain]  Cd Length: 39  Bit Score: 38.77  E-value: 1.95e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 2119497975 2464 IVVQLMEMGFPRKNIEFALKSlTGSASglpgVEALVGWLLDH 2505
Cdd:cd14296      3 AVSQLMSMGFSENAAKRALYY-TGNSS----VEAAMNWLFEH 39
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
2961-3008 2.20e-03

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 38.65  E-value: 2.20e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 2119497975 2961 KVFVWGLNDKDQLG-GLKGSKiKVPSFSETLSALNVVQVAGGSKSLFAV 3008
Cdd:pfam00415    3 RVYTWGRNDYGQLGlGTTENV-LVPQKVEGLSGNKVVQVACGGDHTVAL 50
ANAPC10 pfam03256
Anaphase-promoting complex, subunit 10 (APC10);
2804-2870 2.26e-03

Anaphase-promoting complex, subunit 10 (APC10);


Pssm-ID: 367420  Cd Length: 185  Bit Score: 42.43  E-value: 2.26e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2119497975 2804 DGSEPCWQSSGSQgKHWIRLEIFPDVLVHRLKMIVDPA-DSSYMPSLVVVSGGNSLNNLIELKTININ 2870
Cdd:pfam03256   48 DNLDTYWQSDGSQ-PHLVNIQFRKKTPVKYVAIYLDYKlDESYTPSKISVRAGTGFNDLQEVRVVDLE 114
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
728-777 2.93e-03

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 38.27  E-value: 2.93e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2119497975  728 DSEVHSWGSNDQCQhfdtL----RITKPEPTALPGLDTKHIVGIACGPAQSFAW 777
Cdd:pfam00415    1 DGRVYTWGRNDYGQ----LglgtTENVLVPQKVEGLSGNKVVQVACGGDHTVAL 50
ZZ_EF cd02343
Zinc finger, ZZ type. Zinc finger present in proteins with an EF_hand motif. The ZZ motif ...
2707-2737 3.04e-03

Zinc finger, ZZ type. Zinc finger present in proteins with an EF_hand motif. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding.


Pssm-ID: 239083  Cd Length: 48  Bit Score: 38.45  E-value: 3.04e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 2119497975 2707 VTCDGC-QMFPINgpRFKCRNCDDFDFCETCF 2737
Cdd:cd02343      1 ISCDGCdEIAPWH--RYRCLQCTDMDLCKTCF 30
SH3_15 pfam18346
Mind bomb SH3 repeat domain; The REP domain of Mind bomb which serves as the substrate ...
2640-2697 4.01e-03

Mind bomb SH3 repeat domain; The REP domain of Mind bomb which serves as the substrate recognition domain for a second, membrane-distal epitope of the Notch ligand (C-box). Although the first Mib repeat of REP may play a dominant role in ligand binding, the two repeats appear to cooperate in the engagement of the Jag1 tail. Mind bomb (Mib) proteins are large, multi-domain E3 ligases that promote ubiquitination of the cytoplasmic tails of Notch ligands. The structure and functional analysis, show that Mib1 contains two independent substrate recognition domains that engage two distinct epitopes from the cytoplasmic tail of the ligand Jagged1, one in the intracellular membrane proximal region and the other near the C terminus. REP domains have a five-stranded anti-parallel twisted beta sheet topology similar to that of SH3 domains.


Pssm-ID: 465720  Cd Length: 67  Bit Score: 38.76  E-value: 4.01e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2119497975 2640 IKIGDKVRVKTSVTTPK------YKWG---SVTHRSVGVVKAFSANGkDVIVDFPQQSH-WTGLLSEM 2697
Cdd:pfam18346    1 FEVGDWVRVKDDLEKVKplqeghGGWNggmAETLGSVGTVVKVDADG-DLRVQFPGGGRrWTLNPAAL 67
RCC1_2 pfam13540
Regulator of chromosome condensation (RCC1) repeat;
4042-4072 4.07e-03

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 463914 [Multi-domain]  Cd Length: 30  Bit Score: 37.40  E-value: 4.07e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 2119497975 4042 IKKVAvnSGGKHCLALSSEGEVYSWGEAEDG 4072
Cdd:pfam13540    1 VVSVA--AGDNHTLALTSDGRVYCWGDNSYG 29
UBA_atUPL1_2_like cd14327
UBA domain found in Arabidopsis thaliana E3 ubiquitin-protein ligase UPL1 (atUPL1), UPL2 ...
2463-2505 8.53e-03

UBA domain found in Arabidopsis thaliana E3 ubiquitin-protein ligase UPL1 (atUPL1), UPL2 (atUPL2) and similar proteins; The family includes two highly similar 405-kDa HECT E3 ubiquitin-protein ligases (UPLs), UPL1 and UPL2, from Arabidopsis thaliana. The HECT E3 UPL family plays a prominent role in the ubiquitination of plant proteins. The biological functions of UPL1 and UPL2 remain unclear. Both of them contain a ubiquitin-associated (UBA) domain and a C-terminal HECT domain. UBA domain may be involved in ubiquitin metabolism. HECT domain is necessary and sufficient for their E3 catalytic activity, but requires ATP, E1 and an E2 of the Arabidopsis UBC8 family to ubiquitinate proteins.


Pssm-ID: 270512 [Multi-domain]  Cd Length: 38  Bit Score: 36.89  E-value: 8.53e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 2119497975 2463 PIVVQLMEMGFPRKNIEFALKsltgsASGLPGVEALVGWLLDH 2505
Cdd:cd14327      1 EAVAQLVEMGFSRERAEEALR-----AVGTNSVELAMEWLFTN 38
 
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.
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