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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303077 2765 KQLKRCHSSQP------GMLLDSWSRMVKSLNVSSSVNQASRLIDGSEPCWQSSGSQGKHWIRLEIFPDVLVHRLKMIVD 2838
Cdd:cd08664      1 GKPGKYHRNDPelnageGDLIDDWSRCVRSLTVSSNENQAKRLIDGSGSYWQSSGSQGKHWIRLELHPDVLIHSLKIIVD 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217303077 2839 PADSSYMPSLVVVSGGNSLNNLIELKTININPSDTTVPLLNDCTEYHRYIEIAIKQCRSSGIDCKIHGLILL 2910
Cdd:cd08664     81 PADSSYMPSLVVVSGGDSLNSLKELKTINVNATDTLVTLLQDVKEYYRYIEIAIKQCRNNGIDCKIHGLNII 152

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.

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217303077 2554 RADFLSNDDYAVYVRENIQVGMMVRCCRAYEEVCEGDVGKVIKLDRDGLHDLNVQCDWQQKGGTYWVRYIHVELIGYP 2631
Cdd:pfam11515    1 RSDFASRDDYAEYVRDNLAPGMRVRCCRDYEEVSAGDEGEVIQSNRGGLHDLNVQVDWQSKGRTYWVHWHHVEILGFP 78

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

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217303077 1870 GTRVMRGVDWKWGDQDGPPPGLGRVI-----GELGEDGWIRVQWDTGSTNSYRMGKEGKYDLKLAE 1930
Cdd:pfam06701    1 GARVVRGPDWKWGDQDGGEGHVGTVVeirdwDSESPRSTVRVQWDNGSTNVYRVGYEGKYDLKVVD 66

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.

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217303077 1211 RKADLENHNKDGGFWTVIDGKVYDIKDFQTQSLTGNSILAQFAGEDPVVALEAALQFEDTRESMHA-FCVGQY 1282
Cdd:pfam00173    1 TLEELSKHNGDGDCWVAINGKVYDVTKFLKEHPGGEDVILSAAGKDATDAFEAIGHSEDAAEKLLKkYRIGEL 73

Regulator of chromosome condensation (RCC1) repeat;

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 2217303077 2960 KVFVWGLNDKDQLG-GLKGSKiKVPSFSETLSALNVVQVAGGSKSLFA 3006
Cdd:pfam00415    3 RVYTWGRNDYGQLGlGTTENV-LVPQKVEGLSGNKVVQVACGGDHTVA 49

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303077 2765 KQLKRCHSSQP------GMLLDSWSRMVKSLNVSSSVNQASRLIDGSEPCWQSSGSQGKHWIRLEIFPDVLVHRLKMIVD 2838
Cdd:cd08664      1 GKPGKYHRNDPelnageGDLIDDWSRCVRSLTVSSNENQAKRLIDGSGSYWQSSGSQGKHWIRLELHPDVLIHSLKIIVD 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217303077 2839 PADSSYMPSLVVVSGGNSLNNLIELKTININPSDTTVPLLNDCTEYHRYIEIAIKQCRSSGIDCKIHGLILL 2910
Cdd:cd08664     81 PADSSYMPSLVVVSGGDSLNSLKELKTINVNATDTLVTLLQDVKEYYRYIEIAIKQCRNNGIDCKIHGLNII 152

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.

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217303077 2554 RADFLSNDDYAVYVRENIQVGMMVRCCRAYEEVCEGDVGKVIKLDRDGLHDLNVQCDWQQKGGTYWVRYIHVELIGYP 2631
Cdd:pfam11515    1 RSDFASRDDYAEYVRDNLAPGMRVRCCRDYEEVSAGDEGEVIQSNRGGLHDLNVQVDWQSKGRTYWVHWHHVEILGFP 78

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

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217303077 1870 GTRVMRGVDWKWGDQDGPPPGLGRVI-----GELGEDGWIRVQWDTGSTNSYRMGKEGKYDLKLAE 1930
Cdd:pfam06701    1 GARVVRGPDWKWGDQDGGEGHVGTVVeirdwDSESPRSTVRVQWDNGSTNVYRVGYEGKYDLKVVD 66

Regulator of chromosome condensation (RCC1) repeat;

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2217303077  675 DGQVYSWGKGDNQRLGHGTEEHVRYPKLLEGLQGKKVIDVAAGSTHCLAL 724
Cdd:pfam00415    1 DGRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQVACGGDHTVAL 50

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.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 2217303077 2702 IHPGVTCDGCQMFPINGSRFKCRNCDDFDFCETCFKTKKH 2741
Cdd:pfam00569    1 IHKVYTCNGCSNDPSIGVRYHCLRCSDYDLCQSCFQTHKG 40

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.

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217303077 2639 IKIGDKVRVKASVTTPK------YKWG---SVTHQSVGVVKAFSANGkDIIVDFPQQSH-WTGLLSEM 2696
Cdd:pfam18346    1 FEVGDWVRVKDDLEKVKplqeghGGWNggmAETLGSVGTVVKVDADG-DLRVQFPGGGRrWTLNPAAL 67

Regulator of chromosome condensation (RCC1) repeat;

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 2217303077 2960 KVFVWGLNDKDQLG-GLKGSKiKVPSFSETLSALNVVQVAGGSKSLFA 3006
Cdd:pfam00415    3 RVYTWGRNDYGQLGlGTTENV-LVPQKVEGLSGNKVVQVACGGDHTVA 49

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303077 2765 KQLKRCHSSQP------GMLLDSWSRMVKSLNVSSSVNQASRLIDGSEPCWQSSGSQGKHWIRLEIFPDVLVHRLKMIVD 2838
Cdd:cd08664      1 GKPGKYHRNDPelnageGDLIDDWSRCVRSLTVSSNENQAKRLIDGSGSYWQSSGSQGKHWIRLELHPDVLIHSLKIIVD 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217303077 2839 PADSSYMPSLVVVSGGNSLNNLIELKTININPSDTTVPLLNDCTEYHRYIEIAIKQCRSSGIDCKIHGLILL 2910
Cdd:cd08664     81 PADSSYMPSLVVVSGGDSLNSLKELKTINVNATDTLVTLLQDVKEYYRYIEIAIKQCRNNGIDCKIHGLNII 152

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303077 2779 LDSWsrmVKSLNVSSSVNQASRLIDG-SEPCWQSSGSQGKHWIRLEIFPDVLVHRLKMIVDPADSSYMPSLVVVSGGNSL 2857
Cdd:cd08365      1 TKCY---VESIEVSSNPADASRLTDGnTSTYWQSDGSQGSHWIRLKMKPDVLVRHLSLAVDATDSSYMPQRVVVAGGRSA 77

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2217303077 2858 NNLIELKTININPS-DTTVPLLNDCTEYHRYIEIAIKQCRSSGIDCKIHGLILL 2910
Cdd:cd08365     78 SNLQELRDVNIPPSvTGYVTLLEDATISQPYIEIRIKRCRSDGIDTRIHGLRIL 131

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303077 2786 VKSLNVSSSVNQASRLIDG-SEPCWQSSGSQGKHWIRLEIFPDVLVHRLKMIVDPADSSYMPSLVVVSGGNSLNNLIELK 2864
Cdd:cd08159      4 TASIEVSSNPLPVSRLTDGnYDTYWQSDGSQGSHWIRLFMKKDVLIRVLAIFVDMADSSYMPSLVVVYGGHSPSDLRELK 83

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 2217303077 2865 TININPSDTTVPLLNDCTEYHRYIEIAIKQCRSSGIDCKIHGLILL 2910
Cdd:cd08159     84 DVNIRPSNGWVALLEDDTLKCPYIEIRIKRCRSDGIDTRIRGLRLL 129

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.

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217303077 2554 RADFLSNDDYAVYVRENIQVGMMVRCCRAYEEVCEGDVGKVIKLDRDGLHDLNVQCDWQQKGGTYWVRYIHVELIGYP 2631
Cdd:pfam11515    1 RSDFASRDDYAEYVRDNLAPGMRVRCCRDYEEVSAGDEGEVIQSNRGGLHDLNVQVDWQSKGRTYWVHWHHVEILGFP 78

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.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 2217303077 2706 VTCDGCQMFPINGSRFKCRNCDDFDFCETCFKTKKHNTRHTFGRI 2750
Cdd:cd02344      1 VTCDGCQMFPINGPRFKCRNCDDFDFCENCFKTRKHNTRHTFGRI 45

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303077 2789 LNVSSSVNQASRLIDGS-EPCWQSSGSQGKHWIRLEIFPDVLVHRLKMIVDPADSSYMPSLVVVSGGNSLNNL-IELKTI 2866
Cdd:cd08665      7 VEVSSNPHRANKLTDGNpKTYWESNGSTGSHYINIHMHRGVVIRQLYMLVASEDSSYMPARVVVLGGDSPSCItTELNAV 86

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 2217303077 2867 NINPSDTTVPLLNDCTEYHRYIEIAIKQCRSSGIDCKIHGLILLG 2911
Cdd:cd08665     87 NVSPTASRVVLLENMTRFWPIIQIRIKRCQQGGIDTRVRGLEILG 131

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.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 2217303077 2460 PIVVQLMEMGFSRRNIEFALKSLTGASGnasSLPGVEALVGWLLDHSD 2507
Cdd:cd14402      1 PIVQQLMEMGFPRKNVEFALKSLSGSSG---GLPTPEALVAWLLEHPD 45

Regulator of chromosome condensation (RCC1) repeat;

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2217303077  569 EGELYTWGRGNYGRLGHGSSEDEAIPMLVAGLKGLKVIDVACGSGdaQTLAV 620
Cdd:pfam00415    1 DGRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQVACGGD--HTVAL 50

Regulator of chromosome condensation (RCC1) repeat;

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2217303077  514 GEVYSWGCGDGGRLGHGDTVPLEEPKVISAFSgkqaGKHVVHIACGSTYSAAI 566
Cdd:pfam00415    2 GRVYTWGRNDYGQLGLGTTENVLVPQKVEGLS----GNKVVQVACGGDHTVAL 50

Regulator of chromosome condensation (RCC1) repeat;

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2217303077  623 NGQVWSWGDGDYGKLGRGGSDGCKTPKLIEKLQDLDVVKVRCGSQFSIAL 672
Cdd:pfam00415    1 DGRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQVACGGDHTVAL 50

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.

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 2217303077  2702 IHPGVTCDGCQmFPINGSRFKCRNCDDFDFCETCFKTKKHNTRH 2745
Cdd:smart00291    1 VHHSYSCDTCG-KPIVGVRYHCLVCPDYDLCQSCFAKGSAGGEH 43

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.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 2217303077 2706 VTCDGCQmFPINGSRFKCRNCDDFDFCETCFKTKKHNTrHTFGRI 2750
Cdd:cd02340      1 VICDGCQ-GPIVGVRYKCLVCPDYDLCESCEAKGVHPE-HAMLKI 43

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.

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217303077 1211 RKADLENHNKDGGFWTVIDGKVYDIKDFQTQSLTGNSILAQFAGEDPVVALEAALQFEDTRESMHA-FCVGQY 1282
Cdd:pfam00173    1 TLEELSKHNGDGDCWVAINGKVYDVTKFLKEHPGGEDVILSAAGKDATDAFEAIGHSEDAAEKLLKkYRIGEL 73

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303077 2781 SWSrmvkslnVSSS-----VNQasrLIDGS-EPCWQSSGSQgKHWIRLEIFPDVLVHRLKMIVD-PADSSYMPSLVVVSG 2853
Cdd:cd08366      8 VWS-------LSSAkpgngVDQ---LRDDSlDTYWQSDGPQ-PHLINIQFSKKTDISAVALYLDyKLDESYTPSKISIRA 76

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217303077 2854 GNSLNNLIELKTINI-NPSDTTVPLLNDCTEYH----RYIEIAIKQCRSSGIDCKIHGLILLG 2911
Cdd:cd08366     77 GTSPHDLQEVRTVELeEPNGWVHIPLEDNRDGKplrtFFLQIAILSNHQNGRDTHIRQIKVYG 139

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.

                           10        20        30
                   ....*....|....*....|....*....|.
gi 2217303077 2706 VTCDGCQMFPINGSRFKCRNCDDFDFCETCF 2736
Cdd:cd02342      1 IQCDGCGVLPITGPRYKSKVKEDYDLCTICF 31

Regulator of chromosome condensation (RCC1) repeat;

                           10        20        30
                   ....*....|....*....|....*....|
gi 2217303077  553 VVHIACGSTYSAAITAEGELYTWGRGNYGR 582
Cdd:pfam13540    1 VVSVAAGDNHTLALTSDGRVYCWGDNSYGQ 30

Regulator of chromosome condensation (RCC1) repeat;

                           10        20
                   ....*....|....*....|....*...
gi 2217303077  659 VVKVRCGSQFSIALTKDGQVYSWGKGDN 686
Cdd:pfam13540    1 VVSVAAGDNHTLALTSDGRVYCWGDNSY 28

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.

                           10        20        30
                   ....*....|....*....|....*....|....*
gi 2217303077 2707 TCDGCQMFPinGSRFKCRNCDDFDFCETCFKTKKH 2741
Cdd:cd02337      2 TCNECKHHV--ETRWHCTVCEDYDLCITCYNTKNH 34

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.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 2217303077 2707 TCDGCQMFPINGSRFKCRNCDDFDFCETCF----KTKKHNTRHTFGRI 2750
Cdd:cd02345      2 SCSACRKQDISGIRFPCQVCRDYSLCLGCYtkgrETKRHNSLHIMYEL 49

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.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 2217303077 2464 QLMEMGFSRRNIEFALkSLTGASgnasslpGVEALVGWLLDHSD 2507
Cdd:cd14302      5 TLIEMGFSRNRAEKAL-AKTGNQ-------GVEAAMEWLLAHED 40

Anaphase-promoting complex, subunit 10 (APC10);

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303077 2803 DGSEPCWQSSGSQgKHWIRLEIFPDVLVHRLKMIVDPA-DSSYMPSLVVVSGGNSLNNLIELKTININ-PSD-TTVPLLN 2879
Cdd:pfam03256   48 DNLDTYWQSDGSQ-PHLVNIQFRKKTPVKYVAIYLDYKlDESYTPSKISVRAGTGFNDLQEVRVVDLEePTGwVHIPLRD 126

                           90       100       110
                   ....*....|....*....|....*....|....
gi 2217303077 2880 DCTEYHR--YIEIAIKQCRSSGIDC-----KIHG 2906
Cdd:pfam03256  127 ANGKPLRtfMLQIAVLSNHQNGRDThvrqiKIYG 160