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Conserved domains on  [gi|1002278019|ref|XP_015643339|]
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phosphatidylinositol 4-kinase gamma 4-like [Oryza sativa Japonica Group]

Protein Classification

phosphatidylinositol 4-kinase gamma( domain architecture ID 13217618)

phosphatidylinositol 4-kinase gamma catalyzes the phosphorylation of phosphatidylinositol (PI) to PI4P, the first committed step in the generation of phosphatidylinositol 4,5-bisphosphate (PIP2), a precursor of the second messenger inositol 1,4,5-trisphosphate (InsP3)

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PI3_PI4_kinase pfam00454
Phosphatidylinositol 3- and 4-kinase; Some members of this family probably do not have lipid ...
274-516 3.11e-54

Phosphatidylinositol 3- and 4-kinase; Some members of this family probably do not have lipid kinase activity and are protein kinases,.


:

Pssm-ID: 395364 [Multi-domain]  Cd Length: 241  Bit Score: 183.68  E-value: 3.11e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278019 274 GSGGVYFMQDASGEKN--IAVFKPRDEEPMAKNNP--RGLPVSTDGEGMKRGtLVGEGAFREVAAYILDHPigdheseer 349
Cdd:pfam00454   1 GYGGIYKVGDDLRQDEliLQVFKLMDEELSKDNLDlrRLKPYSVIPLGPKCG-IIEWVPNSETLAYILDEY--------- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278019 350 iGFSGVPPTALVRSLHR---------------GKSFKIGSLQMFIQNNGSCEDMG--PRAFpVKEVHKIAVLDLRLANAD 412
Cdd:pfam00454  71 -GENGVPPTAMVKILHSalnypklklefesriSLPPKVGLLQWFVKKSPDAEEWGeaRKNF-VRSCAGYSVLDYILGNGD 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278019 413 RHAGNILVCKDEEggnyKLVPIDHGYCLPEKFEDCTFEwlywpqAREPFsDETIAYIKSLDAEEDIKLLKFHGWELSARC 492
Cdd:pfam00454 149 RHLDNILVDKTTG----KLFHIDFGLCLPDAGKDLPFP------EKVPF-RLTREMVYAMGPSGDEGLFRELCETAYEAL 217
                         250       260
                  ....*....|....*....|....
gi 1002278019 493 ARVLCISTMLLKKGAARGLTPYDI 516
Cdd:pfam00454 218 RRNLNLLTNLLKLMVADGLPDWSI 241
Ubl1_cv_Nsp3_N-like super family cl28922
first ubiquitin-like (Ubl) domain located at the N-terminus of coronavirus SARS-CoV ...
39-113 2.48e-15

first ubiquitin-like (Ubl) domain located at the N-terminus of coronavirus SARS-CoV non-structural protein 3 (Nsp3) and related proteins; This ubiquitin-like (Ubl) domain (Ubl1) is found at the N-terminus of coronavirus Nsp3, a large multi-functional multi-domain protein which is an essential component of the replication/transcription complex (RTC). The functions of Ubl1 in CoVs are related to single-stranded RNA (ssRNA) binding and to interacting with the nucleocapsid (N) protein. SARS-CoV Ubl1 has been shown to bind ssRNA having AUA patterns, and since the 5'-UTR of the SARS-CoV genome has a number of AUA repeats, it may bind there. In mouse hepatitis virus (MHV), this Ubl1 domain binds the cognate N protein. Adjacent to Ubl1 is a Glu-rich acidic region (also referred to as hypervariable region, HVR); Ubl1 together with HVR has been called Nsp3a. Currently, the function of HVR in CoVs is unknown. This model corresponds to one of two Ubl domains in Nsp3; the other is located N-terminal to the papain-like protease (PLpro) and is not represented by this model.


The actual alignment was detected with superfamily member cd01802:

Pssm-ID: 475130 [Multi-domain]  Cd Length: 74  Bit Score: 70.82  E-value: 2.48e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002278019  39 SIIIFLAVPGAPpMPMSVLGSESIASVKLRIQRFKGFVVNKQRLVLDGHELARNNChVKDYGLADGNVLHLVIRL 113
Cdd:cd01802     1 MELFIETLTGTA-FELRVSPFETVASVKAKIQRLEGIPVSQQHLIWSGRELEDDYC-LHDYNITDGSTLKLVLAM 73
Ubl_ubiquitin_like cd17039
ubiquitin-like (Ubl) domain found in ubiquitin and ubiquitin-like Ubl proteins; Ubiquitin-like ...
119-187 1.81e-08

ubiquitin-like (Ubl) domain found in ubiquitin and ubiquitin-like Ubl proteins; Ubiquitin-like (Ubl) proteins have a similar ubiquitin (Ub) beta-grasp fold and attach to other proteins in a Ubl manner but with biochemically distinct roles. Ub and Ubl proteins conjugate and deconjugate via ligases and peptidases to covalently modify target polypeptides. Some Ubl domains have adaptor roles in Ub-signaling by mediating protein-protein interaction. Prokaryotic sulfur carrier proteins are Ub-related proteins that can be activated in an ATP-dependent manner. Polyubiquitination signals for a diverse set of cellular events via different isopeptide linkages formed between the C terminus of one ubiquitin (Ub) and the epsilon-amine of K6, K11, K27, K29, K33, K48, or K63 of a second Ub. One of these seven lysine residues (K27, Ub numbering) is conserved in this Ubl_ubiquitin_like family. K27-linked Ub chains are versatile and can be recognized by several downstream receptor proteins. K27 has roles beyond chain linkage, such as in Ubl NEDD8 (which contains many of the same lysines (K6, K11, K27, K33, K48) as Ub) where K27 has a role (other than conjugation) in the mechanism of protein neddylation.


:

Pssm-ID: 340559 [Multi-domain]  Cd Length: 68  Bit Score: 51.06  E-value: 1.81e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002278019 119 INIETTSGKKFQFQVDQSRNVKYLKSKLAvegdEDLG---EDHKLECDGKELEDHQLIADISKKDDAVIHLF 187
Cdd:cd17039     1 ITVKTLDGKTYTVEVDPDDTVADLKEKIE----EKTGipvEQQRLIYNGKELKDDKTLSDYGIKDGSTIHLV 68
 
Name Accession Description Interval E-value
PI3_PI4_kinase pfam00454
Phosphatidylinositol 3- and 4-kinase; Some members of this family probably do not have lipid ...
274-516 3.11e-54

Phosphatidylinositol 3- and 4-kinase; Some members of this family probably do not have lipid kinase activity and are protein kinases,.


Pssm-ID: 395364 [Multi-domain]  Cd Length: 241  Bit Score: 183.68  E-value: 3.11e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278019 274 GSGGVYFMQDASGEKN--IAVFKPRDEEPMAKNNP--RGLPVSTDGEGMKRGtLVGEGAFREVAAYILDHPigdheseer 349
Cdd:pfam00454   1 GYGGIYKVGDDLRQDEliLQVFKLMDEELSKDNLDlrRLKPYSVIPLGPKCG-IIEWVPNSETLAYILDEY--------- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278019 350 iGFSGVPPTALVRSLHR---------------GKSFKIGSLQMFIQNNGSCEDMG--PRAFpVKEVHKIAVLDLRLANAD 412
Cdd:pfam00454  71 -GENGVPPTAMVKILHSalnypklklefesriSLPPKVGLLQWFVKKSPDAEEWGeaRKNF-VRSCAGYSVLDYILGNGD 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278019 413 RHAGNILVCKDEEggnyKLVPIDHGYCLPEKFEDCTFEwlywpqAREPFsDETIAYIKSLDAEEDIKLLKFHGWELSARC 492
Cdd:pfam00454 149 RHLDNILVDKTTG----KLFHIDFGLCLPDAGKDLPFP------EKVPF-RLTREMVYAMGPSGDEGLFRELCETAYEAL 217
                         250       260
                  ....*....|....*....|....
gi 1002278019 493 ARVLCISTMLLKKGAARGLTPYDI 516
Cdd:pfam00454 218 RRNLNLLTNLLKLMVADGLPDWSI 241
Ubl_ZFAND4 cd01802
ubiquitin-like (Ubl) domain found in AN1-type zinc finger protein 4 (ZFAND4) and similar ...
39-113 2.48e-15

ubiquitin-like (Ubl) domain found in AN1-type zinc finger protein 4 (ZFAND4) and similar proteins; ZFAND4, also termed AN1-type zinc finger and ubiquitin domain-containing protein-like 1 (ANUBL1), may function as an oncogene that promotes proliferation and regulates relevant tumor suppressor genes in gastric cancer, suggesting a role in gastric cancer initiation and progression. ZFAND4contains an N-terminal ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, a common structure involved in protein-protein interactions, as well as a C-terminal AN1-type zinc finger. Unlike ubiquitin polyproteins and most ubiquitin fusion proteins, the N-terminal Ubl domain of ZFAND4 does not undergo proteolytic processing.


Pssm-ID: 340500 [Multi-domain]  Cd Length: 74  Bit Score: 70.82  E-value: 2.48e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002278019  39 SIIIFLAVPGAPpMPMSVLGSESIASVKLRIQRFKGFVVNKQRLVLDGHELARNNChVKDYGLADGNVLHLVIRL 113
Cdd:cd01802     1 MELFIETLTGTA-FELRVSPFETVASVKAKIQRLEGIPVSQQHLIWSGRELEDDYC-LHDYNITDGSTLKLVLAM 73
ubiquitin pfam00240
Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog) ...
53-113 2.04e-10

Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog), Nedd8, Elongin B, Rub1, and Parkin. A number of them are thought to carry a distinctive five-residue motif termed the proteasome-interacting motif (PIM), which may have a biologically significant role in protein delivery to proteasomes and recruitment of proteasomes to transcription sites.


Pssm-ID: 459726 [Multi-domain]  Cd Length: 72  Bit Score: 56.80  E-value: 2.04e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002278019  53 PMSVLGSESIASVKLRIQRFKGFVVNKQRLVLDGHELaRNNCHVKDYGLADGNVLHLVIRL 113
Cdd:pfam00240  12 TLEVDPTDTVLELKEKIAEKEGVPPEQQRLIYSGKVL-EDDQTLGEYGIEDGSTIHLVLRQ 71
UBI4 COG5272
Ubiquitin [Posttranslational modification, protein turnover, chaperones];
42-119 2.11e-09

Ubiquitin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444084 [Multi-domain]  Cd Length: 213  Bit Score: 57.88  E-value: 2.11e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002278019  42 IFLAVPGAPPMPMSVLGSESIASVKLRIQRFKGFVVNKQRLVLDGHELARNNChVKDYGLADGNVLHLVIRLADLRLI 119
Cdd:COG5272     3 IFVKTLTGKTITLEVEPNDTIEAVKAKIQDKEGIPPDQQRLIFAGKQLEDDRT-LADYNIQKESTLHLVTRTLGISEI 79
Ubl_ubiquitin_like cd17039
ubiquitin-like (Ubl) domain found in ubiquitin and ubiquitin-like Ubl proteins; Ubiquitin-like ...
119-187 1.81e-08

ubiquitin-like (Ubl) domain found in ubiquitin and ubiquitin-like Ubl proteins; Ubiquitin-like (Ubl) proteins have a similar ubiquitin (Ub) beta-grasp fold and attach to other proteins in a Ubl manner but with biochemically distinct roles. Ub and Ubl proteins conjugate and deconjugate via ligases and peptidases to covalently modify target polypeptides. Some Ubl domains have adaptor roles in Ub-signaling by mediating protein-protein interaction. Prokaryotic sulfur carrier proteins are Ub-related proteins that can be activated in an ATP-dependent manner. Polyubiquitination signals for a diverse set of cellular events via different isopeptide linkages formed between the C terminus of one ubiquitin (Ub) and the epsilon-amine of K6, K11, K27, K29, K33, K48, or K63 of a second Ub. One of these seven lysine residues (K27, Ub numbering) is conserved in this Ubl_ubiquitin_like family. K27-linked Ub chains are versatile and can be recognized by several downstream receptor proteins. K27 has roles beyond chain linkage, such as in Ubl NEDD8 (which contains many of the same lysines (K6, K11, K27, K33, K48) as Ub) where K27 has a role (other than conjugation) in the mechanism of protein neddylation.


Pssm-ID: 340559 [Multi-domain]  Cd Length: 68  Bit Score: 51.06  E-value: 1.81e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002278019 119 INIETTSGKKFQFQVDQSRNVKYLKSKLAvegdEDLG---EDHKLECDGKELEDHQLIADISKKDDAVIHLF 187
Cdd:cd17039     1 ITVKTLDGKTYTVEVDPDDTVADLKEKIE----EKTGipvEQQRLIYNGKELKDDKTLSDYGIKDGSTIHLV 68
ubiquitin pfam00240
Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog) ...
119-191 1.95e-08

Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog), Nedd8, Elongin B, Rub1, and Parkin. A number of them are thought to carry a distinctive five-residue motif termed the proteasome-interacting motif (PIM), which may have a biologically significant role in protein delivery to proteasomes and recruitment of proteasomes to transcription sites.


Pssm-ID: 459726 [Multi-domain]  Cd Length: 72  Bit Score: 51.40  E-value: 1.95e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002278019 119 INIETTSGKKFQFQVDQSRNVKYLKSKLAVEGDEDLgEDHKLECDGKELEDHQLIADISKKDDAVIHLFIRKP 191
Cdd:pfam00240   1 ITVKTLDGKKITLEVDPTDTVLELKEKIAEKEGVPP-EQQRLIYSGKVLEDDQTLGEYGIEDGSTIHLVLRQR 72
UBQ smart00213
Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of ...
119-189 2.58e-08

Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of proteins required for controlling cell cycle progression


Pssm-ID: 214563 [Multi-domain]  Cd Length: 72  Bit Score: 50.72  E-value: 2.58e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002278019  119 INIETTSGKKFQFQVDQSRNVKYLKSKLA-VEGDEDlgEDHKLECDGKELEDHQLIADISKKDDAVIHLFIR 189
Cdd:smart00213   3 LTVKTLDGKTITLEVKPSDTVSELKEKIAeLTGIPP--EQQRLIYKGKVLEDDRTLADYGIQDGSTIHLVLR 72
UBQ smart00213
Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of ...
56-112 5.42e-07

Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of proteins required for controlling cell cycle progression


Pssm-ID: 214563 [Multi-domain]  Cd Length: 72  Bit Score: 47.25  E-value: 5.42e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1002278019   56 VLGSESIASVKLRIQRFKGFVVNKQRLVLDGHELaRNNCHVKDYGLADGNVLHLVIR 112
Cdd:smart00213  17 VKPSDTVSELKEKIAELTGIPPEQQRLIYKGKVL-EDDRTLADYGIQDGSTIHLVLR 72
ADCK1-like cd13969
aarF domain containing kinase 1 and similar proteins; This subfamily is composed of ...
411-444 9.94e-05

aarF domain containing kinase 1 and similar proteins; This subfamily is composed of uncharacterized ABC1 kinase-like proteins including the human protein called aarF domain containing kinase 1 (ADCK1). Eukaryotes contain at least three ABC1-like proteins: in humans, these are ADCK3 and the putative protein kinases named ADCK1 and ADCK2. Yeast Abc1p and its human homolog ADCK3 are atypical protein kinases required for the biosynthesis of Coenzyme Q (ubiquinone or Q), which is an essential lipid component in respiratory electron and proton transport. In algae and higher plants, ABC1 kinases have proliferated to more than 15 subfamilies, most of which are located in plastids or mitochondria. Plant subfamilies 14 and 15 (ABC1K14-15) belong to the same group of ABC1 kinases as human ADCK1. ABC1 kinases are not related to the ATP-binding cassette (ABC) membrane transporter family.


Pssm-ID: 270871 [Multi-domain]  Cd Length: 253  Bit Score: 44.01  E-value: 9.94e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1002278019 411 ADRHAGNILVCKDEEGGNYKLVPIDHGYC--LPEKF 444
Cdd:cd13969   191 CDPHPGNLLVRKNPGPGKPQIVLLDHGLYreLDEEF 226
 
Name Accession Description Interval E-value
PI3_PI4_kinase pfam00454
Phosphatidylinositol 3- and 4-kinase; Some members of this family probably do not have lipid ...
274-516 3.11e-54

Phosphatidylinositol 3- and 4-kinase; Some members of this family probably do not have lipid kinase activity and are protein kinases,.


Pssm-ID: 395364 [Multi-domain]  Cd Length: 241  Bit Score: 183.68  E-value: 3.11e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278019 274 GSGGVYFMQDASGEKN--IAVFKPRDEEPMAKNNP--RGLPVSTDGEGMKRGtLVGEGAFREVAAYILDHPigdheseer 349
Cdd:pfam00454   1 GYGGIYKVGDDLRQDEliLQVFKLMDEELSKDNLDlrRLKPYSVIPLGPKCG-IIEWVPNSETLAYILDEY--------- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278019 350 iGFSGVPPTALVRSLHR---------------GKSFKIGSLQMFIQNNGSCEDMG--PRAFpVKEVHKIAVLDLRLANAD 412
Cdd:pfam00454  71 -GENGVPPTAMVKILHSalnypklklefesriSLPPKVGLLQWFVKKSPDAEEWGeaRKNF-VRSCAGYSVLDYILGNGD 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278019 413 RHAGNILVCKDEEggnyKLVPIDHGYCLPEKFEDCTFEwlywpqAREPFsDETIAYIKSLDAEEDIKLLKFHGWELSARC 492
Cdd:pfam00454 149 RHLDNILVDKTTG----KLFHIDFGLCLPDAGKDLPFP------EKVPF-RLTREMVYAMGPSGDEGLFRELCETAYEAL 217
                         250       260
                  ....*....|....*....|....
gi 1002278019 493 ARVLCISTMLLKKGAARGLTPYDI 516
Cdd:pfam00454 218 RRNLNLLTNLLKLMVADGLPDWSI 241
Ubl_ZFAND4 cd01802
ubiquitin-like (Ubl) domain found in AN1-type zinc finger protein 4 (ZFAND4) and similar ...
39-113 2.48e-15

ubiquitin-like (Ubl) domain found in AN1-type zinc finger protein 4 (ZFAND4) and similar proteins; ZFAND4, also termed AN1-type zinc finger and ubiquitin domain-containing protein-like 1 (ANUBL1), may function as an oncogene that promotes proliferation and regulates relevant tumor suppressor genes in gastric cancer, suggesting a role in gastric cancer initiation and progression. ZFAND4contains an N-terminal ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, a common structure involved in protein-protein interactions, as well as a C-terminal AN1-type zinc finger. Unlike ubiquitin polyproteins and most ubiquitin fusion proteins, the N-terminal Ubl domain of ZFAND4 does not undergo proteolytic processing.


Pssm-ID: 340500 [Multi-domain]  Cd Length: 74  Bit Score: 70.82  E-value: 2.48e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002278019  39 SIIIFLAVPGAPpMPMSVLGSESIASVKLRIQRFKGFVVNKQRLVLDGHELARNNChVKDYGLADGNVLHLVIRL 113
Cdd:cd01802     1 MELFIETLTGTA-FELRVSPFETVASVKAKIQRLEGIPVSQQHLIWSGRELEDDYC-LHDYNITDGSTLKLVLAM 73
ubiquitin pfam00240
Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog) ...
53-113 2.04e-10

Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog), Nedd8, Elongin B, Rub1, and Parkin. A number of them are thought to carry a distinctive five-residue motif termed the proteasome-interacting motif (PIM), which may have a biologically significant role in protein delivery to proteasomes and recruitment of proteasomes to transcription sites.


Pssm-ID: 459726 [Multi-domain]  Cd Length: 72  Bit Score: 56.80  E-value: 2.04e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002278019  53 PMSVLGSESIASVKLRIQRFKGFVVNKQRLVLDGHELaRNNCHVKDYGLADGNVLHLVIRL 113
Cdd:pfam00240  12 TLEVDPTDTVLELKEKIAEKEGVPPEQQRLIYSGKVL-EDDQTLGEYGIEDGSTIHLVLRQ 71
UBI4 COG5272
Ubiquitin [Posttranslational modification, protein turnover, chaperones];
42-119 2.11e-09

Ubiquitin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444084 [Multi-domain]  Cd Length: 213  Bit Score: 57.88  E-value: 2.11e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002278019  42 IFLAVPGAPPMPMSVLGSESIASVKLRIQRFKGFVVNKQRLVLDGHELARNNChVKDYGLADGNVLHLVIRLADLRLI 119
Cdd:COG5272     3 IFVKTLTGKTITLEVEPNDTIEAVKAKIQDKEGIPPDQQRLIFAGKQLEDDRT-LADYNIQKESTLHLVTRTLGISEI 79
Ubl_ubiquitin_like cd17039
ubiquitin-like (Ubl) domain found in ubiquitin and ubiquitin-like Ubl proteins; Ubiquitin-like ...
119-187 1.81e-08

ubiquitin-like (Ubl) domain found in ubiquitin and ubiquitin-like Ubl proteins; Ubiquitin-like (Ubl) proteins have a similar ubiquitin (Ub) beta-grasp fold and attach to other proteins in a Ubl manner but with biochemically distinct roles. Ub and Ubl proteins conjugate and deconjugate via ligases and peptidases to covalently modify target polypeptides. Some Ubl domains have adaptor roles in Ub-signaling by mediating protein-protein interaction. Prokaryotic sulfur carrier proteins are Ub-related proteins that can be activated in an ATP-dependent manner. Polyubiquitination signals for a diverse set of cellular events via different isopeptide linkages formed between the C terminus of one ubiquitin (Ub) and the epsilon-amine of K6, K11, K27, K29, K33, K48, or K63 of a second Ub. One of these seven lysine residues (K27, Ub numbering) is conserved in this Ubl_ubiquitin_like family. K27-linked Ub chains are versatile and can be recognized by several downstream receptor proteins. K27 has roles beyond chain linkage, such as in Ubl NEDD8 (which contains many of the same lysines (K6, K11, K27, K33, K48) as Ub) where K27 has a role (other than conjugation) in the mechanism of protein neddylation.


Pssm-ID: 340559 [Multi-domain]  Cd Length: 68  Bit Score: 51.06  E-value: 1.81e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002278019 119 INIETTSGKKFQFQVDQSRNVKYLKSKLAvegdEDLG---EDHKLECDGKELEDHQLIADISKKDDAVIHLF 187
Cdd:cd17039     1 ITVKTLDGKTYTVEVDPDDTVADLKEKIE----EKTGipvEQQRLIYNGKELKDDKTLSDYGIKDGSTIHLV 68
ubiquitin pfam00240
Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog) ...
119-191 1.95e-08

Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog), Nedd8, Elongin B, Rub1, and Parkin. A number of them are thought to carry a distinctive five-residue motif termed the proteasome-interacting motif (PIM), which may have a biologically significant role in protein delivery to proteasomes and recruitment of proteasomes to transcription sites.


Pssm-ID: 459726 [Multi-domain]  Cd Length: 72  Bit Score: 51.40  E-value: 1.95e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002278019 119 INIETTSGKKFQFQVDQSRNVKYLKSKLAVEGDEDLgEDHKLECDGKELEDHQLIADISKKDDAVIHLFIRKP 191
Cdd:pfam00240   1 ITVKTLDGKKITLEVDPTDTVLELKEKIAEKEGVPP-EQQRLIYSGKVLEDDQTLGEYGIEDGSTIHLVLRQR 72
Ubl_ubiquitin_like cd17039
ubiquitin-like (Ubl) domain found in ubiquitin and ubiquitin-like Ubl proteins; Ubiquitin-like ...
42-110 2.10e-08

ubiquitin-like (Ubl) domain found in ubiquitin and ubiquitin-like Ubl proteins; Ubiquitin-like (Ubl) proteins have a similar ubiquitin (Ub) beta-grasp fold and attach to other proteins in a Ubl manner but with biochemically distinct roles. Ub and Ubl proteins conjugate and deconjugate via ligases and peptidases to covalently modify target polypeptides. Some Ubl domains have adaptor roles in Ub-signaling by mediating protein-protein interaction. Prokaryotic sulfur carrier proteins are Ub-related proteins that can be activated in an ATP-dependent manner. Polyubiquitination signals for a diverse set of cellular events via different isopeptide linkages formed between the C terminus of one ubiquitin (Ub) and the epsilon-amine of K6, K11, K27, K29, K33, K48, or K63 of a second Ub. One of these seven lysine residues (K27, Ub numbering) is conserved in this Ubl_ubiquitin_like family. K27-linked Ub chains are versatile and can be recognized by several downstream receptor proteins. K27 has roles beyond chain linkage, such as in Ubl NEDD8 (which contains many of the same lysines (K6, K11, K27, K33, K48) as Ub) where K27 has a role (other than conjugation) in the mechanism of protein neddylation.


Pssm-ID: 340559 [Multi-domain]  Cd Length: 68  Bit Score: 51.06  E-value: 2.10e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002278019  42 IFLAVPGAPPMPMSVLGSESIASVKLRIQRFKGFVVNKQRLVLDGHELaRNNCHVKDYGLADGNVLHLV 110
Cdd:cd17039     1 ITVKTLDGKTYTVEVDPDDTVADLKEKIEEKTGIPVEQQRLIYNGKEL-KDDKTLSDYGIKDGSTIHLV 68
UBQ smart00213
Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of ...
119-189 2.58e-08

Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of proteins required for controlling cell cycle progression


Pssm-ID: 214563 [Multi-domain]  Cd Length: 72  Bit Score: 50.72  E-value: 2.58e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002278019  119 INIETTSGKKFQFQVDQSRNVKYLKSKLA-VEGDEDlgEDHKLECDGKELEDHQLIADISKKDDAVIHLFIR 189
Cdd:smart00213   3 LTVKTLDGKTITLEVKPSDTVSELKEKIAeLTGIPP--EQQRLIYKGKVLEDDRTLADYGIQDGSTIHLVLR 72
UBQ smart00213
Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of ...
56-112 5.42e-07

Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of proteins required for controlling cell cycle progression


Pssm-ID: 214563 [Multi-domain]  Cd Length: 72  Bit Score: 47.25  E-value: 5.42e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1002278019   56 VLGSESIASVKLRIQRFKGFVVNKQRLVLDGHELaRNNCHVKDYGLADGNVLHLVIR 112
Cdd:smart00213  17 VKPSDTVSELKEKIAELTGIPPEQQRLIYKGKVL-EDDRTLADYGIQDGSTIHLVLR 72
ADCK1-like cd13969
aarF domain containing kinase 1 and similar proteins; This subfamily is composed of ...
411-444 9.94e-05

aarF domain containing kinase 1 and similar proteins; This subfamily is composed of uncharacterized ABC1 kinase-like proteins including the human protein called aarF domain containing kinase 1 (ADCK1). Eukaryotes contain at least three ABC1-like proteins: in humans, these are ADCK3 and the putative protein kinases named ADCK1 and ADCK2. Yeast Abc1p and its human homolog ADCK3 are atypical protein kinases required for the biosynthesis of Coenzyme Q (ubiquinone or Q), which is an essential lipid component in respiratory electron and proton transport. In algae and higher plants, ABC1 kinases have proliferated to more than 15 subfamilies, most of which are located in plastids or mitochondria. Plant subfamilies 14 and 15 (ABC1K14-15) belong to the same group of ABC1 kinases as human ADCK1. ABC1 kinases are not related to the ATP-binding cassette (ABC) membrane transporter family.


Pssm-ID: 270871 [Multi-domain]  Cd Length: 253  Bit Score: 44.01  E-value: 9.94e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1002278019 411 ADRHAGNILVCKDEEGGNYKLVPIDHGYC--LPEKF 444
Cdd:cd13969   191 CDPHPGNLLVRKNPGPGKPQIVLLDHGLYreLDEEF 226
Rad60-SLD pfam11976
Ubiquitin-2 like Rad60 SUMO-like; The small ubiquitin-related modifier SUMO-1 is a Ub/Ubl ...
119-188 2.41e-04

Ubiquitin-2 like Rad60 SUMO-like; The small ubiquitin-related modifier SUMO-1 is a Ub/Ubl family member, and although SUMO-1 shares structural similarity to Ub, SUMO's cellular functions remain distinct insomuch as SUMO modification alters protein function through changes in activity, cellular localization, or by protecting substrates from ubiquitination. Rad60 family members contain functionally enigmatic, integral SUMO-like domains (SLDs). Despite their divergence from SUMO, each Rad60 SLD interacts with a subset of SUMO pathway enzymes: SLD2 specifically binds the SUMO E2 conjugating enzyme (Ubc9)), whereas SLD1 binds the SUMO E1 (Fub2, also called Uba2) activating and E3 (Pli1, also called Siz1 and Siz2) specificity enzymes. Structural analysis of PDB:2uyz reveals a mechanistic basis for the near-synonymous roles of Rad60 and SUMO in survival of genotoxic stress and suggest unprecedented DNA-damage-response functions for SLDs in regulating SUMOylation. The Rad60 branch of this family is also known as RENi (Rad60-Esc2-Nip45), and biologically it should be two distinct families SUMO and RENi (Rad60-Esc2-Nip45).


Pssm-ID: 403255 [Multi-domain]  Cd Length: 72  Bit Score: 39.47  E-value: 2.41e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278019 119 INIETTSGKKFQFQVDQSRNVKYLKSKLAVEGDEDLGEDHKLECDGKELEDHQLIADISKKDDAVIHLFI 188
Cdd:pfam11976   3 IILKGKDGKEVFIKVKPTTTVSKLINAYRKKRGIPPSQQVRLIFDGERLDPNSTVEDLDIEDGDTIDVVI 72
Ubl_ubiquitin cd01803
ubiquitin-like (Ubl) domain found in ubiquitin; Ubiquitin is a protein modifier in eukaryotes ...
59-113 7.23e-04

ubiquitin-like (Ubl) domain found in ubiquitin; Ubiquitin is a protein modifier in eukaryotes that is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair. Ubiquitination is comprised of a cascade of E1, E2 and E3 enzymes that results in a covalent bond between the C-terminus of ubiquitin and the epsilon-amino group of a substrate lysine. Ubiquitin-like (Ubl) proteins have similar ubiquitin beta-grasp fold and attach to other proteins in a Ubl manner but with biochemically distinct roles. Ubiquitin (Ub)and Ubl proteins conjugate and deconjugate via ligases and peptidases to covalently modify target polypeptides. Ub includes Ubq/RPL40e and Ubq/RPS27a fusions as well as homopolymeric multiubiquitin protein chains.


Pssm-ID: 340501 [Multi-domain]  Cd Length: 76  Bit Score: 38.58  E-value: 7.23e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1002278019  59 SESIASVKLRIQRFKGFVVNKQRLVLDGHELARNNChVKDYGLADGNVLHLVIRL 113
Cdd:cd01803    20 SDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRT-LSDYNIQKESTLHLVLRL 73
Ubl_Dsk2p_like cd16106
ubiquitin-like (Ubl) domain found in Saccharomyces cerevisiae proteasome interacting protein ...
119-186 1.99e-03

ubiquitin-like (Ubl) domain found in Saccharomyces cerevisiae proteasome interacting protein Dsk2p and similar proteins; The family contains several fungal multiubiquitin receptors, including Saccharomyces cerevisiae Dsk2p and Schizosaccharomyces pombe Dph1p, both of which have been characterized as shuttle proteins transporting ubiquitinated substrates destined for degradation from the E3 ligase to the 26S proteasome. They interact with the proteasome through their N-terminal ubiquitin-like domain (Ubl) and with ubiquitin (Ub) through their C-terminal Ub-associated domain (UBA). S. cerevisiae Dsk2p is a nuclear-enriched protein that may involve in the ubiquitin-proteasome proteolytic pathway through interacting with K48-linked polyubiquitin and the proteasome. Moreover, it has been implicated in spindle pole duplication through assisting in Cdc31 assembly into the new spindle pole body (SPB). S. pombe Dph1p is an ubiquitin (Ub0 receptor working in concert with the class V myosin, Myo52, to target the degradation of the S. pombe CLIP-170 homolog, Tip1. It also can protect Ub chains against disassembly by deubiquitinating enzymes.


Pssm-ID: 340523 [Multi-domain]  Cd Length: 73  Bit Score: 37.23  E-value: 1.99e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002278019 119 INIETTSGKKFQFQVDQSRNVKYLKSKLAVEGDEDlGEDHKLECDGKELEDHQLIADISKKDDAVIHL 186
Cdd:cd16106     3 VTVKCSNGKKFTVEVEPDATVLELKELIAEKSDIP-AEQQRLIYKGKILKDEETLSSYKIQDGHTVHL 69
Rad60-SLD pfam11976
Ubiquitin-2 like Rad60 SUMO-like; The small ubiquitin-related modifier SUMO-1 is a Ub/Ubl ...
78-111 1.99e-03

Ubiquitin-2 like Rad60 SUMO-like; The small ubiquitin-related modifier SUMO-1 is a Ub/Ubl family member, and although SUMO-1 shares structural similarity to Ub, SUMO's cellular functions remain distinct insomuch as SUMO modification alters protein function through changes in activity, cellular localization, or by protecting substrates from ubiquitination. Rad60 family members contain functionally enigmatic, integral SUMO-like domains (SLDs). Despite their divergence from SUMO, each Rad60 SLD interacts with a subset of SUMO pathway enzymes: SLD2 specifically binds the SUMO E2 conjugating enzyme (Ubc9)), whereas SLD1 binds the SUMO E1 (Fub2, also called Uba2) activating and E3 (Pli1, also called Siz1 and Siz2) specificity enzymes. Structural analysis of PDB:2uyz reveals a mechanistic basis for the near-synonymous roles of Rad60 and SUMO in survival of genotoxic stress and suggest unprecedented DNA-damage-response functions for SLDs in regulating SUMOylation. The Rad60 branch of this family is also known as RENi (Rad60-Esc2-Nip45), and biologically it should be two distinct families SUMO and RENi (Rad60-Esc2-Nip45).


Pssm-ID: 403255 [Multi-domain]  Cd Length: 72  Bit Score: 37.16  E-value: 1.99e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1002278019  78 NKQRLVLDGHELARNNcHVKDYGLADGNVLHLVI 111
Cdd:pfam11976  40 QQVRLIFDGERLDPNS-TVEDLDIEDGDTIDVVI 72
Ubl_UBL4A_like cd01807
ubiquitin-like (Ubl) domain found in ubiquitin-like proteins UBL4A and similar proteins; UBL4A, ...
59-112 2.70e-03

ubiquitin-like (Ubl) domain found in ubiquitin-like proteins UBL4A and similar proteins; UBL4A, also termed GdX, is a ubiquitously expressed ubiquitin-like (Ubl) protein that forms a complex with partner proteins and participates in the protein processing through endoplasmic reticulum (ER), acting as a chaperone. As a key component of the BCL2-associated athanogene 6 (BAG6) chaperone complex, UBL4A plays a role in mediating DNA damage signaling and cell death. UBL4A also regulates insulin-induced Akt plasma membrane translocation through promotion of Arp2/3-dependent actin branching. Moreover, UBL4A specifically stabilizes the TC45/STAT3 association and promotes dephosphorylation of STAT3 to repress tumorigenesis. UBL4B is testis-specific, and encoded by an X-derived retrogene Ubl4b, which is specifically expressed in post-meiotic germ cells in mammals. As a germ cell-specific cytoplasmic protein, UBL4B is not present in somatic cells. Moreover, UBL4B is present in elongated spermatids, but not in spermatocytes and round spermatids, suggesting its function is restricted to late spermiogenesis. The function of UBL4A may be compensated by either UBL4B or other Ubl proteins in normal conditions. Both UBL4A and UBL4B contain a conserved Ubl domain with a beta-grasp Ubl fold, a common structure involved in protein-protein interactions.


Pssm-ID: 340505 [Multi-domain]  Cd Length: 72  Bit Score: 36.57  E-value: 2.70e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1002278019  59 SESIASVKLRIQRFKGFVVNKQRLVLDGHELARNNChVKDYGLADGNVLHLVIR 112
Cdd:cd01807    20 TESVLTVKQLVAEQLNVPVSQQRLVFKGKTLADEHS-LSDYSIGPGSKIHLVVK 72
Ubl2_FAT10 cd17053
ubiquitin-like (Ubl) domain 2 found in leukocyte antigen F (HLA-F) adjacent transcript 10 ...
53-110 4.27e-03

ubiquitin-like (Ubl) domain 2 found in leukocyte antigen F (HLA-F) adjacent transcript 10 (FAT10) and similar proteins; FAT10, also termed ubiquitin D (UBD), or diubiquitin, is a cytokine-inducible ubiquitin-like (Ubl) modifer that is highly expressed in the thymus, and targets substrates covalently for 26S proteasomal degradation. It is also associated with cancer development, antigen processing and antimicrobial defense, chromosomal stability and cell cycle regulation. FAT10 is presented on immune cells and under the inflammatory conditions, is synergistically induced by interferon gamma (IFNgamma) and tumor necrosis factor (TNFalpha) in the non-immune (liver parenchymal) cells. FAT10 contains two Ubl domains. The family corresponds to the second Ubl domain of FAT10. Some family members contain only one Ubl domain.


Pssm-ID: 340573  Cd Length: 71  Bit Score: 36.17  E-value: 4.27e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1002278019  53 PMSVLGSESIASVKLRIQRFKGFVVNKQRLVLDGHELARNNCHVKDYGLADGNVLHLV 110
Cdd:cd17053    14 TLQVSRSTTVAQVKAMIEDQSGVPPNEQILVYNGKRLEDGDKTLGEYGIKTGDTLYLL 71
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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