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Conserved domains on  [gi|1390157529|ref|NP_001350337|]
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small conductance calcium-activated potassium channel protein 1 isoform b [Mus musculus]

Protein Classification

SK_channel and CaMBD domain-containing protein( domain architecture ID 10507664)

protein containing domains SK_channel, Ion_trans_2, and CaMBD

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SK_channel pfam03530
Calcium-activated SK potassium channel;
91-200 5.81e-60

Calcium-activated SK potassium channel;


:

Pssm-ID: 460958  Cd Length: 111  Bit Score: 193.58  E-value: 5.81e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157529  91 LGHRRALFEKRKRLSDYALIFGMFGIVVMVTETELSW-GVYTKESLCSFALKCLISLSTVILLGLVILYHAREIQLFLVD 169
Cdd:pfam03530   1 LRRRKELLERRRRLSDFALVLALFGIVLMVIETELTAlGVYSKGSMYSLALKSLISLSTVLLLGLIVAYHAIEIQLFMVD 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1390157529 170 NGADDWRIAMTWERVSLISLELVVCAIHPVP 200
Cdd:pfam03530  81 NGADDWRVAMTSERILQILLELLVCAIHPIP 111
CaMBD smart01053
Calmodulin binding domain; Small-conductance Ca2+-activated K+ channels (SK channels) are ...
 382-457 1.07e-41

Calmodulin binding domain; Small-conductance Ca2+-activated K+ channels (SK channels) are independent of voltage and gated solely by intracellular Ca2+. These membrane channels are heteromeric complexes that comprise pore-forming alpha-subunits and the Ca2+-binding protein calmodulin (CaM). CaM binds to the SK channel through this the CaM-binding domain (CaMBD), which is located in an intracellular region of the alpha-subunit immediately carboxy-terminal to the pore. Channel opening is triggered when Ca2+ binds the EF hands in the N-lobe of CaM. The structure of this domain complexed with CaM is known. This domain forms an elongated dimer with a CaM molecule bound at each end; each CaM wraps around three alpha-helices, two from one CaMBD subunit and one from the other.


:

Pssm-ID: 198121  Cd Length: 76  Bit Score: 144.09  E-value: 1.07e-41
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1390157529  382 DTQLTKRVKNAAANVLRETWLIYKHTRLVKKPDQGRVRKHQRKFLQAIHQLRSVKIEQGKVNDQANTLAELAKAQS 457
Cdd:smart01053   1 DTQLTKRVKNAAANVLRETWLIYKHTKLVKKGDQGRLRKHQRKFLQAIHQFRSVKMKQRKLREQANSLVDLAKTQM 76
Ion_trans_2 pfam07885
Ion channel; This family includes the two membrane helix type ion channels found in bacteria.
 289-368 3.06e-13

Ion channel; This family includes the two membrane helix type ion channels found in bacteria.


:

Pssm-ID: 462301 [Multi-domain]  Cd Length: 78  Bit Score: 64.98  E-value: 3.06e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157529 289 VSSWIVAAWTVrvcerYHDKQEVTSNFLGAMWLISITFLSIGYGDMVPHTYCGKGVCLLTGIMGAGCTALVVAVVARKLE 368
Cdd:pfam07885   3 LLLVLIFGTVY-----YLLEEGWEWSFLDALYFSFVTLTTVGYGDIVPLTDAGRLFTIFYILIGIPLFAIFLAVLGRFLT 77
EnvC super family cl34844
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 422-502 8.75e-04

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


The actual alignment was detected with superfamily member COG4942:

Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 41.67  E-value: 8.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157529 422 QRKFLQAIHQLRSVKIEQGKVNDQantLAELAKAQSIAYEVVSELQAQQEELEARLAALESRLDVLGASLQALPGLIAQA 501
Cdd:COG4942    33 QQEIAELEKELAALKKEEKALLKQ---LAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAEL 109


                  .
gi 1390157529 502 I 502
Cdd:COG4942   110 L 110
 
Name Accession Description Interval E-value
SK_channel pfam03530
Calcium-activated SK potassium channel;
91-200 5.81e-60

Calcium-activated SK potassium channel;


Pssm-ID: 460958  Cd Length: 111  Bit Score: 193.58  E-value: 5.81e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157529  91 LGHRRALFEKRKRLSDYALIFGMFGIVVMVTETELSW-GVYTKESLCSFALKCLISLSTVILLGLVILYHAREIQLFLVD 169
Cdd:pfam03530   1 LRRRKELLERRRRLSDFALVLALFGIVLMVIETELTAlGVYSKGSMYSLALKSLISLSTVLLLGLIVAYHAIEIQLFMVD 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1390157529 170 NGADDWRIAMTWERVSLISLELVVCAIHPVP 200
Cdd:pfam03530  81 NGADDWRVAMTSERILQILLELLVCAIHPIP 111
CaMBD smart01053
Calmodulin binding domain; Small-conductance Ca2+-activated K+ channels (SK channels) are ...
 382-457 1.07e-41

Calmodulin binding domain; Small-conductance Ca2+-activated K+ channels (SK channels) are independent of voltage and gated solely by intracellular Ca2+. These membrane channels are heteromeric complexes that comprise pore-forming alpha-subunits and the Ca2+-binding protein calmodulin (CaM). CaM binds to the SK channel through this the CaM-binding domain (CaMBD), which is located in an intracellular region of the alpha-subunit immediately carboxy-terminal to the pore. Channel opening is triggered when Ca2+ binds the EF hands in the N-lobe of CaM. The structure of this domain complexed with CaM is known. This domain forms an elongated dimer with a CaM molecule bound at each end; each CaM wraps around three alpha-helices, two from one CaMBD subunit and one from the other.


Pssm-ID: 198121  Cd Length: 76  Bit Score: 144.09  E-value: 1.07e-41
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1390157529  382 DTQLTKRVKNAAANVLRETWLIYKHTRLVKKPDQGRVRKHQRKFLQAIHQLRSVKIEQGKVNDQANTLAELAKAQS 457
Cdd:smart01053   1 DTQLTKRVKNAAANVLRETWLIYKHTKLVKKGDQGRLRKHQRKFLQAIHQFRSVKMKQRKLREQANSLVDLAKTQM 76
CaMBD pfam02888
Calmodulin binding domain; Small-conductance Ca2+-activated K+ channels (SK channels) are ...
 382-456 3.73e-41

Calmodulin binding domain; Small-conductance Ca2+-activated K+ channels (SK channels) are independent of voltage and gated solely by intracellular Ca2+. These membrane channels are heteromeric complexes that comprise pore-forming alpha-subunits and the Ca2+-binding protein calmodulin (CaM). CaM binds to the SK channel through this the CaM-binding domain (CaMBD), which is located in an intracellular region of the alpha-subunit immediately carboxy-terminal to the pore. Channel opening is triggered when Ca2+ binds the EF hands in the N-lobe of CaM. The structure of this domain complexed with CaM is known. This domain forms an elongated dimer with a CaM molecule bound at each end; each CaM wraps around three alpha-helices, two from one CaMBD subunit and one from the other.


Pssm-ID: 460739  Cd Length: 75  Bit Score: 142.42  E-value: 3.73e-41
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1390157529 382 DTQLTKRVKNAAANVLRETWLIYKHTRLVKKPDQGRVRKHQRKFLQAIHQLRSVKIEQGKVNDQANTLAELAKAQ 456
Cdd:pfam02888   1 DTQLTKELKNAAANVLRETWLIYKHTKLVKKRDQSRVRKHQRKLLQAIHTFRKVKMKQRKLRDQVNTMVDLSKMQ 75
Ion_trans_2 pfam07885
Ion channel; This family includes the two membrane helix type ion channels found in bacteria.
 289-368 3.06e-13

Ion channel; This family includes the two membrane helix type ion channels found in bacteria.


Pssm-ID: 462301 [Multi-domain]  Cd Length: 78  Bit Score: 64.98  E-value: 3.06e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157529 289 VSSWIVAAWTVrvcerYHDKQEVTSNFLGAMWLISITFLSIGYGDMVPHTYCGKGVCLLTGIMGAGCTALVVAVVARKLE 368
Cdd:pfam07885   3 LLLVLIFGTVY-----YLLEEGWEWSFLDALYFSFVTLTTVGYGDIVPLTDAGRLFTIFYILIGIPLFAIFLAVLGRFLT 77
HR1_ROCK1 cd11639
Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Rho-associated ...
 415-477 5.20e-04

Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Rho-associated coiled-coil containing protein kinase 1; ROCK1 is a serine/threonine kinase and is preferentially expressed in the liver, lung, spleen, testes, and kidney. It mediates signaling from Rho to the actin cytoskeleton. It is implicated in the development of cardiac fibrosis, cardiomyocyte apoptosis, and hyperglycemia. Mice deficient with ROCK1 display eyelids open at birth (EOB) and omphalocele phenotypes due to the disorganization of actin filaments in the eyelids and the umbilical ring. ROCK1 contains an N-terminal extension, a catalytic kinase domain, and a long C-terminal extension, which contains a Rho-binding HR1 domain and a pleckstrin homology (PH) domain. It is auto-inhibited by HR1 and PH domains interacting with the catalytic domain. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family.


Pssm-ID: 212029 [Multi-domain]  Cd Length: 66  Bit Score: 38.45  E-value: 5.20e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1390157529 415 QGRVRKHQRKFLQAIHQLRSVKIEQGKVNDQANTLAELAKAQSIAYEVVSELQAQQEELEARL 477
Cdd:cd11639     4 QHRINEYQRKAEQESEKRRNVENEVSTLKDQLEDLKKISQNSQITNEKINQLQKQLEEANDLL 66
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 422-502 8.75e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 41.67  E-value: 8.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157529 422 QRKFLQAIHQLRSVKIEQGKVNDQantLAELAKAQSIAYEVVSELQAQQEELEARLAALESRLDVLGASLQALPGLIAQA 501
Cdd:COG4942    33 QQEIAELEKELAALKKEEKALLKQ---LAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAEL 109


                  .
gi 1390157529 502 I 502
Cdd:COG4942   110 L 110
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
406-501 8.18e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.13  E-value: 8.18e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157529  406 HTRLVKKPDQ----GRVRKHQRKFLQAIHQLRSVKIEQGKVND-QANTLAELAKAQsiayevVSELQAQQEELEARLAAL 480
Cdd:COG4913    241 HEALEDAREQiellEPIRELAERYAAARERLAELEYLRAALRLwFAQRRLELLEAE------LEELRAELARLEAELERL 314

                           90       100
                   ....*....|....*....|.
gi 1390157529  481 ESRLDVLGASLQALPGLIAQA 501
Cdd:COG4913    315 EARLDALREELDELEAQIRGN 335
 
Name Accession Description Interval E-value
SK_channel pfam03530
Calcium-activated SK potassium channel;
91-200 5.81e-60

Calcium-activated SK potassium channel;


Pssm-ID: 460958  Cd Length: 111  Bit Score: 193.58  E-value: 5.81e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157529  91 LGHRRALFEKRKRLSDYALIFGMFGIVVMVTETELSW-GVYTKESLCSFALKCLISLSTVILLGLVILYHAREIQLFLVD 169
Cdd:pfam03530   1 LRRRKELLERRRRLSDFALVLALFGIVLMVIETELTAlGVYSKGSMYSLALKSLISLSTVLLLGLIVAYHAIEIQLFMVD 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1390157529 170 NGADDWRIAMTWERVSLISLELVVCAIHPVP 200
Cdd:pfam03530  81 NGADDWRVAMTSERILQILLELLVCAIHPIP 111
CaMBD smart01053
Calmodulin binding domain; Small-conductance Ca2+-activated K+ channels (SK channels) are ...
 382-457 1.07e-41

Calmodulin binding domain; Small-conductance Ca2+-activated K+ channels (SK channels) are independent of voltage and gated solely by intracellular Ca2+. These membrane channels are heteromeric complexes that comprise pore-forming alpha-subunits and the Ca2+-binding protein calmodulin (CaM). CaM binds to the SK channel through this the CaM-binding domain (CaMBD), which is located in an intracellular region of the alpha-subunit immediately carboxy-terminal to the pore. Channel opening is triggered when Ca2+ binds the EF hands in the N-lobe of CaM. The structure of this domain complexed with CaM is known. This domain forms an elongated dimer with a CaM molecule bound at each end; each CaM wraps around three alpha-helices, two from one CaMBD subunit and one from the other.


Pssm-ID: 198121  Cd Length: 76  Bit Score: 144.09  E-value: 1.07e-41
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1390157529  382 DTQLTKRVKNAAANVLRETWLIYKHTRLVKKPDQGRVRKHQRKFLQAIHQLRSVKIEQGKVNDQANTLAELAKAQS 457
Cdd:smart01053   1 DTQLTKRVKNAAANVLRETWLIYKHTKLVKKGDQGRLRKHQRKFLQAIHQFRSVKMKQRKLREQANSLVDLAKTQM 76
CaMBD pfam02888
Calmodulin binding domain; Small-conductance Ca2+-activated K+ channels (SK channels) are ...
 382-456 3.73e-41

Calmodulin binding domain; Small-conductance Ca2+-activated K+ channels (SK channels) are independent of voltage and gated solely by intracellular Ca2+. These membrane channels are heteromeric complexes that comprise pore-forming alpha-subunits and the Ca2+-binding protein calmodulin (CaM). CaM binds to the SK channel through this the CaM-binding domain (CaMBD), which is located in an intracellular region of the alpha-subunit immediately carboxy-terminal to the pore. Channel opening is triggered when Ca2+ binds the EF hands in the N-lobe of CaM. The structure of this domain complexed with CaM is known. This domain forms an elongated dimer with a CaM molecule bound at each end; each CaM wraps around three alpha-helices, two from one CaMBD subunit and one from the other.


Pssm-ID: 460739  Cd Length: 75  Bit Score: 142.42  E-value: 3.73e-41
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1390157529 382 DTQLTKRVKNAAANVLRETWLIYKHTRLVKKPDQGRVRKHQRKFLQAIHQLRSVKIEQGKVNDQANTLAELAKAQ 456
Cdd:pfam02888   1 DTQLTKELKNAAANVLRETWLIYKHTKLVKKRDQSRVRKHQRKLLQAIHTFRKVKMKQRKLRDQVNTMVDLSKMQ 75
Ion_trans_2 pfam07885
Ion channel; This family includes the two membrane helix type ion channels found in bacteria.
 289-368 3.06e-13

Ion channel; This family includes the two membrane helix type ion channels found in bacteria.


Pssm-ID: 462301 [Multi-domain]  Cd Length: 78  Bit Score: 64.98  E-value: 3.06e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157529 289 VSSWIVAAWTVrvcerYHDKQEVTSNFLGAMWLISITFLSIGYGDMVPHTYCGKGVCLLTGIMGAGCTALVVAVVARKLE 368
Cdd:pfam07885   3 LLLVLIFGTVY-----YLLEEGWEWSFLDALYFSFVTLTTVGYGDIVPLTDAGRLFTIFYILIGIPLFAIFLAVLGRFLT 77
HR1_ROCK1 cd11639
Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Rho-associated ...
 415-477 5.20e-04

Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Rho-associated coiled-coil containing protein kinase 1; ROCK1 is a serine/threonine kinase and is preferentially expressed in the liver, lung, spleen, testes, and kidney. It mediates signaling from Rho to the actin cytoskeleton. It is implicated in the development of cardiac fibrosis, cardiomyocyte apoptosis, and hyperglycemia. Mice deficient with ROCK1 display eyelids open at birth (EOB) and omphalocele phenotypes due to the disorganization of actin filaments in the eyelids and the umbilical ring. ROCK1 contains an N-terminal extension, a catalytic kinase domain, and a long C-terminal extension, which contains a Rho-binding HR1 domain and a pleckstrin homology (PH) domain. It is auto-inhibited by HR1 and PH domains interacting with the catalytic domain. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family.


Pssm-ID: 212029 [Multi-domain]  Cd Length: 66  Bit Score: 38.45  E-value: 5.20e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1390157529 415 QGRVRKHQRKFLQAIHQLRSVKIEQGKVNDQANTLAELAKAQSIAYEVVSELQAQQEELEARL 477
Cdd:cd11639     4 QHRINEYQRKAEQESEKRRNVENEVSTLKDQLEDLKKISQNSQITNEKINQLQKQLEEANDLL 66
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 422-502 8.75e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 41.67  E-value: 8.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157529 422 QRKFLQAIHQLRSVKIEQGKVNDQantLAELAKAQSIAYEVVSELQAQQEELEARLAALESRLDVLGASLQALPGLIAQA 501
Cdd:COG4942    33 QQEIAELEKELAALKKEEKALLKQ---LAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAEL 109


                  .
gi 1390157529 502 I 502
Cdd:COG4942   110 L 110
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 417-501 1.05e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 41.35  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157529 417 RVRKHQRKFLQAIHQLRSvKIEQgKVNDQANTLAELAKAQSIAYEVVSELQAQQEELEARLAALESRLDVLGASLQALPG 496
Cdd:COG3883   126 KIADADADLLEELKADKA-ELEA-KKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEA 203


                  ....*
gi 1390157529 497 LIAQA 501
Cdd:COG3883   204 ELAAA 208
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
423-502 1.49e-03

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.54  E-value: 1.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157529 423 RKFLQAihQLRSVKIE----QGKVND--QANTLAELAKAQSIAYEVVSELQAQQEELEARLAALESRLDVLGASLQALPG 496
Cdd:COG3206   177 LEFLEE--QLPELRKEleeaEAALEEfrQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPD 254


                  ....*.
gi 1390157529 497 LIAQAI 502
Cdd:COG3206   255 ALPELL 260
Laminin_I pfam06008
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ...
 369-501 2.21e-03

Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.


Pssm-ID: 310534 [Multi-domain]  Cd Length: 258  Bit Score: 40.09  E-value: 2.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157529 369 LTKAEKhVHNFMMDT-----QLTKRVKNAAANVlreTWLIYKHTRLVKKPDQGRVRKHQRKFLQAIHQLRSVKIEQGKVN 443
Cdd:pfam06008  67 LAKAQQ-VNAESERTlghakELAEAIKNLIDNI---KEINEKVATLGENDFALPSSDLSRMLAEAQRMLGEIRSRDFGTQ 142

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1390157529 444 DQANTlAELAKAQSIAYEVVSELQAQQEELEARLAALESRLDVLGASLQALPGLIAQA 501
Cdd:pfam06008 143 LQNAE-AELKAAQDLLSRIQTWFQSPQEENKALANALRDSLAEYEAKLSDLRELLREA 199
RecN COG0497
DNA repair ATPase RecN [Replication, recombination and repair];
428-501 3.32e-03

DNA repair ATPase RecN [Replication, recombination and repair];


Pssm-ID: 440263 [Multi-domain]  Cd Length: 555  Bit Score: 40.06  E-value: 3.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157529 428 AIHQLRSVKIEQGKVNDQANTLAELAKA-QSIAY---EVVSELQAQQEELEA---RLAALESRLDVL-------GASLQA 493
Cdd:COG0497   242 ALDLLGQALRALERLAEYDPSLAELAERlESALIeleEAASELRRYLDSLEFdpeRLEEVEERLALLrrlarkyGVTVEE 321


                  ....*...
gi 1390157529 494 LPGLIAQA 501
Cdd:COG0497   322 LLAYAEEL 329
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
406-501 8.18e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.13  E-value: 8.18e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157529  406 HTRLVKKPDQ----GRVRKHQRKFLQAIHQLRSVKIEQGKVND-QANTLAELAKAQsiayevVSELQAQQEELEARLAAL 480
Cdd:COG4913    241 HEALEDAREQiellEPIRELAERYAAARERLAELEYLRAALRLwFAQRRLELLEAE------LEELRAELARLEAELERL 314

                           90       100
                   ....*....|....*....|.
gi 1390157529  481 ESRLDVLGASLQALPGLIAQA 501
Cdd:COG4913    315 EARLDALREELDELEAQIRGN 335
UbiK COG2960
Ubiquinone biosynthesis accessory factor UbiK [Coenzyme transport and metabolism];
460-485 9.84e-03

Ubiquinone biosynthesis accessory factor UbiK [Coenzyme transport and metabolism];


Pssm-ID: 442200  Cd Length: 83  Bit Score: 35.15  E-value: 9.84e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1390157529 460 YEVVSEL----QAQQEELEARLAALESRLD 485
Cdd:COG2960    51 FDVQRAVlartREKLEALEARLAELEAKLA 80
 
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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