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Conserved domains on  [gi|2250709889|ref|NP_001394979|]
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calmodulin-regulated spectrin-associated protein 1 isoform 5 [Mus musculus]

Protein Classification

CAMSAP_CH and CAMSAP_CKK domain-containing protein( domain architecture ID 13777711)

protein containing domains CAMSAP_CH, CAMSAP_CC1, UDM1_RNF168, and CAMSAP_CKK

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CAMSAP_CKK smart01051
Microtubule-binding calmodulin-regulated spectrin-associated; This is the C-terminal domain of ...
 1464-1592 5.27e-76

Microtubule-binding calmodulin-regulated spectrin-associated; This is the C-terminal domain of a family of eumetazoan proteins collectively defined as calmodulin-regulated spectrin-associated, or CAMSAP, proteins. CAMSAP proteins carry an N-terminal region that includes the CH domain, a central region including a predicted coiled-coil and this C-terminal, or CKK, domain - defined as being present in CAMSAP, KIAA1078 and KIAA1543, The C-terminal domain is the part of the CAMSAP proteins that binds to microtubules. The domain appears to act by producing inhibition of neurite extension, probably by blocking microtubule function. CKK represents a domain that has evolved with the metazoa. The structure of a murine hypothetical protein from RIKEN cDNA has shown the domain to adopt a mainly beta barrel structure with an associated alpha-helical hairpin.


:

Pssm-ID: 198119  Cd Length: 129  Bit Score: 247.66  E-value: 5.27e-76
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250709889  1464 GPKLFKEPSSKSNKPIIHNAISHCCLAGKVNEPHKNSILEELEKCDANHYIILFRDAGCQFRALYCYQPDTEEIYKLTGT 1543
Cdd:smart01051    1 GPKLYKEPSAKSNRFIIHNALSHCCLAGKVNEPQKNKILEEMEKSEANHFLILFRDAKCQFRALYTLNPETEELVKLYGN 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*....
gi 2250709889  1544 GPKSITKKMIDKLYKYSSDRKQFNLIPAKTMSVSVDALTIHNHLWQPKR 1592
Cdd:smart01051   81 GPRVITSKMVESLYKYDSSRKQFTQIPSKTLSVSVDAFTIKNHLWQTKK 129
CAMSAP_CH pfam11971
CAMSAP CH domain; This domain is the N-terminal CH domain from the CAMSAP proteins.
 248-331 2.25e-39

CAMSAP CH domain; This domain is the N-terminal CH domain from the CAMSAP proteins.


:

Pssm-ID: 432229  Cd Length: 85  Bit Score: 141.28  E-value: 2.25e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250709889  248 HLSARQSPYFPLLEDLMRDGSDGAALLAVVHYYCPEQMKLDDICLKEVPSMADSLYNIRLLREFSNEHL-NKCFYLTLED 326
Cdd:pfam11971    1 PLSQRSLPLSPPVEDLLRDLSDGCALAALIHFYCPQLIDLEDICLKESMSLADSLYNIQLLQEFCQRHLgNRCCHLTLED 80


                   ....*
gi 2250709889  327 MLYAP 331
Cdd:pfam11971   81 LLYAR 85
CAMSAP_CC1 pfam17095
Spectrin-binding region of Ca2+-Calmodulin; CAMSAP_CC1 is the conserved region on ...
 879-937 1.79e-22

Spectrin-binding region of Ca2+-Calmodulin; CAMSAP_CC1 is the conserved region on calmodulin-regulated spectrin-associated proteins in eukaryotes that binds spectrin. CAMSAPs are vertebrate microtubule-binding proteins, representatives of a family of cytoskeletal proteins that arose in animals. This conserved CC1 region binds to both spectrin and Ca2+/calmodulin in vitro, although the binding of Ca2+/calmodulin inhibited the binding of spectrin. CC1 appears to be a functional region of CAMSAP1 that links spectrin-binding to neurite outgrowth.


:

Pssm-ID: 465344 [Multi-domain]  Cd Length: 59  Bit Score: 91.98  E-value: 1.79e-22
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2250709889  879 PGRHSKDPASLLASELVQLHMQLEEKRRAIEAQKKKMEALSARQRLKLGKAAFLHVVKK 937
Cdd:pfam17095    1 PGDDSPSASPELASELSQLRLKLEEKRRAIEQQKKRMEAAFARQRQKLGKAAFLQVVKK 59
ARGLU super family cl38471
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...
 1277-1354 1.87e-10

Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is required for the oestrogen-dependent expression of ESR1 target genes. It functions in cooperation with MED1. The family of proteins is found in eukaryotes.


The actual alignment was detected with superfamily member pfam15346:

Pssm-ID: 405931 [Multi-domain]  Cd Length: 151  Bit Score: 60.84  E-value: 1.87e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250709889 1277 EQKAEDELAKKRAAFLLKQQRKAEEARARKQQLEAEVE---LKRDEARRKAEEDRL-------RKEEEKARRELIKQEYL 1346
Cdd:pfam15346   51 EKQVLEELEREREAELEEERRKEEEERKKREELERILEennRKIEEAQRKEAEERLamleeqrRMKEERQRREKEEEERE 130


                   ....*...
gi 2250709889 1347 RRKQQQAL 1354
Cdd:pfam15346  131 KREQQKIL 138
wall_bind_EntB super family cl48942
cell wall-binding protein EntB; This HMM describes the cell wall-binding protein EntB, as ...
 1179-1357 8.08e-05

cell wall-binding protein EntB; This HMM describes the cell wall-binding protein EntB, as found in Bacillus cereus. EntB is related to EntA, EntC, and EndD. All Ent family proteins have a signal peptide, an N-terminal SH3 domain and a C-terminal 3D (Asp-Asp-Asp) domain. EntB and EndC have a central region with a highly variable number of repeats resembling KAXEXX. The gene symbol derives from the notion that at least some members of the family function as enterotoxins, but more recent descriptions focus on roles in stress response and cell wall integrity.


The actual alignment was detected with superfamily member NF040676:

Pssm-ID: 468642 [Multi-domain]  Cd Length: 476  Bit Score: 47.08  E-value: 8.08e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250709889 1179 RTFVLSSCKDANIVSEQVNFKEGLDTS----VKEAGLSSSTITGKEHTPVEEPLRSKAsliEVDLSDLKAPDEDGEV--- 1251
Cdd:NF040676   172 KTQKVAKAKETTKAQEIVKPKEEVKVQevvkPKEEPKVQEIVKPKEEVKVQEEVKPKE---EEKVQEIVKPKEEAKVqee 248

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250709889 1252 --VGHESSVELGGDSDQKPGVGFFF--KDEQKAEDELAKKRAAFLLKQQRKAEEARARkQQLEAEVELKRDEARRKAEED 1327
Cdd:NF040676   249 vkVKEEAKVQEIAKAKEEAKAQEIAkaKEEAKAQEIAKAKEEAKAQEIAKAKEEEKAQ-EIAKAKEEAKAREIAKAKEEE 327

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 2250709889 1328 RLR-----KEEEKARR-ELIKQEYLRRKQQQALEEQ 1357
Cdd:NF040676   328 KAReiakaKEEAKAREiAKAKEEAKAREIAKAKEEE 363
 
Name Accession Description Interval E-value
CAMSAP_CKK smart01051
Microtubule-binding calmodulin-regulated spectrin-associated; This is the C-terminal domain of ...
 1464-1592 5.27e-76

Microtubule-binding calmodulin-regulated spectrin-associated; This is the C-terminal domain of a family of eumetazoan proteins collectively defined as calmodulin-regulated spectrin-associated, or CAMSAP, proteins. CAMSAP proteins carry an N-terminal region that includes the CH domain, a central region including a predicted coiled-coil and this C-terminal, or CKK, domain - defined as being present in CAMSAP, KIAA1078 and KIAA1543, The C-terminal domain is the part of the CAMSAP proteins that binds to microtubules. The domain appears to act by producing inhibition of neurite extension, probably by blocking microtubule function. CKK represents a domain that has evolved with the metazoa. The structure of a murine hypothetical protein from RIKEN cDNA has shown the domain to adopt a mainly beta barrel structure with an associated alpha-helical hairpin.


Pssm-ID: 198119  Cd Length: 129  Bit Score: 247.66  E-value: 5.27e-76
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250709889  1464 GPKLFKEPSSKSNKPIIHNAISHCCLAGKVNEPHKNSILEELEKCDANHYIILFRDAGCQFRALYCYQPDTEEIYKLTGT 1543
Cdd:smart01051    1 GPKLYKEPSAKSNRFIIHNALSHCCLAGKVNEPQKNKILEEMEKSEANHFLILFRDAKCQFRALYTLNPETEELVKLYGN 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*....
gi 2250709889  1544 GPKSITKKMIDKLYKYSSDRKQFNLIPAKTMSVSVDALTIHNHLWQPKR 1592
Cdd:smart01051   81 GPRVITSKMVESLYKYDSSRKQFTQIPSKTLSVSVDAFTIKNHLWQTKK 129
CAMSAP_CKK pfam08683
Microtubule-binding calmodulin-regulated spectrin-associated; This is the C-terminal domain of ...
 1465-1583 1.24e-74

Microtubule-binding calmodulin-regulated spectrin-associated; This is the C-terminal domain of a family of eumetazoan proteins collectively defined as calmodulin-regulated spectrin-associated, or CAMSAP, proteins. CAMSAP proteins carry an N-terminal region that includes the CH domain, a central region including a predicted coiled-coil and this C-terminal, or CKK, domain - defined as being present in CAMSAP, KIAA1078 and KIAA1543, The C-terminal domain is the part of the CAMSAP proteins that binds to microtubules. The domain appears to act by producing inhibition of neurite extension, probably by blocking microtubule function. CKK represents a domain that has evolved with the metazoa. The structure of a murine hypothetical protein from RIKEN cDNA has shown the domain to adopt a mainly beta barrel structure with an associated alpha-helical hairpin.


Pssm-ID: 462558  Cd Length: 119  Bit Score: 243.34  E-value: 1.24e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250709889 1465 PKLFKEPSSKSNKPIIHNAISHCCLAGKVNEPHKNSILEELEKCDANHYIILFRDAGCQFRALYCYQPDTEEIYKLTGTG 1544
Cdd:pfam08683    1 PKLFKKPSAKSNKKIIHNALSHCCLAGKVNEDQKNKILEELEKSESKHFLILFRDSGCQFRALYSYNPETEELVKLHGIG 80

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2250709889 1545 PKSITKKMIDKLYKYSSDRKQFNLIPAKTMSVSVDALTI 1583
Cdd:pfam08683   81 PRVVTPKMIEKFYKYNSGRKQFTEIPTKTLSVSIDAFTI 119
CAMSAP_CH pfam11971
CAMSAP CH domain; This domain is the N-terminal CH domain from the CAMSAP proteins.
 248-331 2.25e-39

CAMSAP CH domain; This domain is the N-terminal CH domain from the CAMSAP proteins.


Pssm-ID: 432229  Cd Length: 85  Bit Score: 141.28  E-value: 2.25e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250709889  248 HLSARQSPYFPLLEDLMRDGSDGAALLAVVHYYCPEQMKLDDICLKEVPSMADSLYNIRLLREFSNEHL-NKCFYLTLED 326
Cdd:pfam11971    1 PLSQRSLPLSPPVEDLLRDLSDGCALAALIHFYCPQLIDLEDICLKESMSLADSLYNIQLLQEFCQRHLgNRCCHLTLED 80


                   ....*
gi 2250709889  327 MLYAP 331
Cdd:pfam11971   81 LLYAR 85
CAMSAP_CC1 pfam17095
Spectrin-binding region of Ca2+-Calmodulin; CAMSAP_CC1 is the conserved region on ...
 879-937 1.79e-22

Spectrin-binding region of Ca2+-Calmodulin; CAMSAP_CC1 is the conserved region on calmodulin-regulated spectrin-associated proteins in eukaryotes that binds spectrin. CAMSAPs are vertebrate microtubule-binding proteins, representatives of a family of cytoskeletal proteins that arose in animals. This conserved CC1 region binds to both spectrin and Ca2+/calmodulin in vitro, although the binding of Ca2+/calmodulin inhibited the binding of spectrin. CC1 appears to be a functional region of CAMSAP1 that links spectrin-binding to neurite outgrowth.


Pssm-ID: 465344 [Multi-domain]  Cd Length: 59  Bit Score: 91.98  E-value: 1.79e-22
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2250709889  879 PGRHSKDPASLLASELVQLHMQLEEKRRAIEAQKKKMEALSARQRLKLGKAAFLHVVKK 937
Cdd:pfam17095    1 PGDDSPSASPELASELSQLRLKLEEKRRAIEQQKKRMEAAFARQRQKLGKAAFLQVVKK 59
ARGLU pfam15346
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...
 1277-1354 1.87e-10

Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is required for the oestrogen-dependent expression of ESR1 target genes. It functions in cooperation with MED1. The family of proteins is found in eukaryotes.


Pssm-ID: 405931 [Multi-domain]  Cd Length: 151  Bit Score: 60.84  E-value: 1.87e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250709889 1277 EQKAEDELAKKRAAFLLKQQRKAEEARARKQQLEAEVE---LKRDEARRKAEEDRL-------RKEEEKARRELIKQEYL 1346
Cdd:pfam15346   51 EKQVLEELEREREAELEEERRKEEEERKKREELERILEennRKIEEAQRKEAEERLamleeqrRMKEERQRREKEEEERE 130


                   ....*...
gi 2250709889 1347 RRKQQQAL 1354
Cdd:pfam15346  131 KREQQKIL 138
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 1277-1352 7.05e-07

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 53.31  E-value: 7.05e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2250709889 1277 EQKAEDELAKKRAAFLLKQQRKAEearaRKQQLEAEVELKRDE-ARRKAEEDRLRKEEEKARReliKQEYLRRKQQQ 1352
Cdd:TIGR02794  108 EQAAKQAEEKQKQAEEAKAKQAAE----AKAKAEAEAERKAKEeAAKQAEEEAKAKAAAEAKK---KAEEAKKKAEA 177
PTZ00121 PTZ00121
MAEBL; Provisional
 1276-1357 5.00e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 51.68  E-value: 5.00e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250709889 1276 DEQKAEDELAKKRAAFLLK---QQRKAEEARARKQQLEAEvELKRDEARRKAEEDRlRKEEEKARRELIKQEYLRRKQQQ 1352
Cdd:PTZ00121  1486 DEAKKKAEEAKKKADEAKKaaeAKKKADEAKKAEEAKKAD-EAKKAEEAKKADEAK-KAEEKKKADELKKAEELKKAEEK 1563


                   ....*
gi 2250709889 1353 ALEEQ 1357
Cdd:PTZ00121  1564 KKAEE 1568
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
1279-1356 2.47e-05

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 48.72  E-value: 2.47e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250709889 1279 KAEDELAKKRAAFLLKQQRK-------AEEARARKQQ-LEAEVELKRDEARRKAEEDRLRKEEEKARRELIKQEYLRRKQ 1350
Cdd:COG2268    241 EAEAELAKKKAEERREAETAraeaeaaYEIAEANAEReVQRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQA 320


                   ....*.
gi 2250709889 1351 QQALEE 1356
Cdd:COG2268    321 AEAEAE 326
wall_bind_EntB NF040676
cell wall-binding protein EntB; This HMM describes the cell wall-binding protein EntB, as ...
 1179-1357 8.08e-05

cell wall-binding protein EntB; This HMM describes the cell wall-binding protein EntB, as found in Bacillus cereus. EntB is related to EntA, EntC, and EndD. All Ent family proteins have a signal peptide, an N-terminal SH3 domain and a C-terminal 3D (Asp-Asp-Asp) domain. EntB and EndC have a central region with a highly variable number of repeats resembling KAXEXX. The gene symbol derives from the notion that at least some members of the family function as enterotoxins, but more recent descriptions focus on roles in stress response and cell wall integrity.


Pssm-ID: 468642 [Multi-domain]  Cd Length: 476  Bit Score: 47.08  E-value: 8.08e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250709889 1179 RTFVLSSCKDANIVSEQVNFKEGLDTS----VKEAGLSSSTITGKEHTPVEEPLRSKAsliEVDLSDLKAPDEDGEV--- 1251
Cdd:NF040676   172 KTQKVAKAKETTKAQEIVKPKEEVKVQevvkPKEEPKVQEIVKPKEEVKVQEEVKPKE---EEKVQEIVKPKEEAKVqee 248

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250709889 1252 --VGHESSVELGGDSDQKPGVGFFF--KDEQKAEDELAKKRAAFLLKQQRKAEEARARkQQLEAEVELKRDEARRKAEED 1327
Cdd:NF040676   249 vkVKEEAKVQEIAKAKEEAKAQEIAkaKEEAKAQEIAKAKEEAKAQEIAKAKEEEKAQ-EIAKAKEEAKAREIAKAKEEE 327

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 2250709889 1328 RLR-----KEEEKARR-ELIKQEYLRRKQQQALEEQ 1357
Cdd:NF040676   328 KAReiakaKEEAKAREiAKAKEEAKAREIAKAKEEE 363
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 1286-1356 9.65e-05

F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 43.97  E-value: 9.65e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2250709889 1286 KKRAAFLLKQQRKAEEARARKQQLEAEVELKRDEARRKAEE--DRLRKEEEKARRELIK--QEYLRRKQQQALEE 1356
Cdd:cd06503     29 DEREEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAQEiiEEARKEAEKIKEEILAeaKEEAERILEQAKAE 103
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 1273-1356 8.21e-04

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 41.42  E-value: 8.21e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250709889  1273 FFKDEQKAEDELAKKRAAFLlkqQRKAEEARARKQQLEAEVELKRDEARRKAEEDRLRKEEEKARRELIKQEYLRRKQQQ 1352
Cdd:smart00935   15 AGKAAQKQLEKEFKKRQAEL---EKLEKELQKLKEKLQKDAATLSEAAREKKEKELQKKVQEFQRKQQKLQQDLQKRQQE 91


                    ....
gi 2250709889  1353 ALEE 1356
Cdd:smart00935   92 ELQK 95
 
Name Accession Description Interval E-value
CAMSAP_CKK smart01051
Microtubule-binding calmodulin-regulated spectrin-associated; This is the C-terminal domain of ...
 1464-1592 5.27e-76

Microtubule-binding calmodulin-regulated spectrin-associated; This is the C-terminal domain of a family of eumetazoan proteins collectively defined as calmodulin-regulated spectrin-associated, or CAMSAP, proteins. CAMSAP proteins carry an N-terminal region that includes the CH domain, a central region including a predicted coiled-coil and this C-terminal, or CKK, domain - defined as being present in CAMSAP, KIAA1078 and KIAA1543, The C-terminal domain is the part of the CAMSAP proteins that binds to microtubules. The domain appears to act by producing inhibition of neurite extension, probably by blocking microtubule function. CKK represents a domain that has evolved with the metazoa. The structure of a murine hypothetical protein from RIKEN cDNA has shown the domain to adopt a mainly beta barrel structure with an associated alpha-helical hairpin.


Pssm-ID: 198119  Cd Length: 129  Bit Score: 247.66  E-value: 5.27e-76
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250709889  1464 GPKLFKEPSSKSNKPIIHNAISHCCLAGKVNEPHKNSILEELEKCDANHYIILFRDAGCQFRALYCYQPDTEEIYKLTGT 1543
Cdd:smart01051    1 GPKLYKEPSAKSNRFIIHNALSHCCLAGKVNEPQKNKILEEMEKSEANHFLILFRDAKCQFRALYTLNPETEELVKLYGN 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*....
gi 2250709889  1544 GPKSITKKMIDKLYKYSSDRKQFNLIPAKTMSVSVDALTIHNHLWQPKR 1592
Cdd:smart01051   81 GPRVITSKMVESLYKYDSSRKQFTQIPSKTLSVSVDAFTIKNHLWQTKK 129
CAMSAP_CKK pfam08683
Microtubule-binding calmodulin-regulated spectrin-associated; This is the C-terminal domain of ...
 1465-1583 1.24e-74

Microtubule-binding calmodulin-regulated spectrin-associated; This is the C-terminal domain of a family of eumetazoan proteins collectively defined as calmodulin-regulated spectrin-associated, or CAMSAP, proteins. CAMSAP proteins carry an N-terminal region that includes the CH domain, a central region including a predicted coiled-coil and this C-terminal, or CKK, domain - defined as being present in CAMSAP, KIAA1078 and KIAA1543, The C-terminal domain is the part of the CAMSAP proteins that binds to microtubules. The domain appears to act by producing inhibition of neurite extension, probably by blocking microtubule function. CKK represents a domain that has evolved with the metazoa. The structure of a murine hypothetical protein from RIKEN cDNA has shown the domain to adopt a mainly beta barrel structure with an associated alpha-helical hairpin.


Pssm-ID: 462558  Cd Length: 119  Bit Score: 243.34  E-value: 1.24e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250709889 1465 PKLFKEPSSKSNKPIIHNAISHCCLAGKVNEPHKNSILEELEKCDANHYIILFRDAGCQFRALYCYQPDTEEIYKLTGTG 1544
Cdd:pfam08683    1 PKLFKKPSAKSNKKIIHNALSHCCLAGKVNEDQKNKILEELEKSESKHFLILFRDSGCQFRALYSYNPETEELVKLHGIG 80

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2250709889 1545 PKSITKKMIDKLYKYSSDRKQFNLIPAKTMSVSVDALTI 1583
Cdd:pfam08683   81 PRVVTPKMIEKFYKYNSGRKQFTEIPTKTLSVSIDAFTI 119
CAMSAP_CH pfam11971
CAMSAP CH domain; This domain is the N-terminal CH domain from the CAMSAP proteins.
 248-331 2.25e-39

CAMSAP CH domain; This domain is the N-terminal CH domain from the CAMSAP proteins.


Pssm-ID: 432229  Cd Length: 85  Bit Score: 141.28  E-value: 2.25e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250709889  248 HLSARQSPYFPLLEDLMRDGSDGAALLAVVHYYCPEQMKLDDICLKEVPSMADSLYNIRLLREFSNEHL-NKCFYLTLED 326
Cdd:pfam11971    1 PLSQRSLPLSPPVEDLLRDLSDGCALAALIHFYCPQLIDLEDICLKESMSLADSLYNIQLLQEFCQRHLgNRCCHLTLED 80


                   ....*
gi 2250709889  327 MLYAP 331
Cdd:pfam11971   81 LLYAR 85
CAMSAP_CC1 pfam17095
Spectrin-binding region of Ca2+-Calmodulin; CAMSAP_CC1 is the conserved region on ...
 879-937 1.79e-22

Spectrin-binding region of Ca2+-Calmodulin; CAMSAP_CC1 is the conserved region on calmodulin-regulated spectrin-associated proteins in eukaryotes that binds spectrin. CAMSAPs are vertebrate microtubule-binding proteins, representatives of a family of cytoskeletal proteins that arose in animals. This conserved CC1 region binds to both spectrin and Ca2+/calmodulin in vitro, although the binding of Ca2+/calmodulin inhibited the binding of spectrin. CC1 appears to be a functional region of CAMSAP1 that links spectrin-binding to neurite outgrowth.


Pssm-ID: 465344 [Multi-domain]  Cd Length: 59  Bit Score: 91.98  E-value: 1.79e-22
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2250709889  879 PGRHSKDPASLLASELVQLHMQLEEKRRAIEAQKKKMEALSARQRLKLGKAAFLHVVKK 937
Cdd:pfam17095    1 PGDDSPSASPELASELSQLRLKLEEKRRAIEQQKKRMEAAFARQRQKLGKAAFLQVVKK 59
ARGLU pfam15346
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...
 1277-1354 1.87e-10

Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is required for the oestrogen-dependent expression of ESR1 target genes. It functions in cooperation with MED1. The family of proteins is found in eukaryotes.


Pssm-ID: 405931 [Multi-domain]  Cd Length: 151  Bit Score: 60.84  E-value: 1.87e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250709889 1277 EQKAEDELAKKRAAFLLKQQRKAEEARARKQQLEAEVE---LKRDEARRKAEEDRL-------RKEEEKARRELIKQEYL 1346
Cdd:pfam15346   51 EKQVLEELEREREAELEEERRKEEEERKKREELERILEennRKIEEAQRKEAEERLamleeqrRMKEERQRREKEEEERE 130


                   ....*...
gi 2250709889 1347 RRKQQQAL 1354
Cdd:pfam15346  131 KREQQKIL 138
DDRGK pfam09756
DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and ...
 1285-1359 9.53e-08

DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and vertebrates. They contain a highly conserved DDRGK motif.


Pssm-ID: 370664 [Multi-domain]  Cd Length: 188  Bit Score: 53.89  E-value: 9.53e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250709889 1285 AKKRAAFLLKQQRKA---------EEARARKQQLEAEV---ELKRDEARRKAEEDRLRKEEEKARREliKQEYLRRKQQQ 1352
Cdd:pfam09756    5 AKKRAKLELKEAKRQqreaeeeerEEREKLEEKREEEYkerEEREEEAEKEKEEEERKQEEEQERKE--QEEYEKLKSQF 82


                   ....*..
gi 2250709889 1353 ALEEQGL 1359
Cdd:pfam09756   83 VVEEEGT 89
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 1275-1355 1.76e-07

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 55.73  E-value: 1.76e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250709889 1275 KDEQKAEDELAKK-RAAFLLKQQRKAEEARARKQQLEAEVELKRDEARR-----KAEEDRLRKEEEKARRELikQEYLRR 1348
Cdd:pfam15709  361 RRLQQEQLERAEKmREELELEQQRRFEEIRLRKQRLEEERQRQEEEERKqrlqlQAAQERARQQQEEFRRKL--QELQRK 438


                   ....*..
gi 2250709889 1349 KQQQALE 1355
Cdd:pfam15709  439 KQQEEAE 445
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 1277-1352 7.05e-07

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 53.31  E-value: 7.05e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2250709889 1277 EQKAEDELAKKRAAFLLKQQRKAEearaRKQQLEAEVELKRDE-ARRKAEEDRLRKEEEKARReliKQEYLRRKQQQ 1352
Cdd:TIGR02794  108 EQAAKQAEEKQKQAEEAKAKQAAE----AKAKAEAEAERKAKEeAAKQAEEEAKAKAAAEAKK---KAEEAKKKAEA 177
PTZ00121 PTZ00121
MAEBL; Provisional
 1276-1357 5.00e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 51.68  E-value: 5.00e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250709889 1276 DEQKAEDELAKKRAAFLLK---QQRKAEEARARKQQLEAEvELKRDEARRKAEEDRlRKEEEKARRELIKQEYLRRKQQQ 1352
Cdd:PTZ00121  1486 DEAKKKAEEAKKKADEAKKaaeAKKKADEAKKAEEAKKAD-EAKKAEEAKKADEAK-KAEEKKKADELKKAEELKKAEEK 1563


                   ....*
gi 2250709889 1353 ALEEQ 1357
Cdd:PTZ00121  1564 KKAEE 1568
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 1277-1357 1.79e-05

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 48.76  E-value: 1.79e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250709889 1277 EQKAEDELAKKRAAFLLKQQRKAEEARARKQQLEAEVELKRDEAR--------RKAEEDRLR----------KEEEKARR 1338
Cdd:pfam13868  146 EKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRaqqekaqdEKAERDELRaklyqeeqerKERQKERE 225

                           90
                   ....*....|....*....
gi 2250709889 1339 ELIKQEYLRRKQQQALEEQ 1357
Cdd:pfam13868  226 EAEKKARQRQELQQAREEQ 244
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 1278-1355 1.80e-05

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 48.69  E-value: 1.80e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250709889 1278 QKAEDELAKKRAAFLLKQ-----QRKAEEARARKQQLEAevELKRDEARRKAEEDRLRKEE--EKARRELIKQEYLRRKQ 1350
Cdd:TIGR02794  126 AKQAAEAKAKAEAEAERKakeeaAKQAEEEAKAKAAAEA--KKKAEEAKKKAEAEAKAKAEaeAKAKAEEAKAKAEAAKA 203


                   ....*
gi 2250709889 1351 QQALE 1355
Cdd:TIGR02794  204 KAAAE 208
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
1279-1356 2.47e-05

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 48.72  E-value: 2.47e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250709889 1279 KAEDELAKKRAAFLLKQQRK-------AEEARARKQQ-LEAEVELKRDEARRKAEEDRLRKEEEKARRELIKQEYLRRKQ 1350
Cdd:COG2268    241 EAEAELAKKKAEERREAETAraeaeaaYEIAEANAEReVQRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQA 320


                   ....*.
gi 2250709889 1351 QQALEE 1356
Cdd:COG2268    321 AEAEAE 326
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 1294-1357 2.69e-05

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 45.80  E-value: 2.69e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2250709889 1294 KQQRKAEEARARKQQL---EAEVELKRDEARRKAEEDRLRKEEEKARRELIKQEYLRRKQQQALEEQ 1357
Cdd:pfam05672   33 ERLEKEEEERLRKEELrrrAEEERARREEEARRLEEERRREEEERQRKAEEEAEEREQREQEEQERL 99
PTZ00121 PTZ00121
MAEBL; Provisional
 1276-1356 3.27e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.98  E-value: 3.27e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250709889 1276 DEQKAEDELAKKRAAFLLKQQRKAEEARARKQQLEAEvELKRDEARRKAEEDrlRKEEEKARRELIKQEYLRRKQQQALE 1355
Cdd:PTZ00121  1519 EEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAE-ELKKAEEKKKAEEA--KKAEEDKNMALRKAEEAKKAEEARIE 1595


                   .
gi 2250709889 1356 E 1356
Cdd:PTZ00121  1596 E 1596
ARGLU pfam15346
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...
 1276-1356 3.87e-05

Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is required for the oestrogen-dependent expression of ESR1 target genes. It functions in cooperation with MED1. The family of proteins is found in eukaryotes.


Pssm-ID: 405931 [Multi-domain]  Cd Length: 151  Bit Score: 45.43  E-value: 3.87e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250709889 1276 DEQKAEDELAKKRAAFLLKqqRKAEEARARKQQLEAEVELKRDEARRKAEEDRLRKEEEKARRELI----KQEYLRRKQQ 1351
Cdd:pfam15346    4 ESKLLEEETARRVEEAVAK--RVEEELEKRKDEIEAEVERRVEEARKIMEKQVLEELEREREAELEeerrKEEEERKKRE 81


                   ....*
gi 2250709889 1352 QaLEE 1356
Cdd:pfam15346   82 E-LER 85
PTZ00121 PTZ00121
MAEBL; Provisional
 1276-1357 4.98e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.21  E-value: 4.98e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250709889 1276 DEQKAEDELAKKRAAFLlkqQRKAEEARARKQQLEAEVELKRDE---ARRKAEEDRLRKEEEKARRELIKQEYLRRKQQQ 1352
Cdd:PTZ00121  1318 DEAKKKAEEAKKKADAA---KKKAEEAKKAAEAAKAEAEAAADEaeaAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKAD 1394


                   ....*
gi 2250709889 1353 ALEEQ 1357
Cdd:PTZ00121  1395 EAKKK 1399
PRK12704 PRK12704
phosphodiesterase; Provisional
 1269-1357 5.12e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 47.85  E-value: 5.12e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250709889 1269 GVGFFF---KDEQKAEDelAKKRAAFLLKQQRKA-------------EEARARKQQLEAEV-----ELKRDEARRKAEED 1327
Cdd:PRK12704    19 VIGYFVrkkIAEAKIKE--AEEEAKRILEEAKKEaeaikkealleakEEIHKLRNEFEKELrerrnELQKLEKRLLQKEE 96

                           90       100       110
                   ....*....|....*....|....*....|...
gi 2250709889 1328 RLRKEEE---KARRELIKQEYLRRKQQQALEEQ 1357
Cdd:PRK12704    97 NLDRKLElleKREEELEKKEKELEQKQQELEKK 129
ATP-synt_B pfam00430
ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is ...
 1275-1356 7.25e-05

ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is thought to translocate protons through membrane (inner membrane in mitochondria, thylakoid membrane in plants, cytoplasmic membrane in bacteria). The B subunits are thought to interact with the stalk of the CF(1) subunits. This domain should not be confused with the ab CF(1) proteins (in the head of the ATP synthase) which are found in pfam00006


Pssm-ID: 425677 [Multi-domain]  Cd Length: 132  Bit Score: 44.23  E-value: 7.25e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250709889 1275 KDEQKAEDELAKKRAAFLLKQQRKAEEARARKQQLEAEVelkRDEARRKAEEDRLRKEEEKARRELIKQEYLRRKQQQAL 1354
Cdd:pfam00430   36 ADEIAEAEERRKDAAAALAEAEQQLKEARAEAQEIIENA---KKRAEKLKEEIVAAAEAEAERIIEQAAAEIEQEKDRAL 112


                   ..
gi 2250709889 1355 EE 1356
Cdd:pfam00430  113 AE 114
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
1275-1357 7.78e-05

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 47.17  E-value: 7.78e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250709889 1275 KDEQKAEDELAKKRAafllKQQRKAEEARARKQ---------QLEAEVELKRDEARRKAEEDRLRKE------EEKARRE 1339
Cdd:COG2268    203 IAEAEAERETEIAIA----QANREAEEAELEQEreietariaEAEAELAKKKAEERREAETARAEAEaayeiaEANAERE 278

                           90
                   ....*....|....*....
gi 2250709889 1340 LIKQ-EYLRRKQQQALEEQ 1357
Cdd:COG2268    279 VQRQlEIAEREREIELQEK 297
CAF-1_p150 pfam11600
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ...
 1276-1357 7.94e-05

Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide subunit of CAF-1, which functions in depositing newly synthesized and acetylated histones H3/H4 into chromatin during DNA replication and repair. CAF-1_p150 includes the HP1 interaction site, the PEST, KER and ED interacting sites. CAF-1_p150 interacts directly with newly synthesized and acetylated histones through the acidic KER and ED domains. The PEST domain is associated with proteins that undergo rapid proteolysis.


Pssm-ID: 402959 [Multi-domain]  Cd Length: 164  Bit Score: 44.68  E-value: 7.94e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250709889 1276 DEQKAEDELAKKRAAFLLKQQRKAEEARARKQQLEAEVELKRDEARRKAEEDRLRKE----EEKARRELIKQEYLRRKQQ 1351
Cdd:pfam11600   12 EKEKQRLEKDKERLRRQLKLEAEKEEKERLKEEAKAEKERAKEEARRKKEEEKELKEkerrEKKEKDEKEKAEKLRLKEE 91


                   ....*.
gi 2250709889 1352 QALEEQ 1357
Cdd:pfam11600   92 KRKEKQ 97
wall_bind_EntB NF040676
cell wall-binding protein EntB; This HMM describes the cell wall-binding protein EntB, as ...
 1179-1357 8.08e-05

cell wall-binding protein EntB; This HMM describes the cell wall-binding protein EntB, as found in Bacillus cereus. EntB is related to EntA, EntC, and EndD. All Ent family proteins have a signal peptide, an N-terminal SH3 domain and a C-terminal 3D (Asp-Asp-Asp) domain. EntB and EndC have a central region with a highly variable number of repeats resembling KAXEXX. The gene symbol derives from the notion that at least some members of the family function as enterotoxins, but more recent descriptions focus on roles in stress response and cell wall integrity.


Pssm-ID: 468642 [Multi-domain]  Cd Length: 476  Bit Score: 47.08  E-value: 8.08e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250709889 1179 RTFVLSSCKDANIVSEQVNFKEGLDTS----VKEAGLSSSTITGKEHTPVEEPLRSKAsliEVDLSDLKAPDEDGEV--- 1251
Cdd:NF040676   172 KTQKVAKAKETTKAQEIVKPKEEVKVQevvkPKEEPKVQEIVKPKEEVKVQEEVKPKE---EEKVQEIVKPKEEAKVqee 248

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250709889 1252 --VGHESSVELGGDSDQKPGVGFFF--KDEQKAEDELAKKRAAFLLKQQRKAEEARARkQQLEAEVELKRDEARRKAEED 1327
Cdd:NF040676   249 vkVKEEAKVQEIAKAKEEAKAQEIAkaKEEAKAQEIAKAKEEAKAQEIAKAKEEEKAQ-EIAKAKEEAKAREIAKAKEEE 327

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 2250709889 1328 RLR-----KEEEKARR-ELIKQEYLRRKQQQALEEQ 1357
Cdd:NF040676   328 KAReiakaKEEAKAREiAKAKEEAKAREIAKAKEEE 363
PTZ00121 PTZ00121
MAEBL; Provisional
 1275-1353 9.44e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.44  E-value: 9.44e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250709889 1275 KDEQKAEDELAKKRAafllKQQRKAEEARARKQqleaEVELKRDEARRKAEE----DRLRKEEEKARRELIKQEYLRRKQ 1350
Cdd:PTZ00121  1465 KAEEAKKADEAKKKA----EEAKKADEAKKKAE----EAKKKADEAKKAAEAkkkaDEAKKAEEAKKADEAKKAEEAKKA 1536


                   ...
gi 2250709889 1351 QQA 1353
Cdd:PTZ00121  1537 DEA 1539
PTZ00121 PTZ00121
MAEBL; Provisional
 1275-1353 9.60e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.44  E-value: 9.60e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250709889 1275 KDEQKAEDELAKKRAAFLLKQ---QRKAEEARARKQQLE--AEVELKRDEARRKAEEDRLRKEEEKARRELIKQEYLRRK 1349
Cdd:PTZ00121  1373 KEEAKKKADAAKKKAEEKKKAdeaKKKAEEDKKKADELKkaAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKK 1452


                   ....
gi 2250709889 1350 QQQA 1353
Cdd:PTZ00121  1453 AEEA 1456
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 1286-1356 9.65e-05

F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 43.97  E-value: 9.65e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2250709889 1286 KKRAAFLLKQQRKAEEARARKQQLEAEVELKRDEARRKAEE--DRLRKEEEKARRELIK--QEYLRRKQQQALEE 1356
Cdd:cd06503     29 DEREEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAQEiiEEARKEAEKIKEEILAeaKEEAERILEQAKAE 103
Pinin_SDK_memA pfam04696
pinin/SDK/memA/ protein conserved region; Members of this family have very varied ...
 1274-1354 9.70e-05

pinin/SDK/memA/ protein conserved region; Members of this family have very varied localizations within the eukaryotic cell. pinin is known to localize at the desmosomes and is implicated in anchoring intermediate filaments to the desmosomal plaque. SDK2/3 is a dynamically localized nuclear protein thought to be involved in modulation of alternative pre-mRNA splicing. memA is a tumour marker preferentially expressed in human melanoma cell lines. A common feature of the members of this family is that they may all participate in regulating protein-protein interactions.


Pssm-ID: 461396 [Multi-domain]  Cd Length: 130  Bit Score: 43.82  E-value: 9.70e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250709889 1274 FKDEQKAEDELAKKRAAFLLKQQRKAEEARARKQQLEAEvELKRDEARRKAEEDRLRKEEEKArrELIKQEYLRRKQQQA 1353
Cdd:pfam04696   21 FKKEESKQKEKEERRAEIEKRLEEKAKQEKEELEERKRE-EREELFEERRAEQIELRALEEKL--ELKELMETWHENLKA 97


                   .
gi 2250709889 1354 L 1354
Cdd:pfam04696   98 L 98
PTZ00121 PTZ00121
MAEBL; Provisional
 1275-1352 1.16e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.06  E-value: 1.16e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2250709889 1275 KDEQKAEDELAKKRAAfllKQQRKAEEARARKQQLEAEVELKRDEARRKAEEdrLRKEEEKARRELIKQEYLRRKQQQ 1352
Cdd:PTZ00121  1478 KAEEAKKADEAKKKAE---EAKKKADEAKKAAEAKKKADEAKKAEEAKKADE--AKKAEEAKKADEAKKAEEKKKADE 1550
PTZ00121 PTZ00121
MAEBL; Provisional
 1276-1357 1.25e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.06  E-value: 1.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250709889 1276 DEQKAEDELAKKraafllKQQRKAEEARARKQQLEAEvELKRDEARRKAEEDRLRKEEEKARRELIKQEYLRRKQQQALE 1355
Cdd:PTZ00121  1339 EEAKKAAEAAKA------EAEAAADEAEAAEEKAEAA-EKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELK 1411


                   ..
gi 2250709889 1356 EQ 1357
Cdd:PTZ00121  1412 KA 1413
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 1275-1357 1.30e-04

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 45.99  E-value: 1.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250709889 1275 KDEQKAEDELAKKRAAflLKQQRKAEEARAR--KQQLEAEVELKRDEARRKAEEDRLRKEEEKARreliKQEYLRRKQQQ 1352
Cdd:TIGR02794   64 KKEQERQKKLEQQAEE--AEKQRAAEQARQKelEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKA----KQAAEAKAKAE 137


                   ....*
gi 2250709889 1353 ALEEQ 1357
Cdd:TIGR02794  138 AEAER 142
PTZ00121 PTZ00121
MAEBL; Provisional
 1275-1353 1.32e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.06  E-value: 1.32e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2250709889 1275 KDEQKAEDELAKKRAafllKQQRKAEEARARkqqleAEVELKRDEARRKAEEDRLRKEEEKARRELIKQEYLRRKQQQA 1353
Cdd:PTZ00121  1413 AAAAKKKADEAKKKA----EEKKKADEAKKK-----AEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEA 1482
PTZ00121 PTZ00121
MAEBL; Provisional
 1275-1357 1.43e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.06  E-value: 1.43e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250709889 1275 KDEQKAEDELAKKRAAFLLKQQRKAEEARARKQQLEAEvELKRDEARRKAEEDRLRKEEEKARRELIKQEYLRRKQQQAL 1354
Cdd:PTZ00121  1256 KFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAD-EAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAA 1334


                   ...
gi 2250709889 1355 EEQ 1357
Cdd:PTZ00121  1335 KKK 1337
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 1277-1353 1.48e-04

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 43.88  E-value: 1.48e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2250709889 1277 EQKAEDELAKKRAAfllKQQRKAEEARARKQQLEAEVELKRDEARRKAEEDRLRKEEEKARRELIKQEYLRRKQQQA 1353
Cdd:pfam05672   41 ERLRKEELRRRAEE---ERARREEEARRLEEERRREEEERQRKAEEEAEEREQREQEEQERLQKQKEEAEAKAREEA 114
PTZ00121 PTZ00121
MAEBL; Provisional
 1276-1353 1.51e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.67  E-value: 1.51e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250709889 1276 DEQKAEDELAKKRAafllKQQRKAEEARARKQQLEAEVELKR--DEARRKAEEDRLRKEEEKARRELIKQEYLRRKQQQA 1353
Cdd:PTZ00121  1394 DEAKKKAEEDKKKA----DELKKAAAAKKKADEAKKKAEEKKkaDEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEA 1469
UDM1_RNF168 cd22265
UDM1 (ubiquitin-dependent DSB recruitment module 1) domain found in RING finger protein 168; ...
 1278-1339 1.65e-04

UDM1 (ubiquitin-dependent DSB recruitment module 1) domain found in RING finger protein 168; RING finger protein 168 (RNF168) is an E3 ubiquitin-protein ligase that promotes noncanonical K27 ubiquitination to signal DNA damage. Together with RNF8, RNF168 functions as a DNA damage response (DDR) factor that promotes a series of ubiquitylation events on substrates such as H2A and H2AX. With H2AK13/15 ubiquitylation, it facilitates recruitment of repair factors p53-binding protein 1 (53BP1) or the RAP80-BRCA1 complex to sites of double-strand breaks (DSBs), and inhibits homologous recombination (HR) in cells deficient in the tumor suppressor BRCA1. RNF168 also promotes H2A neddylation, which antagonizes ubiquitylation of H2A and regulates DNA damage repair. In addition, RNF168 forms a functional complex with RAD6A or RAD6B during the DNA damage response. This model corresponds to the UDM1 (ubiquitin-dependent double-strand break [DSB] recruitment module 1) domain of RNF168, which comprises LRM1 (LR motif 1), UMI (ubiquitin-interacting motif [UIM]- and MIU-related UBD) and MIU1 (motif interacting with ubiquitin 1). Mutations of Ub-interacting residues in UDM1 have little effect on the accumulation of RNF168 to DSB sites, suggesting that it may not be the main site of binding ubiquitylated and polyubiquitylated targets.


Pssm-ID: 409018 [Multi-domain]  Cd Length: 73  Bit Score: 41.39  E-value: 1.65e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2250709889 1278 QKAEDEL----AKKRAafLLKQQRKAEEARARKQQLEAEVELKRDEARRKAEEDRLRKEEEKARRE 1339
Cdd:cd22265      9 QEYEEEIskleAERRA--LEEEENRASEEYIQKLLAEEEEEEKLAEERRRAEEEQLKEDEELARKL 72
PTZ00121 PTZ00121
MAEBL; Provisional
 1275-1357 2.14e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.29  E-value: 2.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250709889 1275 KDEQKAEDELAKKRAafllKQQRKAEEARARKQQL---EAEVELKRDEARRKAEEDRLRKEEEKAR--------RELIKQ 1343
Cdd:PTZ00121  1608 KAEEAKKAEEAKIKA----EELKKAEEEKKKVEQLkkkEAEEKKKAEELKKAEEENKIKAAEEAKKaeedkkkaEEAKKA 1683

                           90
                   ....*....|....
gi 2250709889 1344 EYLRRKQQQALEEQ 1357
Cdd:PTZ00121  1684 EEDEKKAAEALKKE 1697
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 1274-1344 2.57e-04

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 45.29  E-value: 2.57e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250709889 1274 FKDEQKAEDELAKKRAAFLLKQ-QRKAEEARARKQQLEAEVE--------LKRDEARRKAEEDRLRKEEEKARRELIKQE 1344
Cdd:pfam13868  255 EAEREEEEFERMLRKQAEDEEIeQEEAEKRRMKRLEHRRELEkqieereeQRAAEREEELEEGERLREEEAERRERIEEE 334
PTZ00121 PTZ00121
MAEBL; Provisional
 1275-1353 3.12e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.90  E-value: 3.12e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250709889 1275 KDEQKAEDELAKKRAAFLLKQQ----RKAEEARarkqQLEAEVELKRDEARRKAEEDR-----LRKEEEKARReliKQEY 1345
Cdd:PTZ00121  1621 KAEELKKAEEEKKKVEQLKKKEaeekKKAEELK----KAEEENKIKAAEEAKKAEEDKkkaeeAKKAEEDEKK---AAEA 1693


                   ....*...
gi 2250709889 1346 LRRKQQQA 1353
Cdd:PTZ00121  1694 LKKEAEEA 1701
PTZ00121 PTZ00121
MAEBL; Provisional
 1275-1353 3.34e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.52  E-value: 3.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250709889 1275 KDEQKAEDELAKKRAAFLLKQQ---RKAEEAR-ARKQQLEAEVELKRDEARRKAEE-----DRLRK-EEEKARRELIKQE 1344
Cdd:PTZ00121  1439 KAEEAKKADEAKKKAEEAKKAEeakKKAEEAKkADEAKKKAEEAKKADEAKKKAEEakkkaDEAKKaAEAKKKADEAKKA 1518


                   ....*....
gi 2250709889 1345 YLRRKQQQA 1353
Cdd:PTZ00121  1519 EEAKKADEA 1527
PTZ00121 PTZ00121
MAEBL; Provisional
 1275-1357 3.57e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.52  E-value: 3.57e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250709889 1275 KDEQKAEDELAKKRAAFLLKQQRKAEEARARKQQLEAEVELKRDEARRKAEEDRLRKEEEKARRELIKQEYLRRKQQQAL 1354
Cdd:PTZ00121  1344 AAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEA 1423


                   ...
gi 2250709889 1355 EEQ 1357
Cdd:PTZ00121  1424 KKK 1426
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1278-1357 3.71e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.31  E-value: 3.71e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250709889 1278 QKAEDELAKKRAAfLLKQQRKAEEARARKQQLEAEVELKRDEARRKAEE-DRLRKEEEKARRELIKQE----YLRRKQQQ 1352
Cdd:COG1196    235 RELEAELEELEAE-LEELEAELEELEAELAELEAELEELRLELEELELElEEAQAEEYELLAELARLEqdiaRLEERRRE 313


                   ....*
gi 2250709889 1353 ALEEQ 1357
Cdd:COG1196    314 LEERL 318
PTZ00121 PTZ00121
MAEBL; Provisional
 1276-1355 3.82e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.52  E-value: 3.82e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250709889 1276 DEQKAEDELAKKRAAFLLKQQRKAEEARARKQQLEAEvELKRDEARRKAEEDR---LRKEE-----EKARRELIKQEYLR 1347
Cdd:PTZ00121  1525 DEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAE-EKKKAEEAKKAEEDKnmaLRKAEeakkaEEARIEEVMKLYEE 1603


                   ....*...
gi 2250709889 1348 RKQQQALE 1355
Cdd:PTZ00121  1604 EKKMKAEE 1611
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 1294-1357 3.94e-04

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 44.52  E-value: 3.94e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2250709889 1294 KQQRKAEEARARKQQLEAEVELKRDEARRKAEEDRLRKEEEKARRELIKQ-EYLRRKQQQALEEQ 1357
Cdd:pfam13868   32 KRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQiEEREQKRQEEYEEK 96
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
1281-1359 4.01e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.29  E-value: 4.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250709889 1281 EDELAKKRAAFLLKQQRKAEEARARKQQLEAEVELKRDEARRK------AEEDRLRKEEEKARRELIKQEYLRRKQQQAL 1354
Cdd:COG4913    289 RLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQirgnggDRLEQLEREIERLERELEERERRRARLEALL 368


                   ....*
gi 2250709889 1355 EEQGL 1359
Cdd:COG4913    369 AALGL 373
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
1275-1357 4.39e-04

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 44.65  E-value: 4.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250709889 1275 KDEQKAEDELAKKRAAflLKQQRKAEEARARKQQLEAEVELKRDEARRKAEEDRLRKEEEKARRElikQEYLRRKQQQAL 1354
Cdd:COG3064     48 EAKRQAEEEAREAKAE--AEQRAAELAAEAAKKLAEAEKAAAEAEKKAAAEKAKAAKEAEAAAAA---EKAAAAAEKEKA 122


                   ...
gi 2250709889 1355 EEQ 1357
Cdd:COG3064    123 EEA 125
PTZ00121 PTZ00121
MAEBL; Provisional
 1275-1353 4.91e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.13  E-value: 4.91e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250709889 1275 KDEQKAEDELAKKRAAFLLKQ---QRKAEEAR-ARKQQLEAEVELKRDEARRKAEE----DRLRKEEEKARR---ELIKQ 1343
Cdd:PTZ00121  1426 KAEEKKKADEAKKKAEEAKKAdeaKKKAEEAKkAEEAKKKAEEAKKADEAKKKAEEakkaDEAKKKAEEAKKkadEAKKA 1505

                           90
                   ....*....|
gi 2250709889 1344 EYLRRKQQQA 1353
Cdd:PTZ00121  1506 AEAKKKADEA 1515
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
1278-1357 5.17e-04

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 44.65  E-value: 5.17e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250709889 1278 QKAEDELAKKRAAFLLKQQRKAEEARARKQQLEAEVELKRDEARRKAEEDRlRKEEEKARRELIKQEYLRRKQQQALEEQ 1357
Cdd:COG3064     83 EKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEA-KRKAEEERKAAEAEAAAKAEAEAARAAA 161
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 1275-1357 6.42e-04

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 43.75  E-value: 6.42e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250709889 1275 KDEQKAEDELAKKRAAFLLKQQRKAEEARARKQQLEAEVELKRDEA----RRKAEEDRLRKEEEKARRElIKQEYlRRKQ 1350
Cdd:pfam13868  218 KERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFermlRKQAEDEEIEQEEAEKRRM-KRLEH-RREL 295


                   ....*..
gi 2250709889 1351 QQALEEQ 1357
Cdd:pfam13868  296 EKQIEER 302
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 1275-1340 7.61e-04

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 41.06  E-value: 7.61e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2250709889 1275 KDEQKAEDELAKKRAAFLLKQQRKAEEAR---ARKQQLEAE-------VELKRDEARRKAEE-DRLRKEEEKARREL 1340
Cdd:pfam20492   44 RQAEEEAERLEQKRQEAEEEKERLEESAEmeaEEKEQLEAElaeaqeeIARLEEEVERKEEEaRRLQEELEEAREEE 120
PTZ00121 PTZ00121
MAEBL; Provisional
 1275-1357 7.61e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.36  E-value: 7.61e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250709889 1275 KDEQKAEDELAKKRAAFLLKQQRKAEEAR-ARKQQLEAEVELKRDEARRKAEEDRlRKEEEKARRELIKQEYLRRKQQQA 1353
Cdd:PTZ00121  1559 KAEEKKKAEEAKKAEEDKNMALRKAEEAKkAEEARIEEVMKLYEEEKKMKAEEAK-KAEEAKIKAEELKKAEEEKKKVEQ 1637


                   ....
gi 2250709889 1354 LEEQ 1357
Cdd:PTZ00121  1638 LKKK 1641
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 1273-1356 8.21e-04

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 41.42  E-value: 8.21e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250709889  1273 FFKDEQKAEDELAKKRAAFLlkqQRKAEEARARKQQLEAEVELKRDEARRKAEEDRLRKEEEKARRELIKQEYLRRKQQQ 1352
Cdd:smart00935   15 AGKAAQKQLEKEFKKRQAEL---EKLEKELQKLKEKLQKDAATLSEAAREKKEKELQKKVQEFQRKQQKLQQDLQKRQQE 91


                    ....
gi 2250709889  1353 ALEE 1356
Cdd:smart00935   92 ELQK 95
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 1277-1358 8.93e-04

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 43.30  E-value: 8.93e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250709889 1277 EQKAEDELAKKRAAFLLKQ-----QRKAEEARAR-----KQQLEAEVELKRDEARRKAEEDRLRKEEE---KARRELIKQ 1343
Cdd:TIGR02794  141 ERKAKEEAAKQAEEEAKAKaaaeaKKKAEEAKKKaeaeaKAKAEAEAKAKAEEAKAKAEAAKAKAAAEaaaKAEAEAAAA 220

                           90
                   ....*....|....*
gi 2250709889 1344 EYLRRKQQQALEEQG 1358
Cdd:TIGR02794  221 AAAEAERKADEAELG 235
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 1276-1357 8.95e-04

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 43.37  E-value: 8.95e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250709889 1276 DEQKAEDELAKKRAA--FLLKQQRKAEEARARKQQLEAEVELKRDE-ARRKAEEDRLRKEEE---KARRELIKQEyLRRK 1349
Cdd:pfam13868  114 DQAEAEEKLEKQRQLreEIDEFNEEQAEWKELEKEEEREEDERILEyLKEKAEREEEREAEReeiEEEKEREIAR-LRAQ 192


                   ....*...
gi 2250709889 1350 QQQALEEQ 1357
Cdd:pfam13868  193 QEKAQDEK 200
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 1286-1356 8.95e-04

FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase


Pssm-ID: 440475 [Multi-domain]  Cd Length: 152  Bit Score: 41.31  E-value: 8.95e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2250709889 1286 KKRAAFLLKQQRKAEEARARKQQLEAEVELKRDEARRKAEE--DRLRKEEEKARRELIKQ--EYLRRKQQQALEE 1356
Cdd:COG0711     30 DERQEKIADGLAEAERAKEEAEAALAEYEEKLAEARAEAAEiiAEARKEAEAIAEEAKAEaeAEAERIIAQAEAE 104
PTZ00121 PTZ00121
MAEBL; Provisional
 1275-1357 9.24e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.36  E-value: 9.24e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250709889 1275 KDEQKAEDELAKKRAafllKQQRKAEEARARKQqleaEVELKRDEARRKAEEDR-----LRKEEEKARRELIKQEYLRRK 1349
Cdd:PTZ00121  1297 KAEEKKKADEAKKKA----EEAKKADEAKKKAE----EAKKKADAAKKKAEEAKkaaeaAKAEAEAAADEAEAAEEKAEA 1368


                   ....*...
gi 2250709889 1350 QQQALEEQ 1357
Cdd:PTZ00121  1369 AEKKKEEA 1376
PTZ00121 PTZ00121
MAEBL; Provisional
 1276-1359 9.40e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.36  E-value: 9.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250709889 1276 DEQKAEDELAKKRAafllKQQRKAEEARARKQQLEAEVE-LKR--DEARRKAEEDRLRKEEEKARRELIKQEYLR----R 1348
Cdd:PTZ00121  1699 EEAKKAEELKKKEA----EEKKKAEELKKAEEENKIKAEeAKKeaEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKaeeiR 1774

                           90
                   ....*....|.
gi 2250709889 1349 KQQQALEEQGL 1359
Cdd:PTZ00121  1775 KEKEAVIEEEL 1785
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1275-1357 1.04e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.77  E-value: 1.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250709889 1275 KDEQKAEDELAKKRAAfLLKQQRKAEEARARKQQLEAEVE-----LKRDEARRKAEEDRLrKEEEKARRELIKQEYLRRK 1349
Cdd:COG1196    260 AELAELEAELEELRLE-LEELELELEEAQAEEYELLAELArleqdIARLEERRRELEERL-EELEEELAELEEELEELEE 337


                   ....*...
gi 2250709889 1350 QQQALEEQ 1357
Cdd:COG1196    338 ELEELEEE 345
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1277-1359 1.04e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.77  E-value: 1.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250709889 1277 EQKAEDELAKKRAAFLLKQQRKAEEARARKQQLEAEVELKRDEARR-----KAEEDRLRKEEEKARRELIKQEYLRRKQQ 1351
Cdd:COG1196    217 ELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELaeleaELEELRLELEELELELEEAQAEEYELLAE 296


                   ....*...
gi 2250709889 1352 QALEEQGL 1359
Cdd:COG1196    297 LARLEQDI 304
PTZ00121 PTZ00121
MAEBL; Provisional
 1278-1347 1.16e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.98  E-value: 1.16e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250709889 1278 QKAEDeLAKKRAAFLLKQQRKAEEARARKQQLEAEVELKRDEARRKAEEDRlRKEEEKARRELIKQEYLR 1347
Cdd:PTZ00121  1194 RKAED-ARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAK-KAEEERNNEEIRKFEEAR 1261
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 1276-1356 1.17e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 43.66  E-value: 1.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250709889 1276 DEQKAEDELAKkraafLLKQQRKAEEARARKQQLEAEVELKRDEARRKAEEdrLRKEEEKARRELiKQEYlrrkqQQALE 1355
Cdd:PRK00409   514 DKEKLNELIAS-----LEELERELEQKAEEAEALLKEAEKLKEELEEKKEK--LQEEEDKLLEEA-EKEA-----QQAIK 580


                   .
gi 2250709889 1356 E 1356
Cdd:PRK00409   581 E 581
eIF3_subunit pfam08597
Translation initiation factor eIF3 subunit; This is a family of proteins which are subunits of ...
 1275-1336 1.21e-03

Translation initiation factor eIF3 subunit; This is a family of proteins which are subunits of the eukaryotic translation initiation factor 3 (eIF3). In yeast it is called Hcr1. The Saccharomyces cerevisiae protein Swiss:Q05775 has been shown to be required for processing of 20S pre-rRNA and binds to 18S rRNA and eIF3 subunits Rpg1p and Prt1p.


Pssm-ID: 462530  Cd Length: 239  Bit Score: 42.28  E-value: 1.21e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2250709889 1275 KDEQKAEDELAKKRAA-FLLKQQRKAEEARARKQQLEAEVELKRDEARRKAEEDRLRKEEEKA 1336
Cdd:pfam08597   45 EEKEKAAKAAAAKAKKkKKSKKQKIAEKEAERKAEEEAEEEEELTPEDEAARKLRLRKAEEES 107
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1275-1359 1.24e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.77  E-value: 1.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250709889 1275 KDEQKAEDELAKKRAAfLLKQQRKAEEARARKQQLEAEVELKRdEARRKAEEDRLRKEEEKARRELIKQEYLRRKQQQAL 1354
Cdd:COG1196    246 AELEELEAELEELEAE-LAELEAELEELRLELEELELELEEAQ-AEEYELLAELARLEQDIARLEERRRELEERLEELEE 323


                   ....*
gi 2250709889 1355 EEQGL 1359
Cdd:COG1196    324 ELAEL 328
PTZ00121 PTZ00121
MAEBL; Provisional
 1275-1357 1.27e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.59  E-value: 1.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250709889 1275 KDEQKAEDELAKKRAAFLLKQQ------RKAEEAR-ARKQQLEAEVELKRDEARRKAEEDRLRKEEEKARRELIKQ---E 1344
Cdd:PTZ00121  1634 KVEQLKKKEAEEKKKAEELKKAeeenkiKAAEEAKkAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKkeaE 1713

                           90
                   ....*....|...
gi 2250709889 1345 YLRRKQQQALEEQ 1357
Cdd:PTZ00121  1714 EKKKAEELKKAEE 1726
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 1275-1357 1.40e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 42.60  E-value: 1.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250709889 1275 KDEQKAEDELAKKRAAFLLKQQRKAEEARARKQQLEAEVE---LKRDEARRKAEEDRLRKEEEKARRELIKQEYL----- 1346
Cdd:pfam13868   58 EEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLqerEQMDEIVERIQEEDQAEAEEKLEKQRQLREEIdefne 137

                           90
                   ....*....|....
gi 2250709889 1347 ---RRKQQQALEEQ 1357
Cdd:pfam13868  138 eqaEWKELEKEEER 151
ATP-synt_B pfam00430
ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is ...
 1286-1356 1.52e-03

ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is thought to translocate protons through membrane (inner membrane in mitochondria, thylakoid membrane in plants, cytoplasmic membrane in bacteria). The B subunits are thought to interact with the stalk of the CF(1) subunits. This domain should not be confused with the ab CF(1) proteins (in the head of the ATP synthase) which are found in pfam00006


Pssm-ID: 425677 [Multi-domain]  Cd Length: 132  Bit Score: 40.37  E-value: 1.52e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2250709889 1286 KKRAAFLLKQQRKAEEARARKQQLEAEVELKRDEARRKAEE--DRLRKEEEKARRELIKQ--EYLRRKQQQALEE 1356
Cdd:pfam00430   29 DKRRELIADEIAEAEERRKDAAAALAEAEQQLKEARAEAQEiiENAKKRAEKLKEEIVAAaeAEAERIIEQAAAE 103
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1275-1357 1.52e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.39  E-value: 1.52e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250709889 1275 KDEQKAEDELAKKRAAfLLKQQRKAEEARARKQQLEAEVELKRDEARRKAEEdrlRKEEEKARRELIKQEYLRRKQQQAL 1354
Cdd:COG1196    316 ERLEELEEELAELEEE-LEELEEELEELEEELEEAEEELEEAEAELAEAEEA---LLEAEAELAEAEEELEELAEELLEA 391


                   ...
gi 2250709889 1355 EEQ 1357
Cdd:COG1196    392 LRA 394
PRK11637 PRK11637
AmiB activator; Provisional
 1277-1353 1.56e-03

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 42.76  E-value: 1.56e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250709889 1277 EQKAEDELAKKRAAFLL----KQQRKAEEAR-ARKQQLEA-EVELKRDEAR---RKAEEDRLR------KEEEKAR--RE 1339
Cdd:PRK11637   184 AQKAELEEKQSQQKTLLyeqqAQQQKLEQARnERKKTLTGlESSLQKDQQQlseLRANESRLRdsiaraEREAKARaeRE 263

                           90
                   ....*....|....
gi 2250709889 1340 LIKQEYLRRKQQQA 1353
Cdd:PRK11637   264 AREAARVRDKQKQA 277
PTZ00121 PTZ00121
MAEBL; Provisional
 1276-1348 1.58e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.59  E-value: 1.58e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2250709889 1276 DEQKAEDELAKKRAAFLLKQQRKAEEARARKQQLEAEVELKRDEARRKAEEDRlRKEEEKARRELIKQEYLRR 1348
Cdd:PTZ00121  1094 EEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEAR-KAEDAKRVEIARKAEDARK 1165
PTZ00121 PTZ00121
MAEBL; Provisional
 1278-1358 1.78e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 1.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250709889 1278 QKAEDElaKKRAAFLLKqqRKAEEARARKQ--QLEAEvELKRDEARRKAEEDRLRKEEEKARRElikqEYLRRKQQQALE 1355
Cdd:PTZ00121  1681 KKAEED--EKKAAEALK--KEAEEAKKAEElkKKEAE-EKKKAEELKKAEEENKIKAEEAKKEA----EEDKKKAEEAKK 1751


                   ...
gi 2250709889 1356 EQG 1358
Cdd:PTZ00121  1752 DEE 1754
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 1277-1353 1.80e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 42.49  E-value: 1.80e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250709889 1277 EQKAEDELAKKRAAfllKQQRKAEEARARKQ---QLEAEVELKR-DEARRKAEEDRLRKEEEKARReliKQEYLRRKQQQ 1352
Cdd:PRK09510   115 EQKKQAEEAAKQAA---LKQKQAEEAAAKAAaaaKAKAEAEAKRaAAAAKKAAAEAKKKAEAEAAK---KAAAEAKKKAE 188


                   .
gi 2250709889 1353 A 1353
Cdd:PRK09510   189 A 189
PTZ00121 PTZ00121
MAEBL; Provisional
 1275-1353 1.80e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 1.80e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250709889 1275 KDEQKAEDELA----KKRAAFLLKQQ--RKAEEARARKQQLEAEVELKR--DEARRKAEEDRLRKEEEKARRELIKQEYL 1346
Cdd:PTZ00121  1350 AEAEAAADEAEaaeeKAEAAEKKKEEakKKADAAKKKAEEKKKADEAKKkaEEDKKKADELKKAAAAKKKADEAKKKAEE 1429


                   ....*..
gi 2250709889 1347 RRKQQQA 1353
Cdd:PTZ00121  1430 KKKADEA 1436
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 1275-1357 1.88e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 42.21  E-value: 1.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250709889 1275 KDEQKAEDELAKKRAAFLLKQQRKAEEARAR-----KQQLEAEVELKRdeaRRKAEEDRLRKEEEKARRELIKQEYL--R 1347
Cdd:pfam13868   39 KEEERRLDEMMEEERERALEEEEEKEEERKEerkryRQELEEQIEERE---QKRQEEYEEKLQEREQMDEIVERIQEedQ 115

                           90
                   ....*....|
gi 2250709889 1348 RKQQQALEEQ 1357
Cdd:pfam13868  116 AEAEEKLEKQ 125
CCDC47 pfam07946
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of ...
 1272-1338 2.17e-03

PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of the PAT complex, an endoplasmic reticulum (ER)-resident membrane multiprotein complex that facilitates multi-pass membrane proteins insertion into membranes. The PAT complex, formed by CCDC47 and Asterix proteins, acts as an intramembrane chaperone by directly interacting with nascent transmembrane domains (TMDs), releasing its substrates upon correct folding, and is needed for optimal biogenesis of multi-pass membrane proteins. CCDC47 is required to maintain the stability of Asterix. CCDC47 is associated with various membrane-associated processes and is component of a ribosome-associated ER translocon complex involved in multi-pass membrane protein transport into the ER membrane and biogenesis. It is also involved in the regulation of calcium ion homeostasis in the ER, being also required for proper protein degradation via the ERAD (ER-associated degradation) pathway.


Pssm-ID: 462322  Cd Length: 323  Bit Score: 42.17  E-value: 2.17e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2250709889 1272 FFFKDEQKA------EDELAKKRAAfllKQQRKAEEARARKQQLEAEvelKRDEARRKAEEDRLRKEEEKARR 1338
Cdd:pfam07946  252 AKLRPEALKkakktrEEEIEKIKKA---AEEERAEEAQEKKEEAKKK---EREEKLAKLSPEEQRKYEEKERK 318
ATAD3_N pfam12037
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal ...
 1278-1349 2.24e-03

ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal domain of ATPase family AAA domain-containing protein 3 (ATAD3) which is involved in dimerization and interacts with the inner surface of the outer mitochondrial membrane. This domain is found associated with the AAA ATPase domain (pfam00004). ATAD3 is essential for mitochondrial network organization, mitochondrial metabolism and cell growth at organizm and cellular level. It may also play an important role in mitochondrial protein synthesis.


Pssm-ID: 463442 [Multi-domain]  Cd Length: 264  Bit Score: 41.89  E-value: 2.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250709889 1278 QKA--EDELAKKRAAFLLKQQR---------------KAEEAR---ARKQQLEAEVELKRDEARRKAE-EDRLRKEEEKA 1336
Cdd:pfam12037  101 QRAqyQDELARKRYQDQLEAQRrrneellrkqeesvaKQEAMRiqaQRRQTEEHEAELRRETERAKAEaEAEARAKEERE 180

                           90
                   ....*....|...
gi 2250709889 1337 RRELIKqEYLRRK 1349
Cdd:pfam12037  181 NEDLNL-EQLREK 192
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1276-1359 2.36e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 42.74  E-value: 2.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250709889 1276 DEQKAEDELAKKRAAfLLKQQRKAEEARA----RKQQLEA---EVELKRDEARRKAEEDRLRKEEEKARRELIKQEyLRR 1348
Cdd:TIGR02168  863 ELEELIEELESELEA-LLNERASLEEALAllrsELEELSEelrELESKRSELRRELEELREKLAQLELRLEGLEVR-IDN 940

                           90
                   ....*....|.
gi 2250709889 1349 KQQQALEEQGL 1359
Cdd:TIGR02168  941 LQERLSEEYSL 951
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 1275-1357 2.37e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 42.21  E-value: 2.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250709889 1275 KDEQKAEDELAKKR-AAFLLKQQRKAEEARARKQQL-----EAEVELKRDEARRKAEEDRLRKEEE--KARRELIKQEYL 1346
Cdd:pfam13868  171 REAEREEIEEEKEReIARLRAQQEKAQDEKAERDELraklyQEEQERKERQKEREEAEKKARQRQElqQAREEQIELKER 250

                           90
                   ....*....|.
gi 2250709889 1347 RRKQQQALEEQ 1357
Cdd:pfam13868  251 RLAEEAEREEE 261
DUF4200 pfam13863
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ...
 1275-1357 2.52e-03

Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil domain of unknwon function.


Pssm-ID: 464003 [Multi-domain]  Cd Length: 119  Bit Score: 39.47  E-value: 2.52e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250709889 1275 KDEQKAEDELAKKRAAFLLKQQRKAEEARARKQQLEAEVELKRDEARRKAEEDRLRKEE-EKARRELIKQEYLRRKQQQA 1353
Cdd:pfam13863   19 REEIERLEELLKQREEELEKKEQELKEDLIKFDKFLKENDAKRRRALKKAEEETKLKKEkEKEIKKLTAQIEELKSEISK 98


                   ....
gi 2250709889 1354 LEEQ 1357
Cdd:pfam13863   99 LEEK 102
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 1277-1357 2.72e-03

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 40.02  E-value: 2.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250709889 1277 EQKAEDELAKK--RAAFLLKQQRKAEEARARKQQLEAEVELKRdEARRKAEEDRLRKEEEKARRELIKQEYLRRKQQQAL 1354
Cdd:pfam05672   49 RRRAEEERARReeEARRLEEERRREEEERQRKAEEEAEEREQR-EQEEQERLQKQKEEAEAKAREEAERQRQEREKIMQQ 127


                   ...
gi 2250709889 1355 EEQ 1357
Cdd:pfam05672  128 EEQ 130
PTZ00121 PTZ00121
MAEBL; Provisional
 1275-1353 2.93e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 2.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250709889 1275 KDEQKAEdELAKKRAAFLLKQQRKAEEARARKQQLEAEvELKRDEARRKAEEDR----LRKEEEKARRELIKQ-EYLRRK 1349
Cdd:PTZ00121  1161 EDARKAE-EARKAEDAKKAEAARKAEEVRKAEELRKAE-DARKAEAARKAEEERkaeeARKAEDAKKAEAVKKaEEAKKD 1238


                   ....
gi 2250709889 1350 QQQA 1353
Cdd:PTZ00121  1239 AEEA 1242
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 1278-1343 2.93e-03

FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase


Pssm-ID: 440475 [Multi-domain]  Cd Length: 152  Bit Score: 39.77  E-value: 2.93e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2250709889 1278 QKAEDELAKKRAAFLLKQQRKAEEARARKQQL--EAEVELKRDEARRKAE-EDRLRKEEEKARRELIKQ 1343
Cdd:COG0711     51 EAALAEYEEKLAEARAEAAEIIAEARKEAEAIaeEAKAEAEAEAERIIAQaEAEIEQERAKALAELRAE 119
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
1277-1357 2.96e-03

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 41.95  E-value: 2.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250709889 1277 EQKAEDELAKKRAAFLLKQQRKAEEARARKQQLEAEVELKRDEARRKAEEDRLRKEEEKARRELIKQEYLRRKQQQALEE 1356
Cdd:COG3064     32 EQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAE 111


                   .
gi 2250709889 1357 Q 1357
Cdd:COG3064    112 K 112
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 1294-1356 3.33e-03

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 42.03  E-value: 3.33e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2250709889 1294 KQQRKAEEARARKQQLEAEV----ELKRDEARRKAEEDRLRKEEEKARRELIKQEYLRRKQQQALEE 1356
Cdd:pfam17380  355 QEERKRELERIRQEEIAMEIsrmrELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVE 421
PRK07353 PRK07353
F0F1 ATP synthase subunit B'; Validated
 1273-1357 3.50e-03

F0F1 ATP synthase subunit B'; Validated


Pssm-ID: 235999 [Multi-domain]  Cd Length: 140  Bit Score: 39.60  E-value: 3.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250709889 1273 FFKDEQKAEDElakkRAAFLLKQQRKAEEARARKQQLEAEVELKRDEARRKA---------EEDRLRKEE---------- 1333
Cdd:PRK07353    26 FYKPVGKVVEE----REDYIRTNRAEAKERLAEAEKLEAQYEQQLASARKQAqaviaeaeaEADKLAAEAlaeaqaeaqa 101

                           90       100
                   ....*....|....*....|....*.
gi 2250709889 1334 --EKARRELIKQeylRRKQQQALEEQ 1357
Cdd:PRK07353   102 skEKARREIEQQ---KQAALAQLEQQ 124
PTZ00121 PTZ00121
MAEBL; Provisional
 1275-1351 3.93e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.05  E-value: 3.93e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2250709889 1275 KDEQKAEDELAKKRAAFLLKQQRKAEEARARKQQLEAEvELKRDEARRKAEEDRlRKEEEKARRELIKQEYLRRKQQ 1351
Cdd:PTZ00121  1112 EEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAE-DAKRVEIARKAEDAR-KAEEARKAEDAKKAEAARKAEE 1186
PTZ00121 PTZ00121
MAEBL; Provisional
 1276-1351 4.03e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.05  E-value: 4.03e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2250709889 1276 DEQKAEDELAKKraafllKQQRKAEEARARKQQLEAEVELKRDEARRKAEEDRLRKEEEKARRELIKQEYLRRKQQ 1351
Cdd:PTZ00121  1275 EEARKADELKKA------EEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKA 1344
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 1275-1357 4.18e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 41.44  E-value: 4.18e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250709889 1275 KDEQKAEDEL----------AKKRAAFLLKQQRKAEEARARKQQLEAEVELKRDEARRKAEEDR------LRKEEEKARR 1338
Cdd:pfam13868  197 QDEKAERDELraklyqeeqeRKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEeefermLRKQAEDEEI 276

                           90       100
                   ....*....|....*....|..
gi 2250709889 1339 ELIKQEYLRRKQQQ---ALEEQ 1357
Cdd:pfam13868  277 EQEEAEKRRMKRLEhrrELEKQ 298
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 1281-1355 4.49e-03

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 41.65  E-value: 4.49e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2250709889 1281 EDELAKKRAAFLLKQQRKAEEARARKQQlEAEVELKRDEARRKAEEDRLRKEEEKARRELIKQEYLRRKQQQALE 1355
Cdd:pfam17380  519 EKEMEERQKAIYEEERRREAEEERRKQQ-EMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARAEYE 592
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 1275-1357 5.05e-03

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 41.65  E-value: 5.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250709889 1275 KDEQ-KAEDELAKKRAAFLLKQQRKAEEARARKQQLEAEVELKRDEARRKAEEDRLRKEEEKARRELIKQEYLRRKQQQA 1353
Cdd:pfam17380  390 KNERvRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQE 469


                   ....
gi 2250709889 1354 LEEQ 1357
Cdd:pfam17380  470 EERK 473
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
1296-1358 5.46e-03

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 41.38  E-value: 5.46e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2250709889 1296 QRKAEEARARKQQLEAEVELKRDEARRKAEED-----------RLRKEEEKARREL--IKQEYLRRKQQQALEEQG 1358
Cdd:COG2433    433 EAELEEKDERIERLERELSEARSEERREIRKDreisrldreieRLERELEEERERIeeLKRKLERLKELWKLEHSG 508
PTZ00121 PTZ00121
MAEBL; Provisional
 1275-1357 6.09e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.67  E-value: 6.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250709889 1275 KDEQKAEDELAKKRaafllKQQRKAEEARARKQQLEAEVE-LKRDEARR--KAEEDRLRKEEEKAR-RELIKQEYLRRKQ 1350
Cdd:PTZ00121  1685 EDEKKAAEALKKEA-----EEAKKAEELKKKEAEEKKKAEeLKKAEEENkiKAEEAKKEAEEDKKKaEEAKKDEEEKKKI 1759


                   ....*..
gi 2250709889 1351 QQALEEQ 1357
Cdd:PTZ00121  1760 AHLKKEE 1766
PKK pfam12474
Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino ...
 1275-1357 6.26e-03

Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino acids in length. The family is found in association with pfam00069. Polo-like kinase 1 (Plx1) is essential during mitosis for the activation of Cdc25C, for spindle assembly, and for cyclin B degradation. This family is Polo kinase kinase (PKK) which phosphorylates Polo kinase and Polo-like kinase to activate them. PKK is a serine/threonine kinase.


Pssm-ID: 463600 [Multi-domain]  Cd Length: 139  Bit Score: 38.70  E-value: 6.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250709889 1275 KDEQKAEDELAKKRAAFLLKQQRKAEEARARKQqleaeveLKRDEARRKAEEDRL----RKEEEKARRELIKQEyLRRKQ 1350
Cdd:pfam12474   38 IEKLEQRQTQELRRLPKRIRAEQKKRLKMFRES-------LKQEKKELKQEVEKLpkfqRKEAKRQRKEELELE-QKHEE 109


                   ....*..
gi 2250709889 1351 QQALEEQ 1357
Cdd:pfam12474  110 LEFLQAQ 116
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 1292-1356 7.15e-03

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 40.25  E-value: 7.15e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2250709889 1292 LLKQQRKAEEARARKQQLEAEVELKRDEARRKAE--EDRLRKEEEKARRELIKQEYLRRKQQQALEE 1356
Cdd:cd16269    193 LTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQklEDQERSYEEHLRQLKEKMEEERENLLKEQER 259
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1278-1357 7.59e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.08  E-value: 7.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250709889 1278 QKAEDELAKKRAAFLLKQQRkAEEARARKQQLEAEVEL---KRDEARRKAEEDRLRKEEEKARRELIKQEYLRRKQQQAL 1354
Cdd:COG1196    270 EELRLELEELELELEEAQAE-EYELLAELARLEQDIARleeRRRELEERLEELEEELAELEEELEELEEELEELEEELEE 348


                   ...
gi 2250709889 1355 EEQ 1357
Cdd:COG1196    349 AEE 351
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 1277-1343 7.60e-03

F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 38.19  E-value: 7.60e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2250709889 1277 EQKAEDEL--AKKRAAFLLKQQRKaeEARARKQQLEAEVELKRDEARRKAEEDrLRKEEEKARRELIKQ 1343
Cdd:cd06503     53 LAEYEEKLaeARAEAQEIIEEARK--EAEKIKEEILAEAKEEAERILEQAKAE-IEQEKEKALAELRKE 118
NtpE COG1390
Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 [Energy production and conversion]; Archaeal ...
 1300-1357 8.01e-03

Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 [Energy production and conversion]; Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 is part of the Pathway/BioSystem: A/V-type ATP synthase


Pssm-ID: 441000 [Multi-domain]  Cd Length: 196  Bit Score: 39.54  E-value: 8.01e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2250709889 1300 EEARARKQQLEAEVELKRDEARRKAEED---RLRKEEEKARRElIKQEYLRRKQQQALEEQ 1357
Cdd:COG1390     13 EEAEAEAEEILEEAEEEAEKILEEAEEEaeeIKEEILEKAERE-AEREKRRIISSAELEAR 72
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 1220-1357 8.81e-03

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 40.71  E-value: 8.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250709889 1220 EHTPVEEPL---RSKASLIEVDLSDLKAPDEDGEVVGHESSVELGGDSDQKPGVGFFFKDEQKAEDELAKKRAafllkQQ 1296
Cdd:pfam15709  271 SDSVVEDPWlssKYDAEESQVSIDGRSSPTQTFVVTGNMESEEERSEEDPSKALLEKREQEKASRDRLRAERA-----EM 345

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250709889 1297 RKAEEARARKQQ----------------LEAEVELkrdEARRKAEEDRLRK---EEEKARREliKQEYLRRKQQQALEEQ 1357
Cdd:pfam15709  346 RRLEVERKRREQeeqrrlqqeqleraekMREELEL---EQQRRFEEIRLRKqrlEEERQRQE--EEERKQRLQLQAAQER 420
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
1278-1357 9.99e-03

Phage shock protein A [Transcription, Signal transduction mechanisms];


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 39.42  E-value: 9.99e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250709889 1278 QKAEDELAKkraAFLLKQQRKAEEARARKQQLEAeveLKRDEARRKAEEDRLRK--EEEKARRELIKQEYLRRKQQQALE 1355
Cdd:COG1842     79 EKGREDLAR---EALERKAELEAQAEALEAQLAQ---LEEQVEKLKEALRQLESklEELKAKKDTLKARAKAAKAQEKVN 152


                   ..
gi 2250709889 1356 EQ 1357
Cdd:COG1842    153 EA 154
 
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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