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Conserved domains on  [gi|767984364|ref|XP_011519958|]
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S phase cyclin A-associated protein in the endoplasmic reticulum isoform X20 [Homo sapiens]

Protein Classification

C2H2-type zinc finger protein( domain architecture ID 10648429)

Cys2His2 (C2H2)-type zinc finger protein may be involved in transcriptional regulation

CATH:  3.30.160.60
Gene Ontology:  GO:0003676|GO:0008270|GO:0003700
PubMed:  11179890|11361095|10940247|22803940|12665246
SCOP:  4003583

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 19-156 9.41e-06

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.16  E-value: 9.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984364  19 EAQNKRHDVLSKLKEYEQRLNELQEERQrRQEEKQARDEAVQERKRALEAERQARVEELLMKRKEQEARIEQQRQEKEKA 98
Cdd:COG1196  285 EAQAEEYELLAELARLEQDIARLEERRR-ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 767984364  99 REDAARERARDREERLAALTAAQQEAMEELQKKIQLKHDESIRRHMEQIEQRKEKAAE 156
Cdd:COG1196  364 EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421
ZnF_U1 smart00451
U1-like zinc finger; Family of C2H2-type zinc fingers, present in matrin, U1 small nuclear ...
 176-208 5.40e-05

U1-like zinc finger; Family of C2H2-type zinc fingers, present in matrin, U1 small nuclear ribonucleoprotein C and other RNA-binding proteins.


:

Pssm-ID: 197732 [Multi-domain]  Cd Length: 35  Bit Score: 40.70  E-value: 5.40e-05
                           10        20        30
                   ....*....|....*....|....*....|...
gi 767984364   176 RKKQCSLCNVLISSEVYLFSHVKGRKHQQAVRE 208
Cdd:smart00451   2 GGFYCKLCNVTFTDEISVEAHLKGKKHKKNVKK 34
 
Name Accession Description Interval E-value
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 19-156 9.41e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.16  E-value: 9.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984364  19 EAQNKRHDVLSKLKEYEQRLNELQEERQrRQEEKQARDEAVQERKRALEAERQARVEELLMKRKEQEARIEQQRQEKEKA 98
Cdd:COG1196  285 EAQAEEYELLAELARLEQDIARLEERRR-ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 767984364  99 REDAARERARDREERLAALTAAQQEAMEELQKKIQLKHDESIRRHMEQIEQRKEKAAE 156
Cdd:COG1196  364 EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 52-179 2.24e-05

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: 47.64  E-value: 2.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984364   52 KQARDEAVQER--KRALEAERqarveellmKRKEQEariEQQRQEKEKAREDAARErardreerlAALTAAQQEAMEELQ 129
Cdd:pfam15709 332 KASRDRLRAERaeMRRLEVER---------KRREQE---EQRRLQQEQLERAEKMR---------EELELEQQRRFEEIR 390

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 767984364  130 KKIQLKHDESIRRHMEQIEQRKEKAAELSSGRHANTDYAPKLTPYERKKQ 179
Cdd:pfam15709 391 LRKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQ 440
ZnF_U1 smart00451
U1-like zinc finger; Family of C2H2-type zinc fingers, present in matrin, U1 small nuclear ...
 176-208 5.40e-05

U1-like zinc finger; Family of C2H2-type zinc fingers, present in matrin, U1 small nuclear ribonucleoprotein C and other RNA-binding proteins.


Pssm-ID: 197732 [Multi-domain]  Cd Length: 35  Bit Score: 40.70  E-value: 5.40e-05
                           10        20        30
                   ....*....|....*....|....*....|...
gi 767984364   176 RKKQCSLCNVLISSEVYLFSHVKGRKHQQAVRE 208
Cdd:smart00451   2 GGFYCKLCNVTFTDEISVEAHLKGKKHKKNVKK 34
PTZ00121 PTZ00121
MAEBL; Provisional
 19-156 7.76e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.67  E-value: 7.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984364   19 EAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARD--EAVQERKRALE---AERQARVEELLMKRKEQEARIEQQRQ 93
Cdd:PTZ00121 1629 EEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEakKAEEDKKKAEEakkAEEDEKKAAEALKKEAEEAKKAEELK 1708

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767984364   94 EKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQLKHDESIRRHMEQIEQRKEKAAE 156
Cdd:PTZ00121 1709 KKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAE 1771
zf-met pfam12874
Zinc-finger of C2H2 type; This is a zinc-finger domain with the CxxCx(12)Hx(6)H motif, found ...
 180-202 4.79e-04

Zinc-finger of C2H2 type; This is a zinc-finger domain with the CxxCx(12)Hx(6)H motif, found in multiple copies in a wide range of proteins from plants to metazoans. Some member proteins, particularly those from plants, are annotated as being RNA-binding.


Pssm-ID: 463736 [Multi-domain]  Cd Length: 25  Bit Score: 37.86  E-value: 4.79e-04
                          10        20
                  ....*....|....*....|...
gi 767984364  180 CSLCNVLISSEVYLFSHVKGRKH 202
Cdd:pfam12874   3 CELCNVTFNSESQLKSHLQGKKH 25
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 56-160 3.60e-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: 3.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984364  56 DEAVQERKRALEAER-QARVEELLMKR-KEQEARIEQQRQEKEKAredaarerardreerlaaltaaQQEAMEELQKKIQ 133
Cdd:cd16269  190 DQALTEKEKEIEAERaKAEAAEQERKLlEEQQRELEQKLEDQERS----------------------YEEHLRQLKEKME 247

                         90       100
                 ....*....|....*....|....*...
gi 767984364 134 LKHDESIRRHMEQIEQR-KEKAAELSSG 160
Cdd:cd16269  248 EERENLLKEQERALESKlKEQEALLEEG 275
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 19-156 8.07e-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: 39.65  E-value: 8.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984364    19 EAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALE------AERQARVEELLMKRKEQEARIEQ-- 90
Cdd:TIGR02168  709 ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTeleaeiEELEERLEEAEEELAEAEAEIEEle 788

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767984364    91 ---QRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIqlkhdESIRRHMEQIEQRKEKAAE 156
Cdd:TIGR02168  789 aqiEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRI-----AATERRLEDLEEQIEELSE 852
 
Name Accession Description Interval E-value
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 19-156 9.41e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.16  E-value: 9.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984364  19 EAQNKRHDVLSKLKEYEQRLNELQEERQrRQEEKQARDEAVQERKRALEAERQARVEELLMKRKEQEARIEQQRQEKEKA 98
Cdd:COG1196  285 EAQAEEYELLAELARLEQDIARLEERRR-ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 767984364  99 REDAARERARDREERLAALTAAQQEAMEELQKKIQLKHDESIRRHMEQIEQRKEKAAE 156
Cdd:COG1196  364 EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 19-157 2.11e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.01  E-value: 2.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984364  19 EAQNKRHDVLSKLKEYEQRLNELqeerqrRQEEKQARDEAVQERKRALEAERQARVEELLMKRKEQEARIEQQRQEKEKA 98
Cdd:COG1196  348 EAEEELEEAEAELAEAEEALLEA------EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767984364  99 REDAARERARDREERLAALTAAQQEAMEELQkKIQLKHDESIRRHMEQIEQRKEKAAEL 157
Cdd:COG1196  422 ELEELEEALAELEEEEEEEEEALEEAAEEEA-ELEEEEEALLELLAELLEEAALLEAAL 479
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 52-179 2.24e-05

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: 47.64  E-value: 2.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984364   52 KQARDEAVQER--KRALEAERqarveellmKRKEQEariEQQRQEKEKAREDAARErardreerlAALTAAQQEAMEELQ 129
Cdd:pfam15709 332 KASRDRLRAERaeMRRLEVER---------KRREQE---EQRRLQQEQLERAEKMR---------EELELEQQRRFEEIR 390

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 767984364  130 KKIQLKHDESIRRHMEQIEQRKEKAAELSSGRHANTDYAPKLTPYERKKQ 179
Cdd:pfam15709 391 LRKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQ 440
ZnF_U1 smart00451
U1-like zinc finger; Family of C2H2-type zinc fingers, present in matrin, U1 small nuclear ...
 176-208 5.40e-05

U1-like zinc finger; Family of C2H2-type zinc fingers, present in matrin, U1 small nuclear ribonucleoprotein C and other RNA-binding proteins.


Pssm-ID: 197732 [Multi-domain]  Cd Length: 35  Bit Score: 40.70  E-value: 5.40e-05
                           10        20        30
                   ....*....|....*....|....*....|...
gi 767984364   176 RKKQCSLCNVLISSEVYLFSHVKGRKHQQAVRE 208
Cdd:smart00451   2 GGFYCKLCNVTFTDEISVEAHLKGKKHKKNVKK 34
PTZ00121 PTZ00121
MAEBL; Provisional
 19-156 7.76e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.67  E-value: 7.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984364   19 EAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARD--EAVQERKRALE---AERQARVEELLMKRKEQEARIEQQRQ 93
Cdd:PTZ00121 1629 EEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEakKAEEDKKKAEEakkAEEDEKKAAEALKKEAEEAKKAEELK 1708

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767984364   94 EKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQLKHDESIRRHMEQIEQRKEKAAE 156
Cdd:PTZ00121 1709 KKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAE 1771
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 19-156 1.04e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.08  E-value: 1.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984364  19 EAQNKRHDVLSKLKEYEQRLNELqeerqrrqEEKQARDEAVQERKRALEAERQARVEELLMKRKEQEARIEQQRQEKEKA 98
Cdd:COG1196  299 RLEQDIARLEERRRELEERLEEL--------EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA 370

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 767984364  99 REDAARERARDREERLAALTAAQQEAMEELQKKIQLKHDESIRRHMEQIEQRKEKAAE 156
Cdd:COG1196  371 EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE 428
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 19-158 1.48e-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: 1.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984364  19 EAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQARVEELlmkRKEQEARIEQQRQEKEKA 98
Cdd:COG1196  320 ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE---EELEELAEELLEALRAAA 396

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984364  99 REDAARERARDREERLAALTAAQQEAMEELQKKIQLKHDESIRRHMEQIEQRKEKAAELS 158
Cdd:COG1196  397 ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE 456
Caldesmon pfam02029
Caldesmon;
30-157 1.49e-04

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 45.24  E-value: 1.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984364   30 KLKEYEQRLNELqeerqrrqeeKQARDEAVQ---ERKRALEAERQARVEELLMKRKEQEARIEQQRQEKEKaredaarer 106
Cdd:pfam02029 242 VFLEAEQKLEEL----------RRRRQEKESeefEKLRQKQQEAELELEELKKKREERRKLLEEEEQRRKQ--------- 302

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767984364  107 ardreerlaaltaaqqeamEELQKkiQLKHDESIRRHMEQIEQRKEKAAEL 157
Cdd:pfam02029 303 -------------------EEAER--KLREEEEKRRMKEEIERRRAEAAEK 332
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 19-159 1.85e-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: 1.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984364  19 EAQNKRHDVLSKLKEYEQRLNELQEERqrrqeEKQARDEAVQERKRALEAERQARVEELLMKRKEQEARIEQQRQEKEKA 98
Cdd:COG1196  355 EAEAELAEAEEALLEAEAELAEAEEEL-----EELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA 429

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767984364  99 REDAARERARDREERLAALTAAQQEAMEELQKKIQLKHD-ESIRRHMEQIEQRKEKAAELSS 159
Cdd:COG1196  430 LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELlEEAALLEAALAELLEELAEAAA 491
CCDC47 pfam07946
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of ...
 52-135 2.05e-04

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: 44.10  E-value: 2.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984364   52 KQARDEAVQERKRALEAERQarvEELLMKRKEQEarieqqRQEKEKaredaarerardreeRLAALTAAQQEAMEELQKK 131
Cdd:pfam07946 263 KKTREEEIEKIKKAAEEERA---EEAQEKKEEAK------KKEREE---------------KLAKLSPEEQRKYEEKERK 318


                  ....
gi 767984364  132 IQLK 135
Cdd:pfam07946 319 KEQR 322
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 54-157 3.03e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.54  E-value: 3.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984364  54 ARDEAVQERKRALEAER---QARVEELLMKRKEQEARIEQQRQEKEKARedaarerardreerlAALTAAQQEAMEELQK 130
Cdd:COG1196  232 LKLRELEAELEELEAELeelEAELEELEAELAELEAELEELRLELEELE---------------LELEEAQAEEYELLAE 296

                         90       100
                 ....*....|....*....|....*..
gi 767984364 131 KIQLKHDesIRRHMEQIEQRKEKAAEL 157
Cdd:COG1196  297 LARLEQD--IARLEERRRELEERLEEL 321
zf-met pfam12874
Zinc-finger of C2H2 type; This is a zinc-finger domain with the CxxCx(12)Hx(6)H motif, found ...
 180-202 4.79e-04

Zinc-finger of C2H2 type; This is a zinc-finger domain with the CxxCx(12)Hx(6)H motif, found in multiple copies in a wide range of proteins from plants to metazoans. Some member proteins, particularly those from plants, are annotated as being RNA-binding.


Pssm-ID: 463736 [Multi-domain]  Cd Length: 25  Bit Score: 37.86  E-value: 4.79e-04
                          10        20
                  ....*....|....*....|...
gi 767984364  180 CSLCNVLISSEVYLFSHVKGRKH 202
Cdd:pfam12874   3 CELCNVTFNSESQLKSHLQGKKH 25
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 28-157 6.64e-04

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 42.22  E-value: 6.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984364  28 LSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEaERQARVEELLMKRKEQEARIEQQRQEKEKAREDAARERA 107
Cdd:COG1579    9 LLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLE-AAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRN 87

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 767984364 108 RDreerlaALTAAQQEaMEELQKKIQLKHDEsIRRHMEQIEQRKEKAAEL 157
Cdd:COG1579   88 NK------EYEALQKE-IESLKRRISDLEDE-ILELMERIEELEEELAEL 129
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 18-157 6.65e-04

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: 43.02  E-value: 6.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984364   18 LEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQARVEE-----LLMKRKEQEAR----- 87
Cdd:pfam15709 348 LEVERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQRQEEEerkqrLQLQAAQERARqqqee 427

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984364   88 -------IEQQRQEKEKAREDAARERARDREERLAA-----LTAAQQEAMEELQKKiqLKHDESIRRHMEQIEQRKEKAA 155
Cdd:pfam15709 428 frrklqeLQRKKQQEEAERAEAEKQRQKELEMQLAEeqkrlMEMAEEERLEYQRQK--QEAEEKARLEAEERRQKEEEAA 505


                  ..
gi 767984364  156 EL 157
Cdd:pfam15709 506 RL 507
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 19-163 1.15e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.62  E-value: 1.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984364  19 EAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQARVEELlmkrkEQEARIEQQRQEKEKA 98
Cdd:COG1196  334 ELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL-----RAAAELAAQLEELEEA 408

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984364  99 REDAARERARDREERLAALTAAQQEAMEEL-----QKKIQLKHDESIRRHMEQIEQRKEKAAELSSGRHA 163
Cdd:COG1196  409 EEALLERLERLEEELEELEEALAELEEEEEeeeeaLEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
16-153 1.20e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 42.33  E-value: 1.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984364  16 NTLEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQ---ERKRALEAERQ-ARVEELLMKRKEQEARIEQQ 91
Cdd:PRK02224 586 ERIESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAekrERKRELEAEFDeARIEEAREDKERAEEYLEQV 665

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767984364  92 RQEkekaredaarerardreerLAALTaaqqEAMEELQKKI-----QLKHDESIRRHMEQIEQRKEK 153
Cdd:PRK02224 666 EEK-------------------LDELR----EERDDLQAEIgavenELEELEELRERREALENRVEA 709
PTZ00121 PTZ00121
MAEBL; Provisional
 19-171 1.30e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 1.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984364   19 EAQNKRHDVLSKLKEYEQRLNelqeeRQRRQEEKQARDEAVQERKralEAERQARVEELLMKRKEQEARIEQQRQEKEKA 98
Cdd:PTZ00121 1588 KAEEARIEEVMKLYEEEKKMK-----AEEAKKAEEAKIKAEELKK---AEEEKKKVEQLKKKEAEEKKKAEELKKAEEEN 1659

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767984364   99 REDAARERARDREERLAALTAAQQEAmEELQKKIQLKHDESIRRHMEQI----EQRKEKAAELSSGRHANTDYAPKL 171
Cdd:PTZ00121 1660 KIKAAEEAKKAEEDKKKAEEAKKAEE-DEKKAAEALKKEAEEAKKAEELkkkeAEEKKKAEELKKAEEENKIKAEEA 1735
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 13-179 1.45e-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: 41.86  E-value: 1.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984364   13 AFINTLEAQNKRHDVLsKLKEYEQRLNELQEERQRRQEEKQARDEAvQER----KRALEAERQARVEELLMKRKEQEAri 88
Cdd:pfam15709 323 ALLEKREQEKASRDRL-RAERAEMRRLEVERKRREQEEQRRLQQEQ-LERaekmREELELEQQRRFEEIRLRKQRLEE-- 398

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984364   89 EQQRQEKEKAREDAARERARDREERlaaltaAQQEAMEELQKKIQLKHDESIRRHMEQIEQRKEKAAELSSGRHANTDYA 168
Cdd:pfam15709 399 ERQRQEEEERKQRLQLQAAQERARQ------QQEEFRRKLQELQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEMA 472

                         170
                  ....*....|..
gi 767984364  169 -PKLTPYERKKQ 179
Cdd:pfam15709 473 eEERLEYQRQKQ 484
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 18-96 1.53e-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: 1.53e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767984364   18 LEAQNKRHDVLsklKEYEQRLNELQEerqrrqeeKQARDEAVQERKRALEAERQARVEELLMKRKEQEARIEQQRQEKE 96
Cdd:pfam17380 509 IEEERKRKLLE---KEMEERQKAIYE--------EERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMERERE 576
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 53-156 2.33e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 40.95  E-value: 2.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984364  53 QARDEAVQERKRALEAERQARVEEllMKRKEQEARI--EQQRQEKEKAREDAARERARDREERLAALTAAQQeAMEELQK 130
Cdd:PRK09510  93 QQKQAAEQERLKQLEKERLAAQEQ--KKQAEEAAKQaaLKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKK-AAAEAKK 169

                         90       100
                 ....*....|....*....|....*.
gi 767984364 131 KiqlkhdesirrhmEQIEQRKEKAAE 156
Cdd:PRK09510 170 K-------------AEAEAAKKAAAE 182
PTZ00121 PTZ00121
MAEBL; Provisional
 18-156 2.74e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.28  E-value: 2.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984364   18 LEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQARVEELLMKRKEQEARIEQQRQEKEK 97
Cdd:PTZ00121 1607 MKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEED 1686

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767984364   98 AREDAARERARDREERLAALTAAQQEamEELQKKIQLKHDESIRRhmEQIEQRKEKAAE 156
Cdd:PTZ00121 1687 EKKAAEALKKEAEEAKKAEELKKKEA--EEKKKAEELKKAEEENK--IKAEEAKKEAEE 1741
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 23-157 2.82e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.46  E-value: 2.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984364  23 KRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQaRVEELlmKRKEQEARIEQQRQEKEKAREDA 102
Cdd:COG1196  233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELEL-ELEEA--QAEEYELLAELARLEQDIARLEE 309

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 767984364 103 ARERARDREERLAALTAAQQEAMEELQKKIQLKHDESIRRHMEQIEQRKEKAAEL 157
Cdd:COG1196  310 RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE 364
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
18-157 3.37e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.05  E-value: 3.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984364   18 LEAQNKRhDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQARVEELLMKRKEQEARIEQQRQEKEK 97
Cdd:COG4913   245 EDAREQI-ELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALRE 323

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984364   98 aredaarerardreeRLAALTAAQQEAmeELQKKIQLKHDesIRRHMEQIEQRKEKAAEL 157
Cdd:COG4913   324 ---------------ELDELEAQIRGN--GGDRLEQLERE--IERLERELEERERRRARL 364
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
31-166 3.37e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.18  E-value: 3.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984364  31 LKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERqaRVEELLMKRKEQEARIEQQRQEKEKAredaarerardr 110
Cdd:PRK02224 470 IEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAED--RIERLEERREDLEELIAERRETIEEK------------ 535

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 767984364 111 eerlaALTAAQ-QEAMEELQKKIQLKHDESIRRHmEQIEQRKEKAAELSSGRHANTD 166
Cdd:PRK02224 536 -----RERAEElRERAAELEAEAEEKREAAAEAE-EEAEEAREEVAELNSKLAELKE 586
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
31-157 3.38e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 3.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984364  31 LKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEaERQARVEELLMKRKEQEARIEQQRQEKEKAREDAARERARDR 110
Cdd:COG4717   48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAE-EKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ 126

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 767984364 111 EERLAALTAAQQEAMEELQKKIQ--LKHDESIRRHMEQIEQRKEKAAEL 157
Cdd:COG4717  127 LLPLYQELEALEAELAELPERLEelEERLEELRELEEELEELEAELAEL 175
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 56-160 3.60e-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: 3.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984364  56 DEAVQERKRALEAER-QARVEELLMKR-KEQEARIEQQRQEKEKAredaarerardreerlaaltaaQQEAMEELQKKIQ 133
Cdd:cd16269  190 DQALTEKEKEIEAERaKAEAAEQERKLlEEQQRELEQKLEDQERS----------------------YEEHLRQLKEKME 247

                         90       100
                 ....*....|....*....|....*...
gi 767984364 134 LKHDESIRRHMEQIEQR-KEKAAELSSG 160
Cdd:cd16269  248 EERENLLKEQERALESKlKEQEALLEEG 275
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 19-163 5.62e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.31  E-value: 5.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984364  19 EAQNKRHDVLSKLKEYEQRLNELQEERQRrqeeKQARDEAVQERKRALEAErQARVEELLMKRKEQEARIEQQRQEKEKa 98
Cdd:COG1196  250 ELEAELEELEAELAELEAELEELRLELEE----LELELEEAQAEEYELLAE-LARLEQDIARLEERRRELEERLEELEE- 323

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767984364  99 REDAARERARDREERLAALTAAQQEAMEELQKKiQLKHDESIRRHMEQIEQRKEKAAELSSGRHA 163
Cdd:COG1196  324 ELAELEEELEELEEELEELEEELEEAEEELEEA-EAELAEAEEALLEAEAELAEAEEELEELAEE 387
NtpH COG2811
Archaeal/vacuolar-type H+-ATPase subunit H [Energy production and conversion]; Archaeal ...
 54-156 5.77e-03

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


Pssm-ID: 442060 [Multi-domain]  Cd Length: 108  Bit Score: 37.20  E-value: 5.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984364  54 ARDEAVQERKRAlEAERQARVEELlmkRKEQEARIEQQRQEKEKAREdaarerardreerlAALTAAQQEA---MEELQK 130
Cdd:COG2811    2 DRPEVLKEIKEA-EEEADEIIEEA---KEEREERIAEAREEAEEIIE--------------QAEEEAEEEAqerLEEARE 63

                         90       100
                 ....*....|....*....|....*.
gi 767984364 131 KIQLKHDESIRRHMEQIEQRKEKAAE 156
Cdd:COG2811   64 EAEAEAEEIIEEGEKEAEALKKKAED 89
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 60-156 6.49e-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: 39.52  E-value: 6.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984364   60 QERKRALEAERQARvEELLMKRKEQEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQLK---- 135
Cdd:pfam13868  51 EERERALEEEEEKE-EERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQrqlr 129

                          90       100
                  ....*....|....*....|...
gi 767984364  136 --HDESIRRHMEQIEQRKEKAAE 156
Cdd:pfam13868 130 eeIDEFNEEQAEWKELEKEEERE 152
PRK12704 PRK12704
phosphodiesterase; Provisional
 18-156 6.88e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 39.76  E-value: 6.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984364  18 LEAQNKRHDVLSKL-KEYEQRLNELqeerqrrqeekQARDEAVQERKRALEaerqaRVEELLmKRKEQE-----ARIEQQ 91
Cdd:PRK12704  60 LEAKEEIHKLRNEFeKELRERRNEL-----------QKLEKRLLQKEENLD-----RKLELL-EKREEElekkeKELEQK 122

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767984364  92 RQ--EKEKAREDAARERARDREERLAALTA--AQQEAMEELQKKIQLKHDESIRRHMEQIEQRKEKAAE 156
Cdd:PRK12704 123 QQelEKKEEELEELIEEQLQELERISGLTAeeAKEILLEKVEEEARHEAAVLIKEIEEEAKEEADKKAK 191
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 19-156 8.07e-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: 39.65  E-value: 8.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984364    19 EAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALE------AERQARVEELLMKRKEQEARIEQ-- 90
Cdd:TIGR02168  709 ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTeleaeiEELEERLEEAEEELAEAEAEIEEle 788

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767984364    91 ---QRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIqlkhdESIRRHMEQIEQRKEKAAE 156
Cdd:TIGR02168  789 aqiEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRI-----AATERRLEDLEEQIEELSE 852
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 35-156 8.36e-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: 39.13  E-value: 8.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984364   35 EQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQARVEELLMKRKEQEARIEQQRQEKEKAREDAARERARDREERL 114
Cdd:pfam13868  51 EERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLRE 130

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 767984364  115 AALTA-AQQEAMEELQKKIQLKHDESIRRHMEQIEQRKEKAAE 156
Cdd:pfam13868 131 EIDEFnEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREA 173
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 53-160 8.60e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 39.36  E-value: 8.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984364  53 QARDEAVQERKRALEAERQaRVEELLMKRKEQEARIEQQRQEKEKaredaarerardREERLAALTAAQQEAMEELQKKI 132
Cdd:COG4942  156 RADLAELAALRAELEAERA-ELEALLAELEEERAALEALKAERQK------------LLARLEKELAELAAELAELQQEA 222

                         90       100
                 ....*....|....*....|....*...
gi 767984364 133 QlkhdeSIRRHMEQIEQRKEKAAELSSG 160
Cdd:COG4942  223 E-----ELEALIARLEAEAAAAAERTPA 245
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
13-171 8.65e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.90  E-value: 8.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984364   13 AFINTLEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAvQERKRALEAERQA----RVEEL--LMKRKEQE- 85
Cdd:COG4913   276 YLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDAL-REELDELEAQIRGnggdRLEQLerEIERLEREl 354

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984364   86 ARIEQQRQEKEKAREDAARERARDREERLAALTAAQQ--EAMEELQKKIQLKHDESIRRHMEQIEQRKEKAAELSSGRHA 163
Cdd:COG4913   355 EERERRRARLEALLAALGLPLPASAEEFAALRAEAAAllEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434


                  ....*...
gi 767984364  164 NTDYAPKL 171
Cdd:COG4913   435 KSNIPARL 442
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 52-156 9.04e-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: 39.13  E-value: 9.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984364   52 KQARDEAVQERKRALEAERQARVEELLmkrkEQEARIEQQRQEKEKaredaarerardreeRLAALTAAQQEA------M 125
Cdd:pfam13868 164 KAEREEEREAEREEIEEEKEREIARLR----AQQEKAQDEKAERDE---------------LRAKLYQEEQERkerqkeR 224

                          90       100       110
                  ....*....|....*....|....*....|...
gi 767984364  126 EELQKKIQLKHD--ESIRRHMEQIEQRKEKAAE 156
Cdd:pfam13868 225 EEAEKKARQRQElqQAREEQIELKERRLAEEAE 257
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 18-163 9.12e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.53  E-value: 9.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984364  18 LEAQNKRHDVLSKLKEYEQRLNEL---QEERQRRQEEKQARDEAVQERKRALEAERQARVEELlmkRKEQEARIEQQRQE 94
Cdd:COG1196  368 LEAEAELAEAEEELEELAEELLEAlraAAELAAQLEELEEAEEALLERLERLEEELEELEEAL---AELEEEEEEEEEAL 444

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767984364  95 KEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQLKHDESIRRHMEQIEQRKEKAAELSSGRHA 163
Cdd:COG1196  445 EEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAA 513
PTZ00121 PTZ00121
MAEBL; Provisional
 19-303 9.28e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.74  E-value: 9.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984364   19 EAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQARVEEllMKRKEQEARIEQ-------- 90
Cdd:PTZ00121 1159 KAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEE--ARKAEDAKKAEAvkkaeeak 1236

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984364   91 ------QRQEKEKAREDAARERARDR---EERLAALTAAQQEAMEELQKKIQLKHDESIRRHME--QIEQRKEKAAElss 159
Cdd:PTZ00121 1237 kdaeeaKKAEEERNNEEIRKFEEARMahfARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEkkKADEAKKKAEE--- 1313

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984364  160 GRHAntDYAPKLTPYERKKQCSLCNVliSSEVYLFSHVKGRKHQQAVREntsiqgRELSDEEVEHLSLKKYiidivvEST 239
Cdd:PTZ00121 1314 AKKA--DEAKKKAEEAKKKADAAKKK--AEEAKKAAEAAKAEAEAAADE------AEAAEEKAEAAEKKKE------EAK 1377

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767984364  240 APAEALKDGEERQKNKKKAKKIKARMNFRAKEYESLMETKNSGSDSPYKAKLQRLAKDLLKQVQ 303
Cdd:PTZ00121 1378 KKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAE 1441
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 19-157 9.89e-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: 39.65  E-value: 9.89e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984364    19 EAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEaERQARVEEL--LMKRKEQEARIEQQRQ--- 93
Cdd:TIGR02168  236 ELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIE-ELQKELYALanEISRLEQQKQILRERLanl 314

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767984364    94 EKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQLKHDESIRRHMEQiEQRKEKAAEL 157
Cdd:TIGR02168  315 ERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAEL-EELESRLEEL 377
 
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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