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Conserved domains on  [gi|2217306615|ref|XP_047290298|]
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zinc finger protein 821 isoform X1 [Homo sapiens]

Protein Classification

C2H2-type zinc finger protein( domain architecture ID 10442881)

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

CATH:  3.30.160.60
Gene Ontology:  GO:0003677|GO:0008270|GO:0003700
PubMed:  11179890|12665246|11361095|10940247|22803940
SCOP:  4003583

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG2433 super family cl43687
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
260-334 5.57e-06

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


The actual alignment was detected with superfamily member COG2433:

Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 48.70  E-value: 5.57e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217306615 260 LRRQNEPLEVRLQRLERERTAKKSRRDNETPEEREVRRmRDREAKRLQRMQETDEQRARRLQRDREamRLKRANE 334
Cdd:COG2433   432 LEAELEEKDERIERLERELSEARSEERREIRKDREISR-LDREIERLERELEEERERIEELKRKLE--RLKELWK 503
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 150-172 7.49e-03

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


:

Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 33.81  E-value: 7.49e-03
                          10        20
                  ....*....|....*....|...
gi 2217306615 150 YMCPVCGRALSSPGSLGRHLLIH 172
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
260-334 5.57e-06

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 48.70  E-value: 5.57e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217306615 260 LRRQNEPLEVRLQRLERERTAKKSRRDNETPEEREVRRmRDREAKRLQRMQETDEQRARRLQRDREamRLKRANE 334
Cdd:COG2433   432 LEAELEEKDERIERLERELSEARSEERREIRKDREISR-LDREIERLERELEEERERIEELKRKLE--RLKELWK 503
CCDC47 pfam07946
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of ...
 293-354 1.51e-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: 43.33  E-value: 1.51e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217306615 293 REVRRMRDREAKRLQRMQETDEQRARRLQRD---REAMRLKRANETPEKRQARLIREREaKRLKR 354
Cdd:pfam07946 260 KKAKKTREEEIEKIKKAAEEERAEEAQEKKEeakKKEREEKLAKLSPEEQRKYEEKERK-KEQRK 323
U2AF_lg TIGR01642
U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of ...
 275-387 2.99e-04

U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of an N-terminal arginine-rich low complexity domain followed by three tandem RNA recognition motifs (pfam00076). The well-characterized members of this family are auxilliary components of the U2 small nuclear ribonuclearprotein splicing factor (U2AF). These proteins are closely related to the CC1-like subfamily of splicing factors (TIGR01622). Members of this subfamily are found in plants, metazoa and fungi.


Pssm-ID: 273727 [Multi-domain]  Cd Length: 509  Bit Score: 42.96  E-value: 2.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306615 275 ERERTAKKSR-RDNETPEEREVRRMRDREAKR-------LQRMQETDEQRARRLQRDREAMRLK----RANETPEKRQAR 342
Cdd:TIGR01642   4 EPDREREKSRgRDRDRSSERPRRRSRDRSRFRdrhrrsrERSYREDSRPRDRRRYDSRSPRSLRyssvRRSRDRPRRRSR 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2217306615 343 LI------REREAKRLKRRLEKMDMMLRAQFGQDPSAM----AALAAEMNFFQLP 387
Cdd:TIGR01642  84 SVrsieqhRRRLRDRSPSNQWRKDDKKRSLWDIKPPGYelvtADQAKASQVFSVP 138
PTZ00121 PTZ00121
MAEBL; Provisional
 245-358 1.17e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.28  E-value: 1.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306615  245 RKLLEAQTP-SVRKWALRRQNEplEVR----LQRLERERTAKKSRRDNETPEEREVRRMRD-----REAKRLQRMQETDE 314
Cdd:PTZ00121  1176 KKAEAARKAeEVRKAEELRKAE--DARkaeaARKAEEERKAEEARKAEDAKKAEAVKKAEEakkdaEEAKKAEEERNNEE 1253

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 2217306615  315 QRARRLQRDREAMRLKRANETPEKRQARLIREREAKRLKRRLEK 358
Cdd:PTZ00121  1254 IRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKK 1297
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 150-172 7.49e-03

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 33.81  E-value: 7.49e-03
                          10        20
                  ....*....|....*....|...
gi 2217306615 150 YMCPVCGRALSSPGSLGRHLLIH 172
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
260-334 5.57e-06

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 48.70  E-value: 5.57e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217306615 260 LRRQNEPLEVRLQRLERERTAKKSRRDNETPEEREVRRmRDREAKRLQRMQETDEQRARRLQRDREamRLKRANE 334
Cdd:COG2433   432 LEAELEEKDERIERLERELSEARSEERREIRKDREISR-LDREIERLERELEEERERIEELKRKLE--RLKELWK 503
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
242-366 6.07e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.14  E-value: 6.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306615 242 AAYRKLLEAQTPSVRKWALRRQNEPLEVRLQRLERERTAKKSRRDNETPEEREVRRMRDREAKRLQRMQETDEQRARRLQ 321
Cdd:COG4717   119 EKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLA 198

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2217306615 322 RDREAMRLKRANETPEKRQARlireREAKRLKRRLEKMDMMLRAQ 366
Cdd:COG4717   199 EELEELQQRLAELEEELEEAQ----EELEELEEELEQLENELEAA 239
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
259-364 8.35e-05

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 44.85  E-value: 8.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306615 259 ALRRQNEPLEVRlqRLERERTAKKSRRDNETPEEREVRRMRDR------EAKRLQRMQETDEQRARRLQRDREAMRLKRA 332
Cdd:COG2433   381 ALEELIEKELPE--EEPEAEREKEHEERELTEEEEEIRRLEEQverleaEVEELEAELEEKDERIERLERELSEARSEER 458

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2217306615 333 NETPEKRQARlIREREAKRLKRRLEKMDMMLR 364
Cdd:COG2433   459 REIRKDREIS-RLDREIERLERELEEERERIE 489
CCDC47 pfam07946
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of ...
 293-354 1.51e-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: 43.33  E-value: 1.51e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217306615 293 REVRRMRDREAKRLQRMQETDEQRARRLQRD---REAMRLKRANETPEKRQARLIREREaKRLKR 354
Cdd:pfam07946 260 KKAKKTREEEIEKIKKAAEEERAEEAQEKKEeakKKEREEKLAKLSPEEQRKYEEKERK-KEQRK 323
U2AF_lg TIGR01642
U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of ...
 275-387 2.99e-04

U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of an N-terminal arginine-rich low complexity domain followed by three tandem RNA recognition motifs (pfam00076). The well-characterized members of this family are auxilliary components of the U2 small nuclear ribonuclearprotein splicing factor (U2AF). These proteins are closely related to the CC1-like subfamily of splicing factors (TIGR01622). Members of this subfamily are found in plants, metazoa and fungi.


Pssm-ID: 273727 [Multi-domain]  Cd Length: 509  Bit Score: 42.96  E-value: 2.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306615 275 ERERTAKKSR-RDNETPEEREVRRMRDREAKR-------LQRMQETDEQRARRLQRDREAMRLK----RANETPEKRQAR 342
Cdd:TIGR01642   4 EPDREREKSRgRDRDRSSERPRRRSRDRSRFRdrhrrsrERSYREDSRPRDRRRYDSRSPRSLRyssvRRSRDRPRRRSR 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2217306615 343 LI------REREAKRLKRRLEKMDMMLRAQFGQDPSAM----AALAAEMNFFQLP 387
Cdd:TIGR01642  84 SVrsieqhRRRLRDRSPSNQWRKDDKKRSLWDIKPPGYelvtADQAKASQVFSVP 138
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
249-370 3.08e-04

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 42.92  E-value: 3.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306615 249 EAQTPSVRKWALRRQNEPLEVRLQRLERErtAKKSRRDNETpEEREVRRMRDREAKRLQRMQETDEQRARRLQRDREAMR 328
Cdd:COG2433   393 EEPEAEREKEHEERELTEEEEEIRRLEEQ--VERLEAEVEE-LEAELEEKDERIERLERELSEARSEERREIRKDREISR 469

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2217306615 329 LKRANETPEKRQARLirEREAKRLKRRLEKMDMMLRAQFGQD 370
Cdd:COG2433   470 LDREIERLERELEEE--RERIEELKRKLERLKELWKLEHSGE 509
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 261-358 4.58e-04

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: 42.42  E-value: 4.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306615 261 RRQNEPLEVRLQRLERERtakksrrdnetpeEREVRRMRDREAKRLQRM----QETDEQRARRLQRDREAMRLKRA---- 332
Cdd:pfam17380 427 AEQEEARQREVRRLEEER-------------AREMERVRLEEQERQQQVerlrQQEEERKRKKLELEKEKRDRKRAeeqr 493

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2217306615 333 -----NETPEKRQARLIREREAKRLKRRLEK 358
Cdd:pfam17380 494 rkileKELEERKQAMIEEERKRKLLEKEMEE 524
PTZ00121 PTZ00121
MAEBL; Provisional
 245-358 1.17e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.28  E-value: 1.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306615  245 RKLLEAQTP-SVRKWALRRQNEplEVR----LQRLERERTAKKSRRDNETPEEREVRRMRD-----REAKRLQRMQETDE 314
Cdd:PTZ00121  1176 KKAEAARKAeEVRKAEELRKAE--DARkaeaARKAEEERKAEEARKAEDAKKAEAVKKAEEakkdaEEAKKAEEERNNEE 1253

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 2217306615  315 QRARRLQRDREAMRLKRANETPEKRQARLIREREAKRLKRRLEK 358
Cdd:PTZ00121  1254 IRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKK 1297
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 260-366 2.92e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.92  E-value: 2.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306615 260 LRRQNEPLEVRLQRLERERTAKKSRRDNETPEEREVRRMRDREAKRLQRMQETDEQRARRLQRDREAMRLKRANETpEKR 339
Cdd:COG1196   307 LEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE-ELA 385

                          90       100
                  ....*....|....*....|....*..
gi 2217306615 340 QARLIREREAKRLKRRLEKMDMMLRAQ 366
Cdd:COG1196   386 EELLEALRAAAELAAQLEELEEAEEAL 412
PTZ00121 PTZ00121
MAEBL; Provisional
 262-358 3.39e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.74  E-value: 3.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306615  262 RQNEPLEVRLQRLERERTAKKSRRDNETPEEREVRRmrdreAKRLQRMQETDEQRARRLQRD-----REAMRLKRANETP 336
Cdd:PTZ00121  1613 KKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKK-----AEELKKAEEENKIKAAEEAKKaeedkKKAEEAKKAEEDE 1687

                           90       100
                   ....*....|....*....|..
gi 2217306615  337 EKRQARLIREREAKRLKRRLEK 358
Cdd:PTZ00121  1688 KKAAEALKKEAEEAKKAEELKK 1709
PTZ00121 PTZ00121
MAEBL; Provisional
 249-358 4.78e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.35  E-value: 4.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306615  249 EAQTPSVRKWALRRQNEplevrLQRLERERTAKKSRRDNETPEEREVRRM----RDREAKRLQRMQETDEqrARRLQRDR 324
Cdd:PTZ00121  1110 KAEEARKAEEAKKKAED-----ARKAEEARKAEDARKAEEARKAEDAKRVeiarKAEDARKAEEARKAED--AKKAEAAR 1182

                           90       100       110
                   ....*....|....*....|....*....|....
gi 2217306615  325 EAMRLKRANETPEKRQARLIREREAKRLKRRLEK 358
Cdd:PTZ00121  1183 KAEEVRKAEELRKAEDARKAEAARKAEEERKAEE 1216
PRK00247 PRK00247
putative inner membrane protein translocase component YidC; Validated
 256-341 5.52e-03

putative inner membrane protein translocase component YidC; Validated


Pssm-ID: 178945 [Multi-domain]  Cd Length: 429  Bit Score: 38.68  E-value: 5.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306615 256 RKWALRRQN----------EPLEVRLQRLERERTAKKSRRDNETPEEREVRRMRDREA---KRLQRMQETDEQRARRLQR 322
Cdd:PRK00247  304 FLWTLRRNRlrmiitpwraPELHAENAEIKKTRTAEKNEAKARKKEIAQKRRAAEREInreARQERAAAMARARARRAAV 383

                          90
                  ....*....|....*....
gi 2217306615 323 DREAMRLKRANETPEKRQA 341
Cdd:PRK00247  384 KAKKKGLIDASPNEDTPSE 402
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 259-357 5.96e-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: 38.36  E-value: 5.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306615 259 ALRRQNEPLEVRLQRLERERTAKKSRRDNETPEEREVRRMRDREAK-RLQRMQETDEQRARRLQRDREAMRLKRANETPE 337
Cdd:pfam13868 137 EEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKeREIARLRAQQEKAQDEKAERDELRAKLYQEEQE 216

                          90       100
                  ....*....|....*....|
gi 2217306615 338 KRQARLIREREAKRLKRRLE 357
Cdd:pfam13868 217 RKERQKEREEAEKKARQRQE 236
Nop53 pfam07767
Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ...
 268-358 6.63e-03

Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ribosomal biogenesis. They are specifically involved in the processing beyond the 27S stage of 25S rRNA maturation. This family contains sequences that bear similarity to the glioma tumour suppressor candidate region gene 2 protein (p60). This protein has been found to interact with herpes simplex type 1 regulatory proteins.


Pssm-ID: 462259 [Multi-domain]  Cd Length: 353  Bit Score: 38.43  E-value: 6.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306615 268 EVRLQRLERE----RTAKKSRRDNETPEEREVRRM----RDREAKRLQRMQETDEQRARRLQRdREAMRLKRANETPEKR 339
Cdd:pfam07767 206 EAEKKRLKEEekleRVLEKIAESAATAEAREEKRKtkaqRNKEKRRKEEEREAKEEKALKKKL-AQLERLKEIAKEIAEK 284

                          90
                  ....*....|....*....
gi 2217306615 340 QARLIREREAKRLKRRLEK 358
Cdd:pfam07767 285 EKEREEKAEARKREKRKKK 303
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 270-383 6.81e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 38.76  E-value: 6.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306615 270 RLQRLERERTAKKSRRDNETPEEREVRRMRDREAKRLQRMQETDEQRARRLQRDREAMRLKRANETPEKRQARLIREREA 349
Cdd:COG1196   285 EAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE 364

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2217306615 350 KRLKRRLEKMDMMLRAQFGQDPSAMAALAAEMNF 383
Cdd:COG1196   365 EALLEAEAELAEAEEELEELAEELLEALRAAAEL 398
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 150-172 7.49e-03

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 33.81  E-value: 7.49e-03
                          10        20
                  ....*....|....*....|...
gi 2217306615 150 YMCPVCGRALSSPGSLGRHLLIH 172
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
SF-CC1 TIGR01622
splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors ...
 284-358 8.17e-03

splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors including the Pad-1 protein (N. crassa), CAPER (M. musculus) and CC1.3 (H.sapiens). These proteins are characterized by an N-terminal arginine-rich, low complexity domain followed by three (or in the case of 4 H. sapiens paralogs, two) RNA recognition domains (rrm: pfam00706). These splicing factors are closely related to the U2AF splicing factor family (TIGR01642). A homologous gene from Plasmodium falciparum was identified in the course of the analysis of that genome at TIGR and was included in the seed.


Pssm-ID: 273721 [Multi-domain]  Cd Length: 494  Bit Score: 38.36  E-value: 8.17e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217306615 284 RRDNETPEEREVRRMRDREAKRlqrmqETDEQRARRLQRDREAMRLKRANETPEKRQARLIREREAKRLKRRLEK 358
Cdd:TIGR01622   2 YRDRERERLRDSSSAGDRDRRR-----DKGRERSRDRSRDRERSRSRRRDRHRDRDYYRGRERRSRSRRPNRRYR 71
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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