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Conserved domains on  [gi|2462598995|ref|XP_054206865|]
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protein WWC2 isoform X3 [Homo sapiens]

Protein Classification

WW and C2_Kibra domain-containing protein( domain architecture ID 13628918)

protein containing domains WW, Smc, C2_Kibra, and PRK10929

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
C2_Kibra cd08680
C2 domain found in Human protein Kibra; Kibra is thought to be a regulator of the Salvador ...
 700-800 2.31e-47

C2 domain found in Human protein Kibra; Kibra is thought to be a regulator of the Salvador (Sav)/Warts (Wts)/Hippo (Hpo) (SWH) signaling network, which limits tissue growth by inhibiting cell proliferation and promoting apoptosis. The core of the pathway consists of a MST and LATS family kinase cascade that ultimately phosphorylates and inactivates the YAP/Yorkie (Yki) transcription coactivator. The FERM domain proteins Merlin (Mer) and Expanded (Ex) are part of the upstream regulation controlling pathway mechanism. Kibra colocalizes and associates with Mer and Ex and is thought to transduce an extracellular signal via the SWH network. The apical scaffold machinery that contains Hpo, Wts, and Ex recruits Yki to the apical membrane facilitating its inhibitory phosphorlyation by Wts. Since Kibra associates with Ex and is apically located it is hypothesized that KIBRA is part of the scaffold, helps in the Hpo/Wts complex, and helps recruit Yki for inactivation that promotes SWH pathway activity. Kibra contains two amino-terminal WW domains, an internal C2-like domain, and a carboxy-terminal glutamic acid-rich stretch. The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


:

Pssm-ID: 176062  Cd Length: 124  Bit Score: 164.33  E-value: 2.31e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598995 700 AQVQIGLRYNAKSSSFMVIIAQLRNLHAFLIPHTSKVYFRVAVLPSSTDVSCLFRTKVHPPTESILFNDVFRVAISQTAL 779
Cdd:cd08680     1 AQVQIGLRYDSGDSSLVISVEQLRNLSALSIPENSKVYVRVALLPCSSSTSCLFRTKALEDQDKPVFNEVFRVPISSTKL 80

                          90       100
                  ....*....|....*....|.
gi 2462598995 780 QQKTLRVDLCSVSKHRREECL 800
Cdd:cd08680    81 YQKTLQVDVCSVGPDQQEECL 101
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 12-41 7.41e-11

WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.


:

Pssm-ID: 459800 [Multi-domain]  Cd Length: 30  Bit Score: 57.13  E-value: 7.41e-11
                          10        20        30
                  ....*....|....*....|....*....|
gi 2462598995  12 LPRGWEEARDYDGKVFYIDHNTRRTSWIDP 41
Cdd:pfam00397   1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 59-88 4.89e-08

WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.


:

Pssm-ID: 459800 [Multi-domain]  Cd Length: 30  Bit Score: 49.43  E-value: 4.89e-08
                          10        20        30
                  ....*....|....*....|....*....|
gi 2462598995  59 LPWGWEAGFDPQIGVYYIDHINKTTQIEDP 88
Cdd:pfam00397   1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 173-430 6.79e-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: 49.94  E-value: 6.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598995 173 LRVKKLKRELSQMKQELLYKEqgfetLQQIDKKMSGGQSGYELSEAK--AILTELKSIRKAISSGEKEKQDLMQSLAKLQ 250
Cdd:COG1196   213 ERYRELKEELKELEAELLLLK-----LRELEAELEELEAELEELEAEleELEAELAELEAELEELRLELEELELELEEAQ 287

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598995 251 ERFH-LDQNIGRSEPDLRcspvnsHLCLSRQ---------TLDAGSQTSISGDIGVRSRSNLAEKVRLSLQYEEAKRSMA 320
Cdd:COG1196   288 AEEYeLLAELARLEQDIA------RLEERRReleerleelEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA 361

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598995 321 NLKIELSKLDS------EAWpgaLDIEKEKLMLINEKEELLKELQFVTPQ-KRTQDELERLEAERQRLEEELLSVRgtpS 393
Cdd:COG1196   362 EAEEALLEAEAelaeaeEEL---EELAEELLEALRAAAELAAQLEELEEAeEALLERLERLEEELEELEEALAELE---E 435

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 2462598995 394 RALAERLRLEERRKELLQKLEETTKLTTYLHSQLKSL 430
Cdd:COG1196   436 EEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472
 
Name Accession Description Interval E-value
C2_Kibra cd08680
C2 domain found in Human protein Kibra; Kibra is thought to be a regulator of the Salvador ...
 700-800 2.31e-47

C2 domain found in Human protein Kibra; Kibra is thought to be a regulator of the Salvador (Sav)/Warts (Wts)/Hippo (Hpo) (SWH) signaling network, which limits tissue growth by inhibiting cell proliferation and promoting apoptosis. The core of the pathway consists of a MST and LATS family kinase cascade that ultimately phosphorylates and inactivates the YAP/Yorkie (Yki) transcription coactivator. The FERM domain proteins Merlin (Mer) and Expanded (Ex) are part of the upstream regulation controlling pathway mechanism. Kibra colocalizes and associates with Mer and Ex and is thought to transduce an extracellular signal via the SWH network. The apical scaffold machinery that contains Hpo, Wts, and Ex recruits Yki to the apical membrane facilitating its inhibitory phosphorlyation by Wts. Since Kibra associates with Ex and is apically located it is hypothesized that KIBRA is part of the scaffold, helps in the Hpo/Wts complex, and helps recruit Yki for inactivation that promotes SWH pathway activity. Kibra contains two amino-terminal WW domains, an internal C2-like domain, and a carboxy-terminal glutamic acid-rich stretch. The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


Pssm-ID: 176062  Cd Length: 124  Bit Score: 164.33  E-value: 2.31e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598995 700 AQVQIGLRYNAKSSSFMVIIAQLRNLHAFLIPHTSKVYFRVAVLPSSTDVSCLFRTKVHPPTESILFNDVFRVAISQTAL 779
Cdd:cd08680     1 AQVQIGLRYDSGDSSLVISVEQLRNLSALSIPENSKVYVRVALLPCSSSTSCLFRTKALEDQDKPVFNEVFRVPISSTKL 80

                          90       100
                  ....*....|....*....|.
gi 2462598995 780 QQKTLRVDLCSVSKHRREECL 800
Cdd:cd08680    81 YQKTLQVDVCSVGPDQQEECL 101
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 12-41 7.41e-11

WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.


Pssm-ID: 459800 [Multi-domain]  Cd Length: 30  Bit Score: 57.13  E-value: 7.41e-11
                          10        20        30
                  ....*....|....*....|....*....|
gi 2462598995  12 LPRGWEEARDYDGKVFYIDHNTRRTSWIDP 41
Cdd:pfam00397   1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 11-43 6.37e-10

Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.


Pssm-ID: 197736 [Multi-domain]  Cd Length: 33  Bit Score: 54.91  E-value: 6.37e-10
                           10        20        30
                   ....*....|....*....|....*....|...
gi 2462598995   11 PLPRGWEEARDYDGKVFYIDHNTRRTSWIDPRD 43
Cdd:smart00456   1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 13-43 1.84e-09

Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.


Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 53.30  E-value: 1.84e-09
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2462598995  13 PRGWEEARDYDGKVFYIDHNTRRTSWIDPRD 43
Cdd:cd00201     1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 59-88 4.89e-08

WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.


Pssm-ID: 459800 [Multi-domain]  Cd Length: 30  Bit Score: 49.43  E-value: 4.89e-08
                          10        20        30
                  ....*....|....*....|....*....|
gi 2462598995  59 LPWGWEAGFDPQIGVYYIDHINKTTQIEDP 88
Cdd:pfam00397   1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 173-430 6.79e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.94  E-value: 6.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598995 173 LRVKKLKRELSQMKQELLYKEqgfetLQQIDKKMSGGQSGYELSEAK--AILTELKSIRKAISSGEKEKQDLMQSLAKLQ 250
Cdd:COG1196   213 ERYRELKEELKELEAELLLLK-----LRELEAELEELEAELEELEAEleELEAELAELEAELEELRLELEELELELEEAQ 287

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598995 251 ERFH-LDQNIGRSEPDLRcspvnsHLCLSRQ---------TLDAGSQTSISGDIGVRSRSNLAEKVRLSLQYEEAKRSMA 320
Cdd:COG1196   288 AEEYeLLAELARLEQDIA------RLEERRReleerleelEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA 361

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598995 321 NLKIELSKLDS------EAWpgaLDIEKEKLMLINEKEELLKELQFVTPQ-KRTQDELERLEAERQRLEEELLSVRgtpS 393
Cdd:COG1196   362 EAEEALLEAEAelaeaeEEL---EELAEELLEALRAAAELAAQLEELEEAeEALLERLERLEEELEELEEALAELE---E 435

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 2462598995 394 RALAERLRLEERRKELLQKLEETTKLTTYLHSQLKSL 430
Cdd:COG1196   436 EEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 62-89 1.04e-05

Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.


Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 42.90  E-value: 1.04e-05
                          10        20
                  ....*....|....*....|....*...
gi 2462598995  62 GWEAGFDPQIGVYYIDHINKTTQIEDPR 89
Cdd:cd00201     3 GWEERWDPDGRVYYYNHNTKETQWEDPR 30
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 59-89 1.08e-05

Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.


Pssm-ID: 197736 [Multi-domain]  Cd Length: 33  Bit Score: 42.59  E-value: 1.08e-05
                           10        20        30
                   ....*....|....*....|....*....|.
gi 2462598995   59 LPWGWEAGFDPQIGVYYIDHINKTTQIEDPR 89
Cdd:smart00456   2 LPPGWEERKDPDGRPYYYNHETKETQWEKPR 32
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
164-430 1.51e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 48.52  E-value: 1.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598995 164 LKAEISTTRLRVKKLKRELSQMKQ-ELLYKEQG---FETLQQIDKKMSG-GQSGYELSEAKAILTELKSIRKAISSGEKE 238
Cdd:PRK03918  167 LGEVIKEIKRRIERLEKFIKRTENiEELIKEKEkelEEVLREINEISSElPELREELEKLEKEVKELEELKEEIEELEKE 246

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598995 239 KQDLMQSLAKLQERF-HLDQNIGRSEPDLRCspvnshlcLSRQtldAGSQTSISGDIgvrsrsnlAEKVRLSLQYEEAKR 317
Cdd:PRK03918  247 LESLEGSKRKLEEKIrELEERIEELKKEIEE--------LEEK---VKELKELKEKA--------EEYIKLSEFYEEYLD 307

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598995 318 SMANLKIELSKLDSEA------WPGALDIEKEKLMLINEKEELLKELQFVTPQKRTQDELERLEAERQRLEEELLSVrgT 391
Cdd:PRK03918  308 ELREIEKRLSRLEEEIngieerIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGL--T 385

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 2462598995 392 PSRALAERLRLEERRKELLQKLEETTKLTTYLHSQLKSL 430
Cdd:PRK03918  386 PEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKEL 424
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 115-415 6.84e-05

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: 46.59  E-value: 6.84e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598995  115 KELYHVKEQRLALALDEYVRLNDAYKEKSSSHTSLFSGSSSSTKYDPdiLKAEISTTRL-----RVKKLKRELSQMKQEL 189
Cdd:TIGR02168  171 KERRKETERKLERTRENLDRLEDILNELERQLKSLERQAEKAERYKE--LKAELRELELallvlRLEELREELEELQEEL 248

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598995  190 LYKEQGFETLQqidkkmsggqsgyelSEAKAILTELKSIRKAISSGEKEKQDL---MQSLAKLQERfhLDQNIGRSEPDL 266
Cdd:TIGR02168  249 KEAEEELEELT---------------AELQELEEKLEELRLEVSELEEEIEELqkeLYALANEISR--LEQQKQILRERL 311

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598995  267 RcSPVNSHLCLSRQTLDAGSQTSISGDIGVRSRSNLAE----KVRLSLQYEEAKRSMANLKIELSKLDSEawpgaLDIEK 342
Cdd:TIGR02168  312 A-NLERQLEELEAQLEELESKLDELAEELAELEEKLEElkeeLESLEAELEELEAELEELESRLEELEEQ-----LETLR 385

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462598995  343 EKLMLINEKEELL-KELQfvtpqkRTQDELERLEAERQRLEEELLSVRGTPSRALAERL--RLEERRKELLQKLEE 415
Cdd:TIGR02168  386 SKVAQLELQIASLnNEIE------RLEARLERLEDRRERLQQEIEELLKKLEEAELKELqaELEELEEELEELQEE 455
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 93-418 6.26e-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: 43.19  E-value: 6.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598995  93 RGEQEKMLKdylsVAQDALRTQKE-LYHVKEQRLALALDEYVRlnDAYKEKSSShtslfsgssSSTKYDPDILKAEISTT 171
Cdd:pfam17380 287 RQQQEKFEK----MEQERLRQEKEeKAREVERRRKLEEAEKAR--QAEMDRQAA---------IYAEQERMAMERERELE 351

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598995 172 RLRVKKLKRELSQMKQELLYKEqgFETLQQIDKKMSGGQSGYElseakAILTELKSIRKaISSGEKEKQDLMQSLAKLQE 251
Cdd:pfam17380 352 RIRQEERKRELERIRQEEIAME--ISRMRELERLQMERQQKNE-----RVRQELEAARK-VKILEEERQRKIQQQKVEME 423

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598995 252 RFHLDQNIGRSEPDLRCSPVNSHLCLSRQTLDAGSQTSISgdigvRSRSNLAEKVRLSLQYEEAKRSMANLKIELSKLDS 331
Cdd:pfam17380 424 QIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVE-----RLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILE 498

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598995 332 EAWPgaldiEKEKLMLINEKEELLKELQFVTPQKRTQDELERLEAERQRLE----EELLSVRGTPSRALAERLRLE--ER 405
Cdd:pfam17380 499 KELE-----ERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKqqemEERRRIQEQMRKATEERSRLEamER 573

                         330
                  ....*....|...
gi 2462598995 406 RKELLQKLEETTK 418
Cdd:pfam17380 574 EREMMRQIVESEK 586
 
Name Accession Description Interval E-value
C2_Kibra cd08680
C2 domain found in Human protein Kibra; Kibra is thought to be a regulator of the Salvador ...
 700-800 2.31e-47

C2 domain found in Human protein Kibra; Kibra is thought to be a regulator of the Salvador (Sav)/Warts (Wts)/Hippo (Hpo) (SWH) signaling network, which limits tissue growth by inhibiting cell proliferation and promoting apoptosis. The core of the pathway consists of a MST and LATS family kinase cascade that ultimately phosphorylates and inactivates the YAP/Yorkie (Yki) transcription coactivator. The FERM domain proteins Merlin (Mer) and Expanded (Ex) are part of the upstream regulation controlling pathway mechanism. Kibra colocalizes and associates with Mer and Ex and is thought to transduce an extracellular signal via the SWH network. The apical scaffold machinery that contains Hpo, Wts, and Ex recruits Yki to the apical membrane facilitating its inhibitory phosphorlyation by Wts. Since Kibra associates with Ex and is apically located it is hypothesized that KIBRA is part of the scaffold, helps in the Hpo/Wts complex, and helps recruit Yki for inactivation that promotes SWH pathway activity. Kibra contains two amino-terminal WW domains, an internal C2-like domain, and a carboxy-terminal glutamic acid-rich stretch. The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


Pssm-ID: 176062  Cd Length: 124  Bit Score: 164.33  E-value: 2.31e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598995 700 AQVQIGLRYNAKSSSFMVIIAQLRNLHAFLIPHTSKVYFRVAVLPSSTDVSCLFRTKVHPPTESILFNDVFRVAISQTAL 779
Cdd:cd08680     1 AQVQIGLRYDSGDSSLVISVEQLRNLSALSIPENSKVYVRVALLPCSSSTSCLFRTKALEDQDKPVFNEVFRVPISSTKL 80

                          90       100
                  ....*....|....*....|.
gi 2462598995 780 QQKTLRVDLCSVSKHRREECL 800
Cdd:cd08680    81 YQKTLQVDVCSVGPDQQEECL 101
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 12-41 7.41e-11

WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.


Pssm-ID: 459800 [Multi-domain]  Cd Length: 30  Bit Score: 57.13  E-value: 7.41e-11
                          10        20        30
                  ....*....|....*....|....*....|
gi 2462598995  12 LPRGWEEARDYDGKVFYIDHNTRRTSWIDP 41
Cdd:pfam00397   1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 11-43 6.37e-10

Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.


Pssm-ID: 197736 [Multi-domain]  Cd Length: 33  Bit Score: 54.91  E-value: 6.37e-10
                           10        20        30
                   ....*....|....*....|....*....|...
gi 2462598995   11 PLPRGWEEARDYDGKVFYIDHNTRRTSWIDPRD 43
Cdd:smart00456   1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 13-43 1.84e-09

Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.


Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 53.30  E-value: 1.84e-09
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2462598995  13 PRGWEEARDYDGKVFYIDHNTRRTSWIDPRD 43
Cdd:cd00201     1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 59-88 4.89e-08

WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.


Pssm-ID: 459800 [Multi-domain]  Cd Length: 30  Bit Score: 49.43  E-value: 4.89e-08
                          10        20        30
                  ....*....|....*....|....*....|
gi 2462598995  59 LPWGWEAGFDPQIGVYYIDHINKTTQIEDP 88
Cdd:pfam00397   1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
C2C_KIAA1228 cd04030
C2 domain third repeat present in uncharacterized human KIAA1228-like proteins; KIAA proteins ...
 698-790 7.24e-07

C2 domain third repeat present in uncharacterized human KIAA1228-like proteins; KIAA proteins are uncharacterized human proteins. They were compiled by the Kazusa mammalian cDNA project which identified more than 2000 human genes. They are identified by 4 digit codes that precede the KIAA designation. Many KIAA genes are still functionally uncharacterized including KIAA1228. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the third C2 repeat, C2C, and has a type-II topology.


Pssm-ID: 175996 [Multi-domain]  Cd Length: 127  Bit Score: 48.81  E-value: 7.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598995 698 ETAQVQIGLRYNAKSSSFMVIIAQLRNLHAFLIPHTSKVYFRVAVLPSSTdVSCLFRTKVHPPTESILFNDVFRVAISQT 777
Cdd:cd04030     1 PLGRIQLTIRYSSQRQKLIVTVHKCRNLPPCDSSDIPDPYVRLYLLPDKS-KSTRRKTSVKKDNLNPVFDETFEFPVSLE 79

                          90
                  ....*....|...
gi 2462598995 778 ALQQKTLRVDLCS 790
Cdd:cd04030    80 ELKRRTLDVAVKN 92
C2A_Synaptotagmin-8 cd08387
C2A domain first repeat present in Synaptotagmin 8; Synaptotagmin is a membrane-trafficking ...
 699-800 3.74e-06

C2A domain first repeat present in Synaptotagmin 8; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-I topology.


Pssm-ID: 176033 [Multi-domain]  Cd Length: 124  Bit Score: 46.63  E-value: 3.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598995 699 TAQVQIGLRYNAKSSSFMVIIAQLRNLHAFLIPHTSKVYFRVAVLPsstDVSCLFRTKVHPPTESILFNDVFRVAISQTA 778
Cdd:cd08387     2 RGELHFSLEYDKDMGILNVKLIQARNLQPRDFSGTADPYCKVRLLP---DRSNTKQSKIHKKTLNPEFDESFVFEVPPQE 78

                          90       100
                  ....*....|....*....|..
gi 2462598995 779 LQQKTLRVDLCSVSKHRREECL 800
Cdd:cd08387    79 LPKRTLEVLLYDFDQFSRDECI 100
C2A_Synaptotagmin-1-5-6-9-10 cd08385
C2A domain first repeat present in Synaptotagmins 1, 5, 6, 9, and 10; Synaptotagmin is a ...
 702-794 5.04e-06

C2A domain first repeat present in Synaptotagmins 1, 5, 6, 9, and 10; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. Synaptotagmin 1, a member of class 1 synaptotagmins, is located in the brain and endocranium and localized to the synaptic vesicles and secretory granules. It functions as a Ca2+ sensor for fast exocytosis as do synaptotagmins 5, 6, and 10. It is distinguished from the other synaptotagmins by having an N-glycosylated N-terminus. Synaptotagmins 5, 6, and 10, members of class 3 synaptotagmins, are located primarily in the brain and localized to the active zone and plasma membrane. They is distinguished from the other synaptotagmins by having disulfide bonds at its N-terminus. Synaptotagmin 6 also regulates the acrosome reaction, a unique Ca2+-regulated exocytosis, in sperm. Synaptotagmin 9, a class 5 synaptotagmins, is located in the brain and localized to the synaptic vesicles. It is thought to be a Ca2+-sensor for dense-core vesicle exocytosis. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-I topology.


Pssm-ID: 176031 [Multi-domain]  Cd Length: 124  Bit Score: 46.49  E-value: 5.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598995 702 VQIGLRYNAKSSSFMVIIAQLRNLHAFLIPHTSKVYFRVAVLPsstDVSCLFRTKVHPPTESILFNDVFRVAISQTALQQ 781
Cdd:cd08385     5 LQFSLDYDFQSNQLTVGIIQAADLPAMDMGGTSDPYVKVYLLP---DKKKKFETKVHRKTLNPVFNETFTFKVPYSELGN 81

                          90
                  ....*....|....*.
gi 2462598995 782 KTLRV---DLCSVSKH 794
Cdd:cd08385    82 KTLVFsvyDFDRFSKH 97
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 173-430 6.79e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.94  E-value: 6.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598995 173 LRVKKLKRELSQMKQELLYKEqgfetLQQIDKKMSGGQSGYELSEAK--AILTELKSIRKAISSGEKEKQDLMQSLAKLQ 250
Cdd:COG1196   213 ERYRELKEELKELEAELLLLK-----LRELEAELEELEAELEELEAEleELEAELAELEAELEELRLELEELELELEEAQ 287

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598995 251 ERFH-LDQNIGRSEPDLRcspvnsHLCLSRQ---------TLDAGSQTSISGDIGVRSRSNLAEKVRLSLQYEEAKRSMA 320
Cdd:COG1196   288 AEEYeLLAELARLEQDIA------RLEERRReleerleelEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA 361

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598995 321 NLKIELSKLDS------EAWpgaLDIEKEKLMLINEKEELLKELQFVTPQ-KRTQDELERLEAERQRLEEELLSVRgtpS 393
Cdd:COG1196   362 EAEEALLEAEAelaeaeEEL---EELAEELLEALRAAAELAAQLEELEEAeEALLERLERLEEELEELEEALAELE---E 435

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 2462598995 394 RALAERLRLEERRKELLQKLEETTKLTTYLHSQLKSL 430
Cdd:COG1196   436 EEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 62-89 1.04e-05

Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.


Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 42.90  E-value: 1.04e-05
                          10        20
                  ....*....|....*....|....*...
gi 2462598995  62 GWEAGFDPQIGVYYIDHINKTTQIEDPR 89
Cdd:cd00201     3 GWEERWDPDGRVYYYNHNTKETQWEDPR 30
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 59-89 1.08e-05

Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.


Pssm-ID: 197736 [Multi-domain]  Cd Length: 33  Bit Score: 42.59  E-value: 1.08e-05
                           10        20        30
                   ....*....|....*....|....*....|.
gi 2462598995   59 LPWGWEAGFDPQIGVYYIDHINKTTQIEDPR 89
Cdd:smart00456   2 LPPGWEERKDPDGRPYYYNHETKETQWEKPR 32
C2A_SLP cd08521
C2 domain first repeat present in Synaptotagmin-like proteins; All Slp members basically share ...
 701-796 1.19e-05

C2 domain first repeat present in Synaptotagmin-like proteins; All Slp members basically share an N-terminal Slp homology domain (SHD) and C-terminal tandem C2 domains (named the C2A domain and the C2B domain) with the SHD and C2 domains being separated by a linker sequence of various length. Slp1/JFC1 and Slp2/exophilin 4 promote granule docking to the plasma membrane. Additionally, their C2A domains are both Ca2+ independent, unlike the case in Slp3 and Slp4/granuphilin in which their C2A domains are Ca2+ dependent. It is thought that SHD (except for the Slp4-SHD) functions as a specific Rab27A/B-binding domain. In addition to Slps, rabphilin, Noc2, and Munc13-4 also function as Rab27-binding proteins. It has been demonstrated that Slp3 and Slp4/granuphilin promote dense-core vesicle exocytosis. Slp5 mRNA has been shown to be restricted to human placenta and liver suggesting a role in Rab27A-dependent membrane trafficking in specific tissues. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-I topology.


Pssm-ID: 176056 [Multi-domain]  Cd Length: 123  Bit Score: 45.32  E-value: 1.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598995 701 QVQIGLRYNAKSSSFMVIIAQLRNLhAFLIP--HTSKVYFRVAVLPSSTDVSCLfRTKVHPPTESILFNDVFRVAISQTA 778
Cdd:cd08521     2 EIEFSLSYNYKTGSLEVHIKECRNL-AYADEkkKRSNPYVKVYLLPDKSKQSKR-KTSVKKNTTNPVFNETLKYHISKSQ 79

                          90
                  ....*....|....*...
gi 2462598995 779 LQQKTLRVdlcSVSKHRR 796
Cdd:cd08521    80 LETRTLQL---SVWHHDR 94
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
164-430 1.51e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 48.52  E-value: 1.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598995 164 LKAEISTTRLRVKKLKRELSQMKQ-ELLYKEQG---FETLQQIDKKMSG-GQSGYELSEAKAILTELKSIRKAISSGEKE 238
Cdd:PRK03918  167 LGEVIKEIKRRIERLEKFIKRTENiEELIKEKEkelEEVLREINEISSElPELREELEKLEKEVKELEELKEEIEELEKE 246

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598995 239 KQDLMQSLAKLQERF-HLDQNIGRSEPDLRCspvnshlcLSRQtldAGSQTSISGDIgvrsrsnlAEKVRLSLQYEEAKR 317
Cdd:PRK03918  247 LESLEGSKRKLEEKIrELEERIEELKKEIEE--------LEEK---VKELKELKEKA--------EEYIKLSEFYEEYLD 307

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598995 318 SMANLKIELSKLDSEA------WPGALDIEKEKLMLINEKEELLKELQFVTPQKRTQDELERLEAERQRLEEELLSVrgT 391
Cdd:PRK03918  308 ELREIEKRLSRLEEEIngieerIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGL--T 385

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 2462598995 392 PSRALAERLRLEERRKELLQKLEETTKLTTYLHSQLKSL 430
Cdd:PRK03918  386 PEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKEL 424
C2B_Synaptotagmin cd00276
C2 domain second repeat present in Synaptotagmin; Synaptotagmin is a membrane-trafficking ...
 700-800 4.24e-05

C2 domain second repeat present in Synaptotagmin; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. There are several classes of Synaptotagmins. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-I topology.


Pssm-ID: 175975 [Multi-domain]  Cd Length: 134  Bit Score: 44.11  E-value: 4.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598995 700 AQVQIGLRYNAKSSSFMVIIAQLRNLHAFLIPHTSKVYFRVAVLPSSTDVSClFRTKVHPPTESILFNDVFRVAISQTAL 779
Cdd:cd00276     1 GELLLSLSYLPTAERLTVVVLKARNLPPSDGKGLSDPYVKVSLLQGGKKLKK-KKTSVKKGTLNPVFNEAFSFDVPAEQL 79

                          90       100
                  ....*....|....*....|.
gi 2462598995 780 QQKTLRVDLCSVSKHRREECL 800
Cdd:cd00276    80 EEVSLVITVVDKDSVGRNEVI 100
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 176-453 5.60e-05

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: 46.30  E-value: 5.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598995 176 KKLKRELSQMKQELLYKEQGFETLQQidkkmsggqsgyelsEAKAILTELKSIRKAISSGEKEKQDLMQSLAKLQERFH- 254
Cdd:COG4942    23 AEAEAELEQLQQEIAELEKELAALKK---------------EEKALLKQLAALERRIAALARRIRALEQELAALEAELAe 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598995 255 LDQNIGRSEPDLrcspvnshlclsrqtldAGSQTSISGDIGVRSRSNLAEKVRLSLQYEEAKRSMANLKI--ELSKLDSE 332
Cdd:COG4942    88 LEKEIAELRAEL-----------------EAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYlkYLAPARRE 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598995 333 AwpgALDIEKEKLMLINEKEELLKElqfvtpQKRTQDELERLEAERQRLEEELLSVRgtpsRALAerlRLEERRKELLQK 412
Cdd:COG4942   151 Q---AEELRADLAELAALRAELEAE------RAELEALLAELEEERAALEALKAERQ----KLLA---RLEKELAELAAE 214

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 2462598995 413 LEETTKLTTYLHSQLKSLSASTLSMSSGSSLGSLASSRGSL 453
Cdd:COG4942   215 LAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGKL 255
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 164-385 5.85e-05

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: 46.30  E-value: 5.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598995 164 LKAEISTTRLRVKKLKRELSQMKQEllykeqgfetLQQIDKKMSGGQsgyelSEAKAILTELKSIRKAISSGEKEKQDLM 243
Cdd:COG4942    32 LQQEIAELEKELAALKKEEKALLKQ----------LAALERRIAALA-----RRIRALEQELAALEAELAELEKEIAELR 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598995 244 QSLAKLQERF-----HLDQNIGRSEPDLRCSPVNShlclsrqtLDAGSQTSISGDIgVRSRSNLAEKVRLSLQY-EEAKR 317
Cdd:COG4942    97 AELEAQKEELaellrALYRLGRQPPLALLLSPEDF--------LDAVRRLQYLKYL-APARREQAEELRADLAElAALRA 167

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462598995 318 SMANLKIELSKLDSEawpgaLDIEKEKL-MLINEKEELLKELQfvTPQKRTQDELERLEAERQRLEEEL 385
Cdd:COG4942   168 ELEAERAELEALLAE-----LEEERAALeALKAERQKLLARLE--KELAELAAELAELQQEAEELEALI 229
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 115-415 6.84e-05

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: 46.59  E-value: 6.84e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598995  115 KELYHVKEQRLALALDEYVRLNDAYKEKSSSHTSLFSGSSSSTKYDPdiLKAEISTTRL-----RVKKLKRELSQMKQEL 189
Cdd:TIGR02168  171 KERRKETERKLERTRENLDRLEDILNELERQLKSLERQAEKAERYKE--LKAELRELELallvlRLEELREELEELQEEL 248

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598995  190 LYKEQGFETLQqidkkmsggqsgyelSEAKAILTELKSIRKAISSGEKEKQDL---MQSLAKLQERfhLDQNIGRSEPDL 266
Cdd:TIGR02168  249 KEAEEELEELT---------------AELQELEEKLEELRLEVSELEEEIEELqkeLYALANEISR--LEQQKQILRERL 311

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598995  267 RcSPVNSHLCLSRQTLDAGSQTSISGDIGVRSRSNLAE----KVRLSLQYEEAKRSMANLKIELSKLDSEawpgaLDIEK 342
Cdd:TIGR02168  312 A-NLERQLEELEAQLEELESKLDELAEELAELEEKLEElkeeLESLEAELEELEAELEELESRLEELEEQ-----LETLR 385

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462598995  343 EKLMLINEKEELL-KELQfvtpqkRTQDELERLEAERQRLEEELLSVRGTPSRALAERL--RLEERRKELLQKLEE 415
Cdd:TIGR02168  386 SKVAQLELQIASLnNEIE------RLEARLERLEDRRERLQQEIEELLKKLEEAELKELqaELEELEEELEELQEE 455
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 162-432 1.13e-04

chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 45.83  E-value: 1.13e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598995  162 DILKAEISTTRLRVKKLKRELSQMK--QELLYKEQGFEtlqqidkkmsggqsGYEL-SEAKAILTELKSIRKAISSGEKE 238
Cdd:TIGR02169  187 ERLDLIIDEKRQQLERLRREREKAEryQALLKEKREYE--------------GYELlKEKEALERQKEAIERQLASLEEE 252

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598995  239 KQDLMQSLAKLQERFHlDQNIGRSEPDLRCSPVNSHLCLSRQTLDAGSQTSISgdigvRSRSNLAEKVRlslQYEEAKRS 318
Cdd:TIGR02169  253 LEKLTEEISELEKRLE-EIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIA-----SLERSIAEKER---ELEDAEER 323

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598995  319 MANLKIELSKLDSEAWPGALDIEKEKLMLINEKEELlKELQfvtpqkrtqdelERLEAERQRLEEELLSVRGTPSRALAE 398
Cdd:TIGR02169  324 LAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEY-AELK------------EELEDLRAELEEVDKEFAETRDELKDY 390

                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 2462598995  399 RLRLE---ERRKELLQKLEETTKLTTYLHSQLKSLSA 432
Cdd:TIGR02169  391 REKLEklkREINELKRELDRLQEELQRLSEELADLNA 427
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 165-418 1.86e-04

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: 45.05  E-value: 1.86e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598995  165 KAEISTTRLRVKKLKRELSQMKQELLYKEQGFETLQQ--IDKKMSGGQSGYELSEAKAiltELKSIRKAISSGEKEKQDL 242
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEelEQLRKELEELSRQISALRK---DLARLEAEVEQLEERIAQL 752

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598995  243 MQSLAKLQ-ERFHLDQNIGRSEPDLRCSPVNshlclsRQTLDAgSQTSISGDIGVrSRSNLAEkvrLSLQYEEAKRSMAN 321
Cdd:TIGR02168  753 SKELTELEaEIEELEERLEEAEEELAEAEAE------IEELEA-QIEQLKEELKA-LREALDE---LRAELTLLNEEAAN 821

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598995  322 LKIELSKLDSEawpgALDIEKEKLMLINEKEELLKELQFVTPQKRT--------QDELERLEAERQRLEEELLSVRGTPS 393
Cdd:TIGR02168  822 LRERLESLERR----IAATERRLEDLEEQIEELSEDIESLAAEIEEleelieelESELEALLNERASLEEALALLRSELE 897

                          250       260
                   ....*....|....*....|....*
gi 2462598995  394 RALAERLRLEERRKELLQKLEETTK 418
Cdd:TIGR02168  898 ELSEELRELESKRSELRRELEELRE 922
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 206-417 2.94e-04

chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 44.67  E-value: 2.94e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598995  206 MSGG--QSGYELSEAKAILTELKSIRKAISSGEKEKQDLMQSLAKL-QERFHLDQNIGRSEpdlrcspvnshlclsRQTL 282
Cdd:TIGR02169  655 MTGGsrAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIeNRLDELSQELSDAS---------------RKIG 719

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598995  283 DAGSQTSISGDIGVRSRSNLAEKVRlslQYEEAKRSMANLKIELSKLDSEAWPGALDIEKEKLMLINEKEELLKElqfvt 362
Cdd:TIGR02169  720 EIEKEIEQLEQEEEKLKERLEELEE---DLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHS----- 791

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2462598995  363 PQKRTQDELERLEAERQRLEEELLSVRGTPSRALAERLRLEERRKELLQKLEETT 417
Cdd:TIGR02169  792 RIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLK 846
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
78-432 4.17e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.99  E-value: 4.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598995  78 HINKTTQIEDPRKQWRGEQEKMlKDYLSVAQDALRTQKELYHVKEQRLAL-----ALDEYVRLNDAYKEKsssHTSLFSG 152
Cdd:COG4717    66 PELNLKELKELEEELKEAEEKE-EEYAELQEELEELEEELEELEAELEELreeleKLEKLLQLLPLYQEL---EALEAEL 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598995 153 SSSSTKYDpdilkaEISTTRLRVKKLKRELSQMKQELLYKEQGFETLQQIDKKMSGGQSGYELSEAKAILTELKSIRKAI 232
Cdd:COG4717   142 AELPERLE------ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEEL 215

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598995 233 SSGEKEKQDLMQSLAKLQ---ERFHLDQNIGRSEPDLRCSPV------NSHLCLSRQTLDAGSQTSISGDIGVRSRSNLA 303
Cdd:COG4717   216 EEAQEELEELEEELEQLEnelEAAALEERLKEARLLLLIAAAllallgLGGSLLSLILTIAGVLFLVLGLLALLFLLLAR 295

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598995 304 EKVRLSLQYEEAKRSMAnlKIELSKLDSEAWPGALDIEKE-KLMLINEKEELLKELQFVTPQKRTQDELERLEAERQRLE 382
Cdd:COG4717   296 EKASLGKEAEELQALPA--LEELEEEELEELLAALGLPPDlSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIA 373

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462598995 383 EELLSVRGTPSRALAERLRLEERRKELLQKLEEttkLTTYLHSQLKSLSA 432
Cdd:COG4717   374 ALLAEAGVEDEEELRAALEQAEEYQELKEELEE---LEEQLEELLGELEE 420
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 164-415 4.43e-04

chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.90  E-value: 4.43e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598995  164 LKAEISTTRLRVKKLKRELSQMKQELLYKEQGFETLQQ--------IDKKMSGGQS-GYELSEAKAILTE----LKSIRK 230
Cdd:TIGR02169  672 EPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQelsdasrkIGEIEKEIEQlEQEEEKLKERLEEleedLSSLEQ 751

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598995  231 AISSGEKEKQDLMQSLAKLQERFH-LDQNIGRSEPDLRCSPVNShlclSRQTLDagSQTSISGDIGVRSRSNLAEKVRLS 309
Cdd:TIGR02169  752 EIENVKSELKELEARIEELEEDLHkLEEALNDLEARLSHSRIPE----IQAELS--KLEEEVSRIEARLREIEQKLNRLT 825

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598995  310 LQYEEAKRSMANLKIELSKLDSEawpgALDIEKEKLMLINEKEELLKELQFVTPQKRT-QDELERLEAERQRLEEELLSV 388
Cdd:TIGR02169  826 LEKEYLEKEIQELQEQRIDLKEQ----IKSIEKEIENLNGKKEELEEELEELEAALRDlESRLGDLKKERDELEAQLREL 901

                          250       260
                   ....*....|....*....|....*..
gi 2462598995  389 RGTPSRALAERLRLEERRKELLQKLEE 415
Cdd:TIGR02169  902 ERKIEELEAQIEKKRKRLSELKAKLEA 928
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 93-418 6.26e-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: 43.19  E-value: 6.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598995  93 RGEQEKMLKdylsVAQDALRTQKE-LYHVKEQRLALALDEYVRlnDAYKEKSSShtslfsgssSSTKYDPDILKAEISTT 171
Cdd:pfam17380 287 RQQQEKFEK----MEQERLRQEKEeKAREVERRRKLEEAEKAR--QAEMDRQAA---------IYAEQERMAMERERELE 351

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598995 172 RLRVKKLKRELSQMKQELLYKEqgFETLQQIDKKMSGGQSGYElseakAILTELKSIRKaISSGEKEKQDLMQSLAKLQE 251
Cdd:pfam17380 352 RIRQEERKRELERIRQEEIAME--ISRMRELERLQMERQQKNE-----RVRQELEAARK-VKILEEERQRKIQQQKVEME 423

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598995 252 RFHLDQNIGRSEPDLRCSPVNSHLCLSRQTLDAGSQTSISgdigvRSRSNLAEKVRLSLQYEEAKRSMANLKIELSKLDS 331
Cdd:pfam17380 424 QIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVE-----RLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILE 498

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598995 332 EAWPgaldiEKEKLMLINEKEELLKELQFVTPQKRTQDELERLEAERQRLE----EELLSVRGTPSRALAERLRLE--ER 405
Cdd:pfam17380 499 KELE-----ERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKqqemEERRRIQEQMRKATEERSRLEamER 573

                         330
                  ....*....|...
gi 2462598995 406 RKELLQKLEETTK 418
Cdd:pfam17380 574 EREMMRQIVESEK 586
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 162-415 6.71e-04

chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.52  E-value: 6.71e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598995  162 DILKAEISTTRLRVKKLKRELSQMKQELLYKEQGFETLQQIDKKMSGgqsgyelsEAKAILTELKSIRKAISSGEKEKQD 241
Cdd:TIGR02169  691 SSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKE--------RLEELEEDLSSLEQEIENVKSELKE 762

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598995  242 LMQSLAKLQERFH-LDQNIGRSEPDLRCSPVNshlclsrqtldagsqtsisgDIGVRSRSNLAEKVRLSLQYEEAKRSMA 320
Cdd:TIGR02169  763 LEARIEELEEDLHkLEEALNDLEARLSHSRIP--------------------EIQAELSKLEEEVSRIEARLREIEQKLN 822

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598995  321 NLKIELSKLDSEAwpgaLDIEKEKLMLINEKEELLKELQFVTPQKR-TQDELERLEAERQRLEEELLSVRGtpsralaER 399
Cdd:TIGR02169  823 RLTLEKEYLEKEI----QELQEQRIDLKEQIKSIEKEIENLNGKKEeLEEELEELEAALRDLESRLGDLKK-------ER 891

                          250
                   ....*....|....*.
gi 2462598995  400 LRLEERRKELLQKLEE 415
Cdd:TIGR02169  892 DELEAQLRELERKIEE 907
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 95-419 1.06e-03

chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 42.75  E-value: 1.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598995   95 EQEKMLKDYLSVAQDALRTQKELYHVKEQRLALALDEYVRLN------DAYKEKSSSHTSLFSGSSSSTKYDPDILKAEI 168
Cdd:TIGR02169  681 ERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEkeieqlEQEEEKLKERLEELEEDLSSLEQEIENVKSEL 760

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598995  169 STTRLRVKKLKRELSQMKQEL--LYKEQGFETLQQIDKKMSggqsgyelseakAILTELKSIRKAISSGEKEKQDLMQSL 246
Cdd:TIGR02169  761 KELEARIEELEEDLHKLEEALndLEARLSHSRIPEIQAELS------------KLEEEVSRIEARLREIEQKLNRLTLEK 828

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598995  247 AKLQERFHLDQNIgRSEPDLRCSPVNSHLCLSRqtLDAGSQTSISGDIGVRSRSNLAEKVRLSLQYEEAKRSMANLKIEL 326
Cdd:TIGR02169  829 EYLEKEIQELQEQ-RIDLKEQIKSIEKEIENLN--GKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKI 905

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598995  327 SKLDSEawpgaLDIEKEKLMLINEK-EELLKELQFVTPQKRTQDE-------LERLEAERQRLEEELLSVRGTPSRALAE 398
Cdd:TIGR02169  906 EELEAQ-----IEKKRKRLSELKAKlEALEEELSEIEDPKGEDEEipeeelsLEDVQAELQRVEEEIRALEPVNMLAIQE 980

                          330       340       350
                   ....*....|....*....|....*....|....*
gi 2462598995  399 --------------RLRLEERRKELLQKLEETTKL 419
Cdd:TIGR02169  981 yeevlkrldelkekRAKLEEERKAILERIEEYEKK 1015
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
 137-417 1.21e-03

Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.


Pssm-ID: 464932 [Multi-domain]  Cd Length: 329  Bit Score: 41.72  E-value: 1.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598995 137 DAYKEKSSSHTSLFSGSSSSTKYDPDILKAEISTTRLRVKKLKRELSQMKqeLLYKEQGfetlqQIDKKMSGGQSGYELS 216
Cdd:pfam15905  34 AAESQPNLNNSKDASTPATARKVKSLELKKKSQKNLKESKDQKELEKEIR--ALVQERG-----EQDKRLQALEEELEKV 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598995 217 EAK--AILTELKSIRKAISSGEKEKQDLMQSLAKLQERFHLDQNigrsepDLRCSPVNSHLCLSRQTLDAGSQTSISGDI 294
Cdd:pfam15905 107 EAKlnAAVREKTSLSASVASLEKQLLELTRVNELLKAKFSEDGT------QKKMSSLSMELMKLRNKLEAKMKEVMAKQE 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598995 295 GVRSRSNLAEKvrlslQYEEAKRSMANLKIELSkldseawpgalDIEKEKlmlINEKEELLKELQFVTPQKRTQDELERL 374
Cdd:pfam15905 181 GMEGKLQVTQK-----NLEHSKGKVAQLEEKLV-----------STEKEK---IEEKSETEKLLEYITELSCVSEQVEKY 241

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462598995 375 EAERQRLEE-------ELLSVRGTPSRALAERLRLEERRKELLQKLEETT 417
Cdd:pfam15905 242 KLDIAQLEEllkekndEIESLKQSLEEKEQELSKQIKDLNEKCKLLESEK 291
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
84-432 1.90e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.68  E-value: 1.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598995  84 QIEDPRKQWRGEQEKM--LKDYLSVAQDALRTQKELYHVKEQ--RLALALDEYVRLNDAYKEKSSSHTSLFSGSSSSTKY 159
Cdd:COG4717   106 ELEAELEELREELEKLekLLQLLPLYQELEALEAELAELPERleELEERLEELRELEEELEELEAELAELQEELEELLEQ 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598995 160 DPDILKAEISTTRLRVKKLKRELSQMKQELLYKEQGFETLQQ----IDKKMSGGQSGYELSEAK------AILTELKSIR 229
Cdd:COG4717   186 LSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEeleqLENELEAAALEERLKEARlllliaAALLALLGLG 265

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598995 230 KAISSGEKEKQDLMQSLAKLQerFHLDQNIGRSEPDLRCSPVNSHLCLSRQTLDAGSQTSISGDIGVRSRSNLAEKVRLS 309
Cdd:COG4717   266 GSLLSLILTIAGVLFLVLGLL--ALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELL 343

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598995 310 LQYEEAKRSMAnlkiELSKLDSEawpgaLDIEKeklmLINEKEELLKELQFVTPQKRTQ-----DELERLEAERQRLEEE 384
Cdd:COG4717   344 DRIEELQELLR----EAEELEEE-----LQLEE----LEQEIAALLAEAGVEDEEELRAaleqaEEYQELKEELEELEEQ 410

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462598995 385 LLSVRGTPSRALA--ERLRLEERRKELLQKLEETTKLTTYLHSQLKSLSA 432
Cdd:COG4717   411 LEELLGELEELLEalDEEELEEELEELEEELEELEEELEELREELAELEA 460
COG4026 COG4026
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ...
 338-420 2.09e-03

Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];


Pssm-ID: 443204 [Multi-domain]  Cd Length: 287  Bit Score: 40.87  E-value: 2.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598995 338 LDIEKEKLMLINEKEELLKELQfvtpqkRTQDELERLEAERQRLEEELLSVRGTPSRALAERLRLEERRKELLQK-LEET 416
Cdd:COG4026   138 LELKEKIDEIAKEKEKLTKENE------ELESELEELREEYKKLREENSILEEEFDNIKSEYSDLKSRFEELLKKrLLEV 211


                  ....
gi 2462598995 417 TKLT 420
Cdd:COG4026   212 FSLE 215
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 307-432 2.70e-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: 41.58  E-value: 2.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598995  307 RLSLQYEEAKRSMANLKIELSKLDSEAwpgaLDIEKEKLMLINEKEELLKELqfvtpqKRTQDELERLEAERQRLEEELl 386
Cdd:TIGR02168  681 ELEEKIEELEEKIAELEKALAELRKEL----EELEEELEQLRKELEELSRQI------SALRKDLARLEAEVEQLEERI- 749

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 2462598995  387 svrgtpSRALAERLRLEERRKELLQKLEETTKLTTYLHSQLKSLSA 432
Cdd:TIGR02168  750 ------AQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEA 789
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
299-432 3.73e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.66  E-value: 3.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598995 299 RSNLAEKVRLSLQYEEAKRSMANLKIELSKLDSEawpgaLDIEKEKLMLINEK-EELLKELQ-FVTPQKRTQDELERLEA 376
Cdd:COG4372    34 RKALFELDKLQEELEQLREELEQAREELEQLEEE-----LEQARSELEQLEEElEELNEQLQaAQAELAQAQEELESLQE 108

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462598995 377 ERQRLEEELlsvrgtpSRALAERLRLEERRKELLQKLEETTKLTTYLHSQLKSLSA 432
Cdd:COG4372   109 EAEELQEEL-------EELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEE 157
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 303-432 8.68e-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: 8.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598995 303 AEKVRLSLQYEEAKRSMANLKIELSKLDSEawpgaLDIEKEKLMLINEK-EELLKELQfvtpqkRTQDELERLEAERQRL 381
Cdd:COG1196   239 AELEELEAELEELEAELEELEAELAELEAE-----LEELRLELEELELElEEAQAEEY------ELLAELARLEQDIARL 307

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462598995 382 EEELLSVRGTPSRALAERLRLEERRKELLQKLEETTKLTTYLHSQLKSLSA 432
Cdd:COG1196   308 EERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEA 358
 
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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