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Conserved domains on  [gi|21356345|ref|NP_648165|]
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uncharacterized protein Dmel_CG8042 [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Ubl1_cv_Nsp3_N-like super family cl28922
first ubiquitin-like (Ubl) domain located at the N-terminus of coronavirus SARS-CoV ...
 399-476 3.06e-19

first ubiquitin-like (Ubl) domain located at the N-terminus of coronavirus SARS-CoV non-structural protein 3 (Nsp3) and related proteins; This ubiquitin-like (Ubl) domain (Ubl1) is found at the N-terminus of coronavirus Nsp3, a large multi-functional multi-domain protein which is an essential component of the replication/transcription complex (RTC). The functions of Ubl1 in CoVs are related to single-stranded RNA (ssRNA) binding and to interacting with the nucleocapsid (N) protein. SARS-CoV Ubl1 has been shown to bind ssRNA having AUA patterns, and since the 5'-UTR of the SARS-CoV genome has a number of AUA repeats, it may bind there. In mouse hepatitis virus (MHV), this Ubl1 domain binds the cognate N protein. Adjacent to Ubl1 is a Glu-rich acidic region (also referred to as hypervariable region, HVR); Ubl1 together with HVR has been called Nsp3a. Currently, the function of HVR in CoVs is unknown. This model corresponds to one of two Ubl domains in Nsp3; the other is located N-terminal to the papain-like protease (PLpro) and is not represented by this model.


The actual alignment was detected with superfamily member cd01772:

Pssm-ID: 475130 [Multi-domain]  Cd Length: 81  Bit Score: 82.36  E-value: 3.06e-19
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21356345 399 DETRLQIRLPGGIQRTKSFPAGEVLATVRVYVrnEMLAASDVRDFTLATSYPRREFQTEDEVKTLNELNLVPNAVVLV 476
Cdd:cd01772   5 DECRLQVRLTNGSTLTQTFGAKEQLAAVRLYV--ELNRTDGDGPFSLMTTFPRKVFTEEDMEKPLKELGLVPSAVLIV 80
TPH super family cl38442
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 269-367 2.13e-08

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.


The actual alignment was detected with superfamily member pfam13868:

Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 56.47  E-value: 2.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345   269 QRPLEAQDNTESEERLAEVRNILE---------------QKRKERVEEEKRMEKENELRRRRDGREA-QSQQARAKEQEL 332
Cdd:pfam13868 107 VERIQEEDQAEAEEKLEKQRQLREeidefneeqaewkelEKEEEREEDERILEYLKEKAEREEEREAeREEIEEEKEREI 186

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 21356345   333 KNMQEQIKRERQEElAARERIRAQIAADRAEQAQR 367
Cdd:pfam13868 187 ARLRAQQEKAQDEK-AERDELRAKLYQEEQERKER 220
PRK10263 super family cl35903
DNA translocase FtsK; Provisional
 165-369 3.57e-04

DNA translocase FtsK; Provisional


The actual alignment was detected with superfamily member PRK10263:

Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 43.92  E-value: 3.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345   165 DPETTSVSNSPTGGVEEAKTNPPNSPVAAsLASIPAAVSTSSLEgkSGSEAEAASPTAlaaekraaaskvegsATTSGAA 244
Cdd:PRK10263  532 EPVKEPEPIKSSLKAPSVAAVPPVEAAAA-VSPLASGVKKATLA--TGAAATVAAPVF---------------SLANSGG 593

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345   245 ARNFATNNLIPAVPlMTPAVPVPTQRPLEAQDNTESEERLAEVRNILEQKRKERVEEEKRMEKENELRRRRDGRE-AQSQ 323
Cdd:PRK10263  594 PRPQVKEGIGPQLP-RPKRIRVPTRRELASYGIKLPSQRAAEEKAREAQRNQYDSGDQYNDDEIDAMQQDELARQfAQTQ 672

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 21356345   324 QARAKEQELKNMQEQIKrerQEELAARERIRAQIAadrAEQAQRFN 369
Cdd:PRK10263  673 QQRYGEQYQHDVPVNAE---DADAAAEAELARQFA---QTQQQRYS 712
 
Name Accession Description Interval E-value
UBX_UBXN1 cd01772
Ubiquitin regulatory domain X (UBX) found in UBX domain protein 1 (UBXN1) and similar proteins; ...
 399-476 3.06e-19

Ubiquitin regulatory domain X (UBX) found in UBX domain protein 1 (UBXN1) and similar proteins; UBXN1, also termed SAPK substrate protein 1 (SAKS1), UBA/UBX 33.3 kDa protein (Y33K), or UBXD10, is a widely expressed protein containing an N-terminal ubiquitin-associated (UBA) domain, a coiled-coil region, and a C-terminal ubiquitin-like (Ubl or UBX) domain that has a beta-grasp ubiquitin-like fold without the C-terminal double glycine motif. UBXN1 has been identified as a substrate for stress-activated protein kinases (SAPKs). It binds polyubiquitin and valosin-containing protein (VCP), suggesting a role as an adaptor that directs VCP to polyubiquitinated proteins facilitating its destruction by the proteasome. In addition, UBXN1 specifically binds to Homer2b. It may also interact with ubiquitin (Ub) and be involved in the Ub-proteasome proteolytic pathways. UBXN1 can also associate with autoubiquitinated BRCA1 tumor suppressor and inhibit its enzymatic function through its UBA domains.


Pssm-ID: 340470 [Multi-domain]  Cd Length: 81  Bit Score: 82.36  E-value: 3.06e-19
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21356345 399 DETRLQIRLPGGIQRTKSFPAGEVLATVRVYVrnEMLAASDVRDFTLATSYPRREFQTEDEVKTLNELNLVPNAVVLV 476
Cdd:cd01772   5 DECRLQVRLTNGSTLTQTFGAKEQLAAVRLYV--ELNRTDGDGPFSLMTTFPRKVFTEEDMEKPLKELGLVPSAVLIV 80
UBX pfam00789
UBX domain; This domain is present in ubiquitin-regulatory proteins and is a general ...
 399-476 1.37e-15

UBX domain; This domain is present in ubiquitin-regulatory proteins and is a general Cdc48-interacting module.


Pssm-ID: 395637 [Multi-domain]  Cd Length: 80  Bit Score: 71.94  E-value: 1.37e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345   399 DETRLQIRLPGG--IQRTksFPAGEVLATVRVYVRNEMLAASDvrDFTLATSYPRREFQTEDEVKTLNELNLVPNAVVLV 476
Cdd:pfam00789   3 DVTRLQIRLPDGsrLVRR--FNSSDKLQTVYDFVDSNRYDDLE--PFSLNTPFPRRPLTDLDYSKTLKEAGLLPNSTLVL 78
UBX smart00166
Domain present in ubiquitin-regulatory proteins; Present in FAF1 and Shp1p.
 400-476 6.61e-15

Domain present in ubiquitin-regulatory proteins; Present in FAF1 and Shp1p.


Pssm-ID: 197552 [Multi-domain]  Cd Length: 77  Bit Score: 70.02  E-value: 6.61e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21356345    400 ETRLQIRLPGGIQRTKSFPAGEVLATVRVYVRNEMLAASDvrDFTLATSYPRREFQTEDEVKTLNELNLVPNAVVLV 476
Cdd:smart00166   1 VCRLQIRLPDGSRLVRRFPSSDTLRTVYEFVSAALGDGND--PFTLNSPFPRRTFTKDDYSKKLLELALLPSSTLVL 75
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 269-367 2.13e-08

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: 56.47  E-value: 2.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345   269 QRPLEAQDNTESEERLAEVRNILE---------------QKRKERVEEEKRMEKENELRRRRDGREA-QSQQARAKEQEL 332
Cdd:pfam13868 107 VERIQEEDQAEAEEKLEKQRQLREeidefneeqaewkelEKEEEREEDERILEYLKEKAEREEEREAeREEIEEEKEREI 186

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 21356345   333 KNMQEQIKRERQEElAARERIRAQIAADRAEQAQR 367
Cdd:pfam13868 187 ARLRAQQEKAQDEK-AERDELRAKLYQEEQERKER 220
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 268-366 1.44e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.48  E-value: 1.44e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345 268 TQRPLEAQDNTESEERLAEVRNILEQKRKERVEEEKRMEKENELRRRRDGREAQSQQA----RAKEQELKNMQEQIKRER 343
Cdd:COG1196 337 EELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAaaelAAQLEELEEAEEALLERL 416

                        90       100
                ....*....|....*....|...
gi 21356345 344 QEELAARERIRAQIAADRAEQAQ 366
Cdd:COG1196 417 ERLEEELEELEEALAELEEEEEE 439
PRK12704 PRK12704
phosphodiesterase; Provisional
 272-364 1.19e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 48.24  E-value: 1.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345  272 LEAQD-----NTESEERLAEVRNILEQKRKERVEEEKRMEKENE-LRRRRDGREAQSQQARAKEQELKNMQEQIKRERQE 345
Cdd:PRK12704  60 LEAKEeihklRNEFEKELRERRNELQKLEKRLLQKEENLDRKLElLEKREEELEKKEKELEQKQQELEKKEEELEELIEE 139

                         90
                 ....*....|....*....
gi 21356345  346 ELAARERIrAQIAADRAEQ 364
Cdd:PRK12704 140 QLQELERI-SGLTAEEAKE 157
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 165-369 3.57e-04

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 43.92  E-value: 3.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345   165 DPETTSVSNSPTGGVEEAKTNPPNSPVAAsLASIPAAVSTSSLEgkSGSEAEAASPTAlaaekraaaskvegsATTSGAA 244
Cdd:PRK10263  532 EPVKEPEPIKSSLKAPSVAAVPPVEAAAA-VSPLASGVKKATLA--TGAAATVAAPVF---------------SLANSGG 593

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345   245 ARNFATNNLIPAVPlMTPAVPVPTQRPLEAQDNTESEERLAEVRNILEQKRKERVEEEKRMEKENELRRRRDGRE-AQSQ 323
Cdd:PRK10263  594 PRPQVKEGIGPQLP-RPKRIRVPTRRELASYGIKLPSQRAAEEKAREAQRNQYDSGDQYNDDEIDAMQQDELARQfAQTQ 672

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 21356345   324 QARAKEQELKNMQEQIKrerQEELAARERIRAQIAadrAEQAQRFN 369
Cdd:PRK10263  673 QQRYGEQYQHDVPVNAE---DADAAAEAELARQFA---QTQQQRYS 712
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 272-367 5.51e-04

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


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 42.56  E-value: 5.51e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345 272 LEAQDNTESEERLAEVRNILEQKRKERVEEEKRMEKENELRRrrdgREAQSQQARAK-EQELKNMQEQIKRERQEELAAR 350
Cdd:cd16269 193 LTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQERS----YEEHLRQLKEKmEEERENLLKEQERALESKLKEQ 268

                        90
                ....*....|....*..
gi 21356345 351 ERIRAQIAADRAEQAQR 367
Cdd:cd16269 269 EALLEEGFKEQAELLQE 285
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 271-367 2.68e-03

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 41.11  E-value: 2.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345    271 PLEAQDNTESEERLA-EVRNILEQKRKERVEEEKrMEKENELRRRRDGREAQSQQARAKEQELK-------NMQEQIKRE 342
Cdd:TIGR00618  211 PCMPDTYHERKQVLEkELKHLREALQQTQQSHAY-LTQKREAQEEQLKKQQLLKQLRARIEELRaqeavleETQERINRA 289

                           90       100
                   ....*....|....*....|....*.
gi 21356345    343 RQ-EELAARERIRAQIAADRAEQAQR 367
Cdd:TIGR00618  290 RKaAPLAAHIKAVTQIEQQAQRIHTE 315
 
Name Accession Description Interval E-value
UBX_UBXN1 cd01772
Ubiquitin regulatory domain X (UBX) found in UBX domain protein 1 (UBXN1) and similar proteins; ...
 399-476 3.06e-19

Ubiquitin regulatory domain X (UBX) found in UBX domain protein 1 (UBXN1) and similar proteins; UBXN1, also termed SAPK substrate protein 1 (SAKS1), UBA/UBX 33.3 kDa protein (Y33K), or UBXD10, is a widely expressed protein containing an N-terminal ubiquitin-associated (UBA) domain, a coiled-coil region, and a C-terminal ubiquitin-like (Ubl or UBX) domain that has a beta-grasp ubiquitin-like fold without the C-terminal double glycine motif. UBXN1 has been identified as a substrate for stress-activated protein kinases (SAPKs). It binds polyubiquitin and valosin-containing protein (VCP), suggesting a role as an adaptor that directs VCP to polyubiquitinated proteins facilitating its destruction by the proteasome. In addition, UBXN1 specifically binds to Homer2b. It may also interact with ubiquitin (Ub) and be involved in the Ub-proteasome proteolytic pathways. UBXN1 can also associate with autoubiquitinated BRCA1 tumor suppressor and inhibit its enzymatic function through its UBA domains.


Pssm-ID: 340470 [Multi-domain]  Cd Length: 81  Bit Score: 82.36  E-value: 3.06e-19
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21356345 399 DETRLQIRLPGGIQRTKSFPAGEVLATVRVYVrnEMLAASDVRDFTLATSYPRREFQTEDEVKTLNELNLVPNAVVLV 476
Cdd:cd01772   5 DECRLQVRLTNGSTLTQTFGAKEQLAAVRLYV--ELNRTDGDGPFSLMTTFPRKVFTEEDMEKPLKELGLVPSAVLIV 80
UBX cd01767
Ubiquitin regulatory domain X (UBX) structurally similar to a beta-grasp ubiquitin-like fold; ...
 402-476 4.64e-17

Ubiquitin regulatory domain X (UBX) structurally similar to a beta-grasp ubiquitin-like fold; The UBXD family of proteins contains the ubiquitin regulatory domain X (UBX) with a beta-grasp ubiquitin-like fold, but without the C-terminal double glycine motif. UBX domain is typically located at the carboxyl terminus of proteins, and participates broadly in the regulation of protein degradation. Members in this family function as cofactors of p97 (also known as VCP or Cdc48), which is a homohexameric AAA ATPase (ATPase associated with a variety of activities) involved in a variety of functions ranging from cell-cycle regulation to membrane fusion and protein degradation. Based on domain composition, UBXD proteins can be divided into two main groups, with and without ubiquitin-associated (UBA) domain.


Pssm-ID: 340466 [Multi-domain]  Cd Length: 74  Bit Score: 76.15  E-value: 4.64e-17
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21356345 402 RLQIRLPGGIQRTKSFPAGEVLATVRVYVRNEMLAASDvrDFTLATSYPRREFQTEDEVKTLNELNLVPNAVVLV 476
Cdd:cd01767   1 RIQIRLPDGSRIQRRFSKSDTLQDLYDFVESNLGDSPS--SFSLVTSFPRRVLTDEDSDKTLEELGLTPNAVLFV 73
UBX_UBXN4 cd16117
Ubiquitin regulatory domain X (UBX) found in UBX domain protein 4 (UBXN4) and similar proteins; ...
 401-477 1.16e-16

Ubiquitin regulatory domain X (UBX) found in UBX domain protein 4 (UBXN4) and similar proteins; UBXN4, also termed ERAD (endoplasmic-reticulum-associated protein degradation) substrate erasing protein (erasin), or UBX domain-containing protein 2 (UBXD2), or UBXDC1, belongs to the UBXD family of proteins that contains the ubiquitin regulatory domain X (UBX) with a beta-grasp ubiquitin-like fold, but without the C-terminal double glycine motif. UBX domain is typically located at the carboxyl terminus of proteins, and participates broadly in the regulation of protein degradation. UBXN4 is an endoplasmic reticulum (ER) localized protein that interacts with p97 (also known as VCP or Cdc48) via its UBX domain. Erasin exists in a complex with other p97/VCP-associated factors involved in endoplasmic-reticulum-associated protein degradation (ERAD). p97 is a homohexameric AAA ATPase (ATPase associated with a variety of activities) involved in a variety of functions ranging from cell-cycle regulation to membrane fusion and protein degradation. The overexpression of UBXN4 increases degradation of a classical ERAD substrate and UBXN4 levels are increased in ER stressed cells. Anti-UBXN4 staining is increased in neuropathological lesions in brains of patients with Alzheimer's disease.


Pssm-ID: 340534 [Multi-domain]  Cd Length: 77  Bit Score: 75.06  E-value: 1.16e-16
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21356345 401 TRLQIRLPGGIQRTKSFPAGEVLATVRVYVRNEMlaASDVRDFTLATSYPRREFQTEDEVKTLNELNLVPNAVVLVL 477
Cdd:cd16117   2 ARIQFRLPDGSSFTNQFPSDAPLEEARQFVAQTV--GPAYGPFSLATTFPRREFTDDDYQKTLLELELAPSAALVVL 76
UBX pfam00789
UBX domain; This domain is present in ubiquitin-regulatory proteins and is a general ...
 399-476 1.37e-15

UBX domain; This domain is present in ubiquitin-regulatory proteins and is a general Cdc48-interacting module.


Pssm-ID: 395637 [Multi-domain]  Cd Length: 80  Bit Score: 71.94  E-value: 1.37e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345   399 DETRLQIRLPGG--IQRTksFPAGEVLATVRVYVRNEMLAASDvrDFTLATSYPRREFQTEDEVKTLNELNLVPNAVVLV 476
Cdd:pfam00789   3 DVTRLQIRLPDGsrLVRR--FNSSDKLQTVYDFVDSNRYDDLE--PFSLNTPFPRRPLTDLDYSKTLKEAGLLPNSTLVL 78
UBX smart00166
Domain present in ubiquitin-regulatory proteins; Present in FAF1 and Shp1p.
 400-476 6.61e-15

Domain present in ubiquitin-regulatory proteins; Present in FAF1 and Shp1p.


Pssm-ID: 197552 [Multi-domain]  Cd Length: 77  Bit Score: 70.02  E-value: 6.61e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21356345    400 ETRLQIRLPGGIQRTKSFPAGEVLATVRVYVRNEMLAASDvrDFTLATSYPRREFQTEDEVKTLNELNLVPNAVVLV 476
Cdd:smart00166   1 VCRLQIRLPDGSRLVRRFPSSDTLRTVYEFVSAALGDGND--PFTLNSPFPRRTFTKDDYSKKLLELALLPSSTLVL 75
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 269-367 2.13e-08

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: 56.47  E-value: 2.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345   269 QRPLEAQDNTESEERLAEVRNILE---------------QKRKERVEEEKRMEKENELRRRRDGREA-QSQQARAKEQEL 332
Cdd:pfam13868 107 VERIQEEDQAEAEEKLEKQRQLREeidefneeqaewkelEKEEEREEDERILEYLKEKAEREEEREAeREEIEEEKEREI 186

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 21356345   333 KNMQEQIKRERQEElAARERIRAQIAADRAEQAQR 367
Cdd:pfam13868 187 ARLRAQQEKAQDEK-AERDELRAKLYQEEQERKER 220
UBX_UBXN3A cd01771
Ubiquitin regulatory domain X (UBX) found in FAS associated factor 1 (FAF1, also known as ...
 401-470 2.16e-08

Ubiquitin regulatory domain X (UBX) found in FAS associated factor 1 (FAF1, also known as UBXN3A) and similar proteins; UBX domain-containing protein 3A (UBXN3A),also termed UBX domain-containing protein 12 (UBXD12), or FAF1, belongs to the UBXD family of proteins that contains the ubiquitin regulatory domain X (UBX) with a beta-grasp ubiquitin-like fold, but without the C-terminal double glycine motif. UBX domain is typically located at the carboxyl terminus of proteins, and participates broadly in the regulation of protein degradation. In addition, FAF1 contains two tandem ubiquitin-like (Ubl) domains, which shows high structural similarity with UBX domain. FAF1 functions as a cofactor of p97 (also known as VCP or Cdc48), which is a homohexameric AAA ATPase (ATPase associated with a variety of activities) involved in a variety of functions ranging from cell-cycle regulation to membrane fusion and protein degradation. The FAF1-p97 complex inhibits the proteasomal protein degradation in which p97 acts as a co-chaperone. Moreover, FAF1 is an apoptotic signaling molecule that acts downstream in the Fas signal transduction pathway. It interacts with the cytoplasmic domain of Fas, but not to a Fas mutant that is deficient in signal transduction. FAF1 is widely expressed in adult and embryonic tissues, and in tumor cell lines, and is localized not only in the cytoplasm where it interacts with Fas, but also in the nucleus. FAF1 contains phosphorylation sites for protein kinase CK2 within the nuclear targeting domain. Phosphorylation influences nuclear localization of FAF1 but does not affect its potentiation of Fas-induced apoptosis. Other functions have also been attributed to FAF1. It inhibits nuclear factor-kappaB (NF-kappaB) by interfering with the nuclear translocation of the p65 subunit. Although the precise role of FAF1 in the ubiquitination pathway remains unclear, FAF1 interacts with valosin-containing protein (VCP), which is involved in the ubiquitin-proteosome pathway. This family corresponds to UBX domain.


Pssm-ID: 340469  Cd Length: 80  Bit Score: 51.46  E-value: 2.16e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345 401 TRLQIRLPGGIQRTKSFPAGEVLATVRVYVRNEMLAASDvrdFTLATSYPRREFQTEDEVKTLNELNLVP 470
Cdd:cd01771   5 SKLRFRLPGGEFLTRRFLASEPLQVLLNFVASKGYPPDE---YKLLTTFPRRDLTQLDPSKTLEELKLFP 71
UBX_UBXN6 cd16119
Ubiquitin regulatory domain X (UBX) found in UBX domain protein 6 (UBXN6) and similar proteins; ...
 401-474 3.62e-08

Ubiquitin regulatory domain X (UBX) found in UBX domain protein 6 (UBXN6) and similar proteins; UBXN6, also termed UBX domain-containing protein 1 (UBXD1), and UBXDC2, belongs to the UBXD family of proteins that contains the ubiquitin regulatory domain X (UBX) with a beta-grasp ubiquitin-like fold, but without the C-terminal double glycine motif. UBX domain is typically located at the carboxyl terminus of proteins, and participates broadly in the regulation of protein degradation. UBXN6 acts as a cofactor of p97 (also known as VCP or Cdc48), which is a homohexameric AAA ATPase (ATPase associated with a variety of activities) involved in a variety of functions ranging from cell-cycle regulation to membrane fusion and protein degradation. Unlike other p97 cofactors that binds the N-domain of p97 through their UBX domain, UBXN6 binds p97 in two regions, at the p97 C terminus via a PUB domain and at the p97 N-domain with a short linear interaction motif termed VIM. Its UBX domain is not functional for the binding of p97. The UBXN6-p97 complex regulates the endolysosomal sorting of ubiquitylated plasma membrane protein caveolin-1 (CAV1), as well as the trafficking of ERGIC-53-containing vesicles by controlling the interaction of transport factors with the cytoplasmic tail of ERGIC-53. In addition, UBXN6 is a regulatory component of endoplasmic reticulum-associated degradation (ERAD) that may modulate the adaptor binding to p97.


Pssm-ID: 340536  Cd Length: 73  Bit Score: 50.64  E-value: 3.62e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21356345 401 TRLQIRLPGGIQRTKSFPAGEVLATVRVYVRnEMLAaSDVRDFTLATSYPRrefQTEDEVKTLNELNLVPNAVV 474
Cdd:cd16119   2 TLIRVRFPDGVILQGTFYAREKLSAVREFVR-EALA-NDWLPFELVTPGGQ---KLTDEDATLAELGLVPAALL 70
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 273-367 1.42e-07

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: 53.77  E-value: 1.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345   273 EAQDNTESEERLAEVRNILEQKRKERVEEekRMEKENELRRRRDGREAQSQQARAKEQELknmQEQIKRERQEELAARER 352
Cdd:pfam13868 195 KAQDEKAERDELRAKLYQEEQERKERQKE--REEAEKKARQRQELQQAREEQIELKERRL---AEEAEREEEEFERMLRK 269

                          90
                  ....*....|....*
gi 21356345   353 IRAQIAADRAEQAQR 367
Cdd:pfam13868 270 QAEDEEIEQEEAEKR 284
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 280-366 9.36e-07

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


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 51.88  E-value: 9.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345   280 SEERLAEVrnilEQKRKERvEEEKRMEKENELRRRRDGRE-AQSQQARAKEQELKNMQEQIKRERQEELAARERIRAQIA 358
Cdd:pfam15709 343 AEMRRLEV----ERKRREQ-EEQRRLQQEQLERAEKMREElELEQQRRFEEIRLRKQRLEEERQRQEEEERKQRLQLQAA 417


                  ....*...
gi 21356345   359 ADRAEQAQ 366
Cdd:pfam15709 418 QERARQQQ 425
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 268-366 1.44e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.48  E-value: 1.44e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345 268 TQRPLEAQDNTESEERLAEVRNILEQKRKERVEEEKRMEKENELRRRRDGREAQSQQA----RAKEQELKNMQEQIKRER 343
Cdd:COG1196 337 EELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAaaelAAQLEELEEAEEALLERL 416

                        90       100
                ....*....|....*....|...
gi 21356345 344 QEELAARERIRAQIAADRAEQAQ 366
Cdd:COG1196 417 ERLEEELEELEEALAELEEEEEE 439
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 279-367 1.67e-06

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: 50.69  E-value: 1.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345   279 ESEERLAEVRNILEQKRKERVEEEKRMEKENELRR--RRDGREAQSQQARAKEQELKNMQEQIKR------ERQEELAAR 350
Cdd:pfam13868  92 EYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRqlREEIDEFNEEQAEWKELEKEEEREEDERileylkEKAEREEER 171

                          90
                  ....*....|....*..
gi 21356345   351 ERIRAQIAADRAEQAQR 367
Cdd:pfam13868 172 EAEREEIEEEKEREIAR 188
UBX2_UBXN9 cd16118
Ubiquitin regulatory domain X (UBX) 2 found in UBX domain protein 9 (UBXN9, UBXD9, or ASPSCR1) ...
 401-476 3.03e-06

Ubiquitin regulatory domain X (UBX) 2 found in UBX domain protein 9 (UBXN9, UBXD9, or ASPSCR1) and similar proteins; UBXN9, also termed tether containing UBX domain for GLUT4 (TUG), or alveolar soft part sarcoma chromosomal region candidate gene 1 protein (ASPSCR1), or alveolar soft part sarcoma locus (ASPL), or renal papillary cell carcinoma protein 17 (RCC17), belongs to the UBXD family of proteins that contains two ubiquitin regulatory domains X (UBX) with a beta-grasp ubiquitin-like fold, but without the C-terminal double glycine motif. UBX domain is typically located at the carboxyl terminus of proteins, and participates broadly in the regulation of protein degradation. In addition, UBXN9 contains an N-terminal ubiquitin-like (Ubl) domain. UBXN9 functions as a cofactor of p97 (also known as VCP or Cdc48), which is a homohexameric AAA ATPase (ATPase associated with a variety of activities) involved in a variety of functions ranging from cell-cycle regulation to membrane fusion and protein degradation. However, high-affinity interacting protein ASPL efficiently promotes p97 hexamer disassembly, resulting in the formation of stable p97:ASPL heterotetramers; the extended UBX domain (eUBX) in ASPL is critical for p97 hexamer disassembly and facilitates the assembly of p97:ASPL heterotetramers.UBXN9 is involved in insulin-stimulated redistribution of the glucose transporter GLUT4, assembly of the Golgi apparatus. In addition to GLUT4, UBXN9 also controls vesicle translocation by interacting with insulin-regulated aminopeptidase (IRAP), a transmembrane aminopeptidase. UBXN9 and its budding yeast ortholog, Ubx4p, are multifunctional proteins that share some, but not all functions. Yeast Ubx4p is important for endoplasmic reticulum-associated protein degradation (ERAD) but UBXN9 appears not to share this function.


Pssm-ID: 340535  Cd Length: 74  Bit Score: 45.25  E-value: 3.03e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21356345 401 TRLQIRLPGGIQRTKSFPAGEVLATVRVYVRneMLAASDVRDFTLATSYPRREFqtEDEVKTLNELNLVPNAVVLV 476
Cdd:cd16118   1 AVIRVQFPDRLVLQAFFRPLETVRALYDFVK--SHLADPDLPFYLYTTPPKRVL--KDKNKTLYQAGLVPAALVYF 72
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 273-367 7.42e-06

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 48.38  E-value: 7.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345   273 EAQDNTESEERLAEVRNILEQKRKERVEEE----KRMEKENELRRRRDGREAQSQQARAKEQELKNMQEQI--KRERQEE 346
Cdd:pfam13868 175 REEIEEEKEREIARLRAQQEKAQDEKAERDelraKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIelKERRLAE 254

                          90       100
                  ....*....|....*....|....*..
gi 21356345   347 LAARER------IRAQIAADRAEQAQR 367
Cdd:pfam13868 255 EAEREEeefermLRKQAEDEEIEQEEA 281
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 272-367 7.80e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.16  E-value: 7.80e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345 272 LEAQDNTESEERLAEVRNILEQKRKERVEEEKR--MEKENELRRRRDGREAQSQQARAKEQELKNMQEQIKRERQEELAA 349
Cdd:COG1196 294 LAELARLEQDIARLEERRRELEERLEELEEELAelEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373

                        90
                ....*....|....*...
gi 21356345 350 RERIRAQIAADRAEQAQR 367
Cdd:COG1196 374 LAEAEEELEELAEELLEA 391
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 273-366 8.64e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.16  E-value: 8.64e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345 273 EAQDNTESEERLAEVRNILEQKRKERVEEEKRMEKE-NELRRRRDGREAQSQQARAKEQELKNMQEQIKRERQEELAARE 351
Cdd:COG1196 310 RRRELEERLEELEEELAELEEELEELEEELEELEEElEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389

                        90
                ....*....|....*
gi 21356345 352 RIRAQIAADRAEQAQ 366
Cdd:COG1196 390 EALRAAAELAAQLEE 404
PRK12704 PRK12704
phosphodiesterase; Provisional
 272-364 1.19e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 48.24  E-value: 1.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345  272 LEAQD-----NTESEERLAEVRNILEQKRKERVEEEKRMEKENE-LRRRRDGREAQSQQARAKEQELKNMQEQIKRERQE 345
Cdd:PRK12704  60 LEAKEeihklRNEFEKELRERRNELQKLEKRLLQKEENLDRKLElLEKREEELEKKEKELEQKQQELEKKEEELEELIEE 139

                         90
                 ....*....|....*....
gi 21356345  346 ELAARERIrAQIAADRAEQ 364
Cdd:PRK12704 140 QLQELERI-SGLTAEEAKE 157
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 281-367 1.61e-05

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 47.61  E-value: 1.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345   281 EERLAEVRNILEQKRKERVEEEKRMEKENELRR--RRDGREAQSQQARAKEQELKNMQEQIKRERQEELAARERIRAQIA 358
Cdd:pfam13868  36 AEEKEEERRLDEMMEEERERALEEEEEKEEERKeeRKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQ 115


                  ....*....
gi 21356345   359 ADRAEQAQR 367
Cdd:pfam13868 116 AEAEEKLEK 124
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 274-366 2.37e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.62  E-value: 2.37e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345 274 AQDNTESEERLAEVRNI---LEQKRKERVEEEKRMEKENELRRRRDGREAQSQQARAKEQElknMQEQIKRERQEELAAR 350
Cdd:COG1196 249 EELEAELEELEAELAELeaeLEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE---RRRELEERLEELEEEL 325

                        90
                ....*....|....*.
gi 21356345 351 ERIRAQIAADRAEQAQ 366
Cdd:COG1196 326 AELEEELEELEEELEE 341
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 269-367 2.41e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.62  E-value: 2.41e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345 269 QRPLEAQDNTESEERLAEVRNILEQKRKERVEEEKRMEKEN--ELRRRRDGREAQSQQARAKEQELKNMQEQIKRERQEE 346
Cdd:COG1196 389 LEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEAlaELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468

                        90       100
                ....*....|....*....|.
gi 21356345 347 LAARERIRAQIAADRAEQAQR 367
Cdd:COG1196 469 LEEAALLEAALAELLEELAEA 489
PTZ00121 PTZ00121
MAEBL; Provisional
 273-367 4.49e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.06  E-value: 4.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345   273 EAQDNTESEERLAEVRNILEQKRKERVEEEKRMEkenELRRRRDGREAQSQQARAKEQELKNMQEQIKRERQEELAARER 352
Cdd:PTZ00121 1617 EAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAE---ELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEA 1693

                          90
                  ....*....|....*.
gi 21356345   353 I-RAQIAADRAEQAQR 367
Cdd:PTZ00121 1694 LkKEAEEAKKAEELKK 1709
UBX_UBXN2 cd01770
Ubiquitin regulatory domain X (UBX) found in UBX domain-containing proteins UBXN2A, UBXN2B, ...
 402-476 4.83e-05

Ubiquitin regulatory domain X (UBX) found in UBX domain-containing proteins UBXN2A, UBXN2B, NSFL1C/UBXN2C, and similar proteins; This family includes UBX domain-containing proteins UBXN2A, UBXN2B, and NSFL1C/UBXN2C, which contain a SEP (Saccharomyces cerevisiae Shp1, Drosophila melanogaster eyes closed gene (eyc), and vertebrate p47) domain, and a ubiquitin regulatory domain X (UBX) with a beta-grasp ubiquitin-like fold at the C-terminus. UBX domain participates broadly in the regulation of protein degradation. UBXN2A, UBXN2B, and UBXN2C function as the adaptor proteins of p97 (also known as VCP or Cdc48), which is a homohexameric AAA ATPase (ATPase associated with a variety of activities) involved in a variety of functions ranging from cell-cycle regulation to membrane fusion and protein degradation.


Pssm-ID: 340468  Cd Length: 71  Bit Score: 41.78  E-value: 4.83e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21356345 402 RLQIRLPGGIQRTKSFPAGEVLATVRVYVRNEmlAASDVRDFTLATSYPRREFqtEDEVKTLNELNLVpNAVVLV 476
Cdd:cd01770   1 SIQIRLADGSRLVARFNLTHTVGDIRQFIDSA--RPGYSRPFVLMTGFPPKEL--TDESQTLEEAGLL-NAVVVQ 70
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 272-367 4.93e-05

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 46.07  E-value: 4.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345   272 LEAQDNTESEERLAEVrnilEQKRKERVEEEKRMEKENELRRRRDGREAQSQQARAKEQELKNMQE--------QIKRER 343
Cdd:pfam13868  16 LAAKCNKERDAQIAEK----KRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQEleeqieerEQKRQE 91

                          90       100       110
                  ....*....|....*....|....*....|
gi 21356345   344 QEELAARER------IRAQIAADRAEQAQR 367
Cdd:pfam13868  92 EYEEKLQEReqmdeiVERIQEEDQAEAEEK 121
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 269-367 5.71e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.47  E-value: 5.71e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345 269 QRPLEAQDNTESEERLAEVRNILEQKRKERVEEEKRMEKENELRRRRDGR--EAQSQQARAKEQELKNMQEQIKRERQEE 346
Cdd:COG1196 324 ELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAElaEAEEELEELAEELLEALRAAAELAAQLE 403

                        90       100
                ....*....|....*....|.
gi 21356345 347 LAARERIRAQIAADRAEQAQR 367
Cdd:COG1196 404 ELEEAEEALLERLERLEEELE 424
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 273-367 6.09e-05

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 45.68  E-value: 6.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345   273 EAQDNTESEERLAEVRNILEQKRKERVEEEKRMEKENEL-----RRRRDGREAQSQQARAKEQELKNMQEQIKR------ 341
Cdd:pfam13868  64 EEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQmdeivERIQEEDQAEAEEKLEKQRQLREEIDEFNEeqaewk 143

                          90       100
                  ....*....|....*....|....*...
gi 21356345   342 --ERQEELAARERIRAQIAADRAEQAQR 367
Cdd:pfam13868 144 elEKEEEREEDERILEYLKEKAEREEER 171
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 279-367 6.54e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.08  E-value: 6.54e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345 279 ESEERLAEVRNILEQKRKERVEEEKRMEK-ENELRRRRDGREAQSQQARAKEQELKNMQEQIKRE---RQEELAARERIR 354
Cdd:COG1196 243 ELEAELEELEAELEELEAELAELEAELEElRLELEELELELEEAQAEEYELLAELARLEQDIARLeerRRELEERLEELE 322

                        90
                ....*....|...
gi 21356345 355 AQIAADRAEQAQR 367
Cdd:COG1196 323 EELAELEEELEEL 335
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 283-364 7.19e-05

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


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 43.49  E-value: 7.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345   283 RLAEVRNILEQKRKERVEEEKRMEKENELRRRRDGREAQSQQARAKEQELKNMQEQIKRERQEELAARERIRAQIAADRA 362
Cdd:pfam05672  21 RQAREQREREEQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRREEEERQRKAEEEAEEREQREQEEQERLQ 100


                  ..
gi 21356345   363 EQ 364
Cdd:pfam05672 101 KQ 102
CCDC66 pfam15236
Coiled-coil domain-containing protein 66; This protein family, named Coiled-coil ...
 276-367 8.33e-05

Coiled-coil domain-containing protein 66; This protein family, named Coiled-coil domain-containing protein 66 (CCDC) refers to a protein domain found in eukaryotes, and is approximately 160 amino acids in length. CCDC66 protein is detected mainly in the inner segments of photoreceptors in many vertebrates including mice and humans. It has been found in dogs, that a mutation in the CCDC66 gene causes generalized progressive retinal atrophy (gPRA). This shows that the protein encoded for by this gene is vital for healthy vision and guards against photoreceptor cell degeneration. The structure of CCDC66 proteins includes a heptad repeat pattern which contains at least one coiled-coil domain. There are at least two or more alpha-helices which form a cable-like structure.


Pssm-ID: 434558 [Multi-domain]  Cd Length: 154  Bit Score: 43.25  E-value: 8.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345   276 DNTESEERLAEVRNILEQKR--KERVEEEKRMEKENELRRRRDGREAQSQQARAKEQELKNMQEQIKRERQEELAARERI 353
Cdd:pfam15236  40 DPAQLEERERKRQKALEHQNaiKKQLEEKERQKKLEEERRRQEEQEEEERLRREREEEQKQFEEERRKQKEKEEAMTRKT 119

                          90       100
                  ....*....|....*....|..
gi 21356345   354 --------RAQIAADRAEQAQR 367
Cdd:pfam15236 120 qallqamqKAQELAQRLKQEQR 141
Caldesmon pfam02029
Caldesmon;
239-361 8.39e-05

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 45.63  E-value: 8.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345   239 TTSGAAARNFATNNLIPAVPLMTPAVPVPTQRPLEAQDNTESEERLAEVRNILEQKRKERVEE--EKRMEKENEL----- 311
Cdd:pfam02029 205 PEVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLEAEQKLEELRRRRQEKESEEFEKlrQKQQEAELELeelkk 284

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 21356345   312 --RRRRDGREAQSQQARAKEQELKNMQEQIKRERQEELaarERIRAQIAADR 361
Cdd:pfam02029 285 krEERRKLLEEEEQRRKQEEAERKLREEEEKRRMKEEI---ERRRAEAAEKR 333
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 286-367 8.53e-05

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


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 43.11  E-value: 8.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345   286 EVRNILEQKR------KERvEEEKRMEKENELRRRRDGREAQSQQARAK-EQELKNMQEQIKRERQEELAARERIRAQIA 358
Cdd:pfam05672  11 EAARILAEKRrqareqRER-EEQERLEKEEEERLRKEELRRRAEEERARrEEEARRLEEERRREEEERQRKAEEEAEERE 89


                  ....*....
gi 21356345   359 ADRAEQAQR 367
Cdd:pfam05672  90 QREQEEQER 98
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 279-363 8.66e-05

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 45.29  E-value: 8.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345   279 ESEERLAEVRNILEQKRKER-------VEEEKRMEKENELRRRRdGREAQSQQARAKEQELK----NMQEQIKRERQEEL 347
Cdd:pfam13868 167 REEEREAEREEIEEEKEREIarlraqqEKAQDEKAERDELRAKL-YQEEQERKERQKEREEAekkaRQRQELQQAREEQI 245

                          90
                  ....*....|....*..
gi 21356345   348 AARERIRA-QIAADRAE 363
Cdd:pfam13868 246 ELKERRLAeEAEREEEE 262
PTZ00121 PTZ00121
MAEBL; Provisional
 269-367 1.01e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.90  E-value: 1.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345   269 QRPLEAQDNTESEE-RLAEVRNILEQKRKERVEEEKRMEKEN----ELRRRRDGREAQSQQARAKEQELKNMQEQIKRER 343
Cdd:PTZ00121 1632 KKKVEQLKKKEAEEkKKAEELKKAEEENKIKAAEEAKKAEEDkkkaEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKE 1711

                          90       100
                  ....*....|....*....|....*.
gi 21356345   344 QEELAARERIRA--QIAADRAEQAQR 367
Cdd:PTZ00121 1712 AEEKKKAEELKKaeEENKIKAEEAKK 1737
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 279-367 1.14e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.31  E-value: 1.14e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345 279 ESEERLAEVRNILEQKRKERVEEEKRMEKENELRRRRDGREAQSQQARakeQELKNMQEQIKRERQEELAARERIrAQIA 358
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELR---LELEELELELEEAQAEEYELLAEL-ARLE 301


                ....*....
gi 21356345 359 ADRAEQAQR 367
Cdd:COG1196 302 QDIARLEER 310
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 281-367 1.17e-04

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 44.91  E-value: 1.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345   281 EERLAEVRNILEQKRKERvEEEKRMEKENELRRRrdgREAQSQQARAKEQELKNMQEQIKRER----QEELAARERIRAQ 356
Cdd:pfam13868 149 EEREEDERILEYLKEKAE-REEEREAEREEIEEE---KEREIARLRAQQEKAQDEKAERDELRaklyQEEQERKERQKER 224

                          90
                  ....*....|.
gi 21356345   357 IAADRAEQAQR 367
Cdd:pfam13868 225 EEAEKKARQRQ 235
PTZ00121 PTZ00121
MAEBL; Provisional
 243-367 1.19e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.52  E-value: 1.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345   243 AAARNFATNNLIPAVPLMTPAVPVPTQRPLEAQDNTESEERLAEVRNILEQKRKE---RVEEEKRMEKENEL---RRRRD 316
Cdd:PTZ00121 1083 AKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEdarKAEEARKAEDAKRVeiaRKAED 1162

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 21356345   317 GREAQSQQARAKEQELKNMQEQIKRERQEELAARERIRAQIAADRAEQAQR 367
Cdd:PTZ00121 1163 ARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERK 1213
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 269-350 1.62e-04

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


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 44.56  E-value: 1.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345   269 QRPLEAQDNTESEERLAEVRNILEQK-RKERVEEEkRMEKENELRRRRDGREAQSQQARAKEQELKNMQEQIKRERQEEL 347
Cdd:pfam15709 365 QEQLERAEKMREELELEQQRRFEEIRlRKQRLEEE-RQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQEE 443


                  ...
gi 21356345   348 AAR 350
Cdd:pfam15709 444 AER 446
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 269-367 1.67e-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: 44.73  E-value: 1.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345   269 QRPLEAQDNTESEERLAEVRNILEQKRKERVEEEKRMEKENELRRRRDGREAQSQQARAKEQELKNMQEQIKRERQEELA 348
Cdd:pfam17380 459 QQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREA 538

                          90
                  ....*....|....*....
gi 21356345   349 ARERiRAQIAADRAEQAQR 367
Cdd:pfam17380 539 EEER-RKQQEMEERRRIQE 556
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 281-362 1.69e-04

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 44.14  E-value: 1.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345   281 EERLAEVRNILEQKRKERVEEE---KRMEKENELRRRRDGREAQSQQARAKE--QELKNM----QEQIKRERQEELAARE 351
Cdd:pfam13868 239 QAREEQIELKERRLAEEAEREEeefERMLRKQAEDEEIEQEEAEKRRMKRLEhrRELEKQieerEEQRAAEREEELEEGE 318

                          90
                  ....*....|.
gi 21356345   352 RIRAQIAADRA 362
Cdd:pfam13868 319 RLREEEAERRE 329
Pinin_SDK_memA pfam04696
pinin/SDK/memA/ protein conserved region; Members of this family have very varied ...
 275-347 1.82e-04

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


Pssm-ID: 461396 [Multi-domain]  Cd Length: 130  Bit Score: 41.89  E-value: 1.82e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21356345   275 QDNTESEERLAEVrnilEQKRKE---RVEEEKRMEKENELRRRRDGREAQSQQARAKEQELKNMQEQIKRERQEEL 347
Cdd:pfam04696  19 QKFKKEESKQKEK----EERRAEiekRLEEKAKQEKEELEERKREEREELFEERRAEQIELRALEEKLELKELMET 90
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
282-367 2.00e-04

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 44.09  E-value: 2.00e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345 282 ERLAEVRNIleqKRKERVEEEKRMEKENELRRRRDGREAQSQQARA------------KEQELKNMQEQIKRERQEELAA 349
Cdd:COG2268 220 NREAEEAEL---EQEREIETARIAEAEAELAKKKAEERREAETARAeaeaayeiaeanAEREVQRQLEIAEREREIELQE 296

                        90       100
                ....*....|....*....|....*...
gi 21356345 350 RER----------IRAQIAADRAEQAQR 367
Cdd:COG2268 297 KEAereeaeleadVRKPAEAEKQAAEAE 324
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 274-367 2.50e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.54  E-value: 2.50e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345 274 AQDNTESEERLAEVRNILEQK----RKERVEEEKRMEKENELRRRRDGREAQSQQARAKEQELKNMQEQIKrERQEELAA 349
Cdd:COG1196 277 EELELELEEAQAEEYELLAELarleQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELE-EAEEELEE 355

                        90
                ....*....|....*...
gi 21356345 350 RERIRAQIAADRAEQAQR 367
Cdd:COG1196 356 AEAELAEAEEALLEAEAE 373
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 269-357 2.74e-04

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 43.75  E-value: 2.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345   269 QRPLEAQDNTESEERLAEVRNILEQKRKERVEEEKRMEKE----NELRRRRDGREAQSQQARAKEQELKNMQEQIKRERQ 344
Cdd:pfam13868 249 ERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRlehrRELEKQIEEREEQRAAEREEELEEGERLREEEAERR 328

                          90
                  ....*....|...
gi 21356345   345 EELaarERIRAQI 357
Cdd:pfam13868 329 ERI---EEERQKK 338
PTZ00121 PTZ00121
MAEBL; Provisional
 273-354 2.74e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.36  E-value: 2.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345   273 EAQDNTESEERLAEVRNILEQKRK-----ERVEEEKRmeKENELRRRRDGREAQSQQARAKEQELKNMQEQIKRERQEEL 347
Cdd:PTZ00121 1666 EAKKAEEDKKKAEEAKKAEEDEKKaaealKKEAEEAK--KAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDK 1743


                  ....*..
gi 21356345   348 AARERIR 354
Cdd:PTZ00121 1744 KKAEEAK 1750
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
279-370 3.13e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.99  E-value: 3.13e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345 279 ESEERLAEVRNILEQKRKERVEEEK------RMEKENELRRRRDGREAQSQQARAKEQELKNMQEQIKRERQEELAARER 352
Cdd:COG4717  99 ELEEELEELEAELEELREELEKLEKllqllpLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEE 178

                        90
                ....*....|....*...
gi 21356345 353 IRAQIAADRAEQAQRFNT 370
Cdd:COG4717 179 LEELLEQLSLATEEELQD 196
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 274-356 3.52e-04

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 42.60  E-value: 3.52e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345 274 AQDNTESEERLAEVRNILEQKRKERVEEEKRMEK-ENELRRRRDGREAQSQQARAKEQELKNMQEQIKRERQEELAAR-E 351
Cdd:COG1579 102 KRRISDLEDEILELMERIEELEEELAELEAELAElEAELEEKKAELDEELAELEAELEELEAEREELAAKIPPELLALyE 181


                ....*
gi 21356345 352 RIRAQ 356
Cdd:COG1579 182 RIRKR 186
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 165-369 3.57e-04

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 43.92  E-value: 3.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345   165 DPETTSVSNSPTGGVEEAKTNPPNSPVAAsLASIPAAVSTSSLEgkSGSEAEAASPTAlaaekraaaskvegsATTSGAA 244
Cdd:PRK10263  532 EPVKEPEPIKSSLKAPSVAAVPPVEAAAA-VSPLASGVKKATLA--TGAAATVAAPVF---------------SLANSGG 593

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345   245 ARNFATNNLIPAVPlMTPAVPVPTQRPLEAQDNTESEERLAEVRNILEQKRKERVEEEKRMEKENELRRRRDGRE-AQSQ 323
Cdd:PRK10263  594 PRPQVKEGIGPQLP-RPKRIRVPTRRELASYGIKLPSQRAAEEKAREAQRNQYDSGDQYNDDEIDAMQQDELARQfAQTQ 672

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 21356345   324 QARAKEQELKNMQEQIKrerQEELAARERIRAQIAadrAEQAQRFN 369
Cdd:PRK10263  673 QQRYGEQYQHDVPVNAE---DADAAAEAELARQFA---QTQQQRYS 712
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
278-367 3.99e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.49  E-value: 3.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345  278 TESEERLAEVRNILEQKRKERVEEEKRMEK-------ENELRRRRDGREAQSQQARAKEQELKNMQEQI--KRERQEEL- 347
Cdd:PRK02224 471 EEDRERVEELEAELEDLEEEVEEVEERLERaedlveaEDRIERLEERREDLEELIAERRETIEEKRERAeeLRERAAELe 550

                         90       100
                 ....*....|....*....|..
gi 21356345  348 --AARERIRAQIAADRAEQAQR 367
Cdd:PRK02224 551 aeAEEKREAAAEAEEEAEEARE 572
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
278-366 4.10e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.75  E-value: 4.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345  278 TESEERLAEVRNILEQ---KRKERVEEEKRmEKENELRRRRDGREAQSQQAR-------AKEQELKNMQEQIKRERQEEL 347
Cdd:COG4913  319 DALREELDELEAQIRGnggDRLEQLEREIE-RLERELEERERRRARLEALLAalglplpASAEEFAALRAEAAALLEALE 397

                         90
                 ....*....|....*....
gi 21356345  348 AARERIRAQIAADRAEQAQ 366
Cdd:COG4913  398 EELEALEEALAEAEAALRD 416
Casc1_N pfam15927
Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally ...
 295-372 4.46e-04

Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally uncharacterized. This domain family is found in eukaryotes, and is approximately 200 amino acids in length. The family is found in association with pfam12366. There are two completely conserved residues (N and W) that may be functionally important.


Pssm-ID: 464947 [Multi-domain]  Cd Length: 201  Bit Score: 41.96  E-value: 4.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345   295 RKERVEEEKRMEKENELRRrrdgREAQSQQARAKEQELKNMQEQIKRERQE---ELAARERIRAQIAADRAEQAQ--RFN 369
Cdd:pfam15927   1 ARLREEEEERLRAEEEEAE----RLEEERREEEEEERLAAEQDRRAEELEElkhLLEERKEALEKLRAEAREEAEweRYM 76


                  ...
gi 21356345   370 TPD 372
Cdd:pfam15927  77 RCD 79
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 274-367 5.19e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 42.83  E-value: 5.19e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345 274 AQDNTESEERLAEVRNILEQKRKERVEEEKRMEK-ENELRRRRDGREAQSQQARAKEQELKNMQEQIKRERQEElaarER 352
Cdd:COG4942  19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKAlLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI----AE 94

                        90
                ....*....|....*
gi 21356345 353 IRAQIAADRAEQAQR 367
Cdd:COG4942  95 LRAELEAQKEELAEL 109
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 279-360 5.29e-04

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 42.22  E-value: 5.29e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345 279 ESEERLAEVRNI---------LEQKRKERVEEEKRM--------EKENELRRRRDGREAQSQQARAKEQELKNMQEQIKR 341
Cdd:COG1579  77 KYEEQLGNVRNNkeyealqkeIESLKRRISDLEDEIlelmerieELEEELAELEAELAELEAELEEKKAELDEELAELEA 156

                        90
                ....*....|....*....
gi 21356345 342 ERQEELAARERIRAQIAAD 360
Cdd:COG1579 157 ELEELEAEREELAAKIPPE 175
CCDC34 pfam13904
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ...
 279-366 5.29e-04

Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.


Pssm-ID: 464032 [Multi-domain]  Cd Length: 221  Bit Score: 42.00  E-value: 5.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345   279 ESEERLAEVRNILEQ-------KRKERVEEEKRMEKENEL-------RRRRDGRE--AQSQQARAKEQELKNMQEQiKRE 342
Cdd:pfam13904  80 EKEEQEAELRKRLAKekyqewlQRKARQQTKKREESHKQKaaesaskSLAKPERKvsQEEAKEVLQEWERKKLEQQ-QRK 158

                          90       100
                  ....*....|....*....|....
gi 21356345   343 RQEELAARERiRAQIAADRAEQAQ 366
Cdd:pfam13904 159 REEEQREQLK-KEEEEQERKQLAE 181
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 272-367 5.51e-04

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


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 42.56  E-value: 5.51e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345 272 LEAQDNTESEERLAEVRNILEQKRKERVEEEKRMEKENELRRrrdgREAQSQQARAK-EQELKNMQEQIKRERQEELAAR 350
Cdd:cd16269 193 LTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQERS----YEEHLRQLKEKmEEERENLLKEQERALESKLKEQ 268

                        90
                ....*....|....*..
gi 21356345 351 ERIRAQIAADRAEQAQR 367
Cdd:cd16269 269 EALLEEGFKEQAELLQE 285
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 272-367 6.35e-04

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 42.60  E-value: 6.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345   272 LEAQDNTESEERLAEVRNILEQKRKERVE---------EEKRMEKENEL-RRRRDGREAQSQQARAKEQELKNMQEQiKR 341
Cdd:pfam13868  45 LDEMMEEERERALEEEEEKEEERKEERKRyrqeleeqiEEREQKRQEEYeEKLQEREQMDEIVERIQEEDQAEAEEK-LE 123

                          90       100
                  ....*....|....*....|....*.
gi 21356345   342 ERQEELAARERIRAQIAADRAEQAQR 367
Cdd:pfam13868 124 KQRQLREEIDEFNEEQAEWKELEKEE 149
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
 279-367 6.41e-04

Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.


Pssm-ID: 464768 [Multi-domain]  Cd Length: 374  Bit Score: 42.33  E-value: 6.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345   279 ESEERLAEVRNilEQKRKERVEEEKRMEKENELRRRRDGREAQSQQ----ARAKEQELKNMQEQIKRERQEEL-AARERI 353
Cdd:pfam15558  66 EKEQRKARLGR--EERRRADRREKQVIEKESRWREQAEDQENQRQEklerARQEAEQRKQCQEQRLKEKEEELqALREQN 143

                          90
                  ....*....|....
gi 21356345   354 RaQIAADRAEQAQR 367
Cdd:pfam15558 144 S-LQLQERLEEACH 156
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
272-353 6.61e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.13  E-value: 6.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345  272 LEAQDNTESEERLAEVRNILEQKRKE--------RVEEEKRMEKEN-ELRRRRDGREAQSQQARAKEQELKNMQEQIKRE 342
Cdd:PRK03918 623 KLEEELDKAFEELAETEKRLEELRKEleelekkySEEEYEELREEYlELSRELAGLRAELEELEKRREEIKKTLEKLKEE 702

                         90
                 ....*....|.
gi 21356345  343 RQEELAARERI 353
Cdd:PRK03918 703 LEEREKAKKEL 713
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
 279-367 6.93e-04

Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.


Pssm-ID: 464768 [Multi-domain]  Cd Length: 374  Bit Score: 42.33  E-value: 6.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345   279 ESEERLAEVRNILEQKRKERVEEEKRM---EKEN-------ELRRRRDGREAQSQQARAKEQELKNMQEQIKRERQEELA 348
Cdd:pfam15558  36 ELRRRDQKRQETLERERRLLLQQSQEQwqaEKEQrkarlgrEERRRADRREKQVIEKESRWREQAEDQENQRQEKLERAR 115

                          90
                  ....*....|....*....
gi 21356345   349 ARERIRAQiaadraEQAQR 367
Cdd:pfam15558 116 QEAEQRKQ------CQEQR 128
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
279-370 7.90e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.45  E-value: 7.90e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345 279 ESEERLAEVRNILEQKRKERVE-EEKRMEKENELRRRRDGREAQS--QQARAKEQELKNMQEQIK--RERQEELAARERI 353
Cdd:COG4717  85 EKEEEYAELQEELEELEEELEElEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERLEelEERLEELRELEEE 164

                        90
                ....*....|....*..
gi 21356345 354 RAQIAADRAEQAQRFNT 370
Cdd:COG4717 165 LEELEAELAELQEELEE 181
PTZ00121 PTZ00121
MAEBL; Provisional
 269-346 7.93e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.82  E-value: 7.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345   269 QRPLEAQDNTESEERLAEVRNILEQKRKERVEEEKRMEKEN-----ELRRRRDGREAQSQQARAKEQELKNMQEQIKRER 343
Cdd:PTZ00121 1674 KKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEkkkaeELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDE 1753


                  ...
gi 21356345   344 QEE 346
Cdd:PTZ00121 1754 EEK 1756
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
279-363 8.75e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.59  E-value: 8.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345  279 ESEERLAEVRNILEQkRKERVEEEkRMEKENELRRRRDGREAQSQQARAKEQELKNMQEQIKRERQEELAARERIRAQIA 358
Cdd:COG4913  377 ASAEEFAALRAEAAA-LLEALEEE-LEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALG 454


                 ....*
gi 21356345  359 ADRAE 363
Cdd:COG4913  455 LDEAE 459
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
269-366 9.46e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.45  E-value: 9.46e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345 269 QRPLEAQDNTESEErlaEVRNILEQKRKERVEEEKRMEKENELRRRRDGREAQSQQAraKEQELKNMQEQIKRERQEELA 348
Cdd:COG4717 372 IAALLAEAGVEDEE---ELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEAL--DEEELEEELEELEEELEELEE 446

                        90
                ....*....|....*...
gi 21356345 349 ARERIRAQIAADRAEQAQ 366
Cdd:COG4717 447 ELEELREELAELEAELEQ 464
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 292-366 9.91e-04

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


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 39.52  E-value: 9.91e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21356345   292 EQKRKERVEEEKRMEK-ENELRRRRDGREAQSQQARAKEQELKNMQEQIKR---ERQEELAARERIRAQIAADRAEQAQ 366
Cdd:pfam20492   2 EEAEREKQELEERLKQyEEETKKAQEELEESEETAEELEEERRQAEEEAERleqKRQEAEEEKERLEESAEMEAEEKEQ 80
PTZ00121 PTZ00121
MAEBL; Provisional
 270-367 1.04e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 1.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345   270 RPLEAQDNTESEERLAEVRNILEQKRKERV----------EEEKRMEKE---NELRRRRDGREAQSQQARA--------K 328
Cdd:PTZ00121 1200 RKAEAARKAEEERKAEEARKAEDAKKAEAVkkaeeakkdaEEAKKAEEErnnEEIRKFEEARMAHFARRQAaikaeearK 1279

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 21356345   329 EQELKNMQEqiKRERQEELAARERIRAQIAADRAEQAQR 367
Cdd:PTZ00121 1280 ADELKKAEE--KKKADEAKKAEEKKKADEAKKKAEEAKK 1316
ARGLU pfam15346
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...
 267-367 1.06e-03

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


Pssm-ID: 405931 [Multi-domain]  Cd Length: 151  Bit Score: 40.03  E-value: 1.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345   267 PTQRPLEAQDNTESEERLAEVRNILEQKRKERVEEEKR-MEKE--NELRRRRdgreaqsqQARAKEQELKNMQEQIKRER 343
Cdd:pfam15346  11 ETARRVEEAVAKRVEEELEKRKDEIEAEVERRVEEARKiMEKQvlEELERER--------EAELEEERRKEEEERKKREE 82

                          90       100
                  ....*....|....*....|....
gi 21356345   344 QEELaARERIRaqiaadRAEQAQR 367
Cdd:pfam15346  83 LERI-LEENNR------KIEEAQR 99
Caldesmon pfam02029
Caldesmon;
267-367 1.11e-03

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 42.16  E-value: 1.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345   267 PTQRPLEAQDNTESEERLAEVRNILEQKRKE---RVEEEKRMEkenELRRRRDGREAQ-SQQARAKEQELKNMQEQIKRE 342
Cdd:pfam02029 209 SQNGEEEVTKLKVTTKRRQGGLSQSQEREEEaevFLEAEQKLE---ELRRRRQEKESEeFEKLRQKQQEAELELEELKKK 285

                          90       100
                  ....*....|....*....|....*
gi 21356345   343 RQEELAARERIRAQIAADRAEQAQR 367
Cdd:pfam02029 286 REERRKLLEEEEQRRKQEEAERKLR 310
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
281-368 1.17e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.06  E-value: 1.17e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345 281 EERLAEVRNILEQKRKERVEEEKRM--EKENELRRRRDGREAQSQQARAKEQELKNMQEQIKRERQEELAARERIRAQIA 358
Cdd:COG4717 162 EEELEELEAELAELQEELEELLEQLslATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAAL 241

                        90
                ....*....|
gi 21356345 359 ADRAEQAQRF 368
Cdd:COG4717 242 EERLKEARLL 251
PTZ00121 PTZ00121
MAEBL; Provisional
 273-366 1.18e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 1.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345   273 EAQDNTESEERLAEVRNILEQKRKERV----EEEKRMEKEnELRRRRDGReAQSQQARaKEQELKNMQEQIKRERQEELA 348
Cdd:PTZ00121 1571 KAEEDKNMALRKAEEAKKAEEARIEEVmklyEEEKKMKAE-EAKKAEEAK-IKAEELK-KAEEEKKKVEQLKKKEAEEKK 1647

                          90
                  ....*....|....*...
gi 21356345   349 ARERIRAQIAADRAEQAQ 366
Cdd:PTZ00121 1648 KAEELKKAEEENKIKAAE 1665
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 275-359 1.23e-03

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


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 39.34  E-value: 1.23e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345 275 QDNTESEERLAEVRNILEQKRKERVE--EEKRMEKENELRRRRDgrEAQSQQARAKEQElknmQEQIKRERQeelAARER 352
Cdd:cd06503  44 KAKEEAEELLAEYEEKLAEARAEAQEiiEEARKEAEKIKEEILA--EAKEEAERILEQA----KAEIEQEKE---KALAE 114


                ....*..
gi 21356345 353 IRAQIAA 359
Cdd:cd06503 115 LRKEVAD 121
CDC3 COG5019
Septin family protein [Cell cycle control, cell division, chromosome partitioning, ...
 289-357 1.30e-03

Septin family protein [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];


Pssm-ID: 227352 [Multi-domain]  Cd Length: 373  Bit Score: 41.54  E-value: 1.30e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21356345 289 NILEQKRKERVEEEKR-----MEKENELRRRRDGREAQS---QQARAKEQELKNMQEQIKRERQEELAARERIRAQI 357
Cdd:COG5019 282 LLYENYRTEKLSGLKNsgepsLKEIHEARLNEEERELKKkftEKIREKEKRLEELEQNLIEERKELNSKLEEIQKKL 358
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
275-367 1.33e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.43  E-value: 1.33e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345 275 QDNTESEERLAEVRNILEQKRKERVEEEKRM-EKENELRRRRDGREAQSQQARAKEQELKNMQEQIKR---ERQEELAAR 350
Cdd:COG4372  52 EELEQAREELEQLEEELEQARSELEQLEEELeELNEQLQAAQAELAQAQEELESLQEEAEELQEELEElqkERQDLEQQR 131

                        90
                ....*....|....*..
gi 21356345 351 ERIRAQIAADRAEQAQR 367
Cdd:COG4372 132 KQLEAQIAELQSEIAER 148
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 263-367 1.34e-03

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 42.03  E-value: 1.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345   263 AVPVPTQRPLEaQDNTESEERLAEVRNILEQKRKERVEEEKRMEK-------------------ENELRRRRDGREAQSQ 323
Cdd:pfam17380 371 AMEISRMRELE-RLQMERQQKNERVRQELEAARKVKILEEERQRKiqqqkvemeqiraeqeearQREVRRLEEERAREME 449

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 21356345   324 QARAKEQElknMQEQIKRERQEElaaRERIRAQIAADRAEQAQR 367
Cdd:pfam17380 450 RVRLEEQE---RQQQVERLRQQE---EERKRKKLELEKEKRDRK 487
Phosducin pfam02114
Phosducin;
279-493 1.35e-03

Phosducin;


Pssm-ID: 251094 [Multi-domain]  Cd Length: 265  Bit Score: 41.21  E-value: 1.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345   279 ESEERLAEVRNILEQKRKERVEEEKRMEKENELRRRRDGREAQSQQARAKEQEL-------KNMQEQIKRERQEELAARE 351
Cdd:pfam02114  39 ESEDRDEQAHEKEEIIKKLSMSCRSHLDEEEEQQDDKDLKEKFSGKMSLKECELidkdkddEECLQKYRKQCMDDMHQKL 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345   352 RIRAQIAA-----------DRAEQAQRFNTPDISSTTNSVAATAASN--VITTDASVSSVDETRLQIRLPGGIQRTKSfp 418
Cdd:pfam02114 119 HFGPQFGFvleiesgegflDMIDKEQKITLIMVHIYEDGIKGCDALNgcLICLAAEYPMVKFCKIKASNIGAGDRFSR-- 196

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21356345   419 agEVLATVRVYVRNEMLAasdvrDFTLATSYPRREFQTEDEVKTLNELNLVPNAVVLVLTKEQVNRVVQSGGSLM 493
Cdd:pfam02114 197 --DALPALLIYKAGELIG-----NFIRVTDQLAEDFFAGDLEAFLNEFGLLPEKEMHVLEQTNMSATCHSEDEDL 264
DUF4200 pfam13863
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ...
 281-354 1.40e-03

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


Pssm-ID: 464003 [Multi-domain]  Cd Length: 119  Bit Score: 39.09  E-value: 1.40e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21356345   281 EERLAEVRNILEQKR---KERVEEEKRMEKENELRRRRDGREAQ--SQQARAKEQELKNMQEQIKRERQEELAARERIR 354
Cdd:pfam13863  26 EELLKQREEELEKKEqelKEDLIKFDKFLKENDAKRRRALKKAEeeTKLKKEKEKEIKKLTAQIEELKSEISKLEEKLE 104
PTZ00121 PTZ00121
MAEBL; Provisional
 279-367 1.45e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.05  E-value: 1.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345   279 ESEERLAEVRNILEQKRK----ERVEEEKRMEKENELRRRRDGREAQSQQARAKEQELKNMQEQIKRE--RQEELAARER 352
Cdd:PTZ00121 1494 EAKKKADEAKKAAEAKKKadeaKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEekKKAEEAKKAE 1573

                          90
                  ....*....|....*
gi 21356345   353 IRAQIAADRAEQAQR 367
Cdd:PTZ00121 1574 EDKNMALRKAEEAKK 1588
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 269-367 1.62e-03

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


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 41.48  E-value: 1.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345   269 QRPLEAQDNTESEERLAEVRNILEQKRKERVEEEKRmEKENELRRRRDGREAqsQQARAKEQELKNMQEQIKRE--RQEE 346
Cdd:pfam15709 394 QRLEEERQRQEEEERKQRLQLQAAQERARQQQEEFR-RKLQELQRKKQQEEA--ERAEAEKQRQKELEMQLAEEqkRLME 470

                          90       100
                  ....*....|....*....|.
gi 21356345   347 LAARERIRAQIAADRAEQAQR 367
Cdd:pfam15709 471 MAEEERLEYQRQKQEAEEKAR 491
PTZ00121 PTZ00121
MAEBL; Provisional
 281-367 1.75e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.67  E-value: 1.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345   281 EERLAEVRNILEQKRKERVEEEKRMEKE----NELRRRRDGREAQSQQARAKEQELKNmQEQIKRERQEEL--AARERIR 354
Cdd:PTZ00121 1591 EARIEEVMKLYEEEKKMKAEEAKKAEEAkikaEELKKAEEEKKKVEQLKKKEAEEKKK-AEELKKAEEENKikAAEEAKK 1669

                          90
                  ....*....|...
gi 21356345   355 AQIAADRAEQAQR 367
Cdd:PTZ00121 1670 AEEDKKKAEEAKK 1682
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
273-370 1.77e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.29  E-value: 1.77e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345 273 EAQDNTESEERLAEVRNILEQKRKERVEEEKRMEkenELRRRRDGREAQSQQARAKEQELKNMQEQIKRERQEELAARER 352
Cdd:COG4717 116 EELEKLEKLLQLLPLYQELEALEAELAELPERLE---ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEE 192

                        90
                ....*....|....*...
gi 21356345 353 IRAQIAADRAEQAQRFNT 370
Cdd:COG4717 193 ELQDLAEELEELQQRLAE 210
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
291-367 1.94e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.29  E-value: 1.94e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345 291 LEQKRKERVEEEKRMEKENELRRRRDGREAQSQQARAKEQELKNMQEQIKRERQ--EELAARERIRAQIAA--DRAEQAQ 366
Cdd:COG4717  73 LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQllPLYQELEALEAELAElpERLEELE 152


                .
gi 21356345 367 R 367
Cdd:COG4717 153 E 153
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
279-352 2.36e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.20  E-value: 2.36e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21356345  279 ESEERLAEVRNILEQKRKERVEEEKRMEKENELRRRRDGREaqsQQARAKEQELKNMQEQI--KRERQEELAARER 352
Cdd:PRK03918 211 EISSELPELREELEKLEKEVKELEELKEEIEELEKELESLE---GSKRKLEEKIRELEERIeeLKKEIEELEEKVK 283
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
274-366 2.55e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.66  E-value: 2.55e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345 274 AQDNTESEERLAEVRNILEQKRKERVEEEKRMEK-ENELRRRRDGREAQSQQARAKEQELKNMQEQIKrERQEELAAR-- 350
Cdd:COG4372  30 SEQLRKALFELDKLQEELEQLREELEQAREELEQlEEELEQARSELEQLEEELEELNEQLQAAQAELA-QAQEELESLqe 108

                        90
                ....*....|....*...
gi 21356345 351 --ERIRAQIAADRAEQAQ 366
Cdd:COG4372 109 eaEELQEELEELQKERQD 126
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 273-367 2.67e-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: 40.29  E-value: 2.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345   273 EAQDNTESEERLAEVRNI-LEQKRKERVEEEKRMEKENE--LRRRRDGRE---AQSQQARAKEQELKN-MQEQIKRERQE 345
Cdd:pfam13868 226 EAEKKARQRQELQQAREEqIELKERRLAEEAEREEEEFErmLRKQAEDEEieqEEAEKRRMKRLEHRReLEKQIEEREEQ 305

                          90       100
                  ....*....|....*....|..
gi 21356345   346 ELAARERIRAQIAADRAEQAQR 367
Cdd:pfam13868 306 RAAEREEELEEGERLREEEAER 327
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 271-367 2.68e-03

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 41.11  E-value: 2.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345    271 PLEAQDNTESEERLA-EVRNILEQKRKERVEEEKrMEKENELRRRRDGREAQSQQARAKEQELK-------NMQEQIKRE 342
Cdd:TIGR00618  211 PCMPDTYHERKQVLEkELKHLREALQQTQQSHAY-LTQKREAQEEQLKKQQLLKQLRARIEELRaqeavleETQERINRA 289

                           90       100
                   ....*....|....*....|....*.
gi 21356345    343 RQ-EELAARERIRAQIAADRAEQAQR 367
Cdd:TIGR00618  290 RKaAPLAAHIKAVTQIEQQAQRIHTE 315
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
275-363 2.82e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.79  E-value: 2.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345  275 QDNTESEERLAEVRNILE-------------QKRKERVE-EEKRMEKENELRRRRDG-----REAQSQQARAKEQELKNM 335
Cdd:PRK02224 582 AELKERIESLERIRTLLAaiadaedeierlrEKREALAElNDERRERLAEKRERKREleaefDEARIEEAREDKERAEEY 661

                         90       100
                 ....*....|....*....|....*...
gi 21356345  336 QEQIKRERQEELAARERIRAQIAADRAE 363
Cdd:PRK02224 662 LEQVEEKLDELREERDDLQAEIGAVENE 689
UBX_UBXN7 cd01773
Ubiquitin regulatory domain X (UBX) found in UBX domain protein 7 (UBXN7) and similar proteins; ...
 401-476 2.93e-03

Ubiquitin regulatory domain X (UBX) found in UBX domain protein 7 (UBXN7) and similar proteins; UBXN7, also termed UBX domain-containing protein 7 (UBXD7), belongs to the UBXD family of proteins that contains the ubiquitin regulatory domain X (UBX) with a beta-grasp ubiquitin-like fold, but without the C-terminal double glycine motif. UBX domain is typically located at the carboxyl terminus of proteins, and participates broadly in the regulation of protein degradation. UBXN7 functions as a ubiquitin-binding adaptor that mediates the interaction between the AAA+ ATPase p97 (also known as VCP or Cdc48) and the transcription factor HIF1-alpha. It binds only to the active, NEDD8- or Rub1-modified form of cullins. In addition to having a UBX domain, UBXD7 contains a ubiquitin-associated (UBA), ubiquitin-associating (UAS), and ubiquitin-interacting motif (UIM) domains. Either UBA or UIM could serve as a docking site for neddylated-cullins. UBA domain is required for binding ubiquitylated-protein substrates, while the UIM motif is responsible for the binding to cullin RING ligases (CRLs), and the UBX domain is essential for p97 binding.


Pssm-ID: 340471  Cd Length: 76  Bit Score: 36.84  E-value: 2.93e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21356345 401 TRLQIRLPGGIQRTKSFPAGEVLATVRVYVRNEmlaASDVRDFTLATSYPRREFQTEDEVKTLNELNLVPNAVVLV 476
Cdd:cd01773   2 SKLMLRFPDGKREQLSLPASAKLKALVKYVSSK---GYPNERYELVTNFPRRKLSHLDYDITLKEAGLCPQETIFV 74
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 269-353 2.99e-03

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


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 38.87  E-value: 2.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345   269 QRPLEAQDNTESEER-LAEVRN----ILEQKRKERVEEEKRMEKENELRRRRDGREAQSQQARAKEQELKNMQEQIKRER 343
Cdd:pfam05672  50 RRAEEERARREEEARrLEEERRreeeERQRKAEEEAEEREQREQEEQERLQKQKEEAEAKAREEAERQRQEREKIMQQEE 129

                          90
                  ....*....|
gi 21356345   344 QEELAARERI 353
Cdd:pfam05672 130 QERLERKKRI 139
PTZ00121 PTZ00121
MAEBL; Provisional
 273-367 3.06e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.89  E-value: 3.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345   273 EAQDNTESEERLAEVRNILEQKRK-----ERVEEEKRME---KENELRRRRDGREAQSQQARAKEQELKNMQEQikRERQ 344
Cdd:PTZ00121 1435 EAKKKAEEAKKADEAKKKAEEAKKaeeakKKAEEAKKADeakKKAEEAKKADEAKKKAEEAKKKADEAKKAAEA--KKKA 1512

                          90       100
                  ....*....|....*....|...
gi 21356345   345 EELAARERIRAQIAADRAEQAQR 367
Cdd:PTZ00121 1513 DEAKKAEEAKKADEAKKAEEAKK 1535
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 253-359 3.15e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.52  E-value: 3.15e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345 253 LIPAVPLMTPAVPVPTQRPLEAQDNTESEERLAEVRNILEQKRKERVEEEKRMEK-ENELRRRRDGREAQSQQARAKEQE 331
Cdd:COG4942   5 LLLALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAlERRIAALARRIRALEQELAALEAE 84

                        90       100
                ....*....|....*....|....*...
gi 21356345 332 LKNMQEQIKRERQEELAARERIRAQIAA 359
Cdd:COG4942  85 LAELEKEIAELRAELEAQKEELAELLRA 112
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 269-361 3.30e-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: 40.82  E-value: 3.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345    269 QRPLEAQDNTESEERLAEVRNILEQKRKERVEEEKRMEkenELRRRRDGREAQSQQARAKEQELkNMQEQIKRERQEELA 348
Cdd:TIGR02169  848 QIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLG---DLKKERDELEAQLRELERKIEEL-EAQIEKKRKRLSELK 923

                           90
                   ....*....|...
gi 21356345    349 AreriRAQIAADR 361
Cdd:TIGR02169  924 A----KLEALEEE 932
HlpA COG2825
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ...
 286-352 3.45e-03

Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442073 [Multi-domain]  Cd Length: 171  Bit Score: 38.66  E-value: 3.45e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21356345 286 EVRNILEQKRKERVEEEKRMEKE-NELRRR--RDGREAQSQQARAKEQELKNMQEQIKR---ERQEELAARER 352
Cdd:COG2825  43 AAQKKLEKEFKKRQAELQKLEKElQALQEKlqKEAATLSEEERQKKERELQKKQQELQRkqqEAQQDLQKRQQ 115
PRK13831 PRK13831
conjugal transfer protein TrbI; Provisional
 235-392 3.78e-03

conjugal transfer protein TrbI; Provisional


Pssm-ID: 172358 [Multi-domain]  Cd Length: 432  Bit Score: 40.10  E-value: 3.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345  235 EGSATTSGAAARNFA-------TNNLIPAVPLMTPAVPVPTQRPLEaqdntESEErlaevrNILEQKRKERVEEEKRMEK 307
Cdd:PRK13831  56 DGPETSSGTPASTFAdqlkrgvTDGIIGEPQQQQTFQPTPVETQQE-----EKAV------NPFTPQPGQREERRPTLES 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345  308 ENELRRRRdgreaqsqqarAKEQelknmQEQIKRERQEELAARERIRAQ-----IAADRAEQAQRFNTpdiSSTTNSVAA 382
Cdd:PRK13831 125 EEEWRARL-----------KREQ-----EEQYLRERQRQRMARLQANAAaydspLAVDIGKVEKRTAD---TNDTATQTT 185

                        170
                 ....*....|
gi 21356345  383 TAASNVITTD 392
Cdd:PRK13831 186 NATSTAGASD 195
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 268-365 4.08e-03

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 40.54  E-value: 4.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345    268 TQRPLEAQDNTESEERLAEVRNILEQKRKERVEEEKRMEK--------ENELRRRRDGREAQSQQARAKEQELKNMQEQI 339
Cdd:pfam01576  763 KQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKlqaqmkdlQRELEEARASRDEILAQSKESEKKLKNLEAEL 842

                           90       100
                   ....*....|....*....|....*.
gi 21356345    340 KReRQEELAARERIRAQIAADRAEQA 365
Cdd:pfam01576  843 LQ-LQEDLAASERARRQAQQERDELA 867
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
275-367 4.16e-03

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 39.51  E-value: 4.16e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345 275 QDNTESEERLAEVRNILEQKRKERVE-EEKRMEKENELRRRRDGREAQSQQARAKEQELKNMQE----------QIKRER 343
Cdd:COG1340   1 SKTDELSSSLEELEEKIEELREEIEElKEKRDELNEELKELAEKRDELNAQVKELREEAQELREkrdelnekvkELKEER 80

                        90       100
                ....*....|....*....|....
gi 21356345 344 QEELAARERIRAQIAADRAEQAQR 367
Cdd:COG1340  81 DELNEKLNELREELDELRKELAEL 104
PTZ00121 PTZ00121
MAEBL; Provisional
 273-367 4.30e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.51  E-value: 4.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345   273 EAQDNTESEE--RLAEVRNILEQKRKE---RVEEEKRMEKENELRRRRDGREAQSQQARAKEQELKNMQEQIKRE---RQ 344
Cdd:PTZ00121 1123 KAEDARKAEEarKAEDARKAEEARKAEdakRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEdarKA 1202

                          90       100
                  ....*....|....*....|...
gi 21356345   345 EELAARERIRAQIAADRAEQAQR 367
Cdd:PTZ00121 1203 EAARKAEEERKAEEARKAEDAKK 1225
DDRGK pfam09756
DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and ...
 292-358 4.67e-03

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


Pssm-ID: 370664 [Multi-domain]  Cd Length: 188  Bit Score: 38.87  E-value: 4.67e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21356345   292 EQKRKER-VEEEKRMEKE----NELRRRRDGREAQSQQARAKEQELKNMQEQIKRERQEELaarERIRAQIA 358
Cdd:pfam09756  15 EAKRQQReAEEEEREEREkleeKREEEYKEREEREEEAEKEKEEEERKQEEEQERKEQEEY---EKLKSQFV 83
PTZ00121 PTZ00121
MAEBL; Provisional
 269-357 4.72e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.51  E-value: 4.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345   269 QRPLEAQDNTESEE--RLAEVRNILEQKRKE----RVEEEKRMEKENELRRRRDGREAQSQQARAKEQELKNMQEQIKRE 342
Cdd:PTZ00121 1687 EKKAAEALKKEAEEakKAEELKKKEAEEKKKaeelKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEE 1766

                          90
                  ....*....|....*
gi 21356345   343 RQEELAARERIRAQI 357
Cdd:PTZ00121 1767 EKKAEEIRKEKEAVI 1781
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 280-366 5.02e-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: 40.04  E-value: 5.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345    280 SEERLAEVRNILEQKRKERVEEEKRMEKE-NELRRRRDGREAQSQQARAKEQELKNMQEQIKRERQEELAARERIRAQIA 358
Cdd:TIGR02168  317 QLEELEAQLEELESKLDELAEELAELEEKlEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIA 396


                   ....*...
gi 21356345    359 ADRAEQAQ 366
Cdd:TIGR02168  397 SLNNEIER 404
CHIP_TPR_N pfam18391
CHIP N-terminal tetratricopeptide repeat domain; This is N-terminal tetratricopeptide repeat ...
 294-357 5.02e-03

CHIP N-terminal tetratricopeptide repeat domain; This is N-terminal tetratricopeptide repeat (TPR) domain found in C terminus of Hsp70 interacting proteins (CHIP). The TPR domain of CHIP binds directly to EEVD motifs located at the C termini of Hsc/Hsp70 and Hsp90.


Pssm-ID: 436460  Cd Length: 83  Bit Score: 36.41  E-value: 5.02e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21356345   294 KRKERVEEEKRMEKENELR----------RRRDGREAQSQQARAKEQELKNMQEQIKRERQEELAARERIRAQI 357
Cdd:pfam18391   3 KKRWNVQEEKRIKQEIELQsylnrlidedKERQLAELELSEEGSDDEEKEEEIDEIEQECDEYLAELNNLFAQV 76
UDM1_RNF168_RNF169-like cd22249
UDM1 (ubiquitin-dependent DSB recruitment module 1) found in RING finger proteins RNF168, ...
 281-350 5.26e-03

UDM1 (ubiquitin-dependent DSB recruitment module 1) found in RING finger proteins RNF168, RNF169 and similar proteins; This model represents the UDM1 (ubiquitin-dependent double-strand break [DSB] recruitment module 1) found in RING finger proteins, RNF168 and RNF169. RNF168 is an E3 ubiquitin-protein ligase that promotes non-canonical K27 ubiquitination to signal DNA damage. It functions, together with RNF8, as a DNA damage response (DDR) factor that promotes a series of ubiquitylation events on substrates such as H2A and H2AX. With H2AK13/15 ubiquitylation, it facilitates recruitment of repair factors p53-binding protein 1 (53BP1) or the RAP80-BRCA1 complex to sites of double-strand breaks (DSBs), and inhibits homologous recombination (HR) in cells deficient in the tumor suppressor BRCA1. RNF168 also promotes H2A neddylation, which antagonizes ubiquitylation of H2A and regulates DNA damage repair. In addition, RNF168 forms a functional complex with RAD6A or RAD6B during the DNA damage response. RNF169 is an uncharacterized E3 ubiquitin-protein ligase paralogous to RNF168. It functions as a negative regulator of the DNA damage signaling cascade. RNF169 recognizes polyubiquitin structures but does not itself contribute to double-strand break (DSB)-induced chromatin ubiquitylation. It contributes to the regulation of DSB repair pathway utilization via functionally competing with recruiting repair factors, 53BP1 and RAP80-BRCA1, for association with RNF168-modified chromatin, independent of its catalytic activity, limiting the magnitude of the RNF8/RNF168-dependent signaling response to DSBs. The UDM1 domain comprises LRM1 (LR motif 1), UMI (ubiquitin-interacting motif [UIM]- and MIU-related UBD) and MIU1 (motif interacting with ubiquitin 1). Mutations of Ub-interacting residues in UDM1 have little effect on the accumulation of RNF168 to DSB sites, suggesting that it may not be the main site of binding ubiquitylated and polyubiquitylated targets.


Pssm-ID: 409016 [Multi-domain]  Cd Length: 66  Bit Score: 35.71  E-value: 5.26e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345 281 EERLAEVRNILEQKRKERVEEEKRmekenelrrrrdgREAQSQQARAKEQELKNMQEQIKRERQEELAAR 350
Cdd:cd22249   9 EEYEAQLKKLEEERRKEREEEEKA-------------SEELIRKLQEEEERQRKREREEQLKQDEELAKQ 65
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 268-370 5.42e-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: 40.04  E-value: 5.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345    268 TQRPLEAQDNTESEERLAEVRNILEQKRKERVEEEKRMEKENE------------------LRRRRDGREAQSQQARAKE 329
Cdd:TIGR02168  323 AQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAeleelesrleeleeqletLRSKVAQLELQIASLNNEI 402

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 21356345    330 QELKNMQEQIKRERQEELA-ARERIRAQIAADRAEQAQRFNT 370
Cdd:TIGR02168  403 ERLEARLERLEDRRERLQQeIEELLKKLEEAELKELQAELEE 444
PTZ00121 PTZ00121
MAEBL; Provisional
 273-367 5.64e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.12  E-value: 5.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345   273 EAQDNTESEERLAEVRNILEQKRK-----ERVEEEKRME---KENELRRRRDGREAQSQQARaKEQELKNMQEQIKRERQ 344
Cdd:PTZ00121 1422 EAKKKAEEKKKADEAKKKAEEAKKadeakKKAEEAKKAEeakKKAEEAKKADEAKKKAEEAK-KADEAKKKAEEAKKKAD 1500

                          90       100
                  ....*....|....*....|...
gi 21356345   345 EELAARERIRAQIAADRAEQAQR 367
Cdd:PTZ00121 1501 EAKKAAEAKKKADEAKKAEEAKK 1523
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 272-366 6.21e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 39.36  E-value: 6.21e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345 272 LEAQDNTESEERLAEVRNILEQkRKERVEEEKRmeKENELRRRRDGREAQSQQARAKEQELKNMQEQIKRERQEELAARE 351
Cdd:COG4942 126 LSPEDFLDAVRRLQYLKYLAPA-RREQAEELRA--DLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLA 202

                        90
                ....*....|....*
gi 21356345 352 RIRAQIAADRAEQAQ 366
Cdd:COG4942 203 RLEKELAELAAELAE 217
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
 270-352 6.39e-03

Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.


Pssm-ID: 464768 [Multi-domain]  Cd Length: 374  Bit Score: 39.25  E-value: 6.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345   270 RPLEAQDNTESEERLAEVRNILEQKRKERVEEEKrmeKENELRRRRdgreaQSQQARAKEQELKNMQEQIKRERQE--EL 347
Cdd:pfam15558  82 ADRREKQVIEKESRWREQAEDQENQRQEKLERAR---QEAEQRKQC-----QEQRLKEKEEELQALREQNSLQLQErlEE 153


                  ....*
gi 21356345   348 AARER 352
Cdd:pfam15558 154 ACHKR 158
rne PRK10811
ribonuclease E; Reviewed
 263-367 6.74e-03

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 39.64  E-value: 6.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345   263 AVPVPTQRPLEAQDNTESEERlaevRNILEQKRKERveEEKRMEKENelRRRRDGREAQSQQARAKEQELKNMQEQIKRE 342
Cdd:PRK10811  586 TKPQEQPAPKAEAKPERQQDR----RKPRQNNRRDR--NERRDTRDN--RTRREGRENREENRRNRRQAQQQTAETRESQ 657

                          90       100
                  ....*....|....*....|....*
gi 21356345   343 RQEELAARERIRAQIAADRAEQAQR 367
Cdd:PRK10811  658 QAEVTEKARTQDEQQQAPRRERQRR 682
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 273-346 6.88e-03

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


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 36.82  E-value: 6.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345   273 EAQDNTESEERLAEVRNILEQKrKERVEEEKRMEKENELRRRRDGREAQS------QQARAKEQELKNMQEQIKRERQEE 346
Cdd:pfam20492  42 ERRQAEEEAERLEQKRQEAEEE-KERLEESAEMEAEEKEQLEAELAEAQEeiarleEEVERKEEEARRLQEELEEAREEE 120
UBX_UBXN11 cd17077
Ubiquitin regulatory domain X (UBX) found in UBX domain protein 11 (UBXN11) and similar ...
 442-476 6.93e-03

Ubiquitin regulatory domain X (UBX) found in UBX domain protein 11 (UBXN11) and similar proteins; UBXN11, also termed colorectal tumor-associated antigen COA-1, or socius, or UBX domain-containing protein 5 (UBXD5), belongs to the UBXD family of proteins that contains the ubiquitin regulatory domain X (UBX) with a beta-grasp ubiquitin-like fold, but without the C-terminal double glycine motif. UBX domain is typically located at the carboxyl terminus of proteins, and participates broadly in the regulation of protein degradation. UBXN11 may function as a cofactor of p97 (also known as VCP or Cdc48), which is a homohexameric AAA ATPase (ATPase associated with a variety of activities) involved in a variety of functions ranging from cell-cycle regulation to membrane fusion and protein degradation. UBXN11 also acts as a novel interacting partner of Rnd proteins (Rnd1, Rnd2, and Rnd3/RhoE), new members of Rho family of small GTPases. It directly binds to Rnd GTPases through its C-terminal region, and further participates in disassembly of actin stress fibers. UBXN11 also binds directly to Galpha12 and Galpha13 through its N-terminal region. As a novel activator of the Galpha12 family, UBXN11 promotes the Galpha12-induced RhoA activation.


Pssm-ID: 340597  Cd Length: 76  Bit Score: 35.66  E-value: 6.93e-03
                        10        20        30
                ....*....|....*....|....*....|....*
gi 21356345 442 DFTLATSYPRREFQteDEVKTLNELNLVPNAVVLV 476
Cdd:cd17077  43 SYEIVTTFPNKVYD--DDSATLEELGLVPNATLHL 75
RNase_Y_N pfam12072
RNase Y N-terminal region;
272-366 7.56e-03

RNase Y N-terminal region;


Pssm-ID: 463456 [Multi-domain]  Cd Length: 201  Bit Score: 38.33  E-value: 7.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345   272 LEAQDntESEERLAEVRNILEQKRKERVEEEKR-MEKENELRRRRDGREAQSQQARAKEQELKNMQEQIKrERQEELAAR 350
Cdd:pfam12072  56 LEAKE--EIHKLRAEAERELKERRNELQRQERRlLQKEETLDRKDESLEKKEESLEKKEKELEAQQQQLE-EKEEELEEL 132

                          90       100
                  ....*....|....*....|
gi 21356345   351 ERIRAQ----IAADRAEQAQ 366
Cdd:pfam12072 133 IEEQRQelerISGLTSEEAK 152
CDC3 COG5019
Septin family protein [Cell cycle control, cell division, chromosome partitioning, ...
 273-349 7.70e-03

Septin family protein [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];


Pssm-ID: 227352 [Multi-domain]  Cd Length: 373  Bit Score: 39.23  E-value: 7.70e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345 273 EAQDNTESEERLAEVRNILEQKRKERV-EEEKRM-EKENELRRRRDgreaqsqqarAKEQELKNMQEQIK-RERQEELAA 349
Cdd:COG5019 300 EPSLKEIHEARLNEEERELKKKFTEKIrEKEKRLeELEQNLIEERK----------ELNSKLEEIQKKLEdLEKRLEKLK 369
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 270-346 8.38e-03

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


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 37.33  E-value: 8.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345   270 RPLEAQDNTESEERLAEVRNILEQKRKERVEEEKRMEKENE-----LR----RRRDGREAQSQQARAKEQELKNMQEQI- 339
Cdd:pfam05672  64 RRLEEERRREEEERQRKAEEEAEEREQREQEEQERLQKQKEeaeakAReeaeRQRQEREKIMQQEEQERLERKKRIEEIm 143


                  ....*..
gi 21356345   340 KRERQEE 346
Cdd:pfam05672 144 KRTRKSD 150
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
273-365 8.80e-03

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 38.74  E-value: 8.80e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345 273 EAQDNTESEERLAEVRNILEQKRKERVEEEKRM------------------EKENELRRRRDG-----------REAQSQ 323
Cdd:COG1340 151 KAKKALEKNEKLKELRAELKELRKEAEEIHKKIkelaeeaqelheemielyKEADELRKEADElhkeiveaqekADELHE 230

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 21356345 324 QARAKEQELKNMQEQIKRERQEELAARERIRAQIAADRAEQA 365
Cdd:COG1340 231 EIIELQKELRELRKELKKLRKKQRALKREKEKEELEEKAEEI 272
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 293-365 9.37e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 39.02  E-value: 9.37e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21356345  293 QKRKERVEEEKRMEKENELRRrrdgrEAQSQQARAKEQELKNMQEQIKRERQEELAARERIRAQIAADRAEQA 365
Cdd:PRK09510  74 AKRAEEQRKKKEQQQAEELQQ-----KQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKA 141
mS26_PET12 cd23703
Saccharomyces cerevisiae mitochondrial small ribosomal subunit protein mS26 and similar ...
 263-364 9.85e-03

Saccharomyces cerevisiae mitochondrial small ribosomal subunit protein mS26 and similar proteins; mS26, also known as mitochondrial 37S ribosomal protein PET12, is a component of the mitochondrial small ribosomal subunit (mt-SSU) of Saccharomyces cerevisiae mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane. The family also includes a group of uncharacterized proteins from pezizomycotina, which show high sequence similarity with mS26.


Pssm-ID: 467916 [Multi-domain]  Cd Length: 179  Bit Score: 37.53  E-value: 9.85e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356345 263 AVPVPTQRPLEAQDNTESEE---RLAEVRnileqkrkeR-------VEEEKRMEKENELRRRRdGREAQSQQARAKEQE- 331
Cdd:cd23703  31 TTPEPKKEPKPKSPLSEYQEwkrKMAELR---------RqnlreglRELEERKLKTEELRAKR-SERKQAERERALNAPe 100

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 21356345 332 -----------LKNMQEQIKR-----ERQEELAARERIRAQIAADRAEQ 364
Cdd:cd23703 101 rederltlptiESALLGPLMRvrtdpEREERAAKRRANREAKELAKKEA 149
 
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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